ID   PXPA2_RALSO             Reviewed;         260 AA.
AC   Q8XRC2;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=5-oxoprolinase subunit A 2 {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA2 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=RSp0936;
GN   ORFNames=RS05397;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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; AL646053; CAD18087.1; -; Genomic_DNA.
DR   RefSeq; WP_011004229.1; NC_003296.1.
DR   AlphaFoldDB; Q8XRC2; -.
DR   SMR; Q8XRC2; -.
DR   STRING; 267608.RSp0936; -.
DR   EnsemblBacteria; CAD18087; CAD18087; RSp0936.
DR   GeneID; 60503843; -.
DR   KEGG; rso:RSp0936; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_4; -.
DR   OMA; PHGELYF; -.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid; Reference proteome.
FT   CHAIN           1..260
FT                   /note="5-oxoprolinase subunit A 2"
FT                   /id="PRO_0000185035"
SQ   SEQUENCE   260 AA;  27392 MW;  69F605B9D0382E9A CRC64;
     MEIDLNADLG EGYGPWRMGD DEAMMSLISS ANIACGFHAG DPLIMDRTVR LAIEGGVDVG
     AHVGFPDRQG FGRRFMQVDI PDLTAMVTYQ LGALAGIARA HGRRVTHMSF HGALGNRAAA
     DPAWATPLLK AIAAFDPNLI ISTSSSQAIE GAAAAFGLPV GVSFLADRAY DDQGLLVSRG
     LPGAVIHDEA QVLARVRRLL TEGTIVTHAG NVLPMQPRSI LVHGDTPGAV ALTQRLRAEI
     ESLGGRIVPI SQQLGFSTVP