ID K0DJM2_9BURK Unreviewed; 1055 AA. AC K0DJM2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 24-JAN-2024, entry version 54. 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 ORFNames=BUPH_05369 {ECO:0000313|EMBL:AFT84977.1}; OS Paraburkholderia phenoliruptrix BR3459a. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT84977.1, ECO:0000313|Proteomes:UP000010105}; RN [1] {ECO:0000313|EMBL:AFT84977.1, ECO:0000313|Proteomes:UP000010105} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR3459a {ECO:0000313|EMBL:AFT84977.1, RC ECO:0000313|Proteomes:UP000010105}; RX PubMed=23144415; DOI=10.1128/JB.01821-12; RA de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G., RA Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I., RA Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M., RA Ribeiro de Vasconcelos A.T.; RT "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a RT Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa."; RL J. Bacteriol. 194:6675-6676(2012). 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; CP003863; AFT84977.1; -; Genomic_DNA. DR AlphaFoldDB; K0DJM2; -. DR STRING; 1229205.BUPH_05369; -. DR KEGG; bpx:BUPH_05369; -. DR PATRIC; fig|1229205.11.peg.960; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_4; -. DR Proteomes; UP000010105; 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:AFT84977.1}. FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..88 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 265 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 707 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 1055 AA; 115696 MW; C9CBC3EF429A5F87 CRC64; MTSSGSARSA RRNTASPNAS LDDAAASPAA ASSTVETAQP PKAKRATSGA KAANAAKAVK AEKTSAPVKA DKTVKTSKAD KSGEAAPSAK KGKAKAAGKA PVLQAVSEDT VMAAPKTNGR TRDDKDHPLF QDIRYLGRLL GDVLREQEGD AVFDVVETIR QTAVRFRRED DNAAAQTLDK KLRSLSPEQT VSVVRAFSYF SHLANIAEDR HRNRRHRIHA LAGSAAQPGS IAYALERLVE AGAAATPVLQ QFFNDALIVP VLTAHPTEVQ RKSILDAEHD VARLLAERDQ QLTDRERAQN ERMLRARVTS LWQTRMLRDS RLTVADEIEN ALSYYRATFL EEIPALYADI EEALKEHGLE ARLPPFFQMG SWIGGDRDGN PNVTAETLEH AIARQAEVIF EHYLEQVHKL GAELSVSNLL AGASDELKAL AEISPDRSPH RTDEPYRRAL IGMYTRLAAS ARVRLGEGAV PLRSAGRGAA PIRATPYDDA SEFVRDLHVL MDSLAAHHGA PLAAPRLAPL ARAAEVFGFH LASIDLRQSS DIHEAVIAEL LKRAGVHDDY AALDESAKLE VLLAELAQPR PLRLPYAEYS DLVKSELSVL EQARVTREKF GARAVRNYII SHTETVSDLV EVMLLQKETG LLQGQLGNAD NPAKAALMVI PLFETIPDLR NAPHIMRDLL ALPGADSIIE HQGNEQEVML GYSDSNKDGG FLTSNWELYR AELALVSLFN ERGITLRLFH GRGGTVGRGG GPTYQAILSQ PPGTVDGQIR LTEQGEVIAS KFGNPEIGRR NLETVVAATL EASLLPHGNA PADLPAFEET MQQLSDAAMA SYRALVYETP GFKEYFFEST PISEIAELNI GSRPASRKLQ DPKHRKIEDL RAIPWGFSWG QCRLLLTGWY GFGSAVAAYL DSAPSDAERG RRLSLLKKMH KSWPFFSTLL SNMDMVLAKT DLAVASRYAA LVSDKKLRKH VFERIVAEWE RTSKVLSEIT GKRERLAENP LLARSIKNRF PYLDPLNHLQ VELLKRHRAG DTNARVRRGI HLTINGIAAG LRNTG //