ID Q0K7M4_CUPNH Unreviewed; 1012 AA. AC Q0K7M4; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 108. 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:CAJ93997.1}; GN OrderedLocusNames=H16_A2921 {ECO:0000313|EMBL:CAJ93997.1}; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ93997.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ93997.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337 {ECO:0000313|Proteomes:UP000008210}; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). 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; CC Evidence={ECO:0000256|ARBA:ARBA00001946, 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; AM260479; CAJ93997.1; -; Genomic_DNA. DR RefSeq; WP_010813833.1; NZ_CP039287.1. DR AlphaFoldDB; Q0K7M4; -. DR STRING; 381666.H16_A2921; -. DR GeneID; 57645045; -. DR KEGG; reh:H16_A2921; -. DR PATRIC; fig|381666.6.peg.3317; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_4; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000008210; Chromosome 1. 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; IPR033129; PEPCASE_His_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; 1. DR PRINTS; PR00150; PEPCARBXLASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR PROSITE; PS00781; PEPCASE_1; 1. DR PROSITE; PS00393; PEPCASE_2; 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:CAJ93997.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008210}. FT REGION 1..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..65 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 215 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 662 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 1012 AA; 112160 MW; D5765D8914ECE8D1 CRC64; MTQHAARPNG RRTAPAAKDQ SPALGAAQGD ANGASAAEPK RPASRSGTKR SPKPKLSIVS SNGTTIAPTA RRTADKDVPL REDIRFLGRL LGECLREQEG DAAFEVVETI RQTAVRFRRE NDRAAGAELD RLLKRLSRDQ TNQVVRAFSY FSHLANIAED QHHNRRRRVH ALAGSPPQAG SLAHALEAID AAGVTGKQLR KFLDEALIVP VLTAHPTEVQ RKSILDAERE IARLLAERDL PMTARERDHN TAQLRAKVTT LWQTRMLRDS RLTVADEIEN ALSYYRTCFL RGIPQLMSEL EEDIAAVFPT TRKRKGTPGA QPAPLAPFLQ MGSWIGGDRD GNPNVTAETL EHAASQQGQM IIDWYLDEVH ALGAELSMST LMVDASPELL ALAERSPDHS EHRADEPYRR ALIGIYARLA ATSKALTGHA VPRRPVAPAE PYDSAEAFAA DVQVVVDSLR ANHGQALANG RIEALARAIG VFGFHLASVD MRQVSDVHEA VIAELFAAAG IAPDYAALPE ARKLELLLAE LRQPRLLTLP WHEYSEQTRK ELAIFAAARE LRARYGKRIA RNYIISHTET LSDLVEVMLL QKESGMLQGT LGSKTDPARM ELMVIPLFET IEDLRNAAGI MQSLLDLPGF DSVIAHHGVE QEVMLGYSDS NKDGGFLTST WELYKAELEL VQLFEQRQVK LRLFHGRGGT VGRGGGPTYQ AILSQPPGTV NGQIRLTEQG EIINSKFANA EIGRRNLETV VAATLEASLL PQQNAPKDLD MFEAVMQQLS DRAFTAYRDL VYETPGFKDY FFATTPITEI ADLNLGSRPA SRKLMDKKNR RIEDLRAIPW GFSWGQCRLL LPGWYGFGSA VKSLLDTAPD DKARKLAVTT LRRMVKTWPF FSTLLSNMDM VLAKTDLAVA SRYAQLCDDA ALRRTVFNRI SKEWHLTCEM LTLVTGHQER LADNPLLARS IKNRFAYLDP LNHLQVELLK RYRSGKDGDD IRVRRGIHLT INGVAAGLRN TG //