ID   CAPP_VIBPA              Reviewed;         877 AA.
AC   Q87L54;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   27-MAR-2024, entry version 100.
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=VP2761;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC61024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000031; BAC61024.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_799140.2; NC_004603.1.
DR   RefSeq; WP_005465143.1; NC_004603.1.
DR   AlphaFoldDB; Q87L54; -.
DR   SMR; Q87L54; -.
DR   GeneID; 1190311; -.
DR   KEGG; vpa:VP2761; -.
DR   PATRIC; fig|223926.6.peg.2657; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..877
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166648"
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;  99273 MW;  3A61D009D5493105 CRC64;
     MNEKYAALKS NVRMLGHLLG NTIRDAHGEE IFEKVETIRK LSKSAQAGNQ ADRESLIEEI
     KHLPDEQLTP VTRAFNQFLN LTNIAEQYHT ISRHCEEHIC EPDAINSLFS KLVQNDVSKL
     DTAQAVRDLN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSSKE RKKTERRLEQ
     LIAQSWHSDV IRQQRPTPLD EAKWGFAVVE NSLWEAVPDF LREMNDRLKS YLGEGLPIDA
     RPVHFSSWMG GDRDGNPFVT HSVTREVLLL SRWKAADLYL NDINELISEL SMTVSNDQVR
     ELAGEDQHEP YRAILKQLRA LLNETKDILD AKIHGQKLAV KAPLQKVEQL WDPLYACYQS
     LHECGMGVIA DGSLLDTLRR VKAFGVHLVR LDIRQESTRH ADVLSELTRY LGIGDYEQWS
     EQDKIAFLTN ELASKRPLLP RDWEPSEPVK EVLDTCKIIA LQPREAFGAY VISMARTASD
     VLAVHLLLQE AGCPYRMDVC PLFETLDDLN NAESVIKQLM SIDLYRGFIQ NHQMVMIGYS
     DSAKDAGVMS AGWAQYHAME SLVKVAEDEG VELTLFHGRG GTVGRGGAPA HAALLSQPPK
     SLKGGLRVTE QGEMIRFKLG LPDVAVNSFN LYASAILEAN LLPPPEPKQE WRDLMEVLSE
     VSCEAYRGVV RGEPDFVPYF RQATPELELG KLPLGSRPAK RNPNGGVESL RAIPWIFSWS
     QNRLVLPAWL GAGEAIQYSV DKGHQALLEE MCREWPFFST RLGMLEMVYT KCNMEISRYY
     DQRLVEPQLQ PLGDRLREQL QRDIKSVLNV ENNENLMQSD PWGQESIRLR NIYVEPLNML
     QAELLYRTRQ TEEASANLEE ALMVTIAGIA AGMRNTG
//