(data stored in ACNUC7421 zone)

SWISSPROT: PXPA_ECO27

ID   PXPA_ECO27              Reviewed;         244 AA.
AC   B7UKY6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691};
DE   AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691};
GN   OrderedLocusNames=E2348C_0596;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-
CC       glutamate coupled to the hydrolysis of ATP to ADP and inorganic
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00691}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate
CC         + phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216;
CC         EC=3.5.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00691};
CC   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC       {ECO:0000255|HAMAP-Rule:MF_00691}.
CC   -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00691}.
DR   EMBL; FM180568; CAS08144.1; -; Genomic_DNA.
DR   RefSeq; WP_000687123.1; NC_011601.1.
DR   SMR; B7UKY6; -.
DR   EnsemblBacteria; CAS08144; CAS08144; E2348C_0596.
DR   KEGG; ecg:E2348C_0596; -.
DR   KO; K07160; -.
DR   OMA; VNIACGF; -.
DR   BioCyc; ECOL574521:E2348C_RS03160-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00691; PxpA; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR   PANTHER; PTHR30292; PTHR30292; 1.
DR   Pfam; PF03746; LamB_YcsF; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKY6.
DR   SWISS-2DPAGE; B7UKY6.
KW   ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding.
FT   CHAIN         1    244       5-oxoprolinase subunit A.
FT                                /FTId=PRO_1000200458.
SQ   SEQUENCE   244 AA;  25856 MW;  9367E5476E7E3F48 CRC64;
     MKIDLNADLG EGCASDAELL TLVSSANIAC GFHAGDAQTM QACVREAIKN GVAIGAHPSF
     PDRENFGRSA MQLPPETVFA QTLYQIGALA AITRAQGGVM CHVKPHGMLY NQAAKEAQLA
     DAIARAVYAC DPALILVGLA GSELIRAGER YGLVTREEVF ADRGYQADGS LVPRSQPGAL
     IENEEQALAQ TLEMVQYGRV KSITGEWAMV TAQTVCLHGD GEHALAFARR LRATFAEKGI
     VVAA
//

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