ID   F0LK16_THEBM            Unreviewed;       476 AA.
AC   F0LK16;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904};
GN   OrderedLocusNames=TERMP_01753 {ECO:0000313|EMBL:ADT84728.1};
OS   Thermococcus barophilus (strain DSM 11836 / MP).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT84728.1, ECO:0000313|Proteomes:UP000007478};
RN   [1] {ECO:0000313|EMBL:ADT84728.1, ECO:0000313|Proteomes:UP000007478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX   PubMed=21217005; DOI=10.1128/JB.01490-10;
RA   Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT   "Complete genome sequence of the hyperthermophilic, piezophilic,
RT   heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL   J. Bacteriol. 193:1481-1482(2011).
CC   -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC       phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon
CC       dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000256|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; EC=4.1.1.31;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01904};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01904}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002372; ADT84728.1; -; Genomic_DNA.
DR   RefSeq; WP_013468025.1; NC_014804.1.
DR   AlphaFoldDB; F0LK16; -.
DR   GeneID; 10042069; -.
DR   KEGG; tba:TERMP_01753; -.
DR   PATRIC; fig|391623.17.peg.1752; -.
DR   eggNOG; arCOG04435; Archaea.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   OrthoDB; 85849at2157; -.
DR   Proteomes; UP000007478; 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   NCBIfam; TIGR02751; PEPCase_arch; 1.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Pyruvate {ECO:0000313|EMBL:ADT84728.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007478}.
SQ   SEQUENCE   476 AA;  55184 MW;  6F1B7A38A3A4F235 CRC64;
     MIPKTMSTQH PDNVYIPFFA REPQLGGEDE IIEAFYAFSV LGIEEQMWDF EGKEVDEFVV
     KKLLERYPHF FRKHKLGEDF RLTPRVPNPS VEKAEAKLLL ETLESISRSA DYSKIFYGKE
     IAPIFEVILP MTTSANEINR VYDLYKRYIV GKQYKRVYDV KLYEWIGKFF PEEINVIPLF
     ETKDAILNSA EILREYLHGK DFEYQRVFLA RSDPAMNYGL ISAVVYDKYA LFKLQELEEE
     ESVSIYPIIG VGSAPFRGHL VPENVENVLE EYRGAQTFTI QSSFKYDNPP REVIKAVEKI
     KSSKRKEAEP INGQILLILR KYEIEYSKQI KALAKLVREV AKFVPSRRKR KLHIGLFGYA
     RDVNGFALPR AIKFTASLYS LGVPPEVLGL NALSEKDVEV ISNVYNGIYK DLSLAFRYFN
     PKSAEKFKFL RDILKMSQLF EFERNEEHCE ITNKILDGEI NEELIIKAAS IRGFLG
//