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PXPA_PYRAB
ID   PXPA_PYRAB              Reviewed;         255 AA.
AC   Q9V005; G8ZIF8;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=PYRAB09930;
GN   ORFNames=PAB2445;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB49901.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70399.1; -; Genomic_DNA.
DR   PIR; H75074; H75074.
DR   RefSeq; WP_010868110.1; NC_000868.1.
DR   AlphaFoldDB; Q9V005; -.
DR   SMR; Q9V005; -.
DR   STRING; 272844.PAB2445; -.
DR   EnsemblBacteria; CAB49901; CAB49901; PAB2445.
DR   GeneID; 1496343; -.
DR   KEGG; pab:PAB2445; -.
DR   PATRIC; fig|272844.11.peg.1045; -.
DR   eggNOG; arCOG05810; Archaea.
DR   HOGENOM; CLU_069535_0_0_2; -.
DR   OMA; DRTYKQD; -.
DR   OrthoDB; 47446at2157; -.
DR   PhylomeDB; Q9V005; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..255
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185064"
SQ   SEQUENCE   255 AA;  28356 MW;  7DEE86D7F24D3CB5 CRC64;
     MRVDLNSDLG ESFGRYKLGL DEEVMRYITS ANIACGWHAG DPIVMRRTVK LAKENNVQVG
     AHPGYPDLMG FGRRYMKLTP EEARNYILYQ IGALYAFAKA EGVELQHVKP HGALYNAMVK
     EEELARAVIE GILDFDKNLI LVTLSNSRVA EIAEEMGLKV AHEVFADRAY NPDGTLVPRG
     KPGAVIEDKE EIAERVISMV KDGGVRAING EWVELRVDTI CVHGDNPKAL EITSHIRKIL
     EEEGVKVVPL KDFIG
 
 
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