ID   CAPP_VIBCH              Reviewed;         876 AA.
AC   Q9KNT4;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   25-MAY-2022, entry version 107.
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=VC_2646;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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=AAF95787.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE003852; AAF95787.1; ALT_INIT; Genomic_DNA.
DR   PIR; D82049; D82049.
DR   RefSeq; NP_232274.2; NC_002505.1.
DR   RefSeq; WP_001003592.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KNT4; -.
DR   SMR; Q9KNT4; -.
DR   STRING; 243277.VC_2646; -.
DR   DNASU; 2615663; -.
DR   EnsemblBacteria; AAF95787; AAF95787; VC_2646.
DR   GeneID; 57741246; -.
DR   KEGG; vch:VC_2646; -.
DR   PATRIC; fig|243277.26.peg.2524; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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..876
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166646"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        543
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   876 AA;  98317 MW;  BB7EC7C28CF08B4C CRC64;
     MNEKYAALKS NVSMLGRLLG QTIQAADGDV ILAKVETIRK LSKSARAGNQ ADRELLIEEI
     KNLPNHQLTP VARAFNQFLN LTNIAEQYHT ISRHCESHVN ELDAIGSLFA KLAQKSVSKF
     DTAQAIRDLN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSPKE RHKTERRLEQ
     LIAQSWHSDV IRQQRPTPLD EAKWGFAVVE NSLWHAVPEF LRELDEQVKS YLGEGLPIDA
     RPVHFSSWMG GDRDGNPFVT HTITREVLLL SRWKAADLYL TDINELVSEL SMTKCNEAVR
     ALAGEEHEPY RAILKPIRSL LQETIEILDA KLNGQKLAVK APLQTADQLW EPLYACYQSL
     HECGMGVIAD GSLLDTLRRI KAFGVHLVRL DVRQESSRHA EVISELTRHL GIGDYNQWSE
     QDKIAFLTTE LNSKRPLLPR DWQPSPQVKE VLDTCKIIAA QSKDAFGAYV ISMARTASDV
     LAVHLLLQEA GCPYRMDVCP LFETLDDLNN AESVIRQLMN IDLYRGFIQN HQMVMIGYSD
     SAKDAGVMAA GWAQYRAMEA LVKVGEEAGI ELTLFHGRGG TIGRGGAPAH AALLSQPPKS
     LKGGLRVTEQ GEMIRFKLGL PEVAVNSFNM YASAILEANL LPPPEPKNEW RALMDILSEI
     SCNAYRKVVR GEPDFVPYFR QATPELELGK LPLGSRPAKR NPTGGVESLR AIPWIFSWSQ
     NRLILPAWLG AGEAIQIAIN EGHQALLEEM CREWPFFSTR LGMLEMVYTK CSVSIACHYD
     ERLVEPTLRP LGEKLRAQLQ QDIKVVLNVE NNENLMQSDP WGQESIRLRN IYIEPLNMLQ
     AELLYRTRQS ELPAPELEEA LMVTIAGIAA GMRNTG