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Database: UniProt/SWISS-PROT
Entry: CAPPA_PYRAB
LinkDB: CAPPA_PYRAB
Original site: CAPPA_PYRAB 
ID   CAPPA_PYRAB             Reviewed;         469 AA.
AC   Q9V2Q9; G8ZFJ3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 90.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000255|HAMAP-Rule:MF_01904};
GN   OrderedLocusNames=PYRAB00160; ORFNames=PAB2342;
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.,
RA   Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic
RT   archaeon 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
RT   and Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC       phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-
CC       carbon dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_01904}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702;
CC         EC=4.1.1.31; Evidence={ECO:0000255|HAMAP-Rule:MF_01904};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01904}.
DR   EMBL; AJ248283; CAB48939.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69384.1; -; Genomic_DNA.
DR   PIR; D75186; D75186.
DR   RefSeq; WP_010867139.1; NC_000868.1.
DR   ProteinModelPortal; Q9V2Q9; -.
DR   SMR; Q9V2Q9; -.
DR   STRING; 272844.PAB2342; -.
DR   PRIDE; Q9V2Q9; -.
DR   EnsemblBacteria; CAB48939; CAB48939; PAB2342.
DR   GeneID; 1495700; -.
DR   KEGG; pab:PAB2342; -.
DR   PATRIC; fig|272844.11.peg.18; -.
DR   eggNOG; arCOG04435; Archaea.
DR   eggNOG; COG1892; LUCA.
DR   HOGENOM; HOG000038601; -.
DR   KO; K01595; -.
DR   OMA; PAMNYGL; -.
DR   OrthoDB; POG093Z01LI; -.
DR   BioCyc; PABY272844:G1GT8-20-MONOMER; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_01904; PEPcase_type2; 1.
DR   InterPro; IPR007566; PEP_COase_arc-type.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02751; PEPCase_arch; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase; Magnesium.
FT   CHAIN         1    469       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000309611.
SQ   SEQUENCE   469 AA;  53937 MW;  DB6A6584A7E78BC7 CRC64;
     MIPRIMSTQH PDNYSIPFFA NSPVLGGEDE ITEAFYAFNV LGADEQMWDF EGKEVDEFVV
     KKLLERYPSF FRKVILGKDV RLTPRVPNPT VEKAEAKLLL ETLQGITRAA DYARVFYGED
     IAPIFEVILP MTTSLAEIER VHELYRKVVN LADERIYDTT VKEWIGEFYP KEIGIIPLFE
     TKVALLKSAK IIGEYLERRE PEYQRVFLAR SDPAMNYGLI SAVTYVKNAL QEIWELEEET
     SIPIYPIVGV GGPPFRGGMR PDNVDNVLSE YPSVQTYTVQ SSFKFDYPTK EVVKAVEKVK
     STKRKEPYSL EVPDFITLYE VEYQRQVKIL APHIRRLATR IPDRRKRKLH IGLFGYSRNV
     GGLSLPRAIK FTASLYSIGV PPELLGLNAL TDRQLDVVSE YYVNIYEDLE FAMRFFSFRV
     AEKAGLKELV ERIKEFKPEI EEEYVAEAEI VFRGEGDIIK LAQMRGFLG
//
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