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Your query returned 13 entries. Printable version
EC | 1.16.1.9 | ||||||||||||||
Accepted name: | ferric-chelate reductase (NADPH) | ||||||||||||||
Reaction: | 2 Fe(II)-siderophore + NADP+ + H+ = 2 Fe(III)-siderophore + NADPH | ||||||||||||||
Other name(s): | ferric chelate reductase (ambiguous); iron chelate reductase (ambiguous); NADPH:Fe3+-EDTA reductase; NADPH-dependent ferric reductase; yqjH (gene name); Fe(II):NADP+ oxidoreductase | ||||||||||||||
Systematic name: | Fe(II)-siderophore:NADP+ oxidoreductase | ||||||||||||||
Comments: | Contains FAD. The enzyme, which is widespread among bacteria, catalyses the reduction of ferric iron bound to a variety of iron chelators (siderophores), including ferric triscatecholates and ferric dicitrate, resulting in the release of ferrous iron. The enzyme from the bacterium Escherichia coli has the highest efficiency with the hydrolysed ferric enterobactin complex ferric N-(2,3-dihydroxybenzoyl)-L-serine [3]. cf. EC 1.16.1.7, ferric-chelate reductase (NADH) and EC 1.16.1.10, ferric-chelate reductase [NAD(P)H]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 120720-17-4 | ||||||||||||||
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EC | 2.4.1.369 | ||||||||||||||
Accepted name: | enterobactin C-glucosyltransferase | ||||||||||||||
Reaction: | (1) UDP-α-D-glucose + enterobactin = UDP + monoglucosyl-enterobactin (2) UDP-α-D-glucose + monoglucosyl-enterobactin = UDP + diglucosyl-enterobactin (3) UDP-α-D-glucose + diglucosyl-enterobactin = UDP + triglucosyl-enterobactin |
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Glossary: | enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-3→1(3)-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = salmochelin S4 = di-C-glucosyl-enterobactin triglucosyl-enterobactin = N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = tri-C-glucosyl-enterobactin = salmochelin TGE |
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Other name(s): | iroB (gene name) | ||||||||||||||
Systematic name: | UDP-α-D-glucose:enterobactin 5′-C-β-D-glucosyltransferase (configuration-inverting) | ||||||||||||||
Comments: | The enzyme, found in pathogenic strains of the bacteria Escherichia coli and Salmonella enterica, catalyses the transfer of glucosyl groups to C-5 of one, two, or three of the 2,3-hydroxybenzoyl units of the siderophore enterobactin, forming C-glucosylated derivatives known as salmochelins. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 2.7.7.58 | ||||||||||||||
Transferred entry: | (2,3-dihydroxybenzoyl)adenylate synthase. Now included in EC 6.2.1.71, 2,3-dihydroxybenzoate[aryl-carrier protein] ligase | ||||||||||||||
EC | 3.1.1.107 | ||||||||||||||
Accepted name: | apo-salmochelin esterase | ||||||||||||||
Reaction: | (1) enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer (2) triglucosyl-enterobactin + H2O = triglucosyl-(2,3-dihydroxybenzoylserine)3 (3) diglucosyl-enterobactin + H2O = diglucosyl-(2,3-dihydroxybenzoylserine)3 (4) monoglucosyl-enterobactin + H2O = monoglucosyl-(2,3-dihydroxybenzoylserine)3 |
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For diagram of glucosyl enterobactin biosynthesis, click here | |||||||||||||||
Glossary: | N-(2,3-dihydroxybenzoyl)-L-serine trimer = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(2,3-dihydroxybenzoyl)-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine diglucosyl-(2,3-dihydroxybenzoylserine)3 = salmochelin S2 = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl]-N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-3→1(3)-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = salmochelin S4 = di-C-glucosyl-enterobactin triglucosyl-enterobactin = N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-(3→1(3))-lactone = tri-C-glucosyl-enterobactin = salmochelin TGE |
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Other name(s): | iroE (gene name) | ||||||||||||||
Systematic name: | apo-salmochelin esterase | ||||||||||||||
Comments: | This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. Unlike EC 3.1.1.108, iron(III)-enterobactin esterase, which acts only on enterobactin, this enzyme can also act on the C-glucosylated forms known as salmochelins. Unlike EC 3.1.1.109, iron(III)-salmochelin esterase (IroD), IroE prefers apo siderophores as substrates, and is assumed to act before the siderophores are exported out of the cell. It hydrolyses the trilactone only once, producing linearized trimers. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 3.1.1.108 | ||||||||||||||
Accepted name: | iron(III)-enterobactin esterase | ||||||||||||||
Reaction: | iron(III)-enterobactin + 3 H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine complex + 2 N-(2,3-dihydroxybenzoyl)-L-serine (overall reaction) (1a) iron(III)-enterobactin + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine trimer complex (1b) iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine trimer complex + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine dimer complex + N-(2,3-dihydroxybenzoyl)-L-serine (1c) iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine dimer complex + H2O = iron(III)-N-(2,3-dihydroxybenzoyl)-L-serine complex + N-(2,3-dihydroxybenzoyl)-L-serine |
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Other name(s): | fes (gene name); pfeE (gene name); enterochelin hydrolase; enterochelin esterase; ferric enterobactin esterase | ||||||||||||||
Systematic name: | iron(III)-enterobactin hydrolase | ||||||||||||||
Comments: | The enzyme, isolated from the bacterium Escherichia coli, allows the bacterium to grow in limited iron conditions. It can also act on enterobactin (with no complexed iron) and the aluminium(III) analogue of iron(III)-enterobactin. The trimer formed is further hydrolysed to form the dimer and the monomer. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
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EC | 3.1.1.109 | ||||||||||||||
Accepted name: | iron(III)-salmochelin esterase | ||||||||||||||
Reaction: | (1) iron(III)-[diglucosyl-enterobactin] complex + H2O = iron(III)-[salmochelin S2] complex (2) iron(III)-[monoglucosyl-enterobactin] complex + H2O = iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)3] complex (3) iron(III)-[salmochelin S2] complex + H2O = iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)2] complex + N-(2,3-dihydroxybenzoyl)-L-serine (4) iron(III)-[salmochelin S2] complex + H2O = iron(III)-[salmochelin S1] complex + salmochelin SX (5) iron(III)-[monoglucosyl-(2,3-dihydroxybenzoylserine)3] complex + H2O = iron(III)-[salmochelin S1] complex + N-(2,3-dihydroxybenzoyl)-L-serine (6) iron(III)-[diglucosyl-(2,3-dihydroxybenzoylserine)2] complex + H2O = iron(III)-[salmochelin SX] complex + salmochelin SX |
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Glossary: | salmochelin S2 = O-3-{O-3-[N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl]-N-(2,3-dihydroxybenzoyl)-C-5-deoxy-β-D-glucosyl-L-seryl}-N-(2,3-dihydroxybenzoyl)-L-serine salmochelin S1 = O-3-[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine monoglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = mono-C-glucosyl-enterobactin = salmochelin MGE diglucosyl-enterobactin = N-(2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-O-[N-(5-β-D-glucopyranosyl-2,3-dihydroxybenzoyl)-L-seryl]-L-seryl]-L-serine-[3→1(3)]-lactone = salmochelin S4 = di-C-glucosyl-enterobactin salmochelin SX = N-(C-5-deoxy-β-D-glucosyl-2,3-dihydroxybenzoyl)-L-serine |
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Other name(s): | iroD (gene name); ferric-salmochelin esterase | ||||||||||||||
Systematic name: | iron(III)-salmochelin complex hydrolase | ||||||||||||||
Comments: | This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. The enzyme acts on iron(III)-bound enterobactin and C-glucosylated derivatives known as salmochelins. Unlike EC 3.1.1.107, apo-salmochelin esterase (IroE), IroD prefers iron(III)-bound siderophores as substrates, and is assumed to act after the iron-siderophore complexes are imported into the cell. It catalyses several hydrolytic reactions, producing a mixture of iron(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] complex and salmochelin SX. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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EC | 3.3.2.1 | ||||||||||||||
Accepted name: | isochorismatase | ||||||||||||||
Reaction: | isochorismate + H2O = (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + pyruvate | ||||||||||||||
For diagram of shikimate and chorismate biosynthesis, click here | |||||||||||||||
Glossary: | isochorismate = (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylate | ||||||||||||||
Other name(s): | 2,3-dihydro-2,3-dihydroxybenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoate synthase; 2,3-dihydroxy-2,3-dihydrobenzoic synthase | ||||||||||||||
Systematic name: | isochorismate pyruvate-hydrolase | ||||||||||||||
Comments: | The enzyme is involved in the biosynthesis of several siderophores, such as 2,3-dihydroxybenzoylglycine, enterobactin, bacillibactin, and vibriobactin. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-64-5 | ||||||||||||||
References: |
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EC | 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 | 5.4.4.2 | ||||||||||||||
Accepted name: | isochorismate synthase | ||||||||||||||
Reaction: | chorismate = isochorismate | ||||||||||||||
For diagram of shikimate and chorismate biosynthesis, click here | |||||||||||||||
Other name(s): | MenF | ||||||||||||||
Systematic name: | isochorismate hydroxymutase | ||||||||||||||
Comments: | Requires Mg2+. The reaction is reversible. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-53-9 | ||||||||||||||
References: |
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EC | 6.2.1.71 | ||||||||||||||
Accepted name: | 2,3-dihydroxybenzoate—[aryl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + 2,3-dihydroxybenzoate + holo-[aryl-carrier protein] = AMP + diphosphate + 2,3-dihydroxybenzoyl-[aryl-carrier protein] (overall reaction) (1a) ATP + 2,3-dihydroxybenzoate = diphosphate + (2,3-dihydroxybenzoyl)adenylate (1b) (2,3-dihydroxybenzoyl)adenylate + holo-[aryl-carrier protein] = AMP + 2,3-dihydroxybenzoyl-[aryl-carrier protein] |
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Other name(s): | entE (gene name); vibE (gene name); dhbE (gene name); angE (gene name) | ||||||||||||||
Systematic name: | 2,3-dihydroxybenzoate:[aryl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of 2,3-dihydroxybenzoate to (2,3-dihydroxybenzoyl)adenylate, followed by the transfer the activated compound to the free thiol of a phosphopantetheine arm of an aryl-carrier protein domain of a specific non-ribosomal peptide synthase. For example, the EntE enzyme of Escherichia coli is part of the enterobactin synthase complex, the VibE enzyme of Vibrio cholerae is part of the vibriobactin synthase complex, and the DhbE enzyme of Bacillus subtilis is part of the bacillibactin synthase complex. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
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EC | 6.2.1.72 | ||||||||||||||
Accepted name: | L-serine—[L-seryl-carrier protein] ligase | ||||||||||||||
Reaction: | ATP + L-serine + holo-[L-seryl-carrier protein] = AMP + diphosphate + L-seryl-[L-seryl-carrier protein] (overall reaction) (1a) ATP + L-serine = diphosphate + (L-seryl)adenylate (1b) (L-seryl)adenylate + holo-[L-seryl-carrier protein] = AMP + L-seryl-[L-seryl-carrier protein] |
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Other name(s): | entF (gene name); zmaJ (gene name); gdnB (gene name); serine-activating enzyme | ||||||||||||||
Systematic name: | L-serine:[L-seryl-carrier protein] ligase (AMP-forming) | ||||||||||||||
Comments: | The adenylation domain of the enzyme catalyses the activation of L-serine to (L-seryl)adenylate, followed by the transfer of the activated compound to the free thiol of a phosphopantetheine arm of a peptidyl-carrier protein domain. The peptidyl-carrier protein domain may be part of the same protein, or of a different protein. This activity is often found as part of a larger non-ribosomal peptide synthase. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||||||||
References: |
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EC | 6.3.2.14 | ||||||||||||||
Accepted name: | enterobactin synthase | ||||||||||||||
Reaction: | 6 ATP + 3 2,3-dihydroxybenzoate + 3 L-serine = enterobactin + 6 AMP + 6 diphosphate | ||||||||||||||
For diagram of enterobactin biosynthesis, click here | |||||||||||||||
Other name(s): | N-(2,3-dihydroxybenzoyl)-serine synthetase; 2,3-dihydroxybenzoylserine synthetase; 2,3-dihydroxybenzoate—serine ligase | ||||||||||||||
Systematic name: | 2,3-dihydroxybenzoate:L-serine ligase | ||||||||||||||
Comments: | This enzyme complex catalyses the conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to form the siderophore enterobactin. In Escherichia coli the complex is formed by EntB (an aryl carrier protein that has to be activated by 4′-phosphopantetheine), EntD (a phosphopantetheinyl transferase that activates EntB), EntE (catalyses the ATP-dependent condensation of 2,3-dihydroxybenzoate and holo-EntB to form the covalently arylated form of EntB), and EntF (a four domain protein that catalyses the activation of L-serine by ATP, the condensation of the activated L-serine with the activated 2,3-dihydroxybenzoate, and the trimerization of three such moieties to a single enterobactin molecule). | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37318-63-1 | ||||||||||||||
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EC | 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: | 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 Fe3+-enterobactin complexes. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||||||||
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