ID CAPPA_METAC Reviewed; 526 AA. AC Q8TMG9; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, 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}; GN OrderedLocusNames=MA_2690; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., RA Zinder S.H., Lander E., Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and RT physiological diversity."; RL Genome Res. 12:532-542(2002). 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAM06068.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE010299; AAM06068.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_011022649.1; NC_003552.1. DR AlphaFoldDB; Q8TMG9; -. DR SMR; Q8TMG9; -. DR STRING; 188937.MA_2690; -. DR EnsemblBacteria; AAM06068; AAM06068; MA_2690. DR GeneID; 1474582; -. DR KEGG; mac:MA_2690; -. DR HOGENOM; CLU_517433_0_0_2; -. DR InParanoid; Q8TMG9; -. DR OrthoDB; 85849at2157; -. DR PhylomeDB; Q8TMG9; -. DR Proteomes; UP000002487; 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; Reference proteome. FT CHAIN 1..526 FT /note="Phosphoenolpyruvate carboxylase" FT /id="PRO_0000309602" SQ SEQUENCE 526 AA; 58335 MW; 8FB2AC2F5BED5CFD CRC64; MSRKSTYPKV MCTQHPDSAS RYISTQEEPG EAIEAAVVFG CDEYMPDYEG KATPYHQNVQ IVSRLIEETD LVPGKDVFIT PRAPSAVQEN RFRQLMVMMS IAEANHGALE YSDVQAINEF VHPMTGTVRE ILDAQQHMVD VSELAKKEFG FAMEVPRIIP LIEDAPALLH AKELTENTLL AWKERFGTVP EKFRVFLGKS DSALSFGHVA STLSCKYAIN GLSELNFELE TETGIVFGAG TLPFRGHLDL KNAENFFREY RGIGTITLQS ALRYSHEKGD AEALVDLAKE KLPEIPELFS AEEKEELVNL IGIFGTRYSL IIRELASTIN RLSDLLPQQR DRLMHRGSGG YSRSAPDISG IVSLCRTDIG KELLASMPAE DLHLPRAIKF TGALYSIGLP PEFIGTGAAL NEAREKLGDE ACERLLTKYF PSLVSDLNFA TGYLDLNVAS RFLSGACFKE VSKDIEILHE TLGLETHPEP SYRILLEMMQ PELLQAGTSG NCMDEEVSQL VCSTLTKMGK IRKALG //