CAPPA_PYRCJ
ID CAPPA_PYRCJ Reviewed; 459 AA.
AC A3MVZ5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
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}; OrderedLocusNames=Pcal_1392;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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: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; EC=4.1.1.31;
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_01904}.
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DR EMBL; CP000561; ABO08812.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MVZ5; -.
DR SMR; A3MVZ5; -.
DR STRING; 410359.Pcal_1392; -.
DR EnsemblBacteria; ABO08812; ABO08812; Pcal_1392.
DR KEGG; pcl:Pcal_1392; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR OMA; QSAFRYD; -.
DR Proteomes; UP000001431; 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; Lyase; Magnesium.
FT CHAIN 1..459
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309609"
SQ SEQUENCE 459 AA; 51305 MW; 21A5EFFEC819907D CRC64;
MPIPRLMCTQ HPDTTVKITA AEEVDEAIVA FTAYGCDEVM VDYEGKATPY SQPKEVVMKA
AKSELPLGEK FVITVRLPNP RLEEFDRAML ALEAAVVANY FSVKYMGVRA VKWVVLPMVE
DVETMSLVRR MLKRKVEDYK AEAKVDVGNI EVIPLFEDAF VQLKAKALLG EVFKGEEVRE
VRLFLGKSDS AVKHGHLASA LAIAYTLSRL GDVESELGLR IRPILGMGSP PFRGGLNNPR
LAPMEVVQYA GYYTATIQSA VRYDVALEEF LKVREAILNG CCAPRQRAPD EVLHIVQEAS
ARYRALVMKY ADKVIEVARL VPSTRDRVSW TAYGRTLTGG ERVVNMPRAI VYTSAWYATG
LPPTLLDAPY LLELAKSDKL DLVLKVLPTY LKELEYDLEF FDRATAEKYL DGEIVKAVVE
LADYLGLEAR PNPAYATLLR MPRNEANIIA LGKYRKFLG
