ID   PXPA_PYRFU              Reviewed;         255 AA.
AC   Q8U1D7;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=PF1272;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81396.1; -; Genomic_DNA.
DR   RefSeq; WP_011012416.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U1D7; -.
DR   SMR; Q8U1D7; -.
DR   STRING; 186497.PF1272; -.
DR   PRIDE; Q8U1D7; -.
DR   EnsemblBacteria; AAL81396; AAL81396; PF1272.
DR   GeneID; 41713076; -.
DR   KEGG; pfu:PF1272; -.
DR   PATRIC; fig|186497.12.peg.1334; -.
DR   eggNOG; arCOG05810; Archaea.
DR   HOGENOM; CLU_069535_0_0_2; -.
DR   OMA; DRTYKQD; -.
DR   OrthoDB; 47446at2157; -.
DR   PhylomeDB; Q8U1D7; -.
DR   Proteomes; UP000001013; 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..255
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185065"
SQ   SEQUENCE   255 AA;  28402 MW;  276185EB167FA766 CRC64;
     MKVDLNSDLG ESFGRYKLGL DDEVMKYITS ANVACGWHAG DPLVMRKTVR LAKKNNVQVG
     AHPGYPDLMG FGRRYMKLTP EEARNYILYQ IGALYAFVKA EGLELQHVKP HGALYNAMVK
     EEDLARAVIE GILDFDKRLI VVTLAGSRVV EIAREMGARV AQEGFADRAY NPDGTLVPRS
     RPGAVIEDKE EIAERVISMV KDGGIRAING EWIELEVDTI CVHGDNPKAV EITAYIRRRL
     EEEGVKVLPM GDFIK