Enzyme Nomenclature

EC 7

EC 7 Translocases

Sections

EC 7.1 Catalysing the translocation of hydrons
EC 7.2 Catalysing the translocation of inorganic cations
EC 7.3 Catalysing the translocation of inorganic anions and their chelates
EC 7.4 Catalysing the translocation of amino acids and peptides
EC 7.5 Catalysing the translocation of carbohydrates and their derivatives
EC 7.6 Catalysing the translocation of other compounds


EC 7.1 Catalysing the translocation of hydrons

EC 7.1.1 Hydron translocation or charge separation linked to oxidoreductase reactions

EC 7.1.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate

EC 7.1.3 Hydron translocation or charge separation linked to oxidoreductase reactions


Contents

EC 7.1.1 Hydron translocation or charge separation linked to oxidoreductase reactions

EC 7.1.1.1 proton-translocating NAD(P)+ transhydrogenase


Entries

EC 7.1.1.1

Accepted name: proton-translocating NAD(P)+ transhydrogenase

Reaction: NADPH + NAD+ + H+[side 1] = NADP+ + NADH + H+[side 2]

Other name(s): pntA (gene name); pntB (gene name); NNT (gene name)

Systematic name: NADPH:NAD+ oxidoreductase (H+-transporting)

Comments: The enzyme is a membrane bound proton-translocating pyridine nucleotide transhydrogenase that couples the reversible reduction of NADP by NADH to an inward proton translocation across the membrane. In the bacterium Escherichia coli the enzyme provides a major source of cytosolic NADPH. Detoxification of reactive oxygen species in mitochondria by glutathione peroxidases depends on NADPH produced by this enzyme.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Clarke, D.M. and Bragg, P.D. Cloning and expression of the transhydrogenase gene of Escherichia coli. J. Bacteriol. 162 (1985) 367-373. [PMID: 3884596]

2. Clarke, D.M. and Bragg, P.D. Purification and properties of reconstitutively active nicotinamide nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 149 (1985) 517-523. [PMID: 3891338]

3. Glavas, N.A., Hou, C. and Bragg, P.D. Involvement of histidine-91 of the β subunit in proton translocation by the pyridine nucleotide transhydrogenase of Escherichia coli. Biochemistry 34 (1995) 7694-7702. [PMID: 7779816]

4. Sauer, U., Canonaco, F., Heri, S., Perrenoud, A. and Fischer, E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613-6619. [PMID: 14660605]

5. Bizouarn, T., Fjellstrom, O., Meuller, J., Axelsson, M., Bergkvist, A., Johansson, C., Goran Karlsson, B. and Rydstrom, J. Proton translocating nicotinamide nucleotide transhydrogenase from E. coli. Mechanism of action deduced from its structural and catalytic properties. Biochim. Biophys. Acta 1457 (2000) 211-228. [PMID: 10773166]

6. White, S.A., Peake, S.J., McSweeney, S., Leonard, G., Cotton, N.P. and Jackson, J.B. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Structure 8 (2000) 1-12. [PMID: 10673423]

7. Johansson, T., Oswald, C., Pedersen, A., Tornroth, S., Okvist, M., Karlsson, B.G., Rydstrom, J. and Krengel, U. X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli. J. Mol. Biol. 352 (2005) 299-312. [PMID: 16083909]

8. Meimaridou, E., Kowalczyk, J., Guasti, L., Hughes, C.R., Wagner, F., Frommolt, P., Nurnberg, P., Mann, N.P., Banerjee, R., Saka, H.N., Chapple, J.P., King, P.J., Clark, A.J. and Metherell, L.A. Mutations in NNT encoding nicotinamide nucleotide transhydrogenase cause familial glucocorticoid deficiency. Nat. Genet. 44 (2012) 740-742. [PMID: 22634753]

[EC 7.1.1.1 created 2015 as EC 1.6.1.5, transferred 2018 to EC 7.1.1.1]

EC 7.1.1.2

Accepted name: NADH:ubiquinone reductase (H+-translocating)

Reaction: NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2]

Other name(s): ubiquinone reductase (ambiguous); type 1 dehydrogenase; complex 1 dehydrogenase; coenzyme Q reductase (ambiguous); complex I (electron transport chain); complex I (mitochondrial electron transport); complex I (NADH:Q1 oxidoreductase); dihydronicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); DPNH-coenzyme Q reductase (ambiguous); DPNH-ubiquinone reductase (ambiguous); mitochondrial electron transport complex 1; mitochondrial electron transport complex I; NADH coenzyme Q1 reductase; NADH-coenzyme Q oxidoreductase (ambiguous); NADH-coenzyme Q reductase (ambiguous); NADH-CoQ oxidoreductase (ambiguous); NADH-CoQ reductase (ambiguous); NADH-ubiquinone reductase (ambiguous); NADH-ubiquinone oxidoreductase (ambiguous); NADH-ubiquinone-1 reductase; reduced nicotinamide adenine dinucleotide-coenzyme Q reductase (ambiguous); NADH:ubiquinone oxidoreductase complex; NADH-Q6 oxidoreductase (ambiguous); electron transfer complex I; NADH2 dehydrogenase (ubiquinone)

Systematic name: NADH:ubiquinone oxidoreductase

Comments: A flavoprotein (FMN) containing iron-sulfur clusters. The complex is present in mitochondria and aerobic bacteria. Breakdown of the complex can release EC 1.6.99.3, NADH dehydrogenase. In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD+ to NADH.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1-70.

2. Herter, S.M., Kortluke, C.M. and Drews, G. Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169 (1998) 98-105. [PMID: 9446680]

3. Hunte, C., Zickermann, V. and Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science 329 (2010) 448-451. [PMID: 20595580]

4. Efremov, R.G., Baradaran, R. and Sazanov, L.A. The architecture of respiratory complex I. Nature 465 (2010) 441-445. [PMID: 20505720]

5. Wikstrom, M. and Hummer, G. Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications. Proc. Natl. Acad. Sci. USA 109 (2012) 4431-4436. [PMID: 22392981]

[EC 7.1.1.2 created 1961 as EC 1.6.5.3, deleted 1965, reinstated 1983, modified 2011, modified 2013, transferred 2018 to EC 7.1.1.2]


Contents

EC 7.1.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate


Entries

EC 7.1.2.1

Accepted name: H+-exporting ATPase

Reaction: ATP + H2O + H+[side 1] = ADP + phosphate + H+[side 2]

Other name(s): proton-translocating ATPase; yeast plasma membrane H+-ATPase; yeast plasma membrane ATPase; ATP phosphohydrolase (ambiguous)

Systematic name: ATP phosphohydrolase (H+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants, and generates an electrochemical potential gradient of protons across the plasma membrane.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Goffeau, A. and Slayman, C. The proton-translocating ATPase of the fungal plasma membrane. Biochim. Biophys. Acta 639 (1981) 197-223. [PMID: 6461354]

2. Serrano, R., Kielland-Brandt, M.C. and Fink, G.R. Yeast plasma membrane ATPase is essential for growth and has homology with (Na++K+)-, K+-and Ca2+-ATPases. Nature 319 (1986) 689-693. [PMID: 3005867]

3. Serrano, R. and Portillo, F. Catalytic and regulatory sites of yeast plasma membrane H+-ATPase studied by directed mutagenesis. Biochim. Biophys. Acta 1018 (1990) 195-199. [PMID: 2144186]

4. Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53-61. [PMID: 2425739]

[EC 7.1.2.1 created 1984 as EC 3.6.1.35, transferred 2000 to EC 3.6.3.6, transferred 2018 to EC 7.1.2.1]

EC 7.1.2.2

Accepted name: H+-transporting two-sector ATPase

Reaction: ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2]

Glossary: In Fo, the "o" refers to oligomycin. F0 is incorrect

Other name(s): ATP synthase; F1-ATPase; FoF1-ATPase; H+-transporting ATPase; mitochondrial ATPase; coupling factors (F0, F1 and CF1); chloroplast ATPase; bacterial Ca2+/Mg2+ ATPase

Systematic name: ATP phosphohydrolase (H+-transporting)

Comments: A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 α- and 3 β-subunits) is connected via the δ-subunit to the membrane sector by several smaller subunits. Within this complex, the γ- and ε-subunits, as well as the 9-12 c subunits rotate by consecutive 120° angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Perlin, D.S., San Francisco, M.J., Slayman, C.W. and Rosen, B.P. H+/ATP stoichiometry of proton pumps from Neurospora crassa and Escherichia coli. Arch. Biochem. Biophys. 248 (1986) 53-61. [PMID: 2425739]

2. Boyer, P.D. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140 (1993) 215-250. [PMID: 8417777]

3. Abrahams, J.P., Leslie, A.G.W., Lutter, R. and Walker, J.F. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 375 (1994) 621-628. [PMID: 8065448]

4. Blair, A., Ngo, L., Park, J., Paulsen, I.T. and Saier, M.H., Jr. Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the FoF1-ATPases of bacteria, chloroplasts and mitochondria. Microbiology 142 (1996) 17-32. [PMID: 8581162]

5. Noji, H., Yasuda, R., Yoshida, M. and Kinosita, K., Jr. Direct observation of the rotation of F1-ATPase. Nature 386 (1997) 299-302. [PMID: 9069291]

6. Turina, P., Samoray, D. and Graber, P. H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes. EMBO J. 22 (2003) 418-426. [PMID: 12554643]

[EC 7.1.2.2 created 1984 as EC 3.6.1.34, transferred 2000 to EC 3.6.3.14, transferred 2018 to EC 7.1.2.2]


Contents

EC 7.1.3 Hydron translocation linked to the hydrolysis of diphosphate


EC 7.1.3.1

Accepted name: H+-exporting diphosphatase

Reaction: diphosphate + H2O + H+[side 1] = 2 phosphate + H+[side 2]

Other name(s): H+-PPase; proton-pumping pyrophosphatase; vacuolar H+-pyrophosphatase; hydrogen-translocating pyrophosphatase; proton-pumping dihosphatase

Systematic name: diphosphate phosphohydrolase (H+-transporting)

Comments: This enzyme, found in plants and fungi, couples the energy from diphosphate hydrolysis to active proton translocation across the tonoplast into the vacuole. The enzyme acts cooperatively with cytosolic soluble diphosphatases to regulate the cytosolic diphosphate level.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Rea, P.A. and Poole, R.J. Chromatographic resolution of H+-translocating pyrophosphatase from H+-translocating ATPase of higher plant tonoplast. Plant Physiol. 81 (1986) 126-129. [PMID: 16664761]

2. Sarafian, V. and Poole, R.J. Purification of an H+-translocating inorganic pyrophosphatase from vacuole membranes of red beet. Plant Physiol. 91 (1989) 34-38. [PMID: 16667022]

3. Hedrich, R., Kurkdjian, A., Guern, J. and Flugge, U.I. Comparative studies on the electrical properties of the H+ translocating ATPase and pyrophosphatase of the vacuolar-lysosomal compartment. EMBO J. 8 (1989) 2835-2841. [PMID: 2479537]

4. Segami, S., Tomoyama, T., Sakamoto, S., Gunji, S., Fukuda, M., Kinoshita, S., Mitsuda, N., Ferjani, A. and Maeshima, M. Vacuolar H+-pyrophosphatase and cytosolic soluble pyrophosphatases cooperatively regulate pyrophosphate levels in Arabidopsis thaliana, Plant Cell 30 (2018) 1040-1061. [PMID: 29691313]

[EC 7.1.3.1 created 2018]


EC 7.2 Catalysing the translocation of inorganic cations

EC 7.2.1 Linked to oxidoreductase reactions

EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate

EC 7.2.4 Linked to decarboxylation


Contents

EC 7.2.1 Linked to oxidoreductase reactions


Entries

EC 7.2.1.1

Accepted name: NADH:ubiquinone reductase (Na+-transporting)

Reaction: NADH + H+ + ubiquinone + n Na+[side 1] = NAD+ + ubiquinol + n Na+[side 2]

Other name(s): Na+-translocating NADH-quinone reductase; (Na+-NQR)

Systematic name: NADH:ubiquinone oxidoreductase (Na+-translocating)

Comments: An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Beattie, P., Tan, K., Bourne, R.M., Leach, D., Rich, P.R. and Ward, F.B. Cloning and sequencing of four structural genes for the Na+-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus. FEBS Lett. 356 (1994) 333-338. [PMID: 7805867]

2. Nakayama, Y., Hayashi, M. and Unemoto, T. Identification of six subunits constituting Na+-translocating NADH-quinone reductase from the marine Vibrio alginolyticus. FEBS Lett. 422 (1998) 240-242. [PMID: 9490015]

3. Bogachev, A.V., Bertsova, Y.V., Barquera, B. and Verkhovsky, M.I. Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi. Biochemistry 40 (2001) 7318-7323. [PMID: 11401580]

4. Barquera, B., Hellwig, P., Zhou, W., Morgan, J.E., Hase, C.C., Gosink, K.K., Nilges, M., Bruesehoff, P.J., Roth, A., Lancaster, C.R. and Gennis, R.B. Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Biochemistry 41 (2002) 3781-3789. [PMID: 11888296]

5. Barquera, B., Nilges, M.J., Morgan, J.E., Ramirez-Silva, L., Zhou, W. and Gennis, R.B. Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Biochemistry 43 (2004) 12322-12330. [PMID: 15379571]

[EC 7.2.1.1 created 2011 as EC 1.6.5.8, transferred 2018 to EC 7.2.1.1]

EC 7.2.1.2

Accepted name: ferredoxin—NAD+ oxidoreductase (Na+-transporting)

Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + NAD+ + H+ + Na+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + NADH + Na+[side 2]

Other name(s): Rnf complex (ambiguous); Na+-translocating ferredoxin:NAD+ oxidoreductase

Systematic name: ferredoxin:NAD+ oxidoreductase (Na+-transporting)

Comments: This iron-sulfur and flavin-containing electron transport complex, isolated from the bacterium Acetobacterium woodii, couples the energy from reduction of NAD+ by ferredoxin to pumping sodium ions out of the cell, generating a gradient across the cytoplasmic membrane.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Biegel, E., Schmidt, S. and Muller, V. Genetic, immunological and biochemical evidence for a Rnf complex in the acetogen Acetobacterium woodii. Environ Microbiol 11 (2009) 1438-1443. [PMID: 19222539]

2. Biegel, E. and Muller, V. Bacterial Na+-translocating ferredoxin:NAD+ oxidoreductase. Proc. Natl. Acad. Sci. USA 107 (2010) 18138-18142. [PMID: 20921383]

3. Hess, V., Schuchmann, K. and Muller, V. The ferredoxin:NAD+ oxidoreductase (Rnf) from the acetogen Acetobacterium woodii requires Na+ and is reversibly coupled to the membrane potential. J. Biol. Chem. 288 (2013) 31496-31502. [PMID: 24045950]

[EC 7.2.1.2 created 2015 as EC 1.18.1.8, transferred 2018 to EC 7.2.1.2]


Contents

EC 7.2.2 Linked to the hydrolysis of a nucleoside triphosphate


Entries

EC 7.2.2.1

Accepted name: Na+-transporting two-sector ATPase

Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]

Systematic name: ATP phosphohydrolase (two-sector, Na+-transporting)

Comments: A multisubunit ATPase transporter found in some halophilic or alkalophilic bacteria that functions in maintaining sodium homeostasis. The enzyme is similar to EC 7.1.2.2 (H+-transporting two-sector ATPase) but pumps Na+ rather than H+. cf. EC 7.2.2.3, P-type Na+ transporter and EC 7.2.2.4, ABC-type Na+ transporter.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Solioz, M. and Davies, K. Operon of vacuolar-type Na+-ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 9453-9459. [PMID: 8144530]

2. Takase, K., Kakinuma, S., Yamato, I., Konishi, K., Igarashi, K. and Kanikuma, Y. Sequencing and characterization of the ntp gene cluster for vacuolar-type Na+-translocating ATPase of Enterococcus hirae. J. Biol. Chem. 269 (1994) 11037-11044. [PMID: 8157629]

3. Rahlfs, S. and Müller, V. Sequence of subunit c of the Na+-translocating F1Fo-ATPase of Acetobacterium woodii: proposal for determinants of Na+ specificity as revealed by sequence comparisons. FEBS Lett. 404 (1997) 269-271. [PMID: 9119076]

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

EC 7.2.2.2

Accepted name: ABC-type Cd2+ transporter

Reaction: ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2]

Other name(s): cadmium-transporting ATPase (ambiguous); ABC-type cadmium-transporter

Systematic name: ATP phosphohydrolase (ABC-type, heavy-metal-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 some heavy metals, especially Cd2+, from the cytosol into the vacuole.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. 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. [PMID: 8626454]

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 7.2.2.2 created 2000 as EC 3.6.3.46, transferred 2018 to EC 7.2.2.2]

EC 7.2.2.3

Accepted name: P-type Na+ transporter

Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]

Other name(s): Na+-exporting ATPase (ambiguous); ENA1 (gene name); ENA2 (gene name); ENA5 (gene name)

Systematic name: ATP phosphohydrolase (P-type, Na+-exporting)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed. Some forms can also export Li+ ions. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.4, ABC-type Na+ transporter.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wieland, J., Nitsche, A.M., Strayle, J., Steiner, H. and Rudolph, H.K. The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane. EMBO J. 14 (1995) 3870-3882. [PMID: 7664728]

2. Catty, P., de Kerchove d'Exaerde, A. and Goffeau, A. The complete inventory of the yeast Saccharomyces cerevisiae P-type transport ATPases. FEBS Lett. 409 (1997) 325-332. [PMID: 9224683]

3. Benito, B., Quintero, F.J. and Rodriguez-Navarro, A. Overexpression of the sodium ATPase of Saccharomyces cerevisiae: conditions for phosphorylation from ATP and Pi. Biochim. Biophys. Acta 1328 (1997) 214-226. [PMID: 9315618]

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 7.2.2.3 created 2000, as EC 3.6.3.7, modified 2001, transferred 20018 to EC 7.2.2.3]

EC 7.2.2.4

Accepted name: ABC-type Na+ transporter

Reaction: ATP + H2O + Na+[side 1] = ADP + phosphate + Na+[side 2]

Other name(s): natAB (gene names)

Systematic name: ATP phosphohydrolase (ABC-type, Na+-exporting)

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. This bacterial enzyme, characterized from Bacillus subtilis, exports Na+ ions out of the cell. cf. EC 7.2.2.1, Na+-transporting two-sector ATPase and EC 7.2.2.3, P-type Na+ transporter.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Cheng, J., Guffanti, A.A. and Krulwich, T.A. A two-gene ABC-type transport system that extrudes Na+ in Bacillus subtilis is induced by ethanol or protonophore. Mol. Microbiol. 23 (1997) 1107-1120. [PMID: 9106203]

2. Ogura, M., Tsukahara, K., Hayashi, K. and Tanaka, T. The Bacillus subtilis NatK-NatR two-component system regulates expression of the natAB operon encoding an ABC transporter for sodium ion extrusion. Microbiology 153 (2007) 667-675. [PMID: 17322186]

[EC 7.2.2.4 created 2018]


Contents

EC 7.2.4 Linked to decarboxylation


Entries

EC 7.2.4.1

Accepted name: carboxybiotin decarboxylase

Reaction: a carboxybiotinyl-[protein] + n Na+[side 1] + H+[side 2] = CO2 + a biotinyl-[protein] + n Na+[side 2] (n = 1-2)

For diagram of the reaction click here

Other name(s): MadB; carboxybiotin protein decarboxylase

Systematic name: carboxybiotinyl-[protein] carboxy-lyase

Comments: The integral membrane protein MadB from the anaerobic bacterium Malonomonas rubra is a component of the multienzyme complex EC 4.1.1.89, biotin-dependent malonate decarboxylase. The free energy of the decarboxylation reaction is used to pump Na+ out of the cell. The enzyme is a member of the Na+-translocating decarboxylase family, other members of which include EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 7.2.4.3 [(S)-methylmalonyl-CoA decarboxylase (sodium-transporting)] [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Berg, M., Hilbi, H. and Dimroth, P. Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem. 245 (1997) 103-115. [PMID: 9128730]

2. Dimroth, P. and Hilbi, H. Enzymic and genetic basis for bacterial growth on malonate. Mol. Microbiol. 25 (1997) 3-10. [PMID: 11902724]

[EC 7.2.4.1 created 2008 as EC 4.3.99.2, transferred 2018 to EC 7.2.4.1]

EC 7.2.4.2

Accepted name: oxaloacetate decarboxylase (Na+ extruding)

Reaction: oxaloacetate + 2 Na+[side 1] = pyruvate + CO2 + 2 Na+[side 2]

Other name(s): oxaloacetate β-decarboxylase (ambiguous); oxalacetic acid decarboxylase (ambiguous); oxalate β-decarboxylase (ambiguous); oxaloacetate carboxy-lyase (ambiguous)

Systematic name: oxaloacetate carboxy-lyase (pyruvate-forming; Na+-extruding)

Comments: The enzyme from the bacterium Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+. Differs from EC 4.1.1.112 (oxaloacetate decarboxylase) for which there is no evidence for involvement in Na+ transport.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353-358. [PMID: 7016536]

2. Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435-441. [PMID: 7037395]

[EC 7.2.4.2 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, transferred 2018 to EC 7.2.4.2]

EC 7.2.4.3

Accepted name: (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)

Reaction: (S)-methylmalonyl-CoA + Na+[side 1] + H=[side 2] = propanoyl-CoA + CO2 + Na+[side 2]

Other name(s): methylmalonyl-coenzyme A decarboxylase (ambiguous); (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase (ambiguous)

Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)

Comments: This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253-1261. [PMID: 5646172]

2. Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584-585. [PMID: 7070502]

3. Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645-650. [PMID: 2920730]

4. Huder, J.B. and Dimroth, P. Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli. J. Bacteriol. 177 (1995) 3623-3630. [PMID: 7601825]

5. Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. and Dimroth, P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250 (1997) 590-599. [PMID: 9428714]

[EC 7.2.4.3 created 1972 as EC 4.1.1.41, modified 1983, modified 1986, transferred 2018 to EC 7.2.4.3]


EC 7.3 Catalysing the translocation of inorganic anions and their chelates

Contents

EC 7.3.2 Linked to the hydrolysis of a nucleoside triphosphate

Entries

EC 7.3.2.1

Accepted name: ABC-type phosphate transporter

Reaction: ATP + H2O + phosphate-[phosphate-binding protein][side 1] = ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]

Other name(s): phosphate ABC transporter; phosphate-transporting ATPase (ambiguous)

Systematic name: ATP phosphohydrolase (ABC-type, 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. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of phosphate anions. Unlike P-type ATPases, it does not undergo phosphorylation during the transport process.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Webb, D.C., Rosenberg, H. and Cox, G.B. Mutational analysis of the Escherichia coli phosphate-specific transport system, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices. J. Biol. Chem. 267 (1992) 24661-24668. [PMID: 1447208]

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. [PMID: 7569321]

3. Braibant, M., LeFevre, P., de Wit, L., Ooms, J., Peirs, P., Huygen, K., Wattiez, R. and Content, J. Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter. FEBS Lett. 394 (1996) 206-212. [PMID: 8843165]

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 7.3.2.1 created 2000 as EC 3.6.3.27, transferred 2018 to EC 7.3.2.1]

EC 7.3.2.2

Accepted name: ABC-type phosphonate transporter

Reaction: ATP + H2O + phosphonate-[phosphonate-binding protein][side 1] = ADP + phosphate + phosphonate[side 2] + [phosphonate-binding protein][side 1]

Other name(s): phosphonate-transporting ATPase (ambiguous)

Systematic name: ATP phosphohydrolase (ABC-type, phosphonate-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 phosphonate and organophosphate anions.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Wanner, B.L. and Metcalf, W.W. Molecular genetic studies of a 10.9-kb operon in Escherichia coli for phosphonate uptake and biodegradation. FEMS Microbiol. Lett. 79 (1992) 133-139. [PMID: 1335942]

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. [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 7.3.2.2 created 2000 as EC 3.6.3.28, transferred 2018 to EC 7.3.2.2]


EC 7.4 Catalysing the translocation amino acids and peptides

Contents

EC 7.4.2 Linked to the hydrolysis of a nucleoside triphosphate

Entries

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, CAS registry number:

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. [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. [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. [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, CAS registry number:

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. [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 7.5 Catalysing the translocation carbohydrates and their derivatives

Contents

EC 7.5.2 Linked to the hydrolysis of a nucleoside triphosphate

Entries

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, CAS registry number:

References:

1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [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. [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. [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, CAS registry number:

References:

1. Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113. [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. [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. [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 7.6 Catalysing the translocation of other compounds

Contents

EC 7.6.2 Linked to the hydrolysis of a nucleoside triphosphate

Entries 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)

Systematic name: ATP phosphohydrolase (P-type, phospholipid-flipping)

Comments: A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme moves phospholipids such as phosphatidylcholine, phosphatidylserine, and phosphatidylethanolamine from one membrane face to the other (‘flippase’).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

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. [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. [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. [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. [PMID: 20053675]

[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 (redundant, but not identical, to EC 7.6.2.1, P-type phospholipid transporter).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bellamy, W.T. P-glycoproteins and multidrug resistance. Annu. Rev. Pharmacol. Toxicol. 36 (1996) 161-183. [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. [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. [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. [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. [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. [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, CAS registry number:

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. [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]


Continued with EC 6
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