ID   PXPA1_BURPS             Reviewed;         254 AA.
AC   Q63YD1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=5-oxoprolinase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA1 {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=BPSL0257;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(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}.
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DR   EMBL; BX571965; CAH34245.1; -; Genomic_DNA.
DR   RefSeq; WP_009935993.1; NZ_CP009538.1.
DR   RefSeq; YP_106884.1; NC_006350.1.
DR   AlphaFoldDB; Q63YD1; -.
DR   SMR; Q63YD1; -.
DR   STRING; 272560.BPSL0257; -.
DR   EnsemblBacteria; CAH34245; CAH34245; BPSL0257.
DR   KEGG; bps:BPSL0257; -.
DR   PATRIC; fig|272560.51.peg.1451; -.
DR   eggNOG; COG1540; Bacteria.
DR   OMA; DRTYKQD; -.
DR   Proteomes; UP000000605; 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; Reference proteome.
FT   CHAIN           1..254
FT                   /note="5-oxoprolinase subunit A 1"
FT                   /id="PRO_0000184998"
SQ   SEQUENCE   254 AA;  26780 MW;  C65A1DA01A20505C CRC64;
     MEIDLNADLG EGCGSDEALL DLVTSANIAC GWHAGGAQAM RDCVRWAVEK GVSIGAHPSF
     HDPENFGRKE MDLPASEIYA GVLYQLGALS AFAQAEGGRI AHVKPHGALY NQAAREPEIA
     DAVVSAIHDF DPSLAVFGLA KSGFVDAARQ AGLVAVEEVF ADRGYRADGS LVPRSQPGAL
     VDDENEMLAR TLEMVRGQRV RAVTGEWVPL NAQTVCLHGD GPHALAFAKR IRDALEAAGI
     DVHAPGALHA GERA