ID   PXPA_THEKO              Reviewed;         255 AA.
AC   Q5JG28;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A {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 {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=TK0336;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD84525.1; -; Genomic_DNA.
DR   RefSeq; WP_011249291.1; NC_006624.1.
DR   AlphaFoldDB; Q5JG28; -.
DR   SMR; Q5JG28; -.
DR   STRING; 69014.TK0336; -.
DR   EnsemblBacteria; BAD84525; BAD84525; TK0336.
DR   GeneID; 3235703; -.
DR   KEGG; tko:TK0336; -.
DR   PATRIC; fig|69014.16.peg.333; -.
DR   eggNOG; arCOG05810; Archaea.
DR   HOGENOM; CLU_069535_0_0_2; -.
DR   InParanoid; Q5JG28; -.
DR   OMA; DRTYKQD; -.
DR   OrthoDB; 47446at2157; -.
DR   PhylomeDB; Q5JG28; -.
DR   Proteomes; UP000000536; 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   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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..255
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185067"
SQ   SEQUENCE   255 AA;  28183 MW;  36CB1063BC4D1EEB CRC64;
     MKVDLNADLG ESFGRYRLGL DEEVMKYITS ANVATGWHAG DPLVMRKTVK LAKENGVAVG
     AHPGYPDLLG FGRRYMKLTY DEARNYILYQ VGALYAFVRA EGIELQHVKP HGALYNALVK
     EEELARGVIE GIADFDKNLI FVTLSGSRPA EIAEEMGVKV AHEVFADRAY NPDGTLVPRS
     KPGAVIEDKE EIAERVISMV KDGGVRAING EWVELKVDTI CLHGDNPKAV EIAAHIRKVL
     EEEGVKIVPM KEIIR