ID   PXPA1_PSEPK             Reviewed;         252 AA.
AC   Q88IS9;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=PP_2920;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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; AE015451; AAN68528.1; -; Genomic_DNA.
DR   RefSeq; NP_745064.1; NC_002947.4.
DR   RefSeq; WP_010953822.1; NC_002947.4.
DR   AlphaFoldDB; Q88IS9; -.
DR   SMR; Q88IS9; -.
DR   STRING; 160488.PP_2920; -.
DR   EnsemblBacteria; AAN68528; AAN68528; PP_2920.
DR   KEGG; ppu:PP_2920; -.
DR   PATRIC; fig|160488.4.peg.3093; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_6; -.
DR   OMA; MPGSVIC; -.
DR   PhylomeDB; Q88IS9; -.
DR   BioCyc; PPUT160488:G1G01-3098-MON; -.
DR   Proteomes; UP000000556; 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..252
FT                   /note="5-oxoprolinase subunit A 1"
FT                   /id="PRO_0000185029"
SQ   SEQUENCE   252 AA;  27611 MW;  A0824C966B761653 CRC64;
     MQAVDFNSDM GEGFGPWTIG DGVDNELMGY ISSANIATGF HAGDPGTMRR TVERAKALGV
     AVGAHPGFRD LVGFGRRHIN ASAQELVDDM LYQLGALREI ARAQGVRLQH IKPHGALYMH
     LARDEEAARL LVENLRVIEP ELLLYCMPGS VICRIAQELG QPVIREFYAD REYDLSGSIV
     FTRNVRGYEP QAVAERVLRA CRQGVVRTVE GQDLAIEFDS ICLHSDTPGA LDLVEATRKA
     LDAAGIVVRA PR