ID A9QPD2_METI4 Unreviewed; 931 AA. AC A9QPD2; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 04-NOV-2026, entry version 109. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595}; DE Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595}; DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595}; GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595, GN ECO:0000313|EMBL:ABX56590.1}; GN OrderedLocusNames=Minf_1739 {ECO:0000313|EMBL:ACD83793.1}; OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain OS V4)). OC Bacteria; Pseudomonadati; Verrucomicrobiota; Methylacidiphilae; OC Methylacidiphilales; Methylacidiphilaceae; OC Methylacidiphilum (ex Ratnadevi et al. 2023). OX NCBI_TaxID=481448 {ECO:0000313|EMBL:ABX56590.1}; RN [1] {ECO:0000313|EMBL:ABX56590.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=V4 {ECO:0000313|EMBL:ABX56590.1}; RX PubMed=18004300; DOI=10.1038/nature06411; RA Dunfield P.F., Yuryev A., Senin P., Smirnova A.V., Stott M.B., Hou S., RA Ly B., Saw J.H., Zhou Z., Ren Y., Wang J., Mountain B.W., Crowe M.A., RA Weatherby T.M., Bodelier P.L.E., Liesack W., Feng L., Wang L., Alam M.; RT "Methane oxidation by an extremely acidophilic bacterium of the phylum RT Verrucomicrobia."; RL Nature 450:879-882(2007). RN [2] {ECO:0000313|EMBL:ACD83793.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate V4, and V4 {ECO:0000313|EMBL:ACD83793.1}; RX PubMed=18593465; DOI=10.1186/1745-6150-3-26; RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V., RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F., RA Feng L., Wang L., Alam M.; RT "Complete genome sequence of the extremely acidophilic methanotroph isolate RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum RT Verrucomicrobia."; RL Biol. Direct 3:26-26(2008). CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source CC for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670, CC ECO:0000256|HAMAP-Rule:MF_00595}. CC -!- CATALYTIC ACTIVITY: CC Reaction=oxaloacetate + phosphate = phosphoenolpyruvate + CC hydrogencarbonate; 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|ARBA:ARBA00048995, ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00595}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}. CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. CC {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}. 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; EU223848; ABX56590.1; -; Genomic_DNA. DR EMBL; CP000975; ACD83793.1; -; Genomic_DNA. DR RefSeq; WP_012464075.1; NC_010794.1. DR AlphaFoldDB; A9QPD2; -. DR STRING; 481448.Minf_1739; -. DR KEGG; min:Minf_1739; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_0; -. DR OMA; AAAIPQC; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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_00595; PEPcase_type1; 1. DR InterPro; IPR021135; PEP_COase. DR InterPro; IPR022805; PEP_COase_bac/pln-type. DR InterPro; IPR018129; PEP_COase_Lys_AS. DR InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom. DR NCBIfam; NF000584; ppc; 1. DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR Pfam; PF00311; PEPcase; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR PROSITE; PS00781; PEPCASE_1; 1. PE 3: Inferred from homology; KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP- KW Rule:MF_00595}; Coiled coil {ECO:0000256|SAM:Coils}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595}; KW Pyruvate {ECO:0000313|EMBL:ABX56590.1}. FT COILED 128..155 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 161 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 589 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595" SQ SEQUENCE 931 AA; 107056 MW; 7AA27B536340B1FD CRC64; MSVRKQLSSL QRISPEHDFS LLSRTIHFLG DTLGKVITQL EGEKILSIEE TIRKLAKESR KGKEEATRKL SDIVRGLDID MAYRMAMAFT CYFELVNLAE ENYRVRILMK RRINQLNHPQ KAIPKESIES AISQLKKAKV KKEEIQEILE KMEIVLVFTA HPTEIKRQTI LNKLCEISSY LKKESFNSKP SPAIHSTVER LIASLWLTER SRSKNPQVLD EVRTGLWYFE HTLWDVIPEL HNELQRVLDI YYPGVTLKPK WISFGSWIGG DRDGNFQVTT KTTATTFILQ RNLALRKVSQ SLERLSEIFS ISSQRIPPTK KVIRLLNEKL KSFPSLKEEY ERYPNEPYRL VLLALKKEVE NSINKISEND LLDFFHDCKP DTTLKAITEV LEALKENFDA PQTRIFLEGE FQKLAQCIEV FGIHIFSLDI RQHSAIHEEA IEEILRLNGH PEISYALLDE KEKVGLLNKL LEGPLPSLHS LYNRASDKLK EVLGPILVFS RSIAILGKEV CGCYLISMTS GLSDILEVLY LCKICRCSID IAPLFETLSD LKSSPQTLQD LLSHPLYRKY LQERSDKQIV MLGYSDSNKD CGYMTSNWWL FQIQEKLHEV CRVHGVSLVL FHGRGGTIAR GGGPAAKAIL AQPKGLLEGK IRITEQGEVL STRYHDFDIA FRILEQTTYG VLLAIHKSRK KTILPKSWEK TIECIAEESY RAYTHLLHQE PDFLRFWQEV TPINEIGSLK IASRPIFRFR LNNFEDLRAI PWVFSWMQTR FVIPGWYGIG SSLKKVIETS PKALSILQKM YEKWTFFQTV IDNAQLSLAK TDIDIARLYC DLASDKNLAQ RIFSIIEAEY KKTVETILKI TLQNNILDHE PILQRSIQLR NPYVDPLNYI QVEMIKRNRA GQPPTALEID KIKSVIELTI NGISAGLRNT G //