PXPA_THEON
ID PXPA_THEON Reviewed; 255 AA.
AC B6YWS6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=TON_1051;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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; CP000855; ACJ16539.1; -; Genomic_DNA.
DR RefSeq; WP_012572011.1; NC_011529.1.
DR AlphaFoldDB; B6YWS6; -.
DR SMR; B6YWS6; -.
DR STRING; 523850.TON_1051; -.
DR EnsemblBacteria; ACJ16539; ACJ16539; TON_1051.
DR GeneID; 7018073; -.
DR KEGG; ton:TON_1051; -.
DR PATRIC; fig|523850.10.peg.1059; -.
DR eggNOG; arCOG05810; Archaea.
DR HOGENOM; CLU_069535_0_0_2; -.
DR OMA; DRTYKQD; -.
DR OrthoDB; 47446at2157; -.
DR Proteomes; UP000002727; 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_1000132078"
SQ SEQUENCE 255 AA; 28211 MW; 24FAAB686D376F2F CRC64;
MKVDLNSDLG ESFGRYKLGL DEEVMKYITS ANVATGWHAG DPLVMRKTVR LAKEKGVAVG
AHPGYPDLLG FGRRYMKLTP EEARNYILYQ IGALHAFTKA EGMELQHVKP HGALYNALVK
DEELARAVIE GITDFDRRII FVMLSGSRPA EIAEEMGLKV AHEVFADRAY NPDGTLVLRG
KPGAVIHDKE LIAERVVSMV KDGGVKAING EWIELRADTI CVHGDNPKAV EIAAYIRRVL
EDEGINVVPM GEFIR