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   25-MAY-2022, entry version 72.
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=Shal_4095;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; 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;
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; 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   EnsemblBacteria; ABZ78635; ABZ78635; Shal_4095.
DR   KEGG; shl:Shal_4095; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
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   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.
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