ID B2T1D0_PARPJ Unreviewed; 1075 AA. AC B2T1D0; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 97. 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}; DE Flags: Precursor; GN Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595}; GN OrderedLocusNames=Bphyt_1068 {ECO:0000313|EMBL:ACD15487.1}; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD15487.1, ECO:0000313|Proteomes:UP000001739}; RN [1] {ECO:0000313|EMBL:ACD15487.1, ECO:0000313|Proteomes:UP000001739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / LMG 22146 / PsJN RC {ECO:0000313|Proteomes:UP000001739}; RX PubMed=21551308; DOI=10.1128/JB.05055-11; RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.; RT "Complete genome sequence of the plant growth-promoting endophyte RT Burkholderia phytofirmans strain PsJN."; RL J. Bacteriol. 193:3383-3384(2011). 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; CP001052; ACD15487.1; -; Genomic_DNA. DR RefSeq; WP_012432115.1; NC_010681.1. DR AlphaFoldDB; B2T1D0; -. DR STRING; 398527.Bphyt_1068; -. DR KEGG; bpy:Bphyt_1068; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_4; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000001739; 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:ACD15487.1}. FT REGION 1..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..47 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 122..137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 285 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10111" FT ACT_SITE 727 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595, FT ECO:0000256|PROSITE-ProRule:PRU10112" SQ SEQUENCE 1075 AA; 117477 MW; F09767E7C26F0649 CRC64; MTSSGSARPA RRNTALPNAR AADAAQPAAS AIASAAASAT TAAESTSAKR AGKPAQAAHA AKAGKAAKTS TPVKTDKAVK AVKTGKTTQA AATVKAQKPA KAASAKIKVV ANAPQAPALQ AVAEQSPASA NTSAPKGNGR TREDKDHPLF QDIRYLGRLL GDVLREQEGD AVFDVVETIR QNAVRFRRED DSAAAQTLDK KLRSLSPEQT VSVVRAFSYF SHLANIAEDR HRNRRHRIHA LAGSTSQPGT IAHALERLVE ANAAATPVLQ QFFNDALIVP VLTAHPTEVQ RKSILDAQHD VARLLAERDQ QLTERERAHN EAMLRARVTS LWQTRMLRDS RLSVADEIEN ALSYYRATFL TEIPALYADI EEALTEHGID ARLPPFFQMG SWIGGDRDGN PNVTAETLEN AITRQAAVIF EHYMEQVHKL GAELSVSNLL AGASEALKEL AAISPDQSPH RTDEPYRRAL IGMYTRLAAS ARVRLGEGSV PVRSAGRGVA PIRAKPYDDS SEFVRDLHVL IDSLAEHHGA PLAAPRLSPL ARAAEVFGFH LASIDLRQSS DIHEAVIAEL LKRAGVEDDY AALTEEDKLK VLLAELAQPR SLRLPYAEYS DLVKSELGVL EEARITREKF GARAVRNYII SHTETVSDLV EVMLLQKETG LLRGRLGDAN DPAQAGLMVI PLFETIPDLR NAPHIMRDLI ALPGVDALIE HQGNEQEVML GYSDSNKDGG FLTSNWELYR AELALVSLFN ERGVTLRLFH GRGGTVGRGG GPTYQAILSQ PPGTVDGQIR LTEQGEVIAS KFGNPEIGRR NLETVVAATL EASLLPHDIA PAQLPAFEET MQQLSDAAMA SYRALVYETP GFKEYFFEST PIAEIAELNI GSRPASRKLQ DPKQRKIEDL RAIPWGFSWG QCRLLLTGWY GFGSAVATYL DSAPTDAERK SRLALLKKMH KTWPFFANLL SNMDMVLAKT DLAVASRYAA LVSDKKLRKH VFERIVAEWE RTSKVLSEIT GKSERLAENP LLARSIKNRF PYLDPLNHLQ VELLKRHRAG DTNARVRRGI HLSINGIAAG LRNTG //