ID   CAPPA_PICTO             Reviewed;         508 AA.
AC   Q6L0F3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=PTO0964;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828 / KAW 2/3).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=1122961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AE017261; AAT43549.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6L0F3; -.
DR   SMR; Q6L0F3; -.
DR   STRING; 263820.PTO0964; -.
DR   PaxDb; 263820-PTO0964; -.
DR   KEGG; pto:PTO0964; -.
DR   PATRIC; fig|263820.9.peg.1003; -.
DR   eggNOG; arCOG04435; Archaea.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   InParanoid; Q6L0F3; -.
DR   OrthoDB; 85849at2157; -.
DR   Proteomes; UP000000438; 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; Lyase; Magnesium.
FT   CHAIN           1..508
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000309606"
SQ   SEQUENCE   508 AA;  58714 MW;  2EE5AB862B179318 CRC64;
     MAIAMIPKTM STQHPDNAKM PAWASEKSMI RNDDEVEEAY QCYTIGIKEV MWDAEGKDVD
     THVLRKLISK NHEFFEKNVL GSDIFLTYRV PNPAIEGTER KVLTETLESI PVNYDVFNTV
     YKRDIPPIFE VILPFTTSSK DLLNIAKYYE KAVAARDEIE LYDNVMVKNI LGETKPKKIN
     IIPLIEDKDS MFNIDGIVKN FARAVSAKKM RVFIARSDPA MNYGMIPAVL MSKYAASRLC
     KMNDDIENYP IVGVGSSTFR GRFSPENIEK SLYEYSNYYT FTLQSAFKYD YPQDSVKNSI
     NIINRHERSF DYLEDYEEEI IKNAVNKYVI NYQKIIEKLA PAINNITMYL PKRRSRKLHI
     GLFGYSRSTG NVTLPRAISF VGAMYSMGLP PEIIGISSLL NMKDDELDII EKTYINLRSD
     IMESSSYLNY EVFDALKDVY KIDQETINMI KADVKYIENN YGIKSDLGYE RERHNYLSSL
     MNLAFKNHDF ENTRKYILDM ALIRKFIG
//