ID CAPP_SHEHH Reviewed; 878 AA. AC B0TL90; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595}; DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595}; DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595}; DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595}; GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; GN OrderedLocusNames=Shal_4095; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00595}; CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP- CC 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; CP000931; ABZ78635.1; -; Genomic_DNA. DR RefSeq; WP_012279152.1; NC_010334.1. DR AlphaFoldDB; B0TL90; -. DR SMR; B0TL90; -. DR STRING; 458817.Shal_4095; -. DR KEGG; shl:Shal_4095; -. DR eggNOG; COG2352; Bacteria. DR HOGENOM; CLU_006557_2_0_6; -. DR OrthoDB; 9768133at2; -. DR Proteomes; UP000001317; 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; 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; Lyase; Magnesium. FT CHAIN 1..878 FT /note="Phosphoenolpyruvate carboxylase" FT /id="PRO_1000082434" FT ACT_SITE 138 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595" FT ACT_SITE 545 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595" SQ SEQUENCE 878 AA; 98771 MW; 028030C8F374DDDB CRC64; MVDMYASLRS NVGTLGQILG DTIRTDLDDT FLDKIEQIRH LAKSSRQGDS AARKEMLTLL SSLSDDELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVEQLLG RMLGGNIDQE KVLACLKTLD IDLVLTAHPT EISRRTLIQK YSAVIDSLTA QENTQLTEQE KKQHHLRLRQ LIAQIWHTNE IRNERPTPVD EARWGLCTIE ASLWQAVPDF LRQLNQQVEE RTNTQLPTDI APVRFSSWMG GDRDGNPFVT SAVTQEVLDR NRHTAARLYL KDVVLLVNEL SMEGANEALL AYTNNSNEPY RDVLRTLRQK LRNTIDYLNG RLEGQHPDVD PSEIIWHESD LKDPLMMLYQ SLCDRGMSLI ANGLLLDMLR RIACFGIHML RLDVRQDADR HADVIAELTR YLGMGDYAHW DETEKQSFLL RELSSKRPLI PANWQASPEV EEVVKTCRLV ATQPARAMGS YVISMASQPS DVLAVLLLLK ETGCPHPMRV VPLFETLDDL NNASACMSAL FSIDWYRGYT KGIQEVMIGY SDSAKDAGVM AAAWAQYTAQ EKLVAISQEA NIKLTLFHGR GGTIGRGGGP AHEAILSQPP GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPEPKP EWRQCMQQLA EESVLAYRAI VREEPDFVSY FRAATPEIEL GKLPLGSRPA KRRVDGGIES LRAIPWIFAW SQNRLMLPAW LGAGEALKAA SERGDLPLLQ EMEKHWPFFK TRISMLEMVY AKAEPNLSKF YETSLVPKEL HHLGVQLRER LAIGIEAVLE LTQAESLMAH TPWNRESVEL RNPYIDPLNF LQAELLARTR REEQSSKNVE LALMLTIAGV AAGMRNTG //