CAPP_VIBA3
ID CAPP_VIBA3 Reviewed; 876 AA.
AC B7VLL5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 58.
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=VS_2890;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) 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; FM954972; CAV20187.1; -; Genomic_DNA.
DR RefSeq; WP_012604959.1; NC_011753.2.
DR AlphaFoldDB; B7VLL5; -.
DR SMR; B7VLL5; -.
DR STRING; 575788.VS_2890; -.
DR EnsemblBacteria; CAV20187; CAV20187; VS_2890.
DR KEGG; vsp:VS_2890; -.
DR PATRIC; fig|575788.5.peg.4100; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000009100; 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 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_1000146982"
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; 98877 MW; 71DFEEDD8A955F88 CRC64;
MNEKYAALKS NVSMLGRLLG NTIQDAHGDV ILEKVETIRK LSKSARAGNK ADRDSLVEEI
KNLPNEQLTP VARAFNQFLN LTNMAEQYHT ISRHCEEHVC EPDVLQSLFS KLNQNDISKL
DAAQAVRDLN IELVLTAHPT EITRRTMINK LVKINECLSK LELSDLSHKE RAKTERRLEQ
LIAQGWHSDV IRQQRPTPLD EAKWGFAVVE NSLWEAVPDF LREMDGRLKG YLGEGLPIDA
RPVHFSSWMG GDRDGNPFVT HTITKEVLRL SRWKAADLYL GDVNELITEL SMTKCNDAVR
ELAGDEHEAY RAILKSLRTL LNNTLEVLDA KLHDAEVPKK ETLQNIDQLW TPLYACYQSL
HECGMGVIAD GSLLDTLRRL KAFGVHLVRL DVRQESTRHS DVLSELTRYL GIGDYDQWSE
QDKVAFLTNE LSSKRPLLPR DWEPSEQVKE VLDTCKVVAA QPREAFGAYV ISMARTASDV
LAVHLLLQEC GCPYRMDVCP LFETLDDLNN SEAVMKQLMS IDLYRGFIQN HQMVMIGYSD
SAKDAGVMSA GWAQYDAMDK LVKACEEEGI ELTLFHGRGG TVGRGGAPAH AALLSQPPKS
LKGGLRVTEQ GEMIRFKLGL PDVAVNSFNL YASAILEANL LPPPEPKQEW RDLMEVLSEV
SCEAYRNVVR GEEKFVPYFR QATPELELGK LPLGSRPAKR NPNGGVESLR AIPWIFSWSQ
NRLVLPAWLG AGEAIQYSVD QGHQALLEEM CREWPFFSTR LGMLEMVYSK CNMEIAKYYD
QRLVDEELLP LGELLREQLQ KDIKAVLNVE NNENLMQSDP WGLESIRLRN IYVEPLNMLQ
AELLYRTRKC ETPPAELEEA LMVTIAGIAA GMRNTG