ID CAPPA_METMA Reviewed; 526 AA. AC Q8PS70; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 111. 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=MM_3212; OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM OS 11833 / OCM 88) (Methanosarcina frisia). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=192952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88; RX PubMed=12125824; RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., RA Fritz H.-J., Gottschalk G.; RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer RT between Bacteria and Archaea."; RL J. Mol. Microbiol. Biotechnol. 4:453-461(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 --------------------------------------------------------------------------- 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; AE008384; AAM32908.1; -; Genomic_DNA. DR RefSeq; WP_011035107.1; NC_003901.1. DR AlphaFoldDB; Q8PS70; -. DR SMR; Q8PS70; -. DR GeneID; 82162315; -. DR KEGG; mma:MM_3212; -. DR PATRIC; fig|192952.21.peg.3732; -. DR eggNOG; arCOG04435; Archaea. DR HOGENOM; CLU_517433_0_0_2; -. DR Proteomes; UP000000595; 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..526 FT /note="Phosphoenolpyruvate carboxylase" FT /id="PRO_0000309604" SQ SEQUENCE 526 AA; 58177 MW; 7CCCE37156EF8B55 CRC64; MSKKATYPKV MCTQHPDSAS KYISTQEEPG EAIEAAVVFG CDEYMPDYEG KATPYHQNVQ IVSRFIEETD LIPGKDIFIT PRAPSAAQEN RFRQLMVMMS IAEANHGALE YSDVQAINEF VHPMTGTVGE ILDAQQHMVD VGELAKKEFG VAMEVPRIIP LIEDAPALLH AKELAENTLL SWEKRFGAAP EKFRVFLGKS DSALSFGHVA STLSCKYAIS GISELDLELD TSTGIIFGAG TLPFRGHLSL KNAENFFREY RGIGTITLQS AVRYSHDKGE AEALVRLAEE RLPESPEIYS GEEKEEIVNL IGIFGARYNR IIREMSCTIN QLAGLLPQQR DRLMHKGTGG YSRNVPDISG LVCLCRKDVG KELSASMPAE DLNLPRAIKF TGALYSIGLP PEFIGTGTAL EEAREKLGEE ACERLLKKYF PSLASDLSFA SGYLDLNVAS RFLPEACLKE IRKDIEVLRD TFSLKVQPEP SYRILLEMMQ PDLLQAGTKG NCMDEEVSQL VCSTLTKMGK IRKALG //