ID   CAPP_SHESH              Reviewed;         878 AA.
AC   A8G1A9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Ssed_4278;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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}.
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DR   EMBL; CP000821; ABV38882.1; -; Genomic_DNA.
DR   RefSeq; WP_012144611.1; NC_009831.1.
DR   AlphaFoldDB; A8G1A9; -.
DR   SMR; A8G1A9; -.
DR   STRING; 425104.Ssed_4278; -.
DR   KEGG; sse:Ssed_4278; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002015; 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; Reference proteome.
FT   CHAIN           1..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000082436"
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;  98847 MW;  E761A242354DC8D1 CRC64;
     MADMYASLRS NVGTLGQILG ETIRTNLDDA FLEKIEQIRQ LAKSSRQGDE AARDEMLKLL
     TALPDNELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVEQLLG RVLSSNIDQE
     KMLDCLENLD IDLVLTAHPT EISRRTLIQK YASVIDILAA LENPQLTERE KKQQHLRLRQ
     LIAQIWHTNE IRNERPTPVD EARWGLSTIE VSLWQAIPDF LRQLNEQVEE RTGKQLPTDI
     APVRFSSWMG GDRDGNPFVT AKVTQEVLDR NRHTAARLYL KDIVVLVNDL SVEEANAELL
     EYTNNSLEPY RDVLKDLRQK LRNTVDYLNA RLEGHSPEID LSSIIWHESD LKEPLLMLYR
     SLTDSGMSLI AHGLLLDILR RIACFGIHML RLDIRQDAER HSDVIAELTR YLGMGDYNHW
     DESEKQAFLL RELTGKRPLI PSNWQPSDDV AEVVSTCRLI ATQPARALGS YVISMASKPS
     DVLTVLLLLK ETGCPHPMRV VPLFETLDDL NNASSCMTAL FAIDWYRGYT KGHQEVMIGY
     SDSAKDAGVM AAAWAQYHAQ EELVEVSRQA EVKLTLFHGR GGTIGRGGGP AHEAILSQPP
     GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPEPKP EWRACMQKLA
     EESVDAYRSI VRDEPDFVAY FRAATPEVEL GKLPLGSRPA KRRVDGGIES LRAIPWIFAW
     SQNRLMLPAW LGAGEALQAA SDRGEMALLQ EMEQDWPFFK TRISMLEMVY AKAEPNLAKY
     YETCLVPENL HHLGEALRTR LATGIKAVLE LTQSNALMEH TPWNRESVTL RNPYIDPLNF
     VQAELLARTR KEEEASTNVE LALMITIAGV AAGMRNTG
//