CAPPA_PYRFU
ID CAPPA_PYRFU Reviewed; 472 AA.
AC Q8TZL5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=PF1975;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL82099.1; -; Genomic_DNA.
DR RefSeq; WP_011013117.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZL5; -.
DR SMR; Q8TZL5; -.
DR STRING; 186497.PF1975; -.
DR PRIDE; Q8TZL5; -.
DR EnsemblBacteria; AAL82099; AAL82099; PF1975.
DR GeneID; 41713797; -.
DR KEGG; pfu:PF1975; -.
DR PATRIC; fig|186497.12.peg.2048; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR OMA; QSAFRYD; -.
DR OrthoDB; 23334at2157; -.
DR PhylomeDB; Q8TZL5; -.
DR BRENDA; 4.1.1.31; 5243.
DR Proteomes; UP000001013; 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; Reference proteome.
FT CHAIN 1..472
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309612"
SQ SEQUENCE 472 AA; 54315 MW; 430BB52B442C6897 CRC64;
MIPRIMSTQH PDNYSIPFFA SSPILEGEDE ITEAFYAFSV LGADEQMWDF EGKEVDEFVV
KKLLERYPTF FKNNILGKDI RLTPRVPNPS VEKEEAKLLL ETLQGIARSA DYARIFYGDN
IAPIFEVILP MTTSVEEIER VYWLYKKAVV WISREKIYDI TVREWIGDFF PEKINVIPLF
ETKSALIKAA KITEAYILNR KNDIEYQRVF FARSDPAMNY GLITAVTYVK RALYEVLKVE
EELSIPIYPI IGVGGPPLRG GMRPDNVDAV VKEYPSVQTF TIQSSFKYDY PTKDVVKAVE
KIKSTKRKLP IPVEIPPFLV NYEAEYQKQI RILAPYINSV AKRIPRRRKR KLHIGLFGYS
RNVNGITLPR AITFTAALYS IGIPPELLAL NSLTDSQLET ISEYYINVYE DLEFAMRFFS
PKVAEKVGLK ELAERVKEFK PEQIPEYIEE AEIVFKGEGD VMKLAQLRGF LG
