ID   PXPA_CLOD6              Reviewed;         263 AA.
AC   Q18BQ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-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=CD630_13840;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ68246.1; -; Genomic_DNA.
DR   RefSeq; WP_009896287.1; NZ_CP010905.2.
DR   RefSeq; YP_001087884.1; NC_009089.1.
DR   AlphaFoldDB; Q18BQ3; -.
DR   SMR; Q18BQ3; -.
DR   STRING; 272563.CD630_13840; -.
DR   EnsemblBacteria; CAJ68246; CAJ68246; CD630_13840.
DR   KEGG; cdf:CD630_13840; -.
DR   KEGG; pdc:CDIF630_01544; -.
DR   PATRIC; fig|272563.120.peg.1449; -.
DR   eggNOG; COG1540; Bacteria.
DR   OMA; DRTYKQD; -.
DR   PhylomeDB; Q18BQ3; -.
DR   BioCyc; PDIF272563:G12WB-1522-MON; -.
DR   Proteomes; UP000001978; 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; Reference proteome.
FT   CHAIN           1..263
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_1000045200"
SQ   SEQUENCE   263 AA;  29129 MW;  8C4172920E6D56A5 CRC64;
     MYKVDLNSDL GESFGTYKIG LDEEVLKYIS SANIACGFHA GDPSHMEKTV QLAKKNGVKI
     GAHPGFLDLI GFGRREMKIT KQEAKDYTKY QLGALMAFAS SNGCNIQHVK PHGALYNMAA
     KDKELAMGIC EAIYEVDKDI ILLGLYNSEM INSAKEIGLR FANEVFADRA YDNNGFLVPR
     SVEGAVIHDT KHAIDRVVRM VKEGTVETLT GEVIHIKADS ICVHGDNPKA IEFVKEIRKR
     FELESIEVCP LENIEVCSSE NIV