ID   PXPA_YERPS              Reviewed;         245 AA.
AC   Q667T3;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 77.
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}; OrderedLocusNames=YPTB2908;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate
CC       coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
CC       {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; EC=3.5.2.9;
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH22146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH22146.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002209659.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q667T3; -.
DR   SMR; Q667T3; -.
DR   EnsemblBacteria; CAH22146; CAH22146; YPTB2908.
DR   GeneID; 66844670; -.
DR   KEGG; ypo:BZ17_3721; -.
DR   KEGG; yps:YPTB2908; -.
DR   PATRIC; fig|273123.14.peg.3904; -.
DR   OMA; DRTYKQD; -.
DR   Proteomes; UP000001011; 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;
KW   ATP-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..245
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185063"
SQ   SEQUENCE   245 AA;  26281 MW;  B900F998EC841DB5 CRC64;
     MKIDLNADLG EGCANDQALL QLVSSANIAC GFHAGDAQTM RQSVRWALEY GVAIGAHPSF
     PDRENFGRTA MQLPPETVYA QVVYQLGALA AIVQVEGGVM QHVKPHGMLY NQAAVDPLLA
     DAIAQAVKAV DPSLRLVGLA GSELIRAGTR VGLVTRQEVF ADRHYQPDGT LVPRSQPDAL
     IESDELALSQ TLAMVQQHQV QACDGSWVQV QADTVCVHGD GVQALAFARC LRDRFQQEGI
     SVIAQ