ID   PXPA2_PSESM             Reviewed;         251 AA.
AC   Q881F7;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, 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=PSPTO_2936;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO56429.1; -; Genomic_DNA.
DR   RefSeq; NP_792734.1; NC_004578.1.
DR   RefSeq; WP_011104283.1; NC_004578.1.
DR   AlphaFoldDB; Q881F7; -.
DR   SMR; Q881F7; -.
DR   STRING; 223283.PSPTO_2936; -.
DR   EnsemblBacteria; AAO56429; AAO56429; PSPTO_2936.
DR   GeneID; 1184590; -.
DR   KEGG; pst:PSPTO_2936; -.
DR   PATRIC; fig|223283.9.peg.2994; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_6; -.
DR   OMA; MPGSVIC; -.
DR   OrthoDB; 918580at2; -.
DR   PhylomeDB; Q881F7; -.
DR   Proteomes; UP000002515; 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..251
FT                   /note="5-oxoprolinase subunit A 2"
FT                   /id="PRO_0000185032"
SQ   SEQUENCE   251 AA;  27420 MW;  52154DC5310AF22E CRC64;
     MQIDFNSDMG ESFGAWTIGD GVDTELMAFI SSANIATGFH AGDPSTMRRT IEQAKRLGVA
     IGAHPGFRDL VGFGRRHINA PAQELVDDML YQLGALRELA RVQGVPLQHF KPHGALYMHL
     ARDEEAARLL VENLQRLEPD LLLYCMPGSV ICNVAQELGQ PVVREFYADR AYDLSGSIVF
     TRNVRAHDPA EVAARVIRAC QQGLVRTVEG DDLAIQFDSI CLHSDTPGAL ALAQATRQAL
     DGAGIEVRTP R