| EC |
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: |
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 imports putrescine and spermidine. In Escherichia coli the enzyme imports spermidine preferentially. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H. and Igarashi, K. Functions of potA and potD proteins in spermidine - preferential uptake system in Escherichia coli. J. Biol. Chem. 268 (1993) 19358–19363. [PMID: 8366082] |
| 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] |
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| [EC 7.6.2.11 created 2000 as EC 3.6.3.31, transferred 2018 to EC 7.6.2.11] |
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