ID H8MKT9_CORCM Unreviewed; 872 AA. AC H8MKT9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 27-MAR-2024, entry version 52. 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:AFE09951.1}; GN OrderedLocusNames=COCOR_04769 {ECO:0000313|EMBL:AFE09951.1}; OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2) OS (Myxococcus coralloides). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Myxococcaceae; Corallococcus. OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE09951.1, ECO:0000313|Proteomes:UP000007587}; RN [1] {ECO:0000313|EMBL:AFE09951.1, ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; RX PubMed=22582372; DOI=10.1128/JB.00397-12; RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W., RA Sogaard-Andersen L.; RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus RT coralloides DSM 2259."; RL J. Bacteriol. 194:3012-3013(2012). RN [2] {ECO:0000313|Proteomes:UP000007587} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2 RC {ECO:0000313|Proteomes:UP000007587}; RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.; RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides RT DSM 2259."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. 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 = 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:0000256|ARBA:ARBA00001071, 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; CP003389; AFE09951.1; -; Genomic_DNA. DR AlphaFoldDB; H8MKT9; -. DR STRING; 1144275.COCOR_04769; -. DR KEGG; ccx:COCOR_04769; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_7; -. DR InParanoid; H8MKT9; -. DR Proteomes; UP000007587; 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 Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1. 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 PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1. DR Pfam; PF00311; PEPcase; 2. 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}; 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:AFE09951.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007587}. FT ACT_SITE 133 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 539 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595" SQ SEQUENCE 872 AA; 96148 MW; DE8F090B6F899876 CRC64; MGRLLGEVLV EQEGQALFDK EEEVRHLAIQ RRRGPVAGRR AAAAELAAVL RRLPSEQVEP VLRAFSVYFQ LVNLAEQHHR IRRARAHASP TATRPQKGSL ESTLLALKAA GVSADKVRET LGTLKVTLTF TAHPTQAVRR TLLEKLYRLA MLLEERDRCT LTPRESAANL TAMREEITAL WQTDELRRER PTVGDEVKNV HWYVEEMLAE PVARLPEALD WAFERAYGEP LGALDTPVRV HSWVGGDMDG NPLVTPEVFA DTLRAHRARG LRLLLRDVER LGGMLSQSER HARPTQELER SLEEDAKALP DVAKQQGPRT LGEPWRRKLR FMEERLTLAL EHVLARRQGR ESTLPAGAYR SPEALGDDLA VLERSLFAAR AEHAGLREVR RMSERVRALG LGLGELEVRA PAEDAVSAAA SFSGGPAPTE GGQRLLEVLA KLREGQDEGG ESVCRTLILS MASTADDVLA AFQCLKHAGL WDKERQCATV DVAPLFEQLG ALDGGPDVLR QLFAHPEYRQ HLKGRGVQEV MVGYSDSGKE VGLLAASAAL YRAQVALTQV ADENDVPLRL FHGRGETVAR GGGPAQTAIL ALPPGTVAGA YKATEQGEAM DHKYARPELT QRTLELVVGG VLLHTLDAQP RPSPEDESAF RAAFDALAES GRKAYRALVW EDPGFVEFFM KGTPVEEISA LPIGSRPSKR KAGGLDTLRA IPWSFAWTQT RAILPAWYGV GSALEESAAT PEGAALLQRM YKEWPFFRAV IDNVTMVLAK TDMAIAARYA KLAPASTRPL WLRIQQEHSR TRRAVKTITG EAKLLDNNPQ LQRSIALRNP YVDPMSFLQV ELLKRKRDGD AECDRPLLLA LNGIAAGMRN TG //