ID   PXPA2_PSEPK             Reviewed;         258 AA.
AC   Q88E89;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=PP_4577;
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; AAN70150.1; -; Genomic_DNA.
DR   RefSeq; NP_746686.1; NC_002947.4.
DR   RefSeq; WP_010955246.1; NC_002947.4.
DR   AlphaFoldDB; Q88E89; -.
DR   SMR; Q88E89; -.
DR   STRING; 160488.PP_4577; -.
DR   EnsemblBacteria; AAN70150; AAN70150; PP_4577.
DR   KEGG; ppu:PP_4577; -.
DR   PATRIC; fig|160488.4.peg.4880; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_6; -.
DR   OMA; DRTYKQD; -.
DR   PhylomeDB; Q88E89; -.
DR   BioCyc; PPUT160488:G1G01-4885-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..258
FT                   /note="5-oxoprolinase subunit A 2"
FT                   /id="PRO_0000185030"
SQ   SEQUENCE   258 AA;  27871 MW;  A6CF3CBCFCF0BBFA CRC64;
     MHNDKGDRVV ERLLLNCDMG ESFGSWRMGL DAEVMPYIDC ANIACGYHAG DPGIMRRTVT
     LALEHGVTIG AHPAYPDLVG FGRRSMACSP EEIRDLLHYQ IGALDGICKV LGGRVAYVKP
     HGALYNDMMA DPLKLRTVLE AVAAYDSNLP LMLMATADNR AAQALGDEIG VPLWFEAFAD
     RAYTASGHLL SRRLPGAVHH DPARVVEQAV RLARGETLLA DDGSALQLAA RTLCVHGDND
     SSVAAVRQIR QALDGLEV