EC 7.4.2.1 - ABC-type polar-amino-acid transporter

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IntEnz Enzyme Nomenclature
EC 7.4.2.1

Names

Accepted name:
ABC-type polar-amino-acid transporter
Other names:
histidine permease
polar-amino-acid-transporting ATPase
Systematic name:
ATP phosphohydrolase (ABC-type, polar-amino-acid-importing)

Reactions

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. Formerly EC 3.6.3.21.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00185
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102022 , GO:0015426
UniProtKB/Swiss-Prot:

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: 271-278 (1995). [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: 81-136 (1998). [PMID: 9889977]
  3. 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: 27745-27752 (1997). [PMID: 9346917]
  4. 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: 397-401 (1997). [PMID: 9315727]

[EC 7.4.2.1 created 2000 as EC 3.6.3.21, transferred 2018 to EC 7.4.2.1]