ID   CAPP_VIBVY              Reviewed;         877 AA.
AC   Q7MH68;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 101.
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=VV3004;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC95768.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000037; BAC95768.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011151288.1; NC_005139.1.
DR   AlphaFoldDB; Q7MH68; -.
DR   SMR; Q7MH68; -.
DR   STRING; 672.VV93_v1c27320; -.
DR   PRIDE; Q7MH68; -.
DR   EnsemblBacteria; BAC95768; BAC95768; BAC95768.
DR   KEGG; vvy:VV3004; -.
DR   PATRIC; fig|196600.6.peg.2981; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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..877
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166650"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   877 AA;  98927 MW;  6B9038A4BFD62002 CRC64;
     MNEKYAALKS NVSMLGHLLG NTIQEAHGDE ILEKVETIRK LSKSARAGNQ ADRNNLIEEI
     KSLPDEQLTP VARAFNQFLN LTNIAEQYHT ISRHCDAHVC EPDAINTLFA KLGQNGINKL
     DTAQAIRELN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSYKE RHKTEKRLEQ
     LIAQSWHSDV IRKQRPTPLD EAKWGFAVVE NSLWEAVPDF LRELDEKLKD YLDQGLPIDA
     RPVHFSSWMG GDRDGNPFVT HTVTREVLLL SRWKAADLYL KDINELISEL SMTKCNDTVR
     QLAGEDEHEP YRAILKQLRT LLSDTKEILD AKINGQKLAV KAPLQSVEQL WDPLFACYQS
     LRECGMSMIA EGSLLDTLRR VKAFGVHLVR LDIRQESTRH ADVLSELTRY LGIGDYNHWS
     EQDKIAFLTN ELASKRPLLP RDWQPSEPVK EVLDTCKIIA AQSREAFGAY VISMAKTASD
     VLAVHLLLQE SGCPYRMDVC PLFETLDDLN NAEAVIKQLM SIDLYRGFIQ NHQMVMIGYS
     DSAKDAGVMA AGWAQYHAME ALVNVAEQEG IELTLFHGRG GTIGRGGAPA HAALLSQPPK
     SLKGGLRVTE QGEMIRFKLG LPDVAVNSFN MYASAILEAN LLPPPEPKQE WRDLMEVLSQ
     VSCEAYRSVV RGEPDFVPYF RQATPELELG KLPLGSRPAK RNPNGGVESL RAIPWIFSWS
     QNRLLLPAWL GAGEAIQYSI DKGHQALLEE MCREWPFFST RLGMLEMVYL KCNSEISRYY
     DERLADKSLL PLGDRLRDQL QSDIKAVLNV ENNENLMQSD PWGQESIRLR NIYIEPLNML
     QAELLYRTRQ AGVVSEELEE ALMVTIAGIA AGMRNTG