ID   PXPA_VIBC3              Reviewed;         246 AA.
AC   A5EZN1; C3M5G0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=VC0395_0716, VC395_A0539;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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}.
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DR   EMBL; CP000626; ABQ18608.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11373.1; -; Genomic_DNA.
DR   RefSeq; WP_001882609.1; NZ_JAACZH010000025.1.
DR   AlphaFoldDB; A5EZN1; -.
DR   SMR; A5EZN1; -.
DR   STRING; 345073.VC395_A0539; -.
DR   EnsemblBacteria; ABQ18608; ABQ18608; VC0395_0716.
DR   GeneID; 57742159; -.
DR   GeneID; 66940639; -.
DR   KEGG; vco:VC0395_0716; -.
DR   KEGG; vcr:VC395_A0539; -.
DR   PATRIC; fig|345073.21.peg.3281; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_6; -.
DR   OMA; PHGELYF; -.
DR   Proteomes; UP000000249; Chromosome 1.
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..246
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_1000072748"
SQ   SEQUENCE   246 AA;  27057 MW;  2739D27DE86D644A CRC64;
     MSKRTIQLNC DMGESFGVWT MGADEEVMPW IDMANIACGF HASDPHVMSR TIDLALEHEV
     MIGAHPSYPD LQGFGRRSLA MNEQEVSEII LYQVGALKAL CESKNGQLSY VKPHGALYND
     MMSDPSIFRA VVDAVSCFNL PLMVLASANN QDYLDIADRF DVPLLFEAFA DRTYLANGKL
     TPRSQPNAVL SSEEAILNQV RQIARYGKVT SSDGFVIPIE ADTLCVHGDN PNAVSLIARI
     RAALDE