ID   CAPP_SHEPA              Reviewed;         878 AA.
AC   A8GZ16;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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}; OrderedLocusNames=Spea_0225;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
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.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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;
CC         Evidence={ECO:0000255|HAMAP-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; CP000851; ABV85553.1; -; Genomic_DNA.
DR   RefSeq; WP_012153494.1; NC_009901.1.
DR   AlphaFoldDB; A8GZ16; -.
DR   SMR; A8GZ16; -.
DR   STRING; 398579.Spea_0225; -.
DR   PRIDE; A8GZ16; -.
DR   EnsemblBacteria; ABV85553; ABV85553; Spea_0225.
DR   KEGG; spl:Spea_0225; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000002608; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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_1000082435"
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;  98788 MW;  99574E9E96748401 CRC64;
     MVDMYASLRS NVGTLGQILG DTIRTDLDDT FLEKIEQIRH LAKSSRQGDD ASREEMLTLL
     SSLSDDELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVEQLLG RMLGGKIDQE
     KVLACLKTLD IDLVLTAHPT EISRRTLIQK YSAVIDSLTA LENTQLTEQE KKQHHLRLRQ
     LIAQIWHTNE IRNERPTPVD EARWGLSTIE ASLWQAIPDF LRQLNQQVEE RTNTQLPIDI
     APVRFSSWMG GDRDGNPFVT STVTQEVLDR NRHTAARLYL KDVVLLVNEL SMEGANEELL
     AYCNNSNEPY RDVLRDLRKK LRATIDYLNE KLEGHQPDVN PKDIIWHESD LKDPLMMLYK
     SLCDQGMSLI ANGLLLDMLR RIACFGIHML RLDVRQDAQR HADVIAELTR YLGMGDYAHW
     DESEKQSFLL RELSSKRPLI PANWQASAEV EEVVKTCRLV ASQPARAMGS YVISMASQPS
     DVLAVLLLLK ETGCPHPIRV VPLFETLDDL NNASNCMSAL FAIDWYRGYT KGIQEVMIGY
     SDSAKDAGVM AAAWAQYTAQ EKLVAISQEA NIKLTLFHGR GGTIGRGGGP AHQAILSQPP
     GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPEPKP EWRQCMQQLA
     DESVVAYRAI VREEPDFVSY FRAATPEIEL GKLPLGSRPA KRRVDGGIES LRAIPWIFAW
     SQNRLMLPAW LGAGEALKAA SERGDLALLQ EMEKHWPFFK TRISMLEMVY AKAEPNLSKF
     YETSLVPSEL HHLGVQLRER LATGVEAVLE LTQAESLMAH TPWNRESVEL RNPYIDPLNF
     LQAELLARTR REEQSSQNVE LALMLTIAGV AAGMRNTG