ID   PXPA_SALTY              Reviewed;         244 AA.
AC   Q8ZQV6;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; Synonyms=ybgL;
GN   OrderedLocusNames=STM0714;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19658.1; -; Genomic_DNA.
DR   RefSeq; NP_459699.1; NC_003197.2.
DR   RefSeq; WP_001017909.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZQV6; -.
DR   SMR; Q8ZQV6; -.
DR   STRING; 99287.STM0714; -.
DR   PaxDb; Q8ZQV6; -.
DR   EnsemblBacteria; AAL19658; AAL19658; STM0714.
DR   GeneID; 1252234; -.
DR   KEGG; stm:STM0714; -.
DR   PATRIC; fig|99287.12.peg.746; -.
DR   HOGENOM; CLU_069535_0_0_6; -.
DR   OMA; DRTYKQD; -.
DR   PhylomeDB; Q8ZQV6; -.
DR   BioCyc; SENT99287:STM0714-MON; -.
DR   Proteomes; UP000001014; 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   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..244
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185040"
SQ   SEQUENCE   244 AA;  26091 MW;  5084CE42C505D2EB CRC64;
     MNIDLNADLG EGCASDSELL TLVSSANIAC GFHAGDAQTM LTCVREALKN GVAIGAHPSF
     PDRDNFGRTA MVLPPETVYA QTLYQIGALG AIVQAQGGVM RHVKPHGMLY NQAAKDPHLA
     QAIAKAVHDY DPSLILVGLA GSELIRAGER HRLVTRQEVF ADRGYQADGS LVPRMQPGAL
     IHDEEQALAQ TLDMVQAGRV KSVTGVWTTV TAQTVCIHGD GEYALAFARR LRAAFNARNI
     HVIA