Proposed Changes to the Enzyme List

References:

1.	Chen, X. and Facchini, P.J. Short-chain dehydrogenase/reductase catalyzing the final step of noscapine biosynthesis is localized to laticifers in opium poppy. Plant J. 77 (2014) 173–184. [PMID: 24708518]
2.	Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl. Acad. Sci. USA 115 (2018) E3922–E3931. [DOI] [PMID: 29610307]

[EC 1.1.1.415 created 2018]

1.2.1.101

Accepted name:

L-tyrosine reductase

Reaction:

L-tyrosinal + NADP⁺ + AMP + diphosphate = L-tyrosine + NADPH + H⁺ + ATP

Glossary:

L-tyrosinal = (2S)-2-amino-3-(4-hydroxyphenyl)propanal

Other name(s):

lnaA (gene name); lnbA (gene name)

Systematic name:

(2S)-2-amino-3-(4-hydroxyphenyl)propanal:NADP⁺ oxidoreductase (ATP-forming)

Comments:

The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine. It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde.

Links to other databases:

BRENDA, EXPASY, KEGG, CAS registry number: 9074-94-6

References:

1.	Forseth, R.R., Amaike, S., Schwenk, D., Affeldt, K.J., Hoffmeister, D., Schroeder, F.C. and Keller, N.P. Homologous NRPS-like gene clusters mediate redundant small-molecule biosynthesis in Aspergillus flavus. Angew. Chem. Int. Ed. Engl. 52 (2013) 1590–1594. [PMID: 23281040]

[EC 1.2.1.101 created 2018]

1.3.1.118

Accepted name:

meromycolic acid enoyl-[acyl-carrier-protein] reductase

Reaction:

a meromycolyl-[acyl-carrier protein] + NAD⁺ = a trans-Δ²-meromycolyl-[acyl-carrier protein] + NADH + H⁺

Glossary:

meromycolic acids are one of the two precursors of the mycolic acids produced by Mycobacteria. They consist of a long chain typically of 50–60 carbons, which is functionalized by different groups.

Other name(s):

inhA (gene name)

Systematic name:

meromycolyl-[acyl-carrier protein]:NAD⁺ oxidoreductase

Comments:

InhA is a component of the fatty acid synthase (FAS) II system of Mycobacterium tuberculosis, catalysing an enoyl-[acyl-carrier-protein] reductase step. The enzyme acts on very long and unsaturated fatty acids that form the meromycolic component of mycolic acids. It extends FASI-derived C₂₀ fatty acids to form C₆₀ to C₉₀ mycolic acids. The enzyme, which forms a homotetramer, is the target of the preferred antitubercular drug isoniazid.

Links to other databases:

References:

1.	Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R., Jr. and Blanchard, J.S. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995) 8235–8241. [PMID: 7599116]
2.	Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R. and Sacchettini, J.C. Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD⁺ and a C₁₆ fatty acyl substrate. J. Biol. Chem. 274 (1999) 15582–15589. [PMID: 10336454]
3.	Marrakchi, H., Laneelle, G. and Quemard, A. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiology 146 (2000) 289–296. [PMID: 10708367]
4.	Vilcheze, C., Morbidoni, H.R., Weisbrod, T.R., Iwamoto, H., Kuo, M., Sacchettini, J.C. and Jacobs, W.R., Jr. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 4059–4067. [PMID: 10869086]
5.	Gurvitz, A., Hiltunen, J.K. and Kastaniotis, A.J. Function of heterologous Mycobacterium tuberculosis InhA, a type 2 fatty acid synthase enzyme involved in extending C₂₀ fatty acids to C⁶⁰-to-C₉₀ mycolic acids, during de novo lipoic acid synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 74 (2008) 5078–5085. [PMID: 18552191]
6.	Chollet, A., Mourey, L., Lherbet, C., Delbot, A., Julien, S., Baltas, M., Bernadou, J., Pratviel, G., Maveyraud, L. and Bernardes-Genisson, V. Crystal structure of the enoyl-ACP reductase of Mycobacterium tuberculosis (InhA) in the apo-form and in complex with the active metabolite of isoniazid pre-formed by a biomimetic approach. J. Struct. Biol. 190 (2015) 328–337. [PMID: 25891098]

[EC 1.3.1.118 created 2018]

1.3.1.119

Accepted name:

chlorobenzene dihydrodiol dehydrogenase

Reaction:

(1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD⁺ = 3-chlorocatechol + NADH + H⁺

For diagram of chlorobenzene catabolism, click here

Other name(s):

tecB (gene name)

Systematic name:

(1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol:NAD⁺ oxidoreductase

Comments:

This bacterial enzyme can transform various dihydrodiols of chlorobenzenes into the respective catechols, including the dihydrodiols of mono-, di-, tri-, and tetra-chlorinated benzenes. It also accepts the dihydrodiols of various chlorotoluenes. Substrates for the enzyme are generated by the broad spectrum EC 1.14.12.26, chlorobenzene dioxygenase.

Links to other databases:

References:

1.	Spiess, E. and Gorisch, H. Purification and characterization of chlorobenzene cis-dihydrodiol dehydrogenase from Xanthobacter flavus 14p1. Arch. Microbiol. 165 (1996) 201–205. [PMID: 8599538]
2.	Pollmann, K., Beil, S. and Pieper, D.H. Transformation of chlorinated benzenes and toluenes by Ralstonia sp. strain PS12 tecA (tetrachlorobenzene dioxygenase) and tecB (chlorobenzene dihydrodiol dehydrogenase) gene products. Appl. Environ. Microbiol. 67 (2001) 4057–4063. [PMID: 11526005]
3.	Pollmann, K., Wray, V. and Pieper, D.H. Chloromethylmuconolactones as critical metabolites in the degradation of chloromethylcatechols: recalcitrance of 2-chlorotoluene. J. Bacteriol. 187 (2005) 2332–2340. [PMID: 15774876]

[EC 1.3.1.119 created 2018]

1.5.1.52

Accepted name:

staphylopine dehydrogenase

Reaction:

staphylopine + NADP⁺ + H₂O = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + pyruvate + NADPH + H⁺

For diagram of staphylopine biosynthesis, click here

Glossary:

staphylopine = (2S)-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}-2-[(1-carboxyethyl)amino]butanoate

Other name(s):

cntM (gene name); staphylopine synthase

Systematic name:

staphylopine:NADP⁺ oxidoreductase [(2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate]-forming

Comments:

The enzyme, characterized from the bacterium Staphylococcus aureus, catalyses the last reaction in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, copper, and cobalt.

Links to other databases:

References:

1.	Ghssein, G., Brutesco, C., Ouerdane, L., Fojcik, C., Izaute, A., Wang, S., Hajjar, C., Lobinski, R., Lemaire, D., Richaud, P., Voulhoux, R., Espaillat, A., Cava, F., Pignol, D., Borezee-Durant, E. and Arnoux, P. Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus. Science 352 (2016) 1105–1109. [PMID: 27230378]
2.	McFarlane, J.S., Davis, C.L. and Lamb, A.L. Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenase. J. Biol. Chem. 293 (2018) 8009–8019. [PMID: 29618515]

[EC 1.5.1.52 created 2018]

1.6.6.9

Deleted entry:

The activity is now known to be catalysed by EC 1.7.2.3, trimethylamine-N-oxide reductase.

[EC 1.6.6.9 created 1972, deleted 2018]

*EC

1.6.99.3

Deleted entry:

NADH dehydrogenase. The activity is covered by EC 7.1.1.2, NADH:ubiquinone reductase (H⁺-translocating)

[EC 1.6.99.3 created 1961 as EC 1.6.2.1, transferred 1965 to EC 1.6.99.3, modified 2018, deleted 2020]

1.10.2.2

Transferred entry:

quinol—cytochrome-c reductase. Now EC 7.1.1.8, quinol—cytochrome-c reductase

[EC 1.10.2.2 created 1978, modified 2013, deleted 2018]

1.10.3.10

Transferred entry:

ubiquinol oxidase (H⁺-transporting). Now EC 7.1.1.3, ubiquinol oxidase (H⁺-transporting)

[EC 1.10.3.10 created 2011, modified 2014, deleted 2018]

1.10.3.12

Transferred entry:

menaquinol oxidase (H⁺-transporting). Now EC 7.1.1.5, menaquinol oxidase (H⁺-transporting)

[EC 1.10.3.12 created 2011, deleted 2018]

1.10.3.13

Transferred entry:

caldariellaquinol oxidase (H⁺-transporting). Now EC 7.1.1.4, caldariellaquinol oxidase (H⁺-transporting)

[EC 1.10.3.13 created 2013, deleted 2018]

1.10.3.14

Transferred entry:

ubiquinol oxidase (electrogenic, non H⁺-transporting). Now EC 7.1.1.7, ubiquinol oxidase (electrogenic, proton-motive force generating)

[EC 1.10.3.14 created 2014, modified 2017, deleted 2018]

1.10.9.1

Transferred entry:

plastoquinol—plastocyanin reductase. Now EC 7.1.1.6, plastoquinol—plastocyanin reductase

[EC 1.10.9.1 created 1984 as EC 1.10.99.1, transferred 2011 to EC 1.10.9.1, deleted 2018]

1.13.11.87

Accepted name:

endo-cleaving rubber dioxygenase

Reaction:

Cleavage of cis-1,4-polyisoprene polymers into a mixture of compounds, including a C₂₀ compound ((4Z,8Z,12Z,16Z,20Z,24Z)-4,8,12,16,20,24-hexamethyl-28-oxononacosa-4,8,12,16,20,24-hexaenal), a C₂₅ compound ((4Z,8Z,12Z,16Z,20Z)-4,8,12,16,20-pentamethyl-24-oxopentacosa-4,8,12,16,20-pentaenal), a C₃₀ compound ((4Z,8Z,12Z,16Z)-4,8,12,16-tetramethyl-20-oxohenicosa-4,8,12,16-tetraenal), and larger isoprenologes such as C₃₅, C₄₀, C₄₅, and higher analogues.

For diagram of all-cis-polyprenyl diphosphate, click here

Other name(s):

latex clearing protein; lcp (gene name); roxB (gene name)

Systematic name:

cis-1,4-polyisoprene:oxygen dioxygenase (endo-cleaving)

Comments:

The enzyme catalyses the cleavage of the double bonds in natural and synthetic rubber, producing a mixture of C₂₀, C₂₅, C₃₀, and higher oligo-isoprenoids with ketone and aldehyde groups at their ends. Two unrelated bacterial enzymes are known to possess this activity - the enzyme from Streptomyces sp. K30 (Lcp) contains a b-type cytochrome, while the enzyme from Xanthomonas sp. 35Y, (RoxB) contains two c-type cytochromes. Both enzymes attack the substrate at random locations, and are not able to cleave the C₃₅ or smaller products into shorter fragments.

Links to other databases:

References:

1.	Tsuchii, A. and Takeda, K. Rubber-degrading enzyme from a bacterial culture. Appl. Environ. Microbiol. 56 (1990) 269–274. [PMID: 16348100]
2.	Jendrossek, D. and Reinhardt, S. Sequence analysis of a gene product synthesized by Xanthomonas sp. during growth on natural rubber latex. FEMS Microbiol. Lett. 224 (2003) 61–65. [DOI] [PMID: 12855168]
3.	Braaz, R., Fischer, P. and Jendrossek, D. Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene). Appl. Environ. Microbiol. 70 (2004) 7388–7395. [DOI] [PMID: 15574940]
4.	Braaz, R., Armbruster, W. and Jendrossek, D. Heme-dependent rubber oxygenase RoxA of Xanthomonas sp. cleaves the carbon backbone of poly(cis-1,4-Isoprene) by a dioxygenase mechanism. Appl. Environ. Microbiol. 71 (2005) 2473–2478. [DOI] [PMID: 15870336]
5.	Seidel, J., Schmitt, G., Hoffmann, M., Jendrossek, D. and Einsle, O. Structure of the processive rubber oxygenase RoxA from Xanthomonas sp. Proc. Natl. Acad. Sci. USA 110 (2013) 13833–13838. [DOI] [PMID: 23922395]
6.	Birke, J. and Jendrossek, D. Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms. Appl. Environ. Microbiol. 80 (2014) 5012–5020. [DOI] [PMID: 24907333]
7.	Birke, J., Röther, W. and Jendrossek, D. RoxB is a novel type of rubber oxygenase that combines properties of rubber oxygenase RoxA and latex clearing protein (Lcp). Appl. Environ. Microbiol. 83 (2017) e00721-17. [PMID: 28500046]

[EC 1.13.11.87 created 2018]

1.14.11.60

Accepted name:

scopoletin 8-hydroxylase

Reaction:

scopoletin + 2-oxoglutarate + O₂ = fraxetin + succinate + CO₂

Glossary:

fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
scopoletin = 7-hydroxy-6-methoxy-2H-chromen-2-one

Other name(s):

S8H (gene name)

Systematic name:

scopoletin,2-oxoglutarate:oxygen oxidoreductase (8-hydroxylating)

Comments:

Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.

Links to other databases:

References:

1.	Siwinska, J., Siatkowska, K., Olry, A., Grosjean, J., Hehn, A., Bourgaud, F., Meharg, A.A., Carey, M., Lojkowska, E. and Ihnatowicz, A. Scopoletin 8-hydroxylase: a novel enzyme involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis. J. Exp. Bot. 69 (2018) 1735–1748. [PMID: 29361149]
2.	Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442–450. [PMID: 29581584]

[EC 1.14.11.60 created 2018]

1.14.12.26

Accepted name:

chlorobenzene dioxygenase

Reaction:

chlorobenzene + NADH + H⁺ + O₂ = (1R,2R)-3-chlorocyclohexa-3,5-diene-1,2-diol + NAD⁺

For diagram of chlorobenzene catabolism, click here and for diagram of EC 1.14.12, click here

Other name(s):

TecA

Systematic name:

chlorobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating)

Comments:

This bacterial enzyme is a class IIB dioxygenase, comprising three components - a heterodimeric terminal dioxygenase, a ferredoxin protein, and a ferredoxin reductase. The enzyme acts on a range of aromatic compounds, including mono-, di-, tri-, and tetra-chlorinated benzenes and toluenes.

Links to other databases:

References:

1.	Spiess, E., Sommer, C. and Gorisch, H. Degradation of 1,4-dichlorobenzene by Xanthobacter flavus 14p1. Appl. Environ. Microbiol. 61 (1995) 3884–3888. [PMID: 8526500]
2.	Sommer, C. and Gorisch, H. Enzymology of the degradation of (di)chlorobenzenes by Xanthobacter flavus 14p1. Arch. Microbiol. 167 (1997) 384–391. [PMID: 9148781]
3.	Beil, S., Happe, B., Timmis, K.N. and Pieper, D.H. Genetic and biochemical characterization of the broad spectrum chlorobenzene dioxygenase from Burkholderia sp. strain PS12 - dechlorination of 1,2,4,5-tetrachlorobenzene. Eur. J. Biochem. 247 (1997) 190–199. [PMID: 9249026]
4.	Beil, S., Mason, J.R., Timmis, K.N. and Pieper, D.H. Identification of chlorobenzene dioxygenase sequence elements involved in dechlorination of 1,2,4,5-tetrachlorobenzene. J. Bacteriol. 180 (1998) 5520–5528. [PMID: 9791099]

[EC 1.14.12.26 created 2018]

1.14.14.140

Transferred entry:

licodione synthase. Now included with EC 1.14.14.162, flavanone 2-hydroxylase

[EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162, deleted 2018]

1.14.14.159

Accepted name:

dolabradiene monooxygenase

Reaction:

(1) dolabradiene + O₂ + [reduced NADPH—hemoprotein reductase] = 15,16-epoxydolabrene + H₂O + [oxidized NADPH—hemoprotein reductase]
(2) 15,16-epoxydolabrene + O₂ + [reduced NADPH—hemoprotein reductase] = 3β-hydroxy-15,16-epoxydolabrene + H₂O + [oxidized NADPH—hemoprotein reductase]

For diagram of dolabradiene biosynthesis, click here

Glossary:

dolabradiene = (4aS,4bR,7S,8aR,10aS)-7-ethenyl-4b,7,10a-trimethyl-1-methylidenetetradecahydrophenanthrene

Other name(s):

CYP71Z16 (gene name)

Systematic name:

dolabradiene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (3β-hydroxy-15,16-epoxydolabrene-forming)

Comments:

A cytochrome P-450 (heme thiolate) enzyme characterized from maize. The enzyme catalyses the epoxidation of dolabradiene at C-16, followed by hydroxylation at C-3.

Links to other databases:

References:

Mafu, S., Ding, Y., Murphy, K.M., Yaacoobi, O., Addison, J.B., Wang, Q., Shen, Z., Briggs, S.P., Bohlmann, J., Castro-Falcon, G., Hughes, C.C., Betsiashvili, M., Huffaker, A., Schmelz, E.A. and Zerbe, P. Discovery, biosynthesis and stress-related accumulation of dolabradiene-derived defenses in maize. Plant Physiol. 176 (2018) 2677–2690. [PMID: 29475898]

[EC 1.14.14.159 created 2018]

1.14.14.160

Accepted name:

zealexin A1 synthase

Reaction:

(S)-β-macrocarpene + 3 O₂ + 3 [reduced NADPH—hemoprotein reductase] = zealexin A1 + 4 H₂O + 3 [oxidized NADPH—hemoprotein reductase] (overall reaction)
(1a) (S)-β-macrocarpene + O₂ + [reduced NADPH—hemoprotein reductase] = [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl]methanol + H₂O + [oxidized NADPH—hemoprotein reductase]
(1b) [(4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)-cyclohex-1-en-1-yl] methanol + O₂ + [reduced NADPH—hemoprotein reductase] = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + 2 H₂O + [oxidized NADPH—hemoprotein reductase]
(1c) (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carbaldehyde + O₂ + [reduced NADPH—hemoprotein reductase] = zealexin A1 + H₂O + [oxidized NADPH—hemoprotein reductase]

For diagram of zealexin biosynthesis, click here

Glossary:

(S)-β-macrocarpene = (1′S)-4′,5,5-trimethyl-1,1′-bi(cyclohexane)-1,3′-diene
zealexin A1 = (4S)-4-(5,5-dimethylcyclohex-1-en-1-yl)cyclohex-1-ene-1-carboxylate

Other name(s):

CYP71Z18 (gene name)

Systematic name:

(S)-β-macrocarpene,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (zealexin A1-forming)

Comments:

A cytochrome P-450 (heme thiolate) enzyme characterized from maize. The enzyme sequentially oxidizes(S)-β-macrocarpene via alcohol and aldehyde intermediates to form zealexin A1, a maize phytoalexin that provides biochemical protection against fungal infection.

Links to other databases:

References:

1.	Mao, H., Liu, J., Ren, F., Peters, R.J. and Wang, Q. Characterization of CYP71Z18 indicates a role in maize zealexin biosynthesis. Phytochemistry 121 (2016) 4–10. [PMID: 26471326]

[EC 1.14.14.160 created 2018]

1.14.14.161

Accepted name:

nepetalactol monooxygenase

Reaction:

(+)-cis,trans-nepetalactol + 3 [reduced NADPH—hemoprotein reductase] + 3 O₂ = 7-deoxyloganetate + 3 [oxidized NADPH—hemoprotein reductase] + 4 H₂O (overall reaction)
(1a) (+)-cis,trans-nepetalactol + [reduced NADPH—hemoprotein reductase] + O₂ = 7-deoxyloganetic alcohol + [oxidized NADPH—hemoprotein reductase] + H₂O
(1b) 7-deoxyloganetic alcohol + [reduced NADPH—hemoprotein reductase] + O₂ = iridotrial + [oxidized NADPH—hemoprotein reductase] + 2 H₂O
(1c) iridotrial + [reduced NADPH—hemoprotein reductase] + O₂ = 7-deoxyloganetate + [oxidized NADPH—hemoprotein reductase] + H₂O

For diagram of gibberellin A₁₂ biosynthesis, click here

Glossary:

(+)-cis,trans-nepetalactol = (4aS,7S,7aR)-4,7-dimethyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-1-ol
7-deoxyloganetate = (1S,4aS,7S,7aR)-1-hydroxy-7-methyl-1,4a,5,6,7,7a-hexahydrocyclopenta[c]pyran-4-carboxylate

Other name(s):

CYP76A26 (gene name); iridoid oxidase (misleading)

Systematic name:

(+)-cis,trans-nepetalactol,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (hydroxylating)

Comments:

The enzyme, characterized from the plant Catharanthus roseus, is a cytochrome P-450 (heme thiolate) protein. It catalyses three successive reactions in the pathway leading to biosynthesis of monoterpenoid indole alkaloids.

Links to other databases:

References:

Miettinen, K., Dong, L., Navrot, N., Schneider, T., Burlat, V., Pollier, J., Woittiez, L., van der Krol, S., Lugan, R., Ilc, T., Verpoorte, R., Oksman-Caldentey, K.M., Martinoia, E., Bouwmeester, H., Goossens, A., Memelink, J. and Werck-Reichhart, D. The seco-iridoid pathway from Catharanthus roseus. Nat. Commun. 5:3606 (2014). [PMID: 24710322]

[EC 1.14.14.161 created 2018]

1.14.14.162

Accepted name:

flavanone 2-hydroxylase

Reaction:

a flavanone + [reduced NADPH—hemoprotein reductase] + O₂ = a 2-hydroxyflavanone + [oxidized NADPH—hemoprotein reductase] + H₂O

For diagram of licodione biosynthesis, click here

Other name(s):

CYP93G2 (gene name); CYP93B1 (gene name); (2S)-flavanone 2-hydroxylase; licodione synthase

Systematic name:

flavanone,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)

Comments:

A cytochrome P-450 (heme thiolate) plant enzyme that catalyses the 2-hydroxylation of multiple flavanones such as (2S)-naringenin, (2S)-eriodictyol, (2S)-pinocembrin, and (2S)-liquiritigenin. The products are meta-stable and exist in an equilibrium with open forms such as 1-(4-hydroxyphenyl)-3-(2,4,6-trihydroxyphenyl)propane-1,3-dione.

Links to other databases:

References:

1.	Otani, K., Takahashi, T., Furuya, T. and Ayabe, S. Licodione synthase, a cytochrome P₄₅₀ monooxygenase catalyzing 2-hydroxylation of 5-deoxyflavanone, in cultured Glycyrrhiza echinata L. cells. Plant Physiol. 105 (1994) 1427–1432. [PMID: 12232298]
2.	Akashi, T., Aoki, T. and Ayabe, S. Identification of a cytochrome P₄₅₀ cDNA encoding (2S)-flavanone 2-hydroxylase of licorice (Glycyrrhiza echinata L.; Fabaceae) which represents licodione synthase and flavone synthase II. FEBS Lett. 431 (1998) 287–290. [DOI] [PMID: 9708921]
3.	Du, Y., Chu, H., Chu, I.K. and Lo, C. CYP93G2 is a flavanone 2-hydroxylase required for C-glycosylflavone biosynthesis in rice. Plant Physiol. 154 (2010) 324–333. [PMID: 20647377]

[EC 1.14.14.162 created 2018. EC 1.14.14.140 created 2004 as EC 1.14.13.87, transferred 2018 to EC 1.14.14.140, transferred 2018 to EC 1.14.14.162]

1.14.14.163

Accepted name:

(S)-1-hydroxy-N-methylcanadine 13-hydroxylase

Reaction:

(S)-1-hydroxy-cis-N-methylcanadine + [reduced NADPH—hemoprotein reductase] + O₂ = (13S,14R)-1,13-dihydroxy-cis-N-methylcanadine + [oxidized NADPH—hemoprotein reductase] + H₂O

For diagram of noscapine biosynthesis, click here

Other name(s):

CYP82X2 (gene name)

Systematic name:

(S)-1-hydroxy-cis-N-methylcanadine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (13-hydroxylating)

Comments:

The enzyme, characterized from the plant Papaver somniferum (opium poppy), participates in the biosynthesis of the isoquinoline alkaloid noscapine.

Links to other databases:

References:

1.	Dang, T.T., Chen, X. and Facchini, P.J. Acetylation serves as a protective group in noscapine biosynthesis in opium poppy. Nat. Chem. Biol. 11 (2015) 104–106. [DOI] [PMID: 25485687]
2.	Li, Y. and Smolke, C.D. Engineering biosynthesis of the anticancer alkaloid noscapine in yeast. Nat. Commun. 7:12137 (2016). [DOI] [PMID: 27378283]
3.	Li, Y., Li, S., Thodey, K., Trenchard, I., Cravens, A. and Smolke, C.D. Complete biosynthesis of noscapine and halogenated alkaloids in yeast. Proc. Natl. Acad. Sci. USA 115 (2018) E3922–E3931. [DOI] [PMID: 29610307]

[EC 1.14.14.163 created 2018]

1.14.14.164

Accepted name:

fraxetin 5-hydroxylase

Reaction:

fraxetin + [reduced NADPH—hemoprotein reductase] + O₂ = sideretin (reduced form) + [oxidized NADPH—hemoprotein reductase] + H₂O

Glossary:

fraxetin = 7,8-dihydroxy-6-methoxy-2H-chromen-2-one
sideretin (reduced form) = 5,7,8-trihydroxy-6-methoxy-2H-chromen-2-one

Other name(s):

CYP82C4; fraxetin 5-monooxygenase

Systematic name:

fraxetin,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (5-hydroxylating)

Comments:

A cytochrome P-450 (heme-thiolate) protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.

Links to other databases:

References:

1.	Rajniak, J., Giehl, R.FH., Chang, E., Murgia, I., von Wiren, N. and Sattely, E.S. Biosynthesis of redox-active metabolites in response to iron deficiency in plants. Nat. Chem. Biol. 14 (2018) 442–450. [PMID: 29581584]

[EC 1.14.14.164 created 2018]

1.14.14.165

Accepted name:

indole-3-carbonyl nitrile 4-hydroxylase

Reaction:

indole-3-carbonyl nitrile + [reduced NADPH—hemoprotein reductase] + O₂ = 4-hydroxyindole-3-carbonyl nitrile + [oxidized NADPH—hemoprotein reductase] + H₂O

Glossary:

indole-3-carbonyl nitrile = 2-(1H-indole-3-yl)-2-oxoacetonitrile
4-hydroxyindole-3-carbonyl nitrile = 2-(4-hydroxy-1H-indole-3-yl)-2-oxoacetonitrile

Other name(s):

CYP82C2

Systematic name:

indole-3-carbonyl nitrile,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (4-hydroxylating)

Comments:

A cytochrome P-450 (heme-thiolate) protein characterized from the plant Arabidopsis thaliana. Involved in biosynthesis of small cyanogenic compounds that take part in pathogen defense. The enzyme also catalyses the 5-hydroxylation of xanthotoxin [1].

Links to other databases:

References:

1.	Kruse, T., Ho, K., Yoo, H.D., Johnson, T., Hippely, M., Park, J.H., Flavell, R. and Bobzin, S. In planta biocatalysis screen of P450s identifies 8-methoxypsoralen as a substrate for the CYP82C subfamily, yielding original chemical structures. Chem. Biol. 15 (2008) 149–156. [PMID: 18291319]
2.	Rajniak, J., Barco, B., Clay, N.K. and Sattely, E.S. A new cyanogenic metabolite in Arabidopsis required for inducible pathogen defence. Nature 525 (2015) 376–379. [PMID: 26352477]

[EC 1.14.14.165 created 2018]

1.14.19.75

Accepted name:

very-long-chain acyl-lipid ω-9 desaturase

Reaction:

(1) 1-hexacosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = 1-[(17Z)-hexacos-17-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b₅ + 2 H₂O
(2) 1-tetracosanoyl-2-acyl-[phosphoglycerolipid] + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = 1-[(15Z)-tetracos-15-enoyl]-2-acyl-[phosphoglycerolipid] + 2 ferricytochrome b₅ + 2 H₂O

Other name(s):

ADS2 (gene name)

Systematic name:

very-long-chain acyl-[glycerolipid],ferrocytochrome b₅:oxygen oxidoreductase (ω⁹,ω⁸-cis-dehydrogenating)

Comments:

The enzyme, characterized from the plant Arabidopsis thaliana, acts on both 24:0 and 26:0 fatty acids, introducing a cis double bond at a position 9 carbons from the methyl end. These very-long-chain fatty acids are found as a minor component of seed lipids, but also in the membrane phosphatidylethanolamine and phosphatidylserine, in sphingolipids, as precursors and components of cuticular and epicuticular waxes, and in suberin.

Links to other databases:

References:

1.	Fukuchi-Mizutani, M., Tasaka, Y., Tanaka, Y., Ashikari, T., Kusumi, T. and Murata, N. Characterization of δA9 acyl-lipid desaturase homologues from Arabidopsis thaliana. Plant Cell Physiol. 39 (1998) 247–253. [PMID: 9559566]
2.	Smith, M.A., Dauk, M., Ramadan, H., Yang, H., Seamons, L.E., Haslam, R.P., Beaudoin, F., Ramirez-Erosa, I. and Forseille, L. Involvement of Arabidopsis acyl-coenzyme A desaturase-like2 (At2g31360) in the biosynthesis of the very-long-chain monounsaturated fatty acid components of membrane lipids. Plant Physiol. 161 (2013) 81–96. [PMID: 23175755]

[EC 1.14.19.75 created 2018]

1.16.5.1

Transferred entry:

ascorbate ferrireductase (transmembrane). Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane)

[EC 1.16.5.1 created 2011, deleted 2018]

*EC

1.17.4.4

Accepted name:

vitamin-K-epoxide reductase (warfarin-sensitive)

Reaction:

(1) phylloquinone + a protein with a disulfide bond + H₂O = 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues
(2) phylloquinol + a protein with a disulfide bond = phylloquinone + a protein with reduced L-cysteine residues

For diagram of the vitamin K cycle, click here

Glossary:

phylloquinone = vitamin K₁ = 2-methyl-3-phytyl-1,4-naphthoquinone
2,3-epoxyphylloquinone = vitamin K₁ 2,3-epoxide = 2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone

Other name(s):

VKORC1 (gene name); VKORC1L1 (gene name)

Systematic name:

phylloquinone:disulfide oxidoreductase

Comments:

The enzyme catalyses the reduction of vitamin K 2,3-epoxide, which is formed by the activity of EC 4.1.1.90, peptidyl-glutamate 4-carboxylase, back to its phylloquinol active form. The enzyme forms a tight complex with EC 5.3.4.1, protein disulfide-isomerase, which transfers the required electrons from newly-synthesized proteins by catalysing the formation of disulfide bridges. The enzyme acts on the epoxide forms of both phylloquinone (vitamin K₁) and menaquinone (vitamin K₂). Inhibited strongly by (S)-warfarin and ferulenol.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 55963-40-1

References:

1.	Whitlon, D.S., Sadowski, J.A. and Suttie, J.W. Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition. Biochemistry 17 (1978) 1371–1377. [PMID: 646989]
2.	Lee, J.L. and Fasco, M.J. Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide. Biochemistry 23 (1984) 2246–2252. [PMID: 6733086]
3.	Mukharji, I. and Silverman, R.B. Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone. Proc. Natl. Acad. Sci. USA 82 (1985) 2713–2717. [DOI] [PMID: 3857611]
4.	Li, T., Chang, C.Y., Jin, D.Y., Lin, P.J., Khvorova, A. and Stafford, D.W. Identification of the gene for vitamin K epoxide reductase. Nature 427 (2004) 541–544. [PMID: 14765195]
5.	Wajih, N., Hutson, S.M. and Wallin, R. Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K₁ 2,3-epoxide reduction. J. Biol. Chem. 282 (2007) 2626–2635. [PMID: 17124179]
6.	Spohn, G., Kleinridders, A., Wunderlich, F.T., Watzka, M., Zaucke, F., Blumbach, K., Geisen, C., Seifried, E., Muller, C., Paulsson, M., Bruning, J.C. and Oldenburg, J. VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding. Thromb Haemost 101 (2009) 1044–1050. [PMID: 19492146]
7.	Schulman, S., Wang, B., Li, W. and Rapoport, T.A. Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc. Natl. Acad. Sci. USA 107 (2010) 15027–15032. [PMID: 20696932]

[EC 1.17.4.4 created 1989 as EC 1.1.4.1, transferred 2014 to EC 1.17.4.4, modified 2018]

2.1.1.350

Accepted name:

menaquinone C⁸-methyltransferase

Reaction:

(1) 2 S-adenosyl-L-methionine + a menaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + an 8-methylmenaquinone + oxidized flavodoxin
(2) 2 S-adenosyl-L-methionine + a 2-demethylmenaquinone + reduced flavodoxin = S-adenosyl-L-homocysteine + L-methionine + 5′-deoxyadenosine + a 2-demethyl-8-methylmenaquinone + oxidized flavodoxin

For diagram of the vitamin K cycle, click here

Other name(s):

mqnK (gene name); menK (gene name)

Systematic name:

S-adenosyl-L-methionine:menaquinone C⁸-methyltransferase

Comments:

The enzyme, found in a wide range of bacteria and archaea, is a radical SAM (AdoMet) enzyme that utilizes two molecules of S-adenosyl-L-methionine, one as the methyl group donor, and one for the creation of a 5′-deoxyadenosine radical that drives the reaction forward.

Links to other databases:

References:

1.	Hein, S., Klimmek, O., Polly, M., Kern, M. and Simon, J. A class C radical S-adenosylmethionine methyltransferase synthesizes 8-methylmenaquinone. Mol. Microbiol. 104 (2017) 449–462. [PMID: 28164386]

[EC 2.1.1.350 created 2018]

2.3.1.274

Accepted name:

phosphate acyltransferase

Reaction:

an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein]

Other name(s):

plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase

Systematic name:

an acyl-[acyl-carrier protein]:phosphate acyltransferase

Comments:

The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg²⁺, the enzyme does not require a divalent cation.

Links to other databases:

References:

1.	Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765–772. [PMID: 16949372]
2.	Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7:69 (2007). [PMID: 17645809]
3.	Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157–163. [PMID: 19058030]
4.	Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59–66. [PMID: 29199103]

[EC 2.3.1.274 created 2018]

2.3.1.275

Accepted name:

acyl phosphate:glycerol-3-phosphate acyltransferase

Reaction:

an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycerol 3-phosphate + phosphate

Other name(s):

plsY (gene name); G3P acyltransferase; GPAT; lysophosphatidic acid synthase; LPA synthase

Systematic name:

acyl phosphoate:sn-glycerol 3-phosphate acyltransferase

Comments:

The enzyme, found in bacteria, catalyses a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. The enzyme is membrane-bound.

Links to other databases:

References:

1.	Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765–772. [PMID: 16949372]
2.	Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7:69 (2007). [PMID: 17645809]
3.	Lu, Y.J., Zhang, F., Grimes, K.D., Lee, R.E. and Rock, C.O. Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. J. Biol. Chem. 282 (2007) 11339–11346. [PMID: 17308305]
4.	Hara, Y., Seki, M., Matsuoka, S., Hara, H., Yamashita, A. and Matsumoto, K. Involvement of PlsX and the acyl-phosphate dependent sn-glycerol-3-phosphate acyltransferase PlsY in the initial stage of glycerolipid synthesis in Bacillus subtilis. Genes Genet. Syst. 83 (2008) 433–442. [PMID: 19282621]

[EC 2.3.1.275 created 2018]

2.3.1.276

Accepted name:

galactosamine-1-phosphate N-acetyltransferase

Reaction:

acetyl-CoA + α-D-galactosamine 1-phosphate = CoA + N-acetyl-α-D-galactosamine 1-phosphate

Other name(s):

ST0452 (locus name)

Systematic name:

acetyl-CoA:α-D-galactosamine-1-phosphate N-acetyltransferase

Comments:

The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward α-D-glucosamine 1-phosphate (cf. EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase). In addition, that enzyme contains a second domain that catalyses the activities of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, EC 2.7.7.24, glucose-1-phosphate thymidylyltransferase, and EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase.

Links to other databases:

References:

1.	Zhang, Z., Tsujimura, M., Akutsu, J., Sasaki, M., Tajima, H. and Kawarabayasi, Y. Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7. J. Biol. Chem. 280 (2005) 9698–9705. [PMID: 15598657]
2.	Zhang, Z., Akutsu, J. and Kawarabayasi, Y. Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7. J. Bacteriol. 192 (2010) 3287–3293. [PMID: 20400541]
3.	Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]

[EC 2.3.1.276 created 2018]

2.4.1.359

Accepted name:

glucosylglycerol phosphorylase (configuration-retaining)

Reaction:

2-O-α-D-glucopyranosyl-glycerol + phosphate = α-D-glucose 1-phosphate + glycerol

Other name(s):

2-O-α-D-glucosylglycerol phosphorylase (retaining)

Systematic name:

2-O-α-D-glucopyranosyl-glycerol:phosphate α-D-glucosyltransferase (configuration-retaining)

Comments:

The enzyme, characterized from the halotolerant bacterium Marinobacter adhaerens, is likely responsible for degradation of the compatible solute 2-O-α-D-glucopyranosyl-glycerol when the environmental salt concentration decreases. cf. EC 2.4.1.332, 1,2-α-glucosylglycerol phosphorylase.

Links to other databases:

References:

1.	Franceus, J., Decuyper, L., D'hooghe, M. and Desmet, T. Exploring the sequence diversity in glycoside hydrolase family 13_18 reveals a novel glucosylglycerol phosphorylase. Appl. Microbiol. Biotechnol. (2018) . [PMID: 29470619]

[EC 2.4.1.359 created 2018]

2.4.2.61

Accepted name:

α-dystroglycan β1,4-xylosyltransferase

Reaction:

UDP-α-D-xylose + 3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] = UDP + 3-O-[β-D-Xyl-(1→4)-Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein]

Other name(s):

TMEM5 (gene name)

Systematic name:

UDP-α-D-xylose:3-O-[Rib-ol-P-Rib-ol-P-3-β-D-GalNAc-(1→3)-β-D-GlcNAc-(1→4)-O-6-P-α-D-Man]-Ser/Thr-[protein] xylosyltransferase

Comments:

This eukaryotic enzyme catalyses a step in the biosynthesis of the glycan moiety of the membrane protein α-dystroglycan. It is specific for the second ribitol 5-phosphate in the nascent glycan chain as acceptor.

Links to other databases:

References:

Vuillaumier-Barrot, S., Bouchet-Seraphin, C., Chelbi, M., Devisme, L., Quentin, S., Gazal, S., Laquerriere, A., Fallet-Bianco, C., Loget, P., Odent, S., Carles, D., Bazin, A., Aziza, J., Clemenson, A., Guimiot, F., Bonniere, M., Monnot, S., Bole-Feysot, C., Bernard, J.P., Loeuillet, L., Gonzales, M., Socha, K., Grandchamp, B., Attie-Bitach, T., Encha-Razavi, F. and Seta, N. Identification of mutations in TMEM5 and ISPD as a cause of severe cobblestone lissencephaly. Am. J. Hum. Genet. 91 (2012) 1135–1143. [PMID: 23217329]

Manya, H., Yamaguchi, Y., Kanagawa, M., Kobayashi, K., Tajiri, M., Akasaka-Manya, K., Kawakami, H., Mizuno, M., Wada, Y., Toda, T. and Endo, T. The muscular dystrophy gene TMEM5 encodes a ribitol β1,4-xylosyltransferase required for the functional glycosylation of dystroglycan. J. Biol. Chem. 291 (2016) 24618–24627. [PMID: 27733679]

[EC 2.4.2.61 created 2018]

*EC

2.7.1.180

Accepted name:

FAD:protein FMN transferase

Reaction:

FAD + [protein]-L-threonine = [protein]-FMN-L-threonine + AMP

Other name(s):

flavin transferase; apbE (gene name)

Systematic name:

FAD:protein riboflavin-5′-phosphate transferase

Comments:

The enzyme catalyses the transfer of the FMN portion of FAD and its covalent binding to the hydroxyl group of an L-threonine residue in a target flavin-binding protein such as the B and C subunits of EC 7.2.1.1, NADH:ubiquinone reductase (Na⁺-transporting). Requires Mg²⁺.

Links to other databases:

References:

Bertsova, Y.V., Fadeeva, M.S., Kostyrko, V.A., Serebryakova, M.V., Baykov, A.A. and Bogachev, A.V. Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins. J. Biol. Chem. 288 (2013) 14276–14286. [PMID: 23558683]

[EC 2.7.1.180 created 2013, modified 2018]

2.7.1.223

Accepted name:

aminoimidazole riboside kinase

Reaction:

ATP + 5-amino-1-(β-D-ribosyl)imidazole = ADP + 5-amino-1-(5-phospho-β-D-ribosyl)imidazole

Other name(s):

STM4066 (locus name)

Systematic name:

ATP:5-amino-1-(β-D-ribosyl)imidazole 5′-phosphotransferase

Comments:

The enzyme, characterized from the bacterium Salmonella enterica, can phosphorylate exogeneously-provided 5-amino-1-(β-D-ribosyl)imidazole to form 5-amino-1-(5-phospho-β-D-ribosyl)imidazole (AIR), an important intermediate in the production of both purine mononucleotides and the hydroxymethyl pyrimidine moiety of thiamine.

Links to other databases:

References:

1.	Dougherty, M. and Downs, D.M. The stm4066 gene product of Salmonella enterica serovar Typhimurium has aminoimidazole riboside (AIRs) kinase activity and allows AIRs to satisfy the thiamine requirement of pur mutant strains. J. Bacteriol. 185 (2003) 332–339. [PMID: 12486071]
2.	Zhang, Y., Dougherty, M., Downs, D.M. and Ealick, S.E. Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily. Structure 12 (2004) 1809–1821. [PMID: 15458630]

[EC 2.7.1.223 created 2018]

2.7.1.224

Accepted name:

cytidine diphosphoramidate kinase

Reaction:

ATP + cytidine 5′-diphosphoramidate = ADP + cytidine 3′-phospho-5′-diphosphoramidate

Systematic name:

ATP:cytidine 5′-diphosphoramidate 3′-phosphotransferase

Comments:

The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium’s capsular polysaccharides.

Links to other databases:

References:

1.	Taylor, Z.W. and Raushel, F.M. Cytidine diphosphoramidate kinase: an enzyme required for the biosynthesis of the O-methyl phosphoramidate modification in the capsular polysaccharides of Campylobacter jejuni. Biochemistry 57 (2018) 2238–2244. [PMID: 29578334]

[EC 2.7.1.224 created 2018]

2.7.7.101

Accepted name:

DNA primase DnaG

Reaction:

ssDNA + n NTP = ssDNA/pppN(pN)_n-1 hybrid + (n-1) diphosphate

Other name(s):

DnaG

Systematic name:

nucleotide 5′-triphosphate:single-stranded DNA nucleotidyltransferase (DNA-RNA hybrid synthesizing)

Comments:

The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).

Links to other databases:

References:

1.	Rowen, L. and Kornberg, A. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J. Biol. Chem. 253 (1978) 758–764. [PMID: 340457]
2.	Ilyina, T.V., Gorbalenya, A.E. and Koonin, E.V. Organization and evolution of bacterial and bacteriophage primase-helicase systems. J. Mol. Evol. 34 (1992) 351–357. [PMID: 1569588]
3.	Frick, D.N. and Richardson, C.C. DNA primases. Annu. Rev. Biochem. 70 (2001) 39–80. [PMID: 11395402]
4.	Zuo, Z., Rodgers, C.J., Mikheikin, A.L. and Trakselis, M.A. Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system. J. Mol. Biol. 397 (2010) 664–676. [PMID: 20122937]

[EC 2.7.7.101 created 2018]

2.7.7.102

Accepted name:

DNA primase AEP

Reaction:

(1) ssDNA + n NTP = ssDNA/pppN(pN)_n-1 hybrid + (n-1) diphosphate
(2) ssDNA + n dNTP = ssDNA/pppdN(pdN)_n-1 hybrid + (n-1) diphosphate

Other name(s):

archaeo-eukaryotic primase; AEP; PrimPol

Systematic name:

(deoxy)nucleotide 5′-triphosphate:single-stranded DNA (deoxy)nucleotidyltransferase (DNA or DNA-RNA hybrid synthesizing)

Comments:

The enzyme, which is found in eukaryota and archaea, catalyses the synthesis of short RNA or DNA sequences which are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase.

Links to other databases:

References:

1.	Desogus, G., Onesti, S., Brick, P., Rossi, M. and Pisani, F.M. Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii. Nucleic Acids Res. 27 (1999) 4444–4450. [PMID: 10536154]
2.	Arezi, B. and Kuchta, R.D. Eukaryotic DNA primase. Trends Biochem. Sci. 25 (2000) 572–576. [PMID: 11084371]
3.	Liu, L., Komori, K., Ishino, S., Bocquier, A.A., Cann, I.K., Kohda, D. and Ishino, Y. The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. J. Biol. Chem. 276 (2001) 45484–45490. [PMID: 11584001]
4.	Lao-Sirieix, S.H. and Bell, S.D. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3′-terminal nucleotidyl transferase activities. J. Mol. Biol. 344 (2004) 1251–1263. [PMID: 15561142]
5.	Baranovskiy, A.G., Zhang, Y., Suwa, Y., Babayeva, N.D., Gu, J., Pavlov, Y.I. and Tahirov, T.H. Crystal structure of the human primase. J. Biol. Chem. 290 (2015) 5635–5646. [PMID: 25550159]
6.	Guilliam, T.A., Keen, B.A., Brissett, N.C. and Doherty, A.J. Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes. Nucleic Acids Res. 43 (2015) 6651–6664. [PMID: 26109351]

[EC 2.7.7.102 created 2018]

2.7.7.103

Accepted name:

L-glutamine-phosphate cytidylyltransferase

Reaction:

CTP + N⁵-phospho-L-glutamine = diphosphate + N⁵-(cytidine 5′-diphosphoramidyl)-L-glutamine

Systematic name:

CTP:phosphoglutamine cytidylyltransferase

Comments:

Links to other databases:

References:

1.	Taylor, Z.W., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079–6082. [PMID: 29023101]

[EC 2.7.7.103 created 2018]

3.1.1.104

Accepted name:

5-phospho-D-xylono-1,4-lactonase

Reaction:

(1) D-xylono-1,4-lactone 5-phosphate + H₂O = 5-phospho-D-xylonate
(2) L-arabino-1,4-lactone 5-phosphate + H₂O = 5-phospho-L-arabinate

Systematic name:

5-phospho-D-xylono-1,4-lactone hydrolase

Comments:

The enzyme, characterized from Mycoplasma spp., contains a binuclear metal center with two zinc cations. The enzyme is specific for the phosphorylated forms, and is unable to hydrolyse non-phosphorylated 1,4-lactones.

Links to other databases:

References:

Korczynska, M., Xiang, D.F., Zhang, Z., Xu, C., Narindoshvili, T., Kamat, S.S., Williams, H.J., Chang, S.S., Kolb, P., Hillerich, B., Sauder, J.M., Burley, S.K., Almo, S.C., Swaminathan, S., Shoichet, B.K. and Raushel, F.M. Functional annotation and structural characterization of a novel lactonase hydrolyzing D-xylono-1,4-lactone-5-phosphate and L-arabino-1,4-lactone-5-phosphate. Biochemistry 53 (2014) 4727–4738. [PMID: 24955762]

[EC 3.1.1.104 created 2018]

3.2.1.208

Accepted name:

glucosylglycerate hydrolase

Reaction:

2-O-(α-D-glucopyranosyl)-D-glycerate + H₂O = D-glucopyranose + D-glycerate

Other name(s):

GG hydrolase; GgH

Systematic name:

2-O-(α-D-glucopyranosyl)-D-glycerate D-glucohydrolase

Comments:

The enzyme has been isolated from nontuberculous mycobacteria (e.g. Mycobacterium hassiacum), which accumulate 2-O-(α-D-glucopyranosyl)-D-glycerate during growth under nitrogen deprivation.

Links to other databases:

References:

1.	Alarico, S., Costa, M., Sousa, M.S., Maranha, A., Lourenco, E.C., Faria, T.Q., Ventura, M.R. and Empadinhas, N. Mycobacterium hassiacum recovers from nitrogen starvation with up-regulation of a novel glucosylglycerate hydrolase and depletion of the accumulated glucosylglycerate. Sci. Rep. 4:6766 (2014). [PMID: 25341489]
2.	Cereija, T.B., Alarico, S., Empadinhas, N. and Pereira, P.JB. Production, crystallization and structure determination of a mycobacterial glucosylglycerate hydrolase. Acta Crystallogr. F Struct. Biol. Commun. 73 (2017) 536–540. [PMID: 28876234]

[EC 3.2.1.208 created 2018]

3.5.1.129

Accepted name:

N⁵-(cytidine 5′-diphosphoramidyl)-L-glutamine hydrolase

Reaction:

N⁵-(cytidine 5′-diphosphoramidyl)-L-glutamine + H₂O = cytidine 5′-diphosphoramidate + L-glutamate

Other name(s):

N⁵-(cytidine 5′-diphosphoramidyl)-L-glutamine deacylase

Systematic name:

N⁵-(cytidine 5′-diphosphoramidyl)-L-glutamine amidohydrolase

Comments:

Links to other databases:

References:

1.	Taylor, Z.W., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079–6082. [PMID: 29023101]

[EC 3.5.1.129 created 2018]

*EC

3.6.1.1

Accepted name:

inorganic diphosphatase

Reaction:

diphosphate + H₂O = 2 phosphate

Systematic name:

diphosphate phosphohydrolase

Comments:

Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H⁺-exporting diphosphatase.

Links to other databases:

BRENDA, EXPASY, Gene, GTD, KEGG, PDB, CAS registry number: 9024-82-2

References:

1.	Bailey, K. and Webb, E.C. Purification and properties of yeast pyrophosphatase. Biochem. J. 38 (1944) 394–398. [PMID: 16747821]
2.	Kunitz, M. Crystalline inorganic pyrophosphatase isolated from baker's yeast. J. Gen. Physiol. 35 (1952) 423–450. [PMID: 14898026]
3.	Rafter, G.W. Pyrophosphate metabolism in liver mitochondria. J. Biol. Chem. 235 (1960) 2475–2477. [PMID: 14435825]

[EC 3.6.1.1 created 1961, modified 2000, modified 2018]

3.6.3.2

Transferred entry:

Mg²⁺-importing ATPase. Now EC 7.2.2.14, P-type Mg²⁺ transporter

[EC 3.6.3.2 created 2000, modified 2001, deleted 2018]

3.6.3.4

Transferred entry:

Cu²⁺-exporting ATPase. Now EC 7.2.2.9, Cu²⁺-exporting ATPase

[EC 3.6.3.4 created 2000, modified 2013, deleted 2018]

3.6.3.5

Transferred entry:

Zn²⁺-exporting ATPase. Now EC 7.2.2.12, Zn²⁺-exporting ATPase

[EC 3.6.3.5 created 2000, modified 2001, modified 2006, deleted 2018]

3.6.3.8

Transferred entry:

Ca²⁺-transporting ATPase. Now EC 7.2.2.10, Ca²⁺-transporting ATPase

[EC 3.6.3.8 created 1984 as EC 3.6.1.38, transferred 2000 to EC 3.6.3.8, modified 2001, modified 2011, deleted 2018]

3.6.3.9

Transferred entry:

Na⁺/K⁺-exchanging ATPase. Now EC 7.2.2.13, Na⁺/K⁺-exchanging ATPase

[EC 3.6.3.9 created 1984 as EC 3.6.1.37, transferred 2000 to EC 3.6.3.9, modified 2001, deleted 2018]

3.6.3.12

Transferred entry:

K⁺-transporting ATPase. Now EC 7.2.2.6, K⁺-transporting ATPase

[EC 3.6.3.12 created 2000, deleted 2018]

3.6.3.20

Transferred entry:

glycerol-3-phosphate-transporting ATPase. Now EC 7.6.2.10, glycerol-3-phosphate-transporting ATPase

[EC 3.6.3.20 created 2000, deleted 2018]

3.6.3.23

Transferred entry:

oligopeptide-transporting ATPase. Now EC 7.4.2.6, oligopeptide-transporting ATPase

[EC 3.6.3.23 created 2000, deleted 2018]

3.6.3.24

Transferred entry:

nickel-transporting ATPase. Now EC 7.2.2.11, nickel-transporting ATPase

[EC 3.6.3.24 created 2000, deleted 2018]

3.6.3.25

Transferred entry:

sulfate-transporting ATPase. Now EC 7.3.2.3, sulfate-transporting ATPase

[EC 3.6.3.25 created 2000, deleted 2018]

3.6.3.26

Transferred entry:

nitrate-transporting ATPase. Now EC 7.3.2.4, nitrate-transporting ATPase

[EC 3.6.3.26 created 2000, deleted 2018]

3.6.3.29

Transferred entry:

molybdate-transporting ATPase. Now EC 7.3.2.5, molybdate-transporting ATPase

[EC 3.6.3.29 created 2000, deleted 2018]

3.6.3.30

Transferred entry:

Fe³⁺-transporting ATPase. Now EC 7.2.2.7, Fe³⁺-transporting ATPase

[EC 3.6.3.30 created 2000, deleted 2018]

3.6.3.31

Transferred entry:

polyamine-transporting ATPase. Now EC 7.6.2.11, polyamine-transporting ATPase

[EC 3.6.3.31 created 2000, deleted 2018]

3.6.3.32

Transferred entry:

quaternary-amine-transporting ATPase. Now EC 7.6.2.9, quaternary-amine-transporting ATPase

[EC 3.6.3.32 created 2000, deleted 2018]

3.6.3.33

Transferred entry:

vitamin B₁₂-transporting ATPase. Now EC 7.6.2.8, vitamin B₁₂-transporting ATPase

[EC 3.6.3.33 created 2000, deleted 2018]

3.6.3.34

Transferred entry:

iron-chelate-transporting ATPase; now recognized to be at least 3 separate enzymes EC 7.2.2.16, iron(III) hydroxamate ABC transporter, EC 7.2.2.17, ferric enterobactin ABC transporter, and EC 7.2.2.18, ferric citrate ABC transporter

[EC 3.6.3.34 created 2000, deleted 2018]

3.6.3.35

Transferred entry:

manganese-transporting ATPase. Now EC 7.2.2.5, manganese-transporting ATPase

[EC 3.6.3.35 created 2000, deleted 2018]

3.6.3.36

Transferred entry:

taurine-transporting ATPase. Now EC 7.6.2.7, taurine-transporting ATPase

[EC 3.6.3.36 created 2000, deleted 2018]

3.6.3.37

Transferred entry:

guanine-transporting ATPase. Now EC 7.6.2.6, guanine-transporting ATPase

[EC 3.6.3.37 created 2000, deleted 2018]

3.6.3.39

Transferred entry:

lipopolysaccharide-transporting ATPase. Now EC 7.5.2.5, lipopolysaccharide-transporting ATPase

[EC 3.6.3.39 created 2000, deleted 2018]

3.6.3.40

Transferred entry:

teichoic-acid-transporting ATPase. Now EC 7.5.2.4, teichoic-acid-transporting ATPase

[EC 3.6.3.40 created 2000, deleted 2018]

3.6.3.41

Transferred entry:

heme-transporting ATPase. Now EC 7.6.2.5, heme-transporting ATPase

[EC 3.6.3.41 created 2000, deleted 2018]

3.6.3.42

Transferred entry:

β-glucan-transporting ATPase. Now EC 7.5.2.3, β-glucan-transporting ATPase

[EC 3.6.3.42 created 2000, deleted 2018]

3.6.3.43

Transferred entry:

peptide-transporting ATPase. Now EC 7.4.2.5, peptide-transporting ATPase

[EC 3.6.3.43 created 2000, deleted 2018]

3.6.3.47

Transferred entry:

fatty-acyl-CoA-transporting ATPase. Now EC 7.6.2.4, fatty-acyl-CoA-transporting ATPase

[EC 3.6.3.47 created 2000, deleted 2018]

3.6.3.48

Transferred entry:

α-factor-transporting ATPase. Now EC 7.4.2.7 as α-factor-pheromone transporting ATPase

[EC 3.6.3.48 created 2000, deleted 2018]

3.6.3.50

Transferred entry:

protein-secreting ATPase. Now EC 7.4.2.8, protein-secreting ATPase

[EC 3.6.3.50 created 2000, deleted 2018]

3.6.3.51

Transferred entry:

mitochondrial protein-transporting ATPase. Now EC 7.4.2.3, mitochondrial protein-transporting ATPase

[EC 3.6.3.51 created 2000, deleted 2018]

3.6.3.52

Transferred entry:

chloroplast protein-transporting ATPase. Now EC 7.4.2.4, chloroplast protein-transporting ATPase

[EC 3.6.3.52 created 2000, deleted 2018]

3.6.3.53

Transferred entry:

Ag⁺-exporting ATPase. Now EC 7.2.2.15, Ag⁺-exporting ATPase

[EC 3.6.3.53 created 2000, deleted 2018]

3.6.3.54

Transferred entry:

Cu⁺-exporting ATPase. Now EC 7.2.2.8, Cu⁺-exporting ATPase

[EC 3.6.3.54 created 2013, deleted 2018]

3.6.3.55

Transferred entry:

tungstate-importing ATPase. Now EC 7.3.2.6, tungstate-importing ATPase

[EC 3.6.3.55 created 2013, deleted 2018]

*EC

4.1.1.6

Accepted name:

cis-aconitate decarboxylase

Reaction:

cis-aconitate = itaconate + CO₂

Glossary:

itaconate = 2-methylenesuccinate
cis-aconitate = (Z)-prop-1-ene-1,2,3-tricarboxylate

Other name(s):

cis-aconitic decarboxylase; cis-aconitate carboxy-lyase; CAD1 (gene name); IRG1 (gene name)

Systematic name:

cis-aconitate carboxy-lyase (itaconate-forming)

Comments:

The enzyme has been characterized from the fungus Aspergillus terreus and from human macrophages. cf. EC 4.1.1.113, trans-aconitate decarboxylase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 9025-01-8

References:

1.	Bentley, R. and Thiessen, C.P. Biosynthesis of itaconic acid in Aspergillus terreus. III. The properties and reaction mechanism of cis-aconitic acid decarboxylase. J. Biol. Chem. 226 (1957) 703–720. [PMID: 13438855]
2.	Dwiarti, L., Yamane, K., Yamatani, H., Kahar, P. and Okabe, M. Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1. J. Biosci. Bioeng. 94 (2002) 29–33. [PMID: 16233265]
3.	Kanamasa, S., Dwiarti, L., Okabe, M. and Park, E.Y. Cloning and functional characterization of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus. Appl. Microbiol. Biotechnol. 80 (2008) 223–229. [PMID: 18584171]
4.	Michelucci, A., Cordes, T., Ghelfi, J., Pailot, A., Reiling, N., Goldmann, O., Binz, T., Wegner, A., Tallam, A., Rausell, A., Buttini, M., Linster, C.L., Medina, E., Balling, R. and Hiller, K. Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc. Natl. Acad. Sci. USA 110 (2013) 7820–7825. [DOI] [PMID: 23610393]

[EC 4.1.1.6 created 1961, modified 2018]

4.1.1.113

Accepted name:

trans-aconitate decarboxylase

Reaction:

trans-aconitate = itaconate + CO₂

Glossary:

trans-aconitate = (E)-prop-1-ene-1,2,3-tricarboxylate
itaconate = 2-methylenesuccinate

Other name(s):

TAD1 (gene name)

Systematic name:

trans-aconitate carboxy-lyase (itaconate-forming)

Comments:

The enzyme, characterized from the smut fungus Ustilago maydis, is involved in an alternative pathway for the biosynthesis of itaconate. cf. EC 4.1.1.6, cis-aconitate decarboxylase.

Links to other databases:

References:

1.	Geiser, E., Przybilla, S.K., Friedrich, A., Buckel, W., Wierckx, N., Blank, L.M. and Bolker, M. Ustilago maydis produces itaconic acid via the unusual intermediate trans-aconitate. Microb. Biotechnol. 9 (2016) 116–126. [PMID: 26639528]

[EC 4.1.1.113 created 2018]

5.1.3.42

Accepted name:

D-glucosamine-6-phosphate 4-epimerase

Reaction:

D-glucosamine 6-phosphate = D-galactosamine 6-phosphate

For diagram of UDP-N-acetylglucosamine biosynthesis, click here

Other name(s):

ST2245 (locus name)

Systematic name:

D-glucosamine 6-phosphate 4-epimerase

Comments:

The enzyme, characterized from the archaeon Sulfolobus tokodaii, participates in a pathway for the biosynthesis of UDP-N-acetyl-α-D-galactosamine.

Links to other databases:

References:

1.	Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]

[EC 5.1.3.42 created 2018]

5.4.2.13

Accepted name:

phosphogalactosamine mutase

Reaction:

D-galactosamine 6-phosphate = α-D-galactosamine-1-phosphate

For diagram of UDP-N-acetylglucosamine biosynthesis, click here

Other name(s):

ST0242 (locus name)

Systematic name:

α-D-galactosamine 1,6-phosphomutase

Comments:

The enzyme, characterized from the archaeon Sulfolobus tokodaii, is also active toward D-glucosamine 6-phosphate (cf. EC 5.4.2.10, phosphoglucosamine mutase).

Links to other databases:

References:

1.	Dadashipour, M., Iwamoto, M., Hossain, M.M., Akutsu, J.I., Zhang, Z. and Kawarabayasi, Y. Identification of a direct biosynthetic pathway for UDP-N-acetylgalactosamine from glucosamine-6-phosphate in thermophilic crenarchaeon Sulfolobus tokodaii. J. Bacteriol. 200 (2018) . [PMID: 29507091]

[EC 5.4.2.13 created 2018]

7.1.1.3

Accepted name:

ubiquinol oxidase (H⁺-transporting)

Reaction:

2 quinol + O₂_{[side 2]} + 8 H⁺_{[side 2]} = 2 quinone + 2 H₂O_{[side 2]} + 8 H⁺_{[side 1]}

Other name(s):

cyoABCD (gene names); cytochrome bo₃ oxidase; cytochrome bb₃ oxidase; cytochrome bo oxidase; Cyo oxidase; ubiquinol:O₂ oxidoreductase (H⁺-transporting); ubiquinol:oxygen oxidoreductase (H⁺-transporting)

Systematic name:

quinol:oxygen oxidoreductase (H⁺-transporting)

Comments:

Contains a dinuclear centre comprising heme and copper. This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) of enzymes that have been characterized so far is 2. cf. EC 7.1.1.7, ubiquinol oxidase ubiquinol oxidase (electrogenic, proton-motive force generating).

Links to other databases:

References:

1.	Miyoshi-Akiyama, T., Hayashi, M. and Unemoto, T. Purification and properties of cytochrome bo-type ubiquinol oxidase from a marine bacterium Vibrio alginolyticus. Biochim. Biophys Acta 1141 (1993) 283–287. [DOI] [PMID: 8443214]
2.	de Gier, J.W., Lubben, M., Reijnders, W.N., Tipker, C.A., Slotboom, D.J., van Spanning, R.J., Stouthamer, A.H. and van der Oost, J. The terminal oxidases of Paracoccus denitrificans. Mol. Microbiol. 13 (1994) 183–196. [DOI] [PMID: 7984100]
3.	Howitt, C.A. and Vermaas, W.F. Quinol and cytochrome oxidases in the cyanobacterium Synechocystis sp. PCC 6803. Biochemistry 37 (1998) 17944–17951. [DOI] [PMID: 9922162]
4.	Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S. and Wikstrom, M. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. 7 (2000) 910–917. [DOI] [PMID: 11017202]
5.	Morales, G., Ugidos, A. and Rojo, F. Inactivation of the Pseudomonas putida cytochrome o ubiquinol oxidase leads to a significant change in the transcriptome and to increased expression of the CIO and cbb3-1 terminal oxidases. Environ. Microbiol. 8 (2006) 1764–1774. [DOI] [PMID: 16958757]
6.	Stenberg, F., von Heijne, G. and Daley, D.O. Assembly of the cytochrome bo₃ complex. J. Mol. Biol. 371 (2007) 765–773. [PMID: 17583738]
7.	Yap, L.L., Lin, M.T., Ouyang, H., Samoilova, R.I., Dikanov, S.A. and Gennis, R.B. The quinone-binding sites of the cytochrome bo₃ ubiquinol oxidase from Escherichia coli. Biochim. Biophys. Acta 1797 (2010) 1924–1932. [DOI] [PMID: 20416270]
8.	Choi, S.K., Lin, M.T., Ouyang, H. and Gennis, R.B. Searching for the low affinity ubiquinone binding site in cytochrome bo₃ from Escherichia coli. Biochim Biophys Acta Bioenerg 1858 (2017) 366–370. [PMID: 28235459]
9.	Choi, S.K., Schurig-Briccio, L., Ding, Z., Hong, S., Sun, C. and Gennis, R.B. Location of the substrate binding site of the cytochrome bo₃ ubiquinol oxidase from Escherichia coli. J. Am. Chem. Soc. 139 (2017) 8346–8354. [PMID: 28538096]
10.	Graf, S., Brzezinski, P. and von Ballmoos, C. The proton pumping bo oxidase from Vitreoscilla. Sci. Rep. 9:4766 (2019). [DOI] [PMID: 30886219]

[EC 7.1.1.3 created 2011 as EC 1.10.3.10, modified 2014, transferred 2018 to EC 7.1.1.3, modified 2023]

7.1.1.4

Accepted name:

caldariellaquinol oxidase (H⁺-transporting)

Reaction:

2 caldariellaquinol + O₂ + n H⁺_{[side 1]} = 2 caldariellaquinone + 2 H₂O + n H⁺_{[side 2]}

Glossary:

caldariellaquinol = 6-(3,7,11,15,19,23-hexamethyltetracosyl)-5-(methylsulfanyl)-1-benzothiophene-4,7-diol

Other name(s):

SoxABCD quinol oxidase; SoxABCD complex; quinol oxidase SoxABCD; SoxM supercomplex; aa₃-type quinol oxidase; aa₃ quinol oxidase; cytochrome aa₃; terminal quinol oxidase; terminal quinol:oxygen oxidoreductase; caldariella quinol:dioxygen oxidoreductase; cytochrome aa₃-type oxidase; caldariellaquinol:O₂ oxidoreductase (H⁺-transporting)

Systematic name:

caldariellaquinol:oxygen oxidoreductase (H⁺-transporting)

Comments:

A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O₂ to water, accompanied by the extrusion of protons across the cytoplasmic membrane.

Links to other databases:

References:

1.	Gleissner, M., Kaiser, U., Antonopoulos, E. and Schafer, G. The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius. J. Biol. Chem. 272 (1997) 8417–8426. [DOI] [PMID: 9079667]
2.	Purschke, W.G., Schmidt, C.L., Petersen, A. and Schafer, G. The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J. Bacteriol. 179 (1997) 1344–1353. [DOI] [PMID: 9023221]
3.	Gilderson, G., Aagaard, A., Gomes, C.M., Adelroth, P., Teixeira, M. and Brzezinski, P. Kinetics of electron and proton transfer during O₂ reduction in cytochrome aa₃ from A. ambivalens: an enzyme lacking Glu(I-286). Biochim. Biophys. Acta 1503 (2001) 261–270. [DOI] [PMID: 11115638]
4.	Komorowski, L., Verheyen, W. and Schafer, G. The archaeal respiratory supercomplex SoxM from S. acidocaldarius combines features of quinole and cytochrome c oxidases. Biol. Chem. 383 (2002) 1791–1799. [DOI] [PMID: 12530544]
5.	Muller, F.H., Bandeiras, T.M., Urich, T., Teixeira, M., Gomes, C.M. and Kletzin, A. Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate:quinone oxidoreductase. Mol. Microbiol. 53 (2004) 1147–1160. [DOI] [PMID: 15306018]
6.	Bandeiras, T.M., Pereira, M.M., Teixeira, M., Moenne-Loccoz, P. and Blackburn, N.J. Structure and coordination of CuB in the Acidianus ambivalens aa₃ quinol oxidase heme-copper center. J. Biol. Inorg. Chem. 10 (2005) 625–635. [DOI] [PMID: 16163550]

[EC 7.1.1.4 created 2013 as EC 1.10.3.13, transferred 2018 to EC 7.1.1.4]

7.1.1.5

Accepted name:

menaquinol oxidase (H⁺-transporting)

Reaction:

2 menaquinol + O₂ + n H⁺_{[side 1]} = 2 menaquinone + 2 H₂O + n H⁺_{[side 2]}

Other name(s):

cytochrome aa₃-600 oxidase; cytochrome bd oxidase; menaquinol:O₂ oxidoreductase (H⁺-transporting)

Systematic name:

menaquinol:oxygen oxidoreductase (H⁺-transporting)

Comments:

Cytochrome aa₃-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo₃ ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.

Links to other databases:

References:

1.	Lauraeus, M. and Wikstrom, M. The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties. J. Biol. Chem. 268 (1993) 11470–11473. [PMID: 8388393]
2.	Lemma, E., Simon, J., Schagger, H. and Kroger, A. Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis. Arch. Microbiol. 163 (1995) 432–438. [PMID: 7575098]
3.	Yi, S.M., Narasimhulu, K.V., Samoilova, R.I., Gennis, R.B. and Dikanov, S.A. Characterization of the semiquinone radical stabilized by the cytochrome aa₃-600 menaquinol oxidase of Bacillus subtilis. J. Biol. Chem. 285 (2010) 18241–18251. [DOI] [PMID: 20351111]

[EC 7.1.1.5 created 2011 as EC 1.10.3.12, transferred 2018 to EC 7.1.1.5]

7.1.1.6

Accepted name:

plastoquinol—plastocyanin reductase

Reaction:

plastoquinol + 2 oxidized plastocyanin + 2 H⁺_{[side 1]} = plastoquinone + 2 reduced plastocyanin + 4 H⁺_{[side 2]}

Other name(s):

plastoquinol/plastocyanin oxidoreductase; cytochrome f/b₆ complex; cytochrome b₆f complex

Systematic name:

plastoquinol:oxidized-plastocyanin oxidoreductase

Comments:

Contains two b-type cytochromes, two c-type cytochromes (c_n and f), and a [2Fe-2S] Rieske cluster. The enzyme plays a key role in photosynthesis, transferring electrons from photosystem II (EC 1.10.3.9) to photosystem I (EC 1.97.1.12). Cytochrome c-552 can act as acceptor instead of plastocyanin, but more slowly. In chloroplasts, protons are translocated through the thylakoid membrane from the stroma to the lumen. The mechanism occurs through the Q cycle as in EC 7.1.1.8, quinol—cytochrome-c reductase (complex III) and involves electron bifurcation.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 79079-13-3

References:

1.	Hurt, E. and Hauska, G. A cytochrome f/b₆ complex of five polypeptides with plastoquinol-plastocyanin-oxidoreductase activity from spinach chloroplasts. Eur. J. Biochem. 117 (1981) 591–595. [DOI] [PMID: 6269845]
2.	Cramer, W.A. and Zhang, H. Consequences of the structure of the cytochrome b₆f complex for its charge transfer pathways. Biochim. Biophys. Acta 1757 (2006) 339–345. [DOI] [PMID: 16787635]

[EC 7.1.1.6 created 1984 as EC 1.10.99.1, transferred 2011 to EC 1.10.9.1, transferred 2018 to EC 7.1.1.6]

7.1.1.7

Accepted name:

quinol oxidase (electrogenic, proton-motive force generating)

Reaction:

2 quinol + O₂_{[side 2]} + 4 H⁺_{[side 2]} = 2 quinone + 2 H₂O_{[side 2]} + 4 H⁺_{[side 1]} (overall reaction)
(1a) 2 quinol = 2 quinone + 4 H⁺_{[side 1]} + 4 e^-
(1b) O₂_{[side 2]} + 4 H⁺_{[side 2]} + 4 e^- = 2 H₂O_{[side 2]}

Other name(s):

cydAB (gene names); appBC (gene names); cytochrome bd oxidase; cytochrome bd-I oxidase; cytochrome bd-II oxidase; ubiquinol:O₂ oxidoreductase (electrogenic, non H⁺-transporting); ubiquinol oxidase (electrogenic, proton-motive force generating); ubiquinol oxidase (electrogenic, non H⁺-transporting)

Systematic name:

quinol:oxygen oxidoreductase (electrogenic, non H⁺-transporting)

Comments:

This terminal oxidase enzyme is unable to pump protons but generates a proton motive force by transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water. The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) is 1. The bd-I oxidase from the bacterium Escherichia coli is the predominant respiratory oxygen reductase that functions under microaerophilic conditions in that organism. cf. EC 7.1.1.3, ubiquinol oxidase (H⁺-transporting).

Links to other databases:

References:

1.	Miller, M.J., Hermodson, M. and Gennis, R.B. The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits. J. Biol. Chem. 263 (1988) 5235–5240. [PMID: 3281937]
2.	Puustinen, A., Finel, M., Haltia, T., Gennis, R.B. and Wikstrom, M. Properties of the two terminal oxidases of Escherichia coli. Biochemistry 30 (1991) 3936–3942. [PMID: 1850294]
3.	Belevich, I., Borisov, V.B., Zhang, J., Yang, K., Konstantinov, A.A., Gennis, R.B. and Verkhovsky, M.I. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Proc. Natl. Acad. Sci. USA 102 (2005) 3657–3662. [DOI] [PMID: 15728392]
4.	Lenn, T., Leake, M.C. and Mullineaux, C.W. Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo. Mol. Microbiol. 70 (2008) 1397–1407. [DOI] [PMID: 19019148]
5.	Shepherd, M., Sanguinetti, G., Cook, G.M. and Poole, R.K. Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism. J. Biol. Chem. 285 (2010) 18464–18472. [DOI] [PMID: 20392690]
6.	Borisov, V.B., Murali, R., Verkhovskaya, M.L., Bloch, D.A., Han, H., Gennis, R.B. and Verkhovsky, M.I. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc. Natl. Acad. Sci. USA 108 (2011) 17320–17324. [DOI] [PMID: 21987791]
7.	Borisov, V.B., Gennis, R.B., Hemp, J. and Verkhovsky, M.I. The cytochrome bd respiratory oxygen reductases. Biochim. Biophys. Acta 1807 (2011) 1398–1413. [PMID: 21756872]

[EC 7.1.1.7 created 2014 as EC 1.10.3.14, modified 2017, transferred 2018 to EC 7.1.1.7, modified 2020]

7.1.1.8

Accepted name:

quinol—cytochrome-c reductase

Reaction:

quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H⁺_{[side 2]}

Other name(s):

ubiquinol—cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxidoreductase; mitochondrial electron transport complex III; ubiquinol-cytochrome c-2 oxidoreductase; ubiquinone-cytochrome b-c1 oxidoreductase; ubiquinol-cytochrome c₂ reductase; ubiquinol-cytochrome c₁ oxidoreductase; CoQH₂-cytochrome c oxidoreductase; ubihydroquinol:cytochrome c oxidoreductase; coenzyme QH₂-cytochrome c reductase; QH₂:cytochrome c oxidoreductase; ubiquinol:ferricytochrome-c oxidoreductase

Systematic name:

quinol:ferricytochrome-c oxidoreductase

Comments:

The enzyme, often referred to as the cytochrome bc₁ complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment [cf. EC 7.1.1.2, NADH:ubiquinone reductase (H⁺-translocating)].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, PDB, CAS registry number: 9027-03-6

References:

1.	Marres, C.A.M. and Slater, E.C. Polypeptide composition of purified QH₂:cytochrome c oxidoreductase from beef-heart mitochondria. Biochim. Biophys. Acta 462 (1977) 531–548. [DOI] [PMID: 597492]
2.	Rieske, J.S. Composition, structure, and function of complex III of the respiratory chain. Biochim. Biophys. Acta 456 (1976) 195–247. [PMID: 788795]
3.	Wikström, M., Krab, K. and Saraste, M. Proton-translocating cytochrome complexes. Annu. Rev. Biochem. 50 (1981) 623–655. [DOI] [PMID: 6267990]
4.	Sone, N., Tsuchiya, N., Inoue, M. and Noguchi, S. Bacillus stearothermophilus qcr operon encoding rieske FeS protein, cytochrome b₆, and a novel-type cytochrome c₁ of quinol-cytochrome c reductase. J. Biol. Chem. 271 (1996) 12457–12462. [DOI] [PMID: 8647852]
5.	Yu, J. and Le Brun, N.E. Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 273 (1998) 8860–8866. [DOI] [PMID: 9535866]
6.	Elbehti, A., Nitschke, W., Tron, P., Michel, C. and Lemesle-Meunier, D. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc₁-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J. Biol. Chem. 274 (1999) 16760–16765. [DOI] [PMID: 10358017]

[EC 7.1.1.8 created 1978 as EC 1.10.2.2, modified 2013, transferred 2018 to EC 7.1.1.8]

7.2.1.3

Accepted name:

ascorbate ferrireductase (transmembrane)

Reaction:

ascorbate_{[side 1]} + Fe(III)_{[side 2]} = monodehydroascorbate_{[side 1]} + Fe(II)_{[side 2]}

Other name(s):

cytochrome b₅₆₁ (ambiguous)

Systematic name:

Fe(III):ascorbate oxidorectuctase (electron-translocating)

Comments:

A diheme cytochrome that transfers electrons across a single membrane, such as the outer membrane of the enterocyte, or the tonoplast membrane of the plant cell vacuole. Acts on hexacyanoferrate(III) and other ferric chelates.

Links to other databases:

References:

1.	Flatmark, T. and Terland, O. Cytochrome b₅₆₁ of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim. Biophys. Acta 253 (1971) 487–491. [DOI] [PMID: 4332308]
2.	McKie, A.T., Barrow, D., Latunde-Dada, G.O., Rolfs, A., Sager, G., Mudaly, E., Mudaly, M., Richardson, C., Barlow, D., Bomford, A., Peters, T.J., Raja, K.B., Shirali, S., Hediger, M.A., Farzaneh, F. and Simpson, R.J. An iron-regulated ferric reductase associated with the absorption of dietary iron. Science 291 (2001) 1755–1759. [DOI] [PMID: 11230685]
3.	Su, D. and Asard, H. Three mammalian cytochromes b₅₆₁ are ascorbate-dependent ferrireductases. FEBS J. 273 (2006) 3722–3734. [DOI] [PMID: 16911521]
4.	Berczi, A., Su, D. and Asard, H. An Arabidopsis cytochrome b₅₆₁ with trans-membrane ferrireductase capability. FEBS Lett. 581 (2007) 1505–1508. [DOI] [PMID: 17376442]
5.	Wyman, S., Simpson, R.J., McKie, A.T. and Sharp, P.A. Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro. FEBS Lett. 582 (2008) 1901–1906. [DOI] [PMID: 18498772]
6.	Glanfield, A., McManus, D.P., Smyth, D.J., Lovas, E.M., Loukas, A., Gobert, G.N. and Jones, M.K. A cytochrome b₅₆₁ with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum. PLoS Negl. Trop. Dis. 4:e884 (2010). [DOI] [PMID: 21103361]

[EC 7.2.1.3 created 2011 as EC 1.16.5.1, transferred 2018 to EC 7.2.1.3]

*EC

7.2.2.1

Accepted name:

Na⁺-transporting two-sector ATPase

Reaction:

ATP + H₂O + n Na⁺_{[side 1]} = ADP + phosphate + n Na⁺_{[side 2]}

Other name(s):

sodium-transporting two-sector ATPase; Na⁺-translocating ATPase; Na⁺-translocating F_oF₁-ATPase; sodium ion specific ATP synthase

Systematic name:

ATP phosphohydrolase (two-sector, Na⁺-transporting)

Comments:

A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H⁺-transporting two-sector ATPase) but pumps Na⁺ rather than H⁺. By analogy to EC 7.1.2.2, it is likely that the enzyme pumps 4 sodium ions for every ATP molecule that is hydrolysed. cf. EC 7.2.2.3, P-type Na⁺ transporter and EC 7.2.2.4, ABC-type Na⁺ transporter.

Links to other databases:

References:

1.	Solioz, M. and Davies, K. Operon of vacuolar-type Na⁺-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453–9459. [PMID: 8144530]
2.	Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na⁺-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037–11044. [PMID: 8157629]
3.	Rahlfs, S. and Müller, V. Sequence of subunit c of the Na⁺-translocating F₁F_o-ATPase of Acetobacterium woodii: proposal for determinants of Na⁺ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269–271. [DOI] [PMID: 9119076]

[EC 7.2.2.1 created 2000 as EC 3.6.3.15, transferred 2018 to EC 7.2.2.1, modified 2018]

7.2.2.5

Accepted name:

ABC-type Mn²⁺ transporter

Reaction:

ATP + H₂O + Mn²⁺-[manganese-binding protein]_{[side 1]} = ADP + phosphate + Mn²⁺_{[side 2]} + [manganese-binding protein]_{[side 1]}

Other name(s):

ABC-type manganese permease complex; manganese-transporting ATPase (ambiguous); ABC-type manganese transporter

Systematic name:

ATP phosphohydrolase (ABC-type, Mn²⁺-importing)

Comments:

ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Mn²⁺, Zn²⁺ and iron chelates.

Links to other databases:

References:

1.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
3.	Novak, R., Braun, J.S., Charpentier, E. and Tuomanen, E. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 29 (1998) 1285–1296. [DOI] [PMID: 9767595]
4.	Kolenbrander, P.E., Andersen, R.N., Baker, R.A. and Jenkinson, H.F. The adhesion-assoiated aca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn²⁺ uptake. J. Bacteriol. 180 (1998) 290–295. [PMID: 9440518]

[EC 7.2.2.5 created 2000 as EC 3.6.3.35, transferred 2018 to EC 7.2.2.5]

7.2.2.6

Accepted name:

P-type K⁺ transporter

Reaction:

ATP + H₂O + K⁺_{[side 1]} = ADP + phosphate + K⁺_{[side 2]}

Other name(s):

K⁺-translocating Kdp-ATPase; multi-subunit K⁺-transport ATPase; K⁺-transporting ATPase; potassium-importing ATPase; K⁺-importing ATPase

Systematic name:

ATP phosphohydrolase (P-type, K⁺-importing)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that is involved in K⁺ import. The probable stoichiometry is one ion per ATP hydrolysed.

Links to other databases:

References:

1.	Siebers, A. and Altendorf, K. Characterization of the phosphorylated intermediate of the K⁺-translocating Kdp-ATPase from Escherichia coli. J. Biol. Chem. 264 (1989) 5831–5838. [PMID: 2522440]
2.	Gassel, M., Siebers, A., Epstein, W. and Altendorf, K. Assembly of the Kdp complex, the multi-subunit K⁺-transport ATPase of Escherichia coli. Biochim. Biophys. Acta 1415 (1998) 77–84. [DOI] [PMID: 9858692]
3.	Huang, C.S., Pedersen, B.P. and Stokes, D.L. Crystal structure of the potassium-importing KdpFABC membrane complex. Nature 546 (2017) 681–685. [DOI] [PMID: 28636601]

[EC 7.2.2.6 created 2000 as EC 3.6.3.12, transferred 2018 to EC 7.2.2.6]

7.2.2.7

Accepted name:

ABC-type Fe³⁺ transporter

Reaction:

ATP + H₂O + Fe³⁺-[iron-binding protein]_{[side 1]} = ADP + phosphate + Fe³⁺_{[side 2]} + [iron-binding protein]_{[side 1]}

Other name(s):

Fe³⁺-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, Fe³⁺-transporting)

Comments:

ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. A bacterial enzyme that interacts with a periplasmic iron-binding protein to imports Fe³⁺ ions into the cytoplasm.

Links to other databases:

References:

1.	Angerer, A., Klupp, B. and Braun, V. Iron transport systems of Serratia marcescens. J. Bacteriol. 174 (1992) 1378–1387. [DOI] [PMID: 1531225]
2.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.	Khun, H.H., Kirby, S.D. and Lee, B.C. A Neisseria meningitidis fbp ABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66 (1998) 2330–2336. [PMID: 9573125]

[EC 7.2.2.7 created 2000 as EC 3.6.3.30, transferred 2018 to EC 7.2.2.7]

7.2.2.8

Accepted name:

P-type Cu⁺ transporter

Reaction:

ATP + H₂O + Cu⁺_{[side 1]} = ADP + phosphate + Cu⁺_{[side 2]}

Other name(s):

Cu⁺-exporting ATPase (ambiguous); copA (gene name); ATP7A (gene name); ATP7B (gene name)

Systematic name:

ATP phosphohydrolase (P-type, Cu⁺-exporting)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu⁺ or Ag⁺, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu²⁺ transporter, which mainly transports the divalent copper ion.

Links to other databases:

References:

1.	Fan, B. and Rosen, B.P. Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. 277 (2002) 46987–46992. [DOI] [PMID: 12351646]
2.	Banci, L., Bertini, I., Ciofi-Baffoni, S., D'Onofrio, M., Gonnelli, L., Marhuenda-Egea, F.C. and Ruiz-Duenas, F.J. Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states. J. Mol. Biol. 317 (2002) 415–429. [DOI] [PMID: 11922674]
3.	Mandal, A.K. and Arguello, J.M. Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu⁺-ATPase CopA. Biochemistry 42 (2003) 11040–11047. [DOI] [PMID: 12974640]
4.	Gonzalez-Guerrero, M. and Arguello, J.M. Mechanism of Cu⁺-transporting ATPases: soluble Cu⁺ chaperones directly transfer Cu⁺ to transmembrane transport sites. Proc. Natl. Acad. Sci. USA 105 (2008) 5992–5997. [DOI] [PMID: 18417453]
5.	Lewis, D., Pilankatta, R., Inesi, G., Bartolommei, G., Moncelli, M.R. and Tadini-Buoninsegni, F. Distinctive features of catalytic and transport mechanisms in mammalian sarco-endoplasmic reticulum Ca²⁺ ATPase (SERCA) and Cu⁺ (ATP7A/B) ATPases. J. Biol. Chem. 287 (2012) 32717–32727. [DOI] [PMID: 22854969]
6.	Tadini-Buoninsegni, F., Bartolommei, G., Moncelli, M.R., Pilankatta, R., Lewis, D. and Inesi, G. ATP dependent charge movement in ATP7B Cu⁺-ATPase is demonstrated by pre-steady state electrical measurements. FEBS Lett. 584 (2010) 4619–4622. [DOI] [PMID: 20965182]
7.	Mattle, D., Sitsel, O., Autzen, H.E., Meloni, G., Gourdon, P. and Nissen, P. On allosteric modulation of P-type Cu⁺-ATPases. J. Mol. Biol. 425 (2013) 2299–2308. [DOI] [PMID: 23500486]

[EC 7.2.2.8 created 2013 as EC 3.6.3.54, transferred 2018 to EC 7.2.2.8]

7.2.2.9

Accepted name:

P-type Cu²⁺ transporter

Reaction:

ATP + H₂O + Cu²⁺_{[side 1]} = ADP + phosphate + Cu²⁺_{[side 2]}

Other name(s):

Cu²⁺-exporting ATPase; copB (gene name)

Systematic name:

ATP phosphohydrolase (P-type, Cu²⁺-exporting)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].

Links to other databases:

References:

1.	Mana-Capelli, S., Mandal, A.K. and Arguello, J.M. Archaeoglobus fulgidus CopB is a thermophilic Cu²⁺-ATPase: functional role of its histidine-rich-N-terminal metal binding domain. J. Biol. Chem. 278 (2003) 40534–40541. [DOI] [PMID: 12876283]
2.	Jayakanthan, S., Roberts, S.A., Weichsel, A., Arguello, J.M. and McEvoy, M.M. Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Biosci Rep 32 (2012) 443–453. [DOI] [PMID: 22663904]

[EC 7.2.2.9 created 2000 as EC 3.6.3.4, modified 2013, transferred 2018 to EC 7.2.2.9]

7.2.2.10

Accepted name:

P-type Ca²⁺ transporter

Reaction:

ATP + H₂O + Ca²⁺_{[side 1]} = ADP + phosphate + Ca²⁺_{[side 2]}

Other name(s):

sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca²⁺-ATPase; calcium pump; Ca²⁺-pumping ATPase; plasma membrane Ca-ATPase; Ca²⁺-transporting ATPaseP-

Systematic name:

ATP phosphohydrolase (P-type, Ca²⁺-transporting)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca²⁺-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum, in yeast, and in some bacteria. The enzymes from plasma membrane and from yeast have been shown to transport one ion per ATP hydrolysed whereas those from the sarcoplasmic reticulum transport two ions per ATP hydrolysed. In muscle cells Ca²⁺ is transported from the cytosol (side 1) into the sarcoplasmic reticulum (side 2).

Links to other databases:

References:

1.	Schatzmann, H.J. and Vicenzi, F.F. Calcium movements across the membrane of human red cells. J. Physiol. 201 (1969) 369–395. [DOI] [PMID: 4238381]
2.	Inesi, G., Watanabe, T., Coan, C. and Murphy, A. The mechanism of sarcoplasmic reticulum ATPase. Ann. N.Y. Acad. Sci. 402 (1982) 515–532. [DOI] [PMID: 6301340]
3.	Carafoli, E. The Ca²⁺ pump of the plasma membrane. J. Biol. Chem. 267 (1992) 2115–2118. [PMID: 1310307]
4.	MacLennan, D.H., Rice, W.J. and Green, N.M. The mechanism of Ca²⁺ transport by sarco(endo)plasmic reticulum Ca²⁺-ATPases. J. Biol. Chem. 272 (1997) 28815–28818. [DOI] [PMID: 9360942]
5.	Toyoshima, C., Nakasako, M., Nomura, H. and Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647–655. [DOI] [PMID: 10864315]
6.	Andersen, J.L., Gourdon, P., Moller, J.V., Morth, J.P. and Nissen, P. Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA₁. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 (2011) 718–722. [PMID: 21636921]

[EC 7.2.2.10 created 1984 as as EC 3.6.1.38, transferred 2000 to EC 3.6.3.8, modified 2001, modified 2011, transferred 2018 to EC 7.2.2.10]

7.2.2.11

Accepted name:

ABC-type Ni²⁺ transporter

Reaction:

ATP + H₂O + Ni²⁺-[nickel-binding protein]_{[side 1]} = ADP + phosphate + Ni²⁺_{[side 2]} + [nickel-binding protein]_{[side 1]}

Other name(s):

nickel ABC transporter; nickel-transporting ATPase; ABC-type nickel-transporter

Systematic name:

ATP phosphohydrolase (ABC-type, Ni²⁺-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of Ni²⁺; the identity of the nickel species transported has not been conclusively established. Does not undergo phosphorylation during the transport process.

Links to other databases:

References:

1.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.	Hendricks, J.K. and Mobley, H.L. Helicobacter pylori ABC transporter: effect of allelic exchange mutagenesis on urease activity. J. Bacteriol. 179 (1997) 5892–5902. [DOI] [PMID: 9294450]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

[EC 7.2.2.11 created 2000 as EC 3.6.3.24, transferred 2018 to EC 7.2.2.11]

7.2.2.12

Accepted name:

P-type Zn²⁺ transporter

Reaction:

ATP + H₂O + Zn²⁺_{[side 1]} = ADP + phosphate + Zn²⁺_{[side 2]}

Other name(s):

Zn(II)-translocating P-type ATPase; Zn²⁺-exporting ATPase; P1B-type ATPase; HMA4 (gene name); zntA (gene name)

Systematic name:

ATP phosphohydrolase (P-type, Zn²⁺-exporting)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, present in prokaryotes and photosynthetic eukaryotes, exports Zn²⁺ and the related cations Cd²⁺ and Pb²⁺.

Links to other databases:

References:

1.	Beard, S.J., Hashim, R., Membrillo-Hernández, J., Hughes, M.N. and Poole, R.K. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase. Mol. Microbiol. 25 (1997) 883–891. [DOI] [PMID: 9364914]
2.	Rensing, C., Mitra, B. and Rosen, B.P. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc. Natl. Acad. Sci. USA 94 (1997) 14326–14331. [DOI] [PMID: 9405611]
3.	Rensing, C., Sun, Y., Mitra, B. and Rosen, B.P. Pb(II)-translocating P-type ATPases. J. Biol. Chem. 273 (1998) 32614–32617. [DOI] [PMID: 9830000]
4.	Mills, R.F., Francini, A., Ferreira da Rocha, P.S., Baccarini, P.J., Aylett, M., Krijger, G.C. and Williams, L.E. The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels. FEBS Lett. 579 (2005) 783–791. [DOI] [PMID: 15670847]
5.	Eren, E. and Argüello, J.M. Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn²⁺ homeostasis. Plant Physiol. 136 (2004) 3712–3723. [DOI] [PMID: 15475410]

[EC 7.2.2.12 created 2000 as EC 3.6.3.5, modified 2001, modified 2006, transferred 2018 to EC 7.2.2.12]

7.2.2.13

Accepted name:

Na⁺/K⁺-exchanging ATPase

Reaction:

ATP + H₂O + Na⁺_{[side 1]} + K⁺_{[side 2]} = ADP + phosphate + Na⁺_{[side 2]} + K⁺_{[side 1]}

Other name(s):

(Na⁺ + K⁺)-activated ATPase; Na,K-activated ATPase; Na,K-pump; Na⁺,K⁺-ATPase; sodium/potassium-transporting ATPase; Na⁺/K⁺-exchanging ATPase

Systematic name:

ATP phosphohydrolase (P-type, Na⁺/K⁺-exchanging)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This is a plasma membrane enzyme, ubiquitous in animal cells, that catalyses the efflux of three Na⁺ and influx of two K⁺ per ATP hydrolysed. It is involved in generating the plasma membrane electrical potential.

Links to other databases:

References:

1.	Skou, J.C. The influence of some cations on an adenosinetriphosphatase from peripheral nerve. Biochim. Biophys. Acta 23 (1957) 394–401. [DOI] [PMID: 13412736]
2.	Post, R.L., Sen, A.K. and Rosenthal, A.S. A phosphorylated intermediate in adenosine triphosphate-dependent sodium and potassium transport across kidney membrane. J. Biol. Chem. 240 (1965) 1437–1445. [PMID: 14284759]
3.	Skou, J.C. The energy-coupled exchange of Na⁺ for K⁺ across the cell membrane. The Na⁺,K⁺ pump. FEBS Lett. 268 (1990) 314–324. [DOI] [PMID: 2166689]
4.	Castillo, J.P., Rui, H., Basilio, D., Das, A., Roux, B., Latorre, R., Bezanilla, F. and Holmgren, M. Mechanism of potassium ion uptake by the Na⁺/K⁺-ATPase. Nat. Commun. 6:7622 (2015). [PMID: 26205423]

[EC 7.2.2.13 created 1984 EC 3.6.1.37, transferred 2000 to EC 3.6.3.9, modified 2001, transferred 2018 to EC 7.2.2.13]

7.2.2.14

Accepted name:

P-type Mg²⁺ transporter

Reaction:

ATP + H₂O + Mg²⁺_{[side 1]} = ADP + phosphate + Mg²⁺_{[side 2]}

Other name(s):

Mg²⁺-transporting P-type ATPase; Mg²⁺-transporting ATPase; Mg²⁺-importing ATPase; magnesium-translocating P-type ATPase; mgtA (gene name); mgtB (gene name)

Systematic name:

ATP phosphohydrolase (P-type, Mg²⁺-importing)

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. A bacterial enzyme that imports Mg²⁺ with, rather than against, the Mg²⁺ electrochemical gradient. The enzyme is also involved in Ni²⁺ import.

Links to other databases:

References:

1.	Snavely, M.D., Miller, C.G. and Maguire, M.E. The mgtB Mg²⁺ transport locus of Salmonella typhimurium encodes a P-type ATPase. J. Biol. Chem. 266 (1991) 815–823. [PMID: 1824701]
2.	Maguire, M.E. MgtA and MgtB: prokaryotic P-type ATPases that mediate Mg²⁺ influx. J. Bioenerg. Biomembr. 24 (1992) 319–328. [PMID: 1328179]
3.	Tao, T., Snavely, M.D., Farr, S.G. and Maguire, M.E. Magnesium transport in Salmonella typhimurium: mtgA encodes a P-type ATPase and is regulated by Mg²⁺ in a manner similar to that of the mgtB P-type ATPase. J. Bacteriol. 177 (1995) 2654–2662. [DOI] [PMID: 7751273]

[EC 7.2.2.14 created 2000 as EC 3.6.3.2, modified 2001, transferred 2018 to EC 7.2.2.14]

7.2.2.15

Accepted name:

P-type Ag⁺ transporter

Reaction:

ATP + H₂O + Ag⁺_{[side 1]} = ADP + phosphate + Ag⁺_{[side 2]}

Other name(s):

Ag⁺-exporting ATPase

Systematic name:

ATP phosphohydrolase (P-type, Ag⁺-exporting)

Comments:

A P-type ATPase that exports Ag⁺ ions from some bacteria, archaea as well as from some animal tissues. The proteins also transport Cu⁺ ions (cf. EC 7.2.2.8, P-type Cu⁺ transporter).

Links to other databases:

References:

1.	Gupta, A., Matsui, K., Lo, J.F. and Silver, S. Molecular basis for resistance to silver cations in Salmonella. Nature Med. 5 (1999) 183–188. [DOI] [PMID: 9930866]
2.	Bury, N.R., Grosell, M., Grover, A.K. and Wood, C.M. ATP-dependent silver transport across the basolateral membrane of rainbow trout gills. Toxicol. Appl. Pharmacol. 159 (1999) 1–8. [DOI] [PMID: 10448119]

[EC 7.2.2.15 created 2000 as EC 3.6.3.53, transferred 2018 to EC 7.2.2.15]

7.2.2.16

Accepted name:

ABC-type ferric hydroxamate transporter

Reaction:

ATP + H₂O + Fe³⁺-hydroxamate complex-[hydroxamate-binding protein]_{[side 1]} = ADP + phosphate + Fe³⁺-hydroxamate complex_{[side 2]} + [hydroxamate-binding protein]_{[side 1]}

Other name(s):

iron(III) hydroxamate transporting ATPase; iron(III) hydroxamate ABC transporter; fhuCDB (gene names)

Systematic name:

ATP phosphohydrolase [ABC-type, iron(III) hydroxamate-importing]

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of Fe³⁺-complexed hydroxamate siderophores such as coprogen, ferrichrome and the ferric hydroxamate antibiotic, albomycin.

Links to other databases:

References:

1.	Koster, W. Iron(III) hydroxamate transport across the cytoplasmic membrane of Escherichia coli. Biol. Met. 4 (1991) 23–32. [PMID: 1830209]
2.	Speziali, C.D., Dale, S.E., Henderson, J.A., Vines, E.D. and Heinrichs, D.E. Requirement of Staphylococcus aureus ATP-binding cassette-ATPase FhuC for iron-restricted growth and evidence that it functions with more than one iron transporter. J. Bacteriol. 188 (2006) 2048–2055. [PMID: 16513734]

[EC 7.2.2.16 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.16]

7.2.2.17

Accepted name:

ABC-type ferric enterobactin transporter

Reaction:

ATP + H₂O + Fe³⁺-enterobactin complex-[enterobactin-binding protein]_{[side 1]} = ADP + phosphate + Fe³⁺-enterobactin complex_{[side 2]} + [enterobactin-binding protein]_{[side 1]}

Other name(s):

ferric enterobactin transporting ATPase; ferric enterobactin ABC transporter; fepBCDG (gene names)

Systematic name:

ATP phosphohydrolase (ABC-type, iron(III) enterobactin-importing)

Comments:

Links to other databases:

References:

1.	Chenault, S.S. and Earhart, C.F. Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease. Mol. Microbiol. 5 (1991) 1405–1413. [PMID: 1787794]
2.	Shea, C.M. and McIntosh, M.A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding-protein-dependent systems in Escherichia coli. Mol. Microbiol. 5 (1991) 1415–1428. [DOI] [PMID: 1838574]

[EC 7.2.2.17 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.17]

7.2.2.18

Accepted name:

ABC-type ferric citrate transporter

Reaction:

ATP + H₂O + Fe³⁺-dicitrate-[dicitrate-binding protein]_{[side 1]} = ADP + phosphate + Fe³⁺-dicitrate_{[side 2]} + [dicitrate-binding protein]_{[side 1]}

Other name(s):

ferric citrate transporting ATPase; ferric citrate ABC transporter; fecBCDE (gene names)

Systematic name:

ATP phosphohydrolase (ABC-type, iron(III) dicitrate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of Fe³⁺-citrate in the form of a mononuclear (containing one iron(III) ion and two citrate molecules) or dinuclear (containing 2 iron(III) ions) complexes.

Links to other databases:

References:

1.	Staudenmaier, H., Van Hove, B., Yaraghi, Z. and Braun, V. Nucleotide sequences of the fecBCDE genes and locations of the proteins suggest a periplasmic-binding-protein-dependent transport mechanism for iron(III) dicitrate in Escherichia coli. J. Bacteriol. 171 (1989) 2626–2633. [PMID: 2651410]
2.	Banerjee, S., Paul, S., Nguyen, L.T., Chu, B.C. and Vogel, H.J. FecB, a periplasmic ferric-citrate transporter from E. coli, can bind different forms of ferric-citrate as well as a wide variety of metal-free and metal-loaded tricarboxylic acids. Metallomics 8 (2016) 125–133. [PMID: 26600288]

[EC 7.2.2.18 created 2000 as EC 3.6.3.34, part transferred 2018 to EC 7.2.2.18]

7.3.2.3

Accepted name:

ABC-type sulfate transporter

Reaction:

ATP + H₂O + sulfate-[sulfate-binding protein]_{[side 1]} = ADP + phosphate + sulfate_{[side 2]} + [sulfate-binding protein]_{[side 1]}

Other name(s):

sulfate ABC transporter; sulfate-transporting ATPase (ambiguous)

Systematic name:

ATP phosphohydrolase (ABC-type, sulfate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme from Escherichia coli can interact with either of two periplasmic binding proteins and mediates the high affinity uptake of sulfate and thiosulfate. May also be involved in the uptake of selenite, selenate and possibly molybdate. Does not undergo phosphorylation during the transport.

Links to other databases:

References:

1.	Sirko, A., Zatyka, M., Sadowy, E. and Hulanicka, D. Sulfate and thiosulfate transport in Escherichia coli K-12: evidence for a functional overlapping of sulfate- and thiosulfate-binding proteins. J. Bacteriol. 177 (1995) 4134–4136. [DOI] [PMID: 7608089]
2.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.3.2.3 created 2000 as EC 3.6.3.25, transferred 2018 to EC 7.3.2.3]

7.3.2.4

Accepted name:

ABC-type nitrate transporter

Reaction:

ATP + H₂O + nitrate-[nitrate-binding protein]_{[side 1]} = ADP + phosphate + nitrate_{[side 2]} + [nitrate-binding protein]_{[side 1]}

Other name(s):

nitrate-transporting ATPase (ambiguous)

Systematic name:

ATP phosphohydrolase (ABC-type, nitrate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of nitrate, nitrite, and cyanate.

Links to other databases:

References:

1.	Omata, T. Structure, function and regulation of the nitrate transport system of the cyanobacterium Synechococcus sp. PCC7942. Plant Cell Physiol. 36 (1995) 207–213. [PMID: 7767600]
2.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

[EC 7.3.2.4 created 2000 as EC 3.6.3.26, transferred 2018 to EC 7.3.2.4]

7.3.2.5

Accepted name:

ABC-type molybdate transporter

Reaction:

ATP + H₂O + molybdate-[molybdate-binding protein]_{[side 1]} = ADP + phosphate + molybdate_{[side 2]} + [molybdate-binding protein]_{[side 1]}

Glossary:

molybdate = tetraoxidomolybdate(2^-) = MoO₄^2-

Other name(s):

molybdate ABC transporter; molybdate-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, molybdate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the high-affinity import of molybdate and tungstate. Does not undergo phosphorylation during the transport process.

Links to other databases:

References:

1.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.	Grunden, A.M. and Shanmugam, K.T. Molybdate transport and regulation in bacteria. Arch. Mikrobiol. 168 (1997) 345–354. [PMID: 9325422]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

[EC 7.3.2.5 created 2000 as EC 3.6.3.29, transferred 2018 to EC 7.3.2.5]

7.3.2.6

Accepted name:

ABC-type tungstate transporter

Reaction:

ATP + H₂O + tungstate-[tungstate-binding protein]_{[side 1]} = ADP + phosphate + tungstate_{[side 2]} + [tungstate-binding protein]_{[side 1]}

Other name(s):

tungstate transporter; tungstate-importing ATPase; tungstate-specific ABC transporter; WtpABC; TupABC

Systematic name:

ATP phosphohydrolase (ABC-type, tungstate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, characterized from the archaeon Pyrococcus furiosus, the Gram-positive bacterium Eubacterium acidaminophilum and the Gram-negative bacterium Campylobacter jejuni, interacts with an extracytoplasmic substrate binding protein and mediates the import of tungstate into the cell for incorporation into tungsten-dependent enzymes.

Links to other databases:

References:

1.	Makdessi, K., Andreesen, J.R. and Pich, A. Tungstate uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. J. Biol. Chem. 276 (2001) 24557–24564. [DOI] [PMID: 11292832]
2.	Bevers, L.E., Hagedoorn, P.L., Krijger, G.C. and Hagen, W.R. Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. J. Bacteriol. 188 (2006) 6498–6505. [DOI] [PMID: 16952940]
3.	Smart, J.P., Cliff, M.J. and Kelly, D.J. A role for tungsten in the biology of Campylobacter jejuni: tungstate stimulates formate dehydrogenase activity and is transported via an ultra-high affinity ABC system distinct from the molybdate transporter. Mol. Microbiol. 74 (2009) 742–757. [DOI] [PMID: 19818021]

[EC 7.3.2.6 created 2013 as EC 3.6.3.55, transferred 2018 to EC 7.3.2.6]

7.4.2.3

Accepted name:

mitochondrial protein-transporting ATPase

Reaction:

ATP + H₂O + mitochondrial-protein_{[side 1]} = ADP + phosphate + mitochondrial-protein_{[side 2]}

Systematic name:

ATP phosphohydrolase (mitochondrial protein-importing)

Comments:

A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase involved in the transport of proteins or preproteins into mitochondria using the TIM protein complex. TIM is the protein transport machinery of the mitochondrial inner membrane that contains three essential Tim proteins: Tim17 and Tim23 are thought to build a preprotein translocation channel while Tim44 interacts transiently with the matrix heat-shock protein Hsp70 to form an ATP-driven import motor.

Links to other databases:

References:

1.	Bomer, U., Meijer, M., Maarse, A.C., Honlinger, A., Dekker, P.J., Pfanner, N. and Rassow, J. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. EMBO J. 16 (1997) 2205–2216. [DOI] [PMID: 9171336]
2.	Berthold, J., Bauer, M.F., Schneider, H.C., Klaus, C., Dietmeier, K., Neupert, W. and Brunner, M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP-driving system. Cell 81 (1995) 1085–1093. [DOI] [PMID: 7600576]
3.	Voos, W., Martin, H., Krimmer, T. and Pfanner, N. Mechanisms of protein translocation into mitochondria. Biochim. Biophys. Acta 1422 (1999) 235–254. [DOI] [PMID: 10548718]

[EC 7.4.2.3 created 2000 as EC 3.6.3.51, transferred 2018 to EC 7.4.2.3]

7.4.2.4

Accepted name:

chloroplast protein-transporting ATPase

Reaction:

ATP + H₂O + chloroplast-protein_{[side 1]} = ADP + phosphate + chloroplast-protein_{[side 2]}

Systematic name:

ATP phosphohydrolase (chloroplast protein-importing)

Comments:

A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. Involved in the transport of proteins or preproteins into chloroplast stroma (several ATPases may participate in this process).

Links to other databases:

References:

1.	Cline, K., Ettinger, N.F. and Theg, S.M. Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J. Biol. Chem. 267 (1992) 2688–2696. [PMID: 1733965]
2.	Nakai, M., Goto, A., Nohara, T., Sugito, D. and Endo, T. Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269 (1994) 31338–33341. [PMID: 7989297]
3.	Scott, S.V. and Theg, S.M. A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implications. J. Cell Biol. 132 (1996) 63–75. [PMID: 8567731]

[EC 7.4.2.4 created 2000 as EC 3.6.3.52, transferred 2018 to EC 7.4.2.4]

7.4.2.5

Accepted name:

bacterial ABC-type protein transporter

Reaction:

ATP + H₂O + protein_{[side 1]} = ADP + phosphate + protein_{[side 2]}

Other name(s):

PrtDEF (gene names); hasDEF (gene names); peptide-transporting ATPase (ambiguous)

Systematic name:

ATP phosphohydrolase (ABC-type, peptide-exporting)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include α-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.

Links to other databases:

References:

1.	Letoffe, S., Delepelaire, P. and Wandersman, C. Protease secretion by Erwinia chrysanthemi: the specific secretion functions are analogous to those of Escherichia coli α-haemolysin. EMBO J. 9 (1990) 1375–1382. [PMID: 2184029]
2.	Klein, C. and Entian, K.D. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl. Environ. Microbiol. 60 (1994) 2793–2801. [PMID: 8085823]
3.	Binet, R., Létoffé, S., Ghigo, J.M., Delepaire, P. and Wanderman, C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene 192 (1997) 7–11. [DOI] [PMID: 9224868]

[EC 7.4.2.5 created 2000 as EC 3.6.3.43, transferred 2018 to EC 7.4.2.5, modified 2019]

7.4.2.6

Accepted name:

ABC-type oligopeptide transporter

Reaction:

ATP + H₂O + oligopeptide-[oligopeptide-binding protein]_{[side 1]} = ADP + phosphate + oligopeptide_{[side 2]} + [oligopeptide-binding protein]_{[side 1]}

Other name(s):

oligopeptide permease; OppBCDF; oligopeptide ABC transporter; oligopeptide-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, oligopeptide-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the import of oligopeptides of varying nature. The binding protein determines the specificity of the system. cf. EC 7.4.2.9, ABC-type dipeptide transporter.

Links to other databases:

References:

1.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
3.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
4.	Pearce, S.R., Mimmack, M.L., Gallagher, M.P., Gileadi, U., Hyde, S.C. and Higgins, C.F. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Mol. Microbiol. 6 (1992) 47–57. [DOI] [PMID: 1738314]

[EC 7.4.2.6 created 2000 as EC 3.6.3.23, transferred 2018 to EC 7.4.2.6]

7.4.2.7

Accepted name:

ABC-type α-factor-pheromone transporter

Reaction:

ATP + H₂O + α-factor_{[side 1]} = ADP + phosphate + α-factor_{[side 2]}

Other name(s):

α-factor-transporting ATPase; α-factor-pheromone transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, α-factor-exporting)

Comments:

Links to other databases:

References:

1.	Michaelis, S. STE6, the yeast α-factor exporter. Semin. Cell Biol. 4 (1993) 17–27. [PMID: 8095825]
2.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.4.2.7 created 2000 as EC 3.6.3.48, transferred 2018 to EC 7.4.2.7]

7.4.2.8

Accepted name:

protein-secreting ATPase

Reaction:

ATP + H₂O + cellular protein_{[side 1]} = ADP + phosphate + cellular protein_{[side 2]}

Systematic name:

ATP phosphohydrolase (protein-secreting)

Comments:

A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.

Links to other databases:

References:

1.	Saier, M.H., Jr. , Tam. R., Reizer, A. and Reizer, J. Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11 (1994) 841–847. [DOI] [PMID: 8022262]
2.	Mecsas, J. and Strauss, E.J. Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands. Emerg. Infect. Diseases. 2 (1996) 270–288. [DOI] [PMID: 8969244]
3.	Thomas, J.D., Reeves, P.J. and Salmond, G.P. The general secretion pathway of Erwinia carotovora subsp. carotovora: analysis of the membrane topology of OutC and OutF. Microbiology 143 (1997) 713–720. [DOI] [PMID: 9084158]
4.	Baker, B., Zambryski, P., Staskawicz, B. and Dinesh-Kumar, S.P. Signaling in plant-microbe interactions. Science 276 (1997) 726–733. [DOI] [PMID: 9115193]
5.	Martinez, A., Ostrovsky, P. and Nunn, D.N. Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion. Mol. Microbiol. 28 (1998) 1235–1246. [DOI] [PMID: 9680212]
6.	Schuch, R. and Maurelli, A.T. The mxi-Spa type III secretory pathway of Shigella flexneri requires an outer membrane lipoprotein, MxiM, for invasin translocation. Infect. Immun. 67 (1999) 1982–1991. [PMID: 10085046]

[EC 7.4.2.8 created 2000 as EC 3.6.3.50, transferred 2018 to EC 7.4.2.8]

7.4.2.9

Accepted name:

ABC-type dipeptide transporter

Reaction:

ATP + H₂O + a dipeptide-[dipeptide-binding protein]_{[side 1]} = ADP + phosphate + a dipeptide_{[side 2]} + [dipeptide-binding protein]_{[side 1]}

Other name(s):

dipeptide transporting ATPase; dipeptide ABC transporter; dppBCDF (gene names)

Systematic name:

ATP phosphohydrolase (ABC-type, dipeptide-transporting)

Comments:

ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the uptake of di- and tripeptides. The enzyme from Pseudomonas aeruginosa can interact with five different substrate binding proteins.

Links to other databases:

References:

1.	Abouhamad, W.N., Manson, M., Gibson, M.M. and Higgins, C.F. Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. Mol. Microbiol. 5 (1991) 1035–1047. [PMID: 1956284]
2.	Sanz, Y., Lanfermeijer, F.C., Renault, P., Bolotin, A., Konings, W.N. and Poolman, B. Genetic and functional characterization of dpp genes encoding a dipeptide transport system in Lactococcus lactis. Arch. Microbiol. 175 (2001) 334–343. [PMID: 11409543]
3.	Li, X., Zhuo, W., Yu, J., Ge, J., Gu, J., Feng, Y., Yang, M., Wang, L. and Wang, N. Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domain. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 256–265. [PMID: 23385461]
4.	Pletzer, D., Lafon, C., Braun, Y., Kohler, T., Page, M.G., Mourez, M. and Weingart, H. High-throughput screening of dipeptide utilization mediated by the ABC transporter DppBCDF and its substrate-binding proteins DppA¹-A⁵ in Pseudomonas aeruginosa. PLoS One 9:e111311 (2014). [PMID: 25338022]

[EC 7.4.2.9 created 2018]

7.5.2.3

Accepted name:

ABC-type β-glucan transporter

Reaction:

ATP + H₂O + β-glucan_{[side 1]} = ADP + phosphate + β-glucan_{[side 2]}

Other name(s):

β-glucan-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, β-glucan-exporting)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. An enzyme found in Gram-negative bacteria that exports β-glucans.

Links to other databases:

References:

1.	Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995–1017. [PMID: 8302219]
2.	Becker, A., Kuster, H., Niehaus, K. and Puhler, A. Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster: identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis. Mol. Gen. Genet. 249 (1995) 487–497. [PMID: 8544814]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

[EC 7.5.2.3 created 2000 as EC 3.6.3.42, transferred 2018 to EC 7.5.2.3]

7.5.2.4

Accepted name:

ABC-type teichoic-acid transporter

Reaction:

ATP + H₂O + teichoic acid_{[side 1]} = ADP + phosphate + teichoic acid_{[side 2]}

Other name(s):

teichoic-acid-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, teichoic-acid-exporting)

Comments:

Links to other databases:

References:

1.	Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995–1017. [PMID: 8302219]
2.	Lazarevic, V. and Karamoto, D. The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids. Mol. Microbiol. 16 (1995) 345–355. [DOI] [PMID: 7565096]
3.	Paulsen, I.T., Beness, A.M. and Saier, M.H., Jr. Computer-based analysis of the protein constituents of transport systems catalysing export of complex carbohydrates in bacteria. Microbiology 143 (1997) 2685–2699. [DOI] [PMID: 9274022]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.

[EC 7.5.2.4 created 2000 as EC 3.6.3.40, transferred 2018 to EC 7.5.2.4]

7.5.2.5

Accepted name:

ABC-type lipopolysaccharide transporter

Reaction:

ATP + H₂O + lipopolysaccharide_{[side 1]} = ADP + phosphate + lipopolysaccharide_{[side 2]}

Other name(s):

lptB (gene name); lipopolysaccharide transport system; lipopolysaccharide-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, lipopolysaccharide-exporting)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzyme, characterized from the bacterium Escherichia coli, functions as part of the lipopolysaccharide (LPS) export system, a seven protein system that translocates LPS from the inner- to the outer membrane. The ATPase activity in this system is implicated in releasing LPS from the inner membrane.

Links to other databases:

References:

1.	Sperandeo, P., Cescutti, R., Villa, R., Di Benedetto, C., Candia, D., Deho, G. and Polissi, A. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J. Bacteriol. 189 (2007) 244–253. [PMID: 17056748]
2.	Ruiz, N., Gronenberg, L.S., Kahne, D. and Silhavy, T.J. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 105 (2008) 5537–5542. [PMID: 18375759]
3.	Narita, S. and Tokuda, H. Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides. FEBS Lett. 583 (2009) 2160–2164. [PMID: 19500581]
4.	Tran, A.X., Dong, C. and Whitfield, C. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. J. Biol. Chem. 285 (2010) 33529–33539. [PMID: 20720015]
5.	Okuda, S., Freinkman, E. and Kahne, D. Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli. Science 338 (2012) 1214–1217. [PMID: 23138981]
6.	Chng, S.S., Gronenberg, L.S. and Kahne, D. Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 49 (2010) 4565–4567. [PMID: 20446753]

[EC 7.5.2.5 created 2000 as EC 3.6.3.39, transferred 2018 to EC 7.5.2.5]

7.5.2.6

Accepted name:

ABC-type lipid A-core oligosaccharide transporter

Reaction:

ATP + H₂O + lipid A-core oligosaccharide_{[side 1]} = ADP + phosphate + lipid A-core oligosaccharide_{[side 2]}

Other name(s):

MsbA; lipid flippase; ATP-dependent lipid A-core flippase

Systematic name:

ATP phosphohydrolase (ABC-type, lipid A-core oligosaccharide-translocating)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, best characterized from the bacterium Escherichia coli, is located in the inner membrane and mediates the movement of lipid A attached to the core oligosaccharide from the cytoplasm to the periplasmic side of the inner membrane, an important step in the lipopolysaccharide biosynthetic pathway. Not to be confused with EC 7.5.2.5, ABC-type lipopolysaccharide transporter (LptB), which is implicated in the translocation of LPS from the inner membrane to the outer membrane and acts later in the process.

Links to other databases:

References:

1.	Karow, M. and Georgopoulos, C. The essential Escherichia coli msbA gene, a multicopy suppressor of null mutations in the htrB gene, is related to the universally conserved family of ATP-dependent translocators. Mol. Microbiol. 7 (1993) 69–79. [PMID: 8094880]
2.	Zhou, Z., White, K.A., Polissi, A., Georgopoulos, C. and Raetz, C.R. Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis. J. Biol. Chem. 273 (1998) 12466–12475. [PMID: 9575204]
3.	Singh, H., Velamakanni, S., Deery, M.J., Howard, J., Wei, S.L. and van Veen, H.W. ATP-dependent substrate transport by the ABC transporter MsbA is proton-coupled. Nat. Commun. 7:12387 (2016). [PMID: 27499013]

[EC 7.5.2.6 created 2018]

7.6.2.4

Accepted name:

ABC-type fatty-acyl-CoA transporter

Reaction:

ATP + H₂O + fatty acyl CoA_{[side 1]} = ADP + phosphate + fatty acyl CoA_{[side 2]}

Other name(s):

fatty-acyl-CoA-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger’s syndrome.

Links to other databases:

References:

1.	Kamijo, K., Taketani, S., Yokota, S., Osumi, T. and Hashimoto, T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glcoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 265 (1990) 4534–4540. [PMID: 1968461]
2.	Hettema, E.H., van Roermund, C.W.T., Distel, B. , van den Berg. M., Vilela, C., Rodrigues-Posada, C., Wanders, R.J.A. and Tabak, H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 15 (1996) 3813–3822. [PMID: 8670886]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.6.2.4 created 2000 as EC 3.6.3.47, transferred 2018 to EC 7.6.2.4]

7.6.2.5

Accepted name:

ABC-type heme transporter

Reaction:

ATP + H₂O + heme_{[side 1]} = ADP + phosphate + heme_{[side 2]}

Other name(s):

heme-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, heme-exporting)

Comments:

Links to other databases:

References:

1.	Ramseier, T.M., Winteler, H.V. and Hennecke, H. Discovery and sequence analysis of bacterial genes involved in the biogenesis of c-type cytochromes. J. Biol. Chem. 266 (1991) 7793–7803. [PMID: 1850420]
2.	Jekabsons, W. and Schuster, W. orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria. Mol. Gen. Genet. 246 (1995) 166–173. [PMID: 7862087]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.6.2.5 created 2000 as EC 3.6.3.41, transferred 2018 to EC 7.6.2.5]

7.6.2.6

Accepted name:

ABC-type guanine transporter

Reaction:

ATP + H₂O + guanine_{[side 1]} = ADP + phosphate + guanine_{[side 2]}

Other name(s):

guanine-transporting ATPase; white (gene name); brown (gene name)

Systematic name:

ATP phosphohydrolase (ABC-type, guanine-importing)

Comments:

An ATP-binding cassette (ABC) type transporter found in insects that transports guanine and other purines into pigment granules in the eye, where they are converted to pteridine pigments. The transporter is a hererodimer composed of two different peptides, each containing one membrane-spanning and one cytoplasmic ATP-binding domain. In Drosophila, this transporter is encoded by the white and brown genes.

Links to other databases:

References:

1.	Sullivan, D.T., Bell, L.A., Paton, D.R. and Sullivan, M.C. Purine transport by malpighian tubules of pteridine-deficient eye color mutants of Drosophila melanogaster. Biochem. Genet. 17 (1979) 565–573. [PMID: 117796]
2.	Dreesen, T.D., Johnson, D.H and Henikoff, S. The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes. Mol. Cell Biol. 8 (1988) 5206–5215. [DOI] [PMID: 3149712]
3.	Tearle, R.G., Belote, J.M., McKeown, M., Baker, B.S. and Howells, A.J. Cloning and characterization of the scarlet gene of Drosophila melanogaster. Genetics 122 (1989) 595–606. [PMID: 2503416]
4.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
5.	Mackenzie, S.M., Brooker, M.R., Gill, T.R., Cox, G.B., Howells, A.J. and Ewart, G.D. Mutations in the white gene of Drosophila melanogaster affecting ABC transporters that determine eye colouration. Biochim. Biophys. Acta 1419 (1999) 173–185. [PMID: 10407069]

[EC 7.6.2.6 created 2000 as EC 3.6.3.37, transferred 2018 to EC 7.6.2.6]

7.6.2.7

Accepted name:

ABC-type taurine transporter

Reaction:

ATP + H₂O + taurine-[taurine-binding protein]_{[side 1]} = ADP + phosphate + taurine_{[side 2]} + [taurine-binding protein]_{[side 1]}

Other name(s):

tauABC (gene names); taurine ABC transporter; taurine-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, taurine-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of taurine. In Escherichia coli the enzyme imports a range of sulfonates (including taurine) that can be used as a source of sulfur.

Links to other databases:

References:

van der Ploeg, J.R., Weiss, M.A., Saller, E., Nashimoto, H., Saito, N., Kertesz, M.A. and Leisinger, T. Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source. J. Bacteriol. 178 (1996) 5438–5446. [DOI] [PMID: 8808933]

[EC 7.6.2.7 created 2000 as EC 3.6.3.36, transferred 2018 to EC 7.6.2.7]

7.6.2.8

Accepted name:

ABC-type vitamin B₁₂ transporter

Reaction:

ATP + H₂O + vitamin B₁₂-[cobalamin-binding protein]_{[side 1]} = ADP + phosphate + vitamin B₁₂_{[side 2]} + [cobalamin-binding protein]_{[side 1]}

Other name(s):

BtuCDF; vitamin B₁₂ ABC transporter; vitamin B₁₂-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, vitamin B₁₂-importing)

Comments:

Links to other databases:

References:

1.	Friedrich, M.J., de Veaux, L.C. and Kadner, R.J. Nucleotide sequence of the btuCED genes involved in vitamin B₁₂ transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems. J. Bacteriol. 167 (1986) 928–934. [DOI] [PMID: 3528129]
2.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.6.2.8 created 2000 as EC 3.6.3.33, transferred 2018 to EC 7.6.2.8]

7.6.2.9

Accepted name:

ABC-type quaternary amine transporter

Reaction:

ATP + H₂O + quaternary amine-[quaternary amine-binding protein]_{[side 1]} = ADP + phosphate + quaternary amine_{[side 2]} + [quaternary amine-binding protein]_{[side 1]}

Other name(s):

glycine betaine ABC transporter; ProVWX; quaternary-amine ABC transporter; quaternary-amine-transporting ATPase (ambiguous)

Systematic name:

ATP phosphohydrolase (ABC-type, quaternary-amine-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of quaternary amine derivatives.

Links to other databases:

References:

1.	Kuan, G., Dassa, E., Saurin, N., Hofnung, M. and Saier, M.H., Jr. Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases. Res. Microbiol. 146 (1995) 271–278. [DOI] [PMID: 7569321]
2.	Kempf, B., Gade, J. and Bremer, E. Lipoprotein from the osmoregulated ABC transport system OpuA of Bacillus subtilis: purification of the glycine betaine binding protein and characterization of a functional lipidless mutant. J. Bacteriol. 179 (1997) 6213–6220. [DOI] [PMID: 9335265]
3.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]

[EC 7.6.2.9 created 2000 as EC 3.6.3.32, transferred 2018 to EC 7.6.2.9]

7.6.2.10

Accepted name:

ABC-type glycerol 3-phosphate transporter

Reaction:

ATP + H₂O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein]_{[side 1]} = ADP + phosphate + sn-glycerol 3-phosphate_{[side 2]} + [glycerol 3-phosphate-binding protein]_{[side 1]}

Other name(s):

glycerol-3-phosphate ABC transporter; glycerol-3-phosphate-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, sn-glycerol 3-phosphate-importing)

Comments:

An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.

Links to other databases:

References:

1.	Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. Adv. Microb. Physiol. 40 (1998) 81–136. [PMID: 9889977]
2.	Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
3.	Bahl, H., Burchhardt, G. and Wienecke, A. Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes homologous to Escherichia coli genes encoding integral membrane components of binding-protein-dependent transport systems. FEMS Microbiol. Lett. 65 (1991) 83–87. [PMID: 1874408]

[EC 7.6.2.10 created 2000 as EC 3.6.3.20, transferred 2018 to EC 7.6.2.10]

7.6.2.11

Accepted name:

ABC-type polyamine transporter

Reaction:

ATP + H₂O + polyamine-[polyamine-binding protein]_{[side 1]} = ADP + phosphate + polyamine_{[side 2]} + [polyamine-binding protein]_{[side 1]}

Other name(s):

polyamine ABC transporter; polyamine-transporting ATPase

Systematic name:

ATP phosphohydrolase (ABC-type, polyamine-importing)

Comments:

Links to other databases: