ID   CAPPA_METBF             Reviewed;         526 AA.
AC   Q469A3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=Mbar_A2632;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71539.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q469A3; -.
DR   SMR; Q469A3; -.
DR   STRING; 269797.Mbar_A2632; -.
DR   PaxDb; 269797-Mbar_A2632; -.
DR   KEGG; mba:Mbar_A2632; -.
DR   eggNOG; arCOG04435; Archaea.
DR   HOGENOM; CLU_517433_0_0_2; -.
DR   OrthoDB; 85849at2157; -.
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..526
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000309603"
SQ   SEQUENCE   526 AA;  58068 MW;  A08490FAE19B6E42 CRC64;
     MSRKTVFPKV MCTQHPDSAS KYIATQEEPG EAIEAAQIFG CDEYMPDYEG KATPYHQNVQ
     VVSKFIEETD LIPGKDIIIT PRAPSAVQEN QFRQLMVMMS IAEANYNALE YSDVQAINEF
     VHPMTDSVRE IIGAQQHMVD VSELAKKEFG FSMEVPCIIP LIEDAPALLH AKELAENTLF
     AWKGHFGTVP DKFRVFLGKS DSALSFGHVA STLSCKYAIN GICELNSELD TQTGIIFGAG
     TLPFRGHLDL MNAENFFKEY RGVGTITLQS ALRYSHKKGD AESLVKLAKA RLPETPELFS
     AEEKEEIINL IGIFGASYSR IIRQLAPTIN RIADLLPQQR DRLMHKGTGG YSRSAPDISG
     LVNLCRTDIG KELEASMPAE DLQLPRAIKF TGALYSIGLP PEFIGTGRAL EEAREKLGEA
     ACENLLTKYF PSLAGDLNFA SEYLDLNVAS RFLSSECLKE VSKDLDILHG AFALETSPEP
     SYRILVEMMQ PDLLQAGSRG NCMDEEVSQL VCSTLTKMGK IRKALG
//