The Enzyme Database

Displaying entries 51-99 of 99.

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EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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-) = MoO42-
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 7.3.2.7     
Accepted name: arsenite-transporting ATPase
Reaction: ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
Other name(s): arsAB (gene names)
Systematic name: ATP phosphohydrolase (arsenite-exporting)
Comments: This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the ’channel’ part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Silver, S., Misra, T.K. and Laddaga, R.A. DNA sequence analysis of bacterial toxic heavy metal resistance. Biol. Trace Elem. Res. 21 (1989) 145–163. [PMID: 2484581]
2.  Rosen, B.P., Weigel, U., Monticello, R.A. and Edwards, B.P. Molecular analysis of an anion pump: purification of the ArsC protein. Arch. Biochem. Biophys. 284 (1991) 381–385. [DOI] [PMID: 1703401]
3.  Bruhn, D.F., Li, J., Silver, S., Roberto, F. and Rosen, B.P. The arsenical resistance operon of IncN plasmid R46. FEMS Microbiol. Lett. 139 (1996) 149–153. [PMID: 8674982]
4.  Zhou, T., Rosen, B.P. and Gatti, D.L. Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 921–924. [PMID: 10089335]
[EC 7.3.2.7 created 2000 as EC 3.6.3.16, transferred 2019 to EC 7.3.2.7]
 
 
EC 7.4.2.1     
Accepted name: ABC-type polar-amino-acid transporter
Reaction: ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1] = ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
Glossary: nopaline = N-{(1R)-1-carboxy-4-[(diaminomethylene)amino]butyl}-L-glutamate
Other name(s): histidine permease; polar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, polar-amino-acid-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 polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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.  Nikaido, K., Liu, P.Q. and Ferro-Luzzi Ames, G. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubilization, dimerization , and ATPase activity. J. Biol. Chem. 272 (1997) 27745–27752. [DOI] [PMID: 9346917]
3.  Walshaw, D.L., Lowthorpe, S., East, A. and Poole, P.S. Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity. FEBS Lett. 414 (1997) 397–401. [DOI] [PMID: 9315727]
4.  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 7.4.2.1 created 2000 as EC 3.6.3.21, transferred 2018 to EC 7.4.2.1]
 
 
EC 7.4.2.2     
Accepted name: ABC-type nonpolar-amino-acid transporter
Reaction: ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1] = ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
Other name(s): nonpolar-amino-acid-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, nonpolar-amino-acid-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. This entry comprises enzymes that import Leu, Ile and Val.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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.
[EC 7.4.2.2 created 2000 as EC 3.6.3.22, transferred 2018 to EC 7.4.2.2]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: 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 yeast enzyme that exports the α-factor sex pheromone.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 7.4.2.10     
Accepted name: ABC-type glutathione transporter
Reaction: ATP + H2O + glutathione-[glutathione-binding protein][side 1] = ADP + phosphate + glutathione[side 2] + [glutathione-binding protein][side 1]
Other name(s): glutathione transporting ATPase; glutathione ABC transporter; gsiACD (gene names)
Systematic name: ATP phosphohydrolase (ABC-type,glutathione-importing)
Comments: A prokaryotic 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 the bacterium Escherichia coli is a heterotrimeric complex that interacts with an extracytoplasmic substrate binding protein to mediate the uptake of glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Suzuki, H., Koyanagi, T., Izuka, S., Onishi, A. and Kumagai, H. The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J. Bacteriol. 187 (2005) 5861–5867. [PMID: 16109926]
2.  Moussatova, A., Kandt, C., O'Mara, M.L. and Tieleman, D.P. ATP-binding cassette transporters in Escherichia coli. Biochim. Biophys. Acta 1778 (2008) 1757–1771. [PMID: 18634750]
[EC 7.4.2.10 created 2019]
 
 
EC 7.4.2.11     
Accepted name: ABC-type methionine transporter
Reaction: (1) ATP + H2O + L-methionine-[methionine-binding protein][side 1] = ADP + phosphate + L-methionine[side 2] + [methionine-binding protein][side 1]
(2) ATP + H2O + D-methionine-[methionine-binding protein][side 1] = ADP + phosphate + D-methionine[side 2] + [methionine-binding protein][side 1]
Other name(s): methionine transporting ATPase; methionine ABC transporter; metNIQ (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, methionine-importing)
Comments: ABC-type (ATP-binding cassette-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 functions to import methionine. The enzyme from Escherichia coli K-12 mediates the high affinity transport of both L- and D-methionine, as well as methionine-S-oxide and N-acetyl-DL-methionine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Merlin, C., Gardiner, G., Durand, S. and Masters, M. The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ). J. Bacteriol. 184 (2002) 5513–5517. [PMID: 12218041]
2.  Zhang, Z., Feige, J.N., Chang, A.B., Anderson, I.J., Brodianski, V.M., Vitreschak, A.G., Gelfand, M.S. and Saier, M.H., Jr. A transporter of Escherichia coli specific for L- and D-methionine is the prototype for a new family within the ABC superfamily. Arch. Microbiol. 180 (2003) 88–100. [PMID: 12819857]
3.  Moussatova, A., Kandt, C., O'Mara, M.L. and Tieleman, D.P. ATP-binding cassette transporters in Escherichia coli. Biochim. Biophys. Acta 1778 (2008) 1757–1771. [PMID: 18634750]
[EC 7.4.2.11 created 2019]
 
 
EC 7.4.2.12     
Accepted name: ABC-type cystine transporter
Reaction: (1) ATP + H2O + L-cystine-[cystine-binding protein][side 1] = ADP + phosphate + L-cystine[side 2] + [cystine-binding protein][side 1]
(2) ATP + H2O + D-cystine-[cystine-binding protein][side 1] = ADP + phosphate + D-cystine[side 2] + [cystine-binding protein][side 1]
Other name(s): cystine transporting ATPase; cystine ABC transporter
Systematic name: ATP phosphohydrolase (ABC-type, cystine-importing)
Comments: ABC-type (ATP-binding cassette-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 import of trace cystine. The enzyme from Escherichia coli K-12 can import both isomers of cystine and a variety of related molecules including djenkolate, lanthionine, diaminopimelate and homocystine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Berger, E.A. and Heppel, L.A. A binding protein involved in the transport of cystine and diaminopimelic acid in Escherichia coli. J. Biol. Chem. 247 (1972) 7684–7694. [PMID: 4564569]
2.  Chonoles Imlay, K.R., Korshunov, S. and Imlay, J.A. Physiological roles and adverse effects of the two cystine importers of Escherichia coli. J. Bacteriol. 197 (2015) 3629–3644. [PMID: 26350134]
[EC 7.4.2.12 created 2019]
 
 
EC 7.4.2.13     
Accepted name: ABC-type tyrosine transporter
Reaction: ATP + H2O + L-tyrosinyl-[tyrosine-binding protein][side 1] = ADP + phosphate + L-tyrosine[side 2] + [tyrosine-binding protein][side 1]
Systematic name: ATP phosphohydrolase (ABC-type, L-tyrosine-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 Clostridioides, interacts with an extracytoplasmic substrate binding lipoprotein and mediates the import of L-tyrosine. L-phenylalanine is also tranported however with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Steglich, M., Hofmann, J.D., Helmecke, J., Sikorski, J., Sproer, C., Riedel, T., Bunk, B., Overmann, J., Neumann-Schaal, M. and Nubel, U. Convergent loss of ABC transporter genes from Clostridioides difficile genomes Is associated with impaired tyrosine uptake and p-cresol production. Front. Microbiol. 9:901 (2018). [PMID: 29867812]
[EC 7.4.2.13 created 2019]
 
 
EC 7.4.2.14     
Accepted name: ABC-type antigen peptide transporter
Reaction: ATP + H2O + antigen peptide[side 1] = ADP + phosphate + antigen peptide[side 2]
Other name(s): TAP1 (gene name); TAP2 (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, antigen 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. Does not undergo phosphorylation during the transport process. This entry describes vertebrate transporters involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with major histocompatibility complex (MHC) class I molecules. The substrates are generated mainly from degradation of cytosolic proteins by the proteasome.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bahram, S., Arnold, D., Bresnahan, M., Strominger, J.L. and Spies, T. Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region. Proc. Natl. Acad. Sci. USA 88 (1991) 10094–10098. [DOI] [PMID: 1946428]
2.  Momburg, F., Roelse, J., Howard, J.C., Butcher, G.W., Hammerling, G.J. and Neefjes, J.J. Selectivity of MHC-encoded peptide transporters from human, mouse and rat. Nature 367 (1994) 648–651. [DOI] [PMID: 8107849]
3.  Nijenhuis, M. and Hammerling, G.J. Multiple regions of the transporter associated with antigen processing (TAP) contribute to its peptide binding site. J. Immunol. 157 (1996) 5467–5477. [PMID: 8955196]
[EC 7.4.2.14 created 2021]
 
 
EC 7.5.2.1     
Accepted name: ABC-type maltose transporter
Reaction: ATP + H2O + maltose-[maltose-binding protein][side 1] = ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1]
Other name(s): maltose ABC transporter; maltose-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, maltose-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 maltose and maltose oligosaccharides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67–113. [DOI] [PMID: 1282354]
2.  Dassa, E. and Muir, S. Membrane topology of MalG, an inner membrane protein from the maltose transport system of Escherichia coli. Mol. Microbiol. 7 (1993) 29–38. [DOI] [PMID: 8437518]
3.  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]
4.  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]
5.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.5.2.1 created 2000 as EC 3.6.3.19, transferred 2018 to EC 7.5.2.1]
 
 
EC 7.5.2.2     
Accepted name: ABC-type oligosaccharide transporter
Reaction: ATP + H2O + oligosaccharide-[oligosaccharide-binding protein][side 1] = ADP + phosphate + oligosaccharide[side 2] + [oligosaccharide-binding protein][side 1]
Other name(s): oligosaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, oligosaccharide-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 lactose, melibiose and raffinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67–113. [DOI] [PMID: 1282354]
2.  Williams, S.G., Greenwood, J.A. and Jones, C.W. Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and β-galactosidase in Agrobacterium radiobacter. Mol. Microbiol. 6 (1992) 1755–1768. [DOI] [PMID: 1630315]
3.  Tam, R. and Saier, M.H., Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57 (1993) 320–346. [PMID: 8336670]
4.  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]
5.  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 7.5.2.2 created 2000 as EC 3.6.3.18, transferred 2018 to EC 7.5.2.2]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: 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 enzyme found in Gram-positive bacteria that exports teichoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 7.5.2.7     
Accepted name: ABC-type D-ribose transporter
Reaction: ATP + H2O + D-ribose-[ribose-binding protein][side 1] = ADP + phosphate + D-ribose[side 2] + [ribose-binding protein][side 1]
Other name(s): D-ribose transporting ATPase; D-ribose ABC transporter; rbsACB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-ribose-importing)
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 high affinity uptake of D-ribose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bell, A.W., Buckel, S.D., Groarke, J.M., Hope, J.N., Kingsley, D.H. and Hermodson, M.A. The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12. J. Biol. Chem. 261 (1986) 7652–7658. [PMID: 3011793]
2.  Clifton, M.C., Simon, M.J., Erramilli, S.K., Zhang, H., Zaitseva, J., Hermodson, M.A. and Stauffacher, C.V. In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes. J. Biol. Chem. 290 (2015) 5555–5565. [PMID: 25533465]
[EC 7.5.2.7 created 2019]
 
 
EC 7.5.2.8     
Accepted name: ABC-type D-allose transporter
Reaction: ATP + H2O + D-allose-[allose-binding protein][side 1] = ADP + phosphate + D-allose[side 2] + [allose-binding protein][side 1]
Other name(s): D-allose transporting ATPase; D-allose ABC transporter; alsBAC (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-allose-importing)
Comments: 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 the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of D-allose, which can be used by the bacterium as a sole carbon source.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, C., Song, S. and Park, C. The D-allose operon of Escherichia coli K-12. J. Bacteriol. 179 (1997) 7631–7637. [PMID: 9401019]
[EC 7.5.2.8 created 2019]
 
 
EC 7.5.2.9     
Accepted name: ABC-type D-galactofuranose transporter
Reaction: ATP + H2O + D-galactofuranose-[galactofuranose-binding protein][side 1] = ADP + phosphate + D-galactofuranose[side 2] + [galactofuranose-binding protein][side 1]
Other name(s): D-galactofuranose transporting ATPase; D-galactofuranose ABC transporter
Systematic name: ATP phosphohydrolase (ABC-type, D-galactofuranose-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. The enzyme from Escherichai coli interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactofuranose. The periplasmic binding protein exhibits selective binding of D-galactofuranose over D-galactopyranose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Horler, R.S., Muller, A., Williamson, D.C., Potts, J.R., Wilson, K.S. and Thomas, G.H. Furanose-specific sugar transport: characterization of a bacterial galactofuranose-binding protein. J. Biol. Chem. 284 (2009) 31156–31163. [PMID: 19744923]
[EC 7.5.2.9 created 2019]
 
 
EC 7.5.2.10     
Accepted name: ABC-type D-xylose transporter
Reaction: ATP + H2O + D-xylose-[xylose-binding protein][side 1] = ADP + phosphate + D-xylose[side 2] + [xylose-binding protein][side 1]
Other name(s): D-xylose transporting ATPase; D-xylose ABC transporter; xylFGH (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-xylose-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 high affinity uptake of D-xylose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Song, S. and Park, C. Organization and regulation of the D-xylose operons in Escherichia coli K-12: XylR acts as a transcriptional activator. J. Bacteriol. 179 (1997) 7025–7032. [PMID: 9371449]
2.  Linton, K.J. and Higgins, C.F. The Escherichia coli ATP-binding cassette (ABC) proteins. Mol. Microbiol. 28 (1998) 5–13. [PMID: 9593292]
[EC 7.5.2.10 created 2019]
 
 
EC 7.5.2.11     
Accepted name: ABC-type D-galactose transporter
Reaction: ATP + H2O + D-galactose-[galactose-binding protein][side 1] = ADP + phosphate + D-galactose[side 2] + [galactose-binding protein][side 1]
Other name(s): D-galactose transporting ATPase; D-galactose ABC transporter; mglBAC (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, D-galactose-importing)
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, best characterized from Escherichia coli where it interacts with a periplasmic substrate binding protein and mediates the high affinity uptake of D-galactose and methyl-β-D-galactoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hogg, R.W., Voelker, C. and Von Carlowitz, I. Nucleotide sequence and analysis of the mgl operon of Escherichia coli K12. Mol. Gen. Genet. 229 (1991) 453–459. [PMID: 1719366]
[EC 7.5.2.11 created 2019]
 
 
EC 7.5.2.12     
Accepted name: ABC-type L-arabinose transporter
Reaction: ATP + H2O + L-arabinose-[arabinose-binding protein][side 1] = ADP + phosphate + L-arabinose[side 2] + [arabinose-binding protein][side 1]
Other name(s): L-arabinose transporting ATPase; L-arabinose ABC transporter; araFGH (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, L-arabinose-importing)
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 high-affinity uptake of L-arabinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Scripture, J.B., Voelker, C., Miller, S., O'Donnell, R.T., Polgar, L., Rade, J., Horazdovsky, B.F. and Hogg, R.W. High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products. J. Mol. Biol. 197 (1987) 37–46. [PMID: 2445996]
2.  Horazdovsky, B.F. and Hogg, R.W. Genetic reconstitution of the high-affinity L-arabinose transport system. J. Bacteriol. 171 (1989) 3053–3059. [PMID: 2656640]
[EC 7.5.2.12 created 2019]
 
 
EC 7.5.2.13     
Accepted name: ABC-type D-xylose/L-arabinose transporter
Reaction: (1) ATP + H2O + D-xylose-[xylose-binding protein][side 1] = ADP + phosphate + D-xylose[side 2] + [xylose-binding protein][side 1]
(2) ATP + H2O + L-arabinose-[arabinose-binding protein][side 1] = ADP + phosphate + L-arabinose[side 2] + [arabinose-binding protein][side 1]
Systematic name: ATP phosphohydrolase (ABC-type, D-xylose/L-arabinose-importing)
Comments: ATP-binding cassette (ABC) type transporter with a 10-transmembrane-spanning (TMD) subunit and a single nucleotide binding domain. The enzyme from the archaeon Sulfolobus acidocaldarius interacts with an extracytoplasmic sugar-binding protein and mediates the uptake of of D-xylose and L-arabinose (cf. EC 7.5.2.10, ABC-type D-xylose transporter and EC 7.5.2.12, ABC-type L-arabinose transporter).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wagner, M., Shen, L., Albersmeier, A., van der Kolk, N., Kim, S., Cha, J., Braesen, C., Kalinowski, J., Siebers, B. and Albers, S.-V. Sulfolobus acidocaldarius transports pentoses via a carbohydrate uptake transporter 2 (CUT2)-type ABC transporter and metabolizes them through the aldolase-independent Weimberg pathway. Appl. Environ. Microbiol. 84 (2018) e01273–17. [PMID: 29150511]
[EC 7.5.2.13 created 2019]
 
 
EC 7.5.2.14     
Accepted name: ABC-type homopolymeric O-antigen exporter
Reaction: ATP + a lipid-linked O antigen[cytosol] + H2O = ADP + phosphate + a lipid-linked O antigen[periplasm]
Other name(s): wzm (gene name); wzt (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, homopolymeric O-antigen exporting)
Comments: Unlike heteropolymeric O antigens, which are polymerized in the periplasm by EC 2.4.99.27, O antigen polymerase Wzy, homopolymeric O antigens are polymerized inside the cytoplasm by a progressive transfer of sugar monomers to a growing chain attached to a polyprenyl diphosphate membrane anchor. When the chain reaches its full length it is transported across the cytoplasmic membrane by this ABC-type transporter, which consists of an ATP-binding subunit (Wzt) and an integral membrane protein (Wzm). Wzm proteins are poorly conserved in their primary sequence. Once in the periplasm, the O antigen is ligated to the lipid A-core complex by EC 2.4.99.26, O-antigen ligase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kido, N., Torgov, V.I., Sugiyama, T., Uchiya, K., Sugihara, H., Komatsu, T., Kato, N. and Jann, K. Expression of the O9 polysaccharide of Escherichia coli: sequencing of the E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and evidence for an ATP-binding cassette transport system. J. Bacteriol. 177 (1995) 2178–2187. [DOI] [PMID: 7536735]
2.  Rocchetta, H.L. and Lam, J.S. Identification and functional characterization of an ABC transport system involved in polysaccharide export of A-band lipopolysaccharide in Pseudomonas aeruginosa. J. Bacteriol. 179 (1997) 4713–4724. [DOI] [PMID: 9244257]
3.  Cuthbertson, L., Powers, J. and Whitfield, C. The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a. J. Biol. Chem. 280 (2005) 30310–30319. [DOI] [PMID: 15980069]
4.  Cuthbertson, L., Kimber, M.S. and Whitfield, C. Substrate binding by a bacterial ABC transporter involved in polysaccharide export. Proc. Natl. Acad. Sci. USA 104 (2007) 19529–19534. [DOI] [PMID: 18032609]
5.  Mann, E., Mallette, E., Clarke, B.R., Kimber, M.S. and Whitfield, C. The Klebsiella pneumoniae O12 ATP-binding cassette (ABC) transporter recognizes the terminal residue of its O-antigen polysaccharide substrate. J. Biol. Chem. 291 (2016) 9748–9761. [DOI] [PMID: 26934919]
6.  Mann, E., Kelly, S.D., Al-Abdul-Wahid, M.S., Clarke, B.R., Ovchinnikova, O.G., Liu, B. and Whitfield, C. Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a. J. Biol. Chem. 294 (2019) 14978–14990. [DOI] [PMID: 31416837]
[EC 7.5.2.14 created 2023]
 
 
EC 7.6.2.1     
Accepted name: P-type phospholipid transporter
Reaction: ATP + H2O + phospholipid[side 1] = ADP + phosphate + phospholipid[side 2]
Other name(s): Mg2+-ATPase (ambiguous); flippase (ambiguous); aminophospholipid-transporting ATPase (ambiguous); phospholipid-translocating ATPase (ambiguous); phospholipid-transporting ATPase (ambiguous)
Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)
Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other (‘flippase’).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Morris, M.B., Auland, M.E., Xu, Y.H. and Roufogalis, B.D. Characterization of the Mg2+-ATPase activity of the human erythrocyte membrane. Biochem. Mol. Biol. Int. 31 (1993) 823–832. [PMID: 8136700]
2.  Vermeulen, W.P., Briede, J.J. and Rolofsen, B. Manipulation of the phosphatidylethanolamine pool in the human red cell membrane affects its Mg2+-ATPase activity. Mol. Membr. Biol. 13 (1996) 95–102. [PMID: 8839453]
3.  Suzuki, H., Kamakura, M., Morii, M. and Takeguchi, N. The phospholipid flippase activity of gastric vesicles. J. Biol. Chem. 272 (1997) 10429–10434. [DOI] [PMID: 9099684]
4.  Auland, M.E., Roufogalis, B.D., Devaux, P.F. and Zachowski, A. Reconstitution of ATP-dependent aminophospholipid translocation in proteoliposomes. Proc. Natl. Acad. Sci. USA 91 (1994) 10938–10942. [DOI] [PMID: 7971987]
5.  Alder-Baerens, N., Lisman, Q., Luong, L., Pomorski, T. and Holthuis, J.C. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17 (2006) 1632–1642. [DOI] [PMID: 16452632]
6.  Lopez-Marques, R.L., Poulsen, L.R., Hanisch, S., Meffert, K., Buch-Pedersen, M.J., Jakobsen, M.K., Pomorski, T.G. and Palmgren, M.G. Intracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA α-subunit. Mol. Biol. Cell 21 (2010) 791–801. [DOI] [PMID: 20053675]
7.  Jensen, M.S., Costa, S.R., Duelli, A.S., Andersen, P.A., Poulsen, L.R., Stanchev, L.D., Gourdon, P., Palmgren, M., Günther Pomorski, T. and Lopez-Marques, R.L. Phospholipid flipping involves a central cavity in P4 ATPases. Sci. Rep. 7:17621 (2017). [PMID: 29247234]
[EC 7.6.2.1 created 2000 as EC 3.6.3.1 (EC 3.6.3.13 created 2000, incorporated 2001), transferred 2018 to EC 7.6.2.1]
 
 
EC 7.6.2.2     
Accepted name: ABC-type xenobiotic transporter
Reaction: ATP + H2O + xenobiotic[side 1] = ADP + phosphate + xenobiotic[side 2]
Other name(s): xenobiotic-transporting ATPase; multidrug-resistance protein; MDR protein; P-glycoprotein; pleiotropic-drug-resistance protein; PDR protein; steroid-transporting ATPase; ATP phosphohydrolase (steroid-exporting)
Systematic name: ATP phosphohydrolase (ABC-type, xenobiotic-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 enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione—drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some ’flippase’ activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161–183. [DOI] [PMID: 8725386]
2.  Frijters, C.M., Ottenhoff, R., Van Wijland, M.J., Van Nieuwkerk, C., Groen, A.K. and Oude-Elferink, R.P. Influence of bile salts on hepatic mdr2 P-glycoprotein expression. Adv. Enzyme Regul. 36 (1996) 351–363. [DOI] [PMID: 8869755]
3.  Keppler, D., König, J. and Buchler, M. The canalicular multidrug resistance protein, cMRP/MRP2, a novel conjugate export pump expressed in the apical membrane of hepatocytes. Adv. Enzyme Regul. 37 (1997) 321–333. [DOI] [PMID: 9381978]
4.  Loe, D.W., Deeley, R.G. and Cole, S.P. Characterization of vincristine transport by the Mr 190,000 multidrug resistance protein (MRP): evidence for cotransport with reduced glutathione. Cancer Res. 58 (1998) 5130–5136. [PMID: 9823323]
5.  van Veen, H.W. and Konings, W.N. The ABC family of multidrug transporters in microorganisms. Biochim. Biophys. Acta 1365 (1998) 31–36. [DOI] [PMID: 9693718]
6.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
7.  Prasad, R., De Wergifosse, P., Goffeau, A. and Balzi, E. Molecular cloning and characterization of a novel gene of Candida albicans, CDR1, conferring multiple resistance to drugs and antifungals. Curr. Genet. 27 (1995) 320–329. [PMID: 7614555]
8.  Nagao, K., Taguchi, Y., Arioka, M., Kadokura, H., Takatsuki, A., Yoda, K. and Yamasaki, M. bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily. J. Bacteriol. 177 (1995) 1536–1543. [DOI] [PMID: 7883711]
9.  Mahé, Y., Lemoine, Y. and Kuchler, K. The ATP-binding cassette transporters Pdr5 and Snq2 of Saccharomyces cerevisiae can mediate transport of steroids in vivo. J. Biol. Chem. 271 (1996) 25167–25172. [DOI] [PMID: 8810273]
[EC 7.6.2.2 created 2000 as EC 3.6.3.44 (EC 3.6.3.45 incorporated 2006), modified 2006, transferred 2018 to EC 7.6.2.2]
 
 
EC 7.6.2.3     
Accepted name: ABC-type glutathione-S-conjugate transporter
Reaction: ATP + H2O + glutathione-S-conjugate[side 1] = ADP + phosphate + glutathione-S-conjugate[side 2]
Other name(s): multidrug resistance-associated protein 1; glutathione-S-conjugate-translocating ATPase; MRP; MRP1; ABCC1 (gene name); YBT1 (gene name); YCF1 (gene name)
Systematic name: ATP phosphohydrolase (ABC-type, glutathione-S-conjugate-exporting)
Comments: A eukaryotic ATP-binding cassette (ABC) type transporter that mediates the transport of glutathione-S-conjugates. The mammalian enzyme, which also transports some glucuronides, exports the substrates out of the cell, while plant and fungal transporters export them into the vacuole. Over-expression confers resistance to anticancer drugs by their efficient exportation in glutathione-S-conjugate form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zaman, G.J., Flens, M.J., van Leusden, M.R., de Haas, M., Mulder, H.S., Lankelma, J., Pinedo, H.M., Scheper, R.J., Baas, F., Broxterman, H.J. and et al. The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump. Proc. Natl. Acad. Sci. USA 91 (1994) 8822–8826. [PMID: 7916458]
2.  Lautier, D., Canitrot, Y., Deeley, R.G. and Cole, S.P. Multidrug resistance mediated by the multidrug resistance protein (MRP) gene. Biochem. Pharmacol. 52 (1996) 967–977. [PMID: 8831715]
3.  Li, Z.S., Szczypka, M., Lu, Y.P., Thiele, D.J. and Rea, P.A. The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump. J. Biol. Chem. 271 (1996) 6509–6517. [DOI] [PMID: 8626454]
4.  Lu, Y.P., Li, Z.S. and Rea, P.A. AtMRP1 gene of Arabidopsis encodes a glutathione S-conjugate pump: isolation and functional definition of a plant ATP-binding cassette transporter gene. Proc. Natl. Acad. Sci. USA 94 (1997) 8243–8248. [PMID: 9223346]
5.  Cole, S.P. Multidrug resistance protein 1 (MRP1, ABCC1), a "multitasking" ATP-binding cassette (ABC) transporter. J. Biol. Chem. 289 (2014) 30880–30888. [PMID: 25281745]
6.  Cordente, A.G., Capone, D.L. and Curtin, C.D. Unravelling glutathione conjugate catabolism in Saccharomyces cerevisiae: the role of glutathione/dipeptide transporters and vacuolar function in the release of volatile sulfur compounds 3-mercaptohexan-1-ol and 4-mercapto-4-methylpentan-2-one. Appl. Microbiol. Biotechnol. 99 (2015) 9709–9722. [PMID: 26227410]
[EC 7.6.2.3 created 2018]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: 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 has been described from Gram-negative bacteria and green plants.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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]
 
 
EC 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: 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 cobalamin derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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]
 
 
EC 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: BRENDA, EXPASY, KEGG, MetaCyc
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]
 
 
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, KEGG, MetaCyc
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]
[EC 7.6.2.11 created 2000 as EC 3.6.3.31, transferred 2018 to EC 7.6.2.11]
 
 
EC 7.6.2.12     
Accepted name: ABC-type capsular-polysaccharide transporter
Reaction: ATP + H2O + capsular polysaccharide-[capsular polysaccharide-binding protein][side 1] = ADP + phosphate + capsular polysaccharide[side 2] + [capsular polysaccharide-binding protein][side 1]
Other name(s): capsular-polysaccharide-transporting ATPase
Systematic name: ATP phosphohydrolase (ABC-type, capsular-polysaccharide-exporting)
Comments: ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme that exports capsular polysaccharide in Gram-negative bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fath, M.J. and Kolter, R. ABC transporters: bacterial exporters. Microbiol. Rev. 57 (1993) 995–1017. [PMID: 8302219]
2.  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]
3.  Pigeon, R.P. and Silver, R.P. Analysis of the G93E mutant allele of KpsM, the membrane component of an ABC transporter involved in polysialic acid translocation in Escherichia coli K1. FEMS Microbiol. Lett. 156 (1997) 217–222. [DOI] [PMID: 9513268]
4.  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]
5.  Griffiths, J.K. and Sansom, C.E. The Transporter Factsbook, Academic Press, San Diego, 1998.
[EC 7.6.2.12 created 2000 as EC 3.6.3.38, transferred 2018 to EC 7.6.2.12]
 
 
EC 7.6.2.13     
Accepted name: ABC-type autoinducer-2 transporter
Reaction: ATP + H2O + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran-[AI-2-binding protein][side 1] = ADP + phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran[side 2] + [AI-2-binding protein][side 1]
Glossary: autoinducer-2 = AI-2 = (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran
Other name(s): autoinducer-2 transporting ATPase; autoinducer-2 ABC transporter; LsrACDB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, AI-2 importing)
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 the signalling molecule (2R,4S)-2-methyl-2,3,3,4-tetrahydoxytetrahydrofuran (also known as autoinducer-2).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Taga, M.E., Semmelhack, J.L. and Bassler, B.L. The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium. Mol. Microbiol. 42 (2001) 777–793. [PMID: 11722742]
2.  Xavier, K.B. and Bassler, B.L. Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli. J. Bacteriol. 187 (2005) 238–248. [PMID: 15601708]
[EC 7.6.2.13 created 2019]
 
 
EC 7.6.2.14     
Accepted name: ABC-type aliphatic sulfonate transporter
Reaction: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein][side 1] = ADP + phosphate + aliphatic sulfonate[side 2] + [sulfonate-binding protein][side 1]
Other name(s): aliphatic sulfonate transporting ATPase; alkane sulfonate ABC transporter; aliphatic sulfonate ABC transporter; ssuACB (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, aliphatic sulfonate-importing)
Comments: 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 the bacterium Escherichia coli K-12 interacts with an extracytoplasmic substrate binding protein and imports a broad range of aliphatic sulfonates for use as a source of sulfur.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  van Der Ploeg, J.R., Iwanicka-Nowicka, R., Bykowski, T., Hryniewicz, M.M. and Leisinger, T. The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl. J. Biol. Chem. 274 (1999) 29358–29365. [PMID: 10506196]
2.  Kertesz, M.A. Bacterial transporters for sulfate and organosulfur compounds. Res. Microbiol. 152 (2001) 279–290. [PMID: 11421275]
3.  Davidson, A.L., Dassa, E., Orelle, C. and Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72 (2008) 317–364. [PMID: 18535149]
[EC 7.6.2.14 created 2019]
 
 
EC 7.6.2.15     
Accepted name: ABC-type thiamine transporter
Reaction: ATP + H2O + thiamine-[thiamine-binding protein][side 1] = ADP + phosphate + thiamine[side 2] + [thiamine-binding protein][side 1]
Other name(s): thiamin transporting ATPase; thiamine ABC transporter; thiamin ABC transporter; thiamine transporting ATPase; thiBPQ (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, thiamine-importing)
Comments: 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 bacterium Salmonella typhimurium, is a heterodimeric complex that interacts with an extracytoplasmic substrate binding protein and functions to import thiamine, thiamine monophosphate and thiamine diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Webb, E., Claas, K. and Downs, D. thiBPQ encodes an ABC transporter required for transport of thiamine and thiamine pyrophosphate in Salmonella typhimurium. J. Biol. Chem. 273 (1998) 8946–8950. [PMID: 9535878]
[EC 7.6.2.15 created 2019]
 
 
EC 7.6.2.16     
Accepted name: ABC-type putrescine transporter
Reaction: ATP + H2O + putrescine-[putrescine-binding protein][side 1] = ADP + phosphate + putrescine[side 2] + [putrescine-binding protein][side 1]
Other name(s): putrescine transporting ATPase; putrescine ABC transporter; potFGHI (gene names)
Systematic name: ATP phosphohydrolase (ABC-type, putrescine-importing)
Comments: 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 the bacterium Escherichia coli interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of putrescine. Differs in specificity from EC 7.6.2.11, ABC-type polyamine transporter.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pistocchi, R., Kashiwagi, K., Miyamoto, S., Nukui, E., Sadakata, Y., Kobayashi, H. and Igarashi, K. Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. J. Biol. Chem. 268 (1993) 146–152. [PMID: 8416922]
2.  Terui, Y., Saroj, S.D., Sakamoto, A., Yoshida, T., Higashi, K., Kurihara, S., Suzuki, H., Toida, T., Kashiwagi, K. and Igarashi, K. Properties of putrescine uptake by PotFGHI and PuuP and their physiological significance in Escherichia coli. Amino Acids 46 (2014) 661–670. [PMID: 23719730]
[EC 7.6.2.16 created 2019]
 
 


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