ID   D3S0D1_FERPA            Unreviewed;       476 AA.
AC   D3S0D1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=Ferp_2060 {ECO:0000313|EMBL:ADC66194.1};
OS   Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Ferroglobus.
OX   NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC66194.1, ECO:0000313|Proteomes:UP000002613};
RN   [1] {ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA   Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT   "Complete sequence of Ferroglobus placidus DSM 10642.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADC66194.1, ECO:0000313|Proteomes:UP000002613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX   PubMed=22180810; DOI=10.4056/sigs.2225018;
RA   Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA   Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA   Lovley D., Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL   Stand. Genomic Sci. 5:50-60(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}.
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DR   EMBL; CP001899; ADC66194.1; -; Genomic_DNA.
DR   RefSeq; WP_012966533.1; NC_013849.1.
DR   AlphaFoldDB; D3S0D1; -.
DR   STRING; 589924.Ferp_2060; -.
DR   PaxDb; 589924-Ferp_2060; -.
DR   GeneID; 8779594; -.
DR   KEGG; fpl:Ferp_2060; -.
DR   eggNOG; arCOG04435; Archaea.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   OrthoDB; 85849at2157; -.
DR   Proteomes; UP000002613; 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, ECO:0000313|EMBL:ADC66194.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Pyruvate {ECO:0000313|EMBL:ADC66194.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002613}.
SQ   SEQUENCE   476 AA;  54881 MW;  2E682501DEDD8658 CRC64;
     MVPRVMSTQH PDNANVPFFA RGEYLNGEDE VKEAYYVFSH FGCDEQMWDF EGKEVDDFVV
     RKLLSNYPDF FKKKPLGKCF RLTPRIPNPS VEKEEAKLLS EILEMIPRSY DYVKSFDIDH
     EPIFEVILPM TRTHEEVLRI YYFYKDFVAG KGKLSLRDGT KISEWLGEFK PEEIKVIPLL
     EDKNSLLNAE KIVSKIVEET GSENIRVFLA RSDPALNYGF VSATIYVKYA LMRLEDVNAE
     VYPILGVGSC PFRGGLSPKN LQPVDEFPSV ETFTVQSAFK YDYEFSEVRK AVERIKEKRR
     GKAEVIDEEH LKVAEKLTEA YRMRIPLIAN FVNSFSKNIP RRRMRKLHIG LFGYSRGEGV
     KLPRAITFCA ALYSIGFPPE LLGIAELSDK DYEVVTEVFR GFENMMREAL KYFNPNSLKV
     LNSKLEKDVE RAKELFEIEV DEEHEKVTNE IINTLGKGLD LKERVAEAGI LRGFLG
//