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Database: UniProt/TrEMBL
Entry: C3LRV7_VIBCM
LinkDB: C3LRV7_VIBCM
Original site: C3LRV7_VIBCM 
ID   C3LRV7_VIBCM            Unreviewed;       887 AA.
AC   C3LRV7;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:ACP06862.1};
GN   OrderedLocusNames=VCM66_2566 {ECO:0000313|EMBL:ACP06862.1};
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP06862.1, ECO:0000313|Proteomes:UP000001217};
RN   [1] {ECO:0000313|EMBL:ACP06862.1, ECO:0000313|Proteomes:UP000001217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2 {ECO:0000313|EMBL:ACP06862.1,
RC   ECO:0000313|Proteomes:UP000001217};
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP001233; ACP06862.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3LRV7; -.
DR   KEGG; vcm:VCM66_2566; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001217; 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   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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        554
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   887 AA;  99644 MW;  8CE06221BA3F28EA CRC64;
     MDVIFFQGRM TMNEKYAALK SNVSMLGRLL GQTIQAADGD VILAKVETIR KLSKSARAGN
     QADRELLIEE IKNLPNHQLT PVARAFNQFL NLTNIAEQYH TISRHCESHV NELDAIGSLF
     AKLAQKSVSK FDTAQAIRDL NIELVLTAHP TEITRRTMIN KLVKINECLS KLELSDLSPK
     ERHKTERRLE QLIAQSWHSD VIRQQRPTPL DEAKWGFAVV ENSLWHAVPE FLRELDEQVK
     SYLGEGLPID ARPVHFSSWM GGDRDGNPFV THTITREVLL LSRWKAADLY LTDINELVSE
     LSMTKCNEAV RALAGEEHEP YRAILKPIRS LLQETIEILD AKLNGQKLAV KAPLQTADQL
     WEPLYACYQS LHECGMGVIA DGSLLDTLRR IKAFGVHLVR LDVRQESSRH AEVISELTRH
     LGIGDYNQWS EQDKIAFLTT ELNSKRPLLP RDWQPSPQVK EVLDTCKIIA AQSKDAFGAY
     VISMARTASD VLAVHLLLQE AGCPYRMDVC PLFETLDDLN NAESVIRQLM NIDLYRGFIQ
     NHQMVMIGYS DSAKDAGVMA AGWAQYRAME ALVKVGEEAG IELTLFHGRG GTIGRGGAPA
     HAALLSQPPK SLKGGLRVTE QGEMIRFKLG LPEVAVNSFN MYASAILEAN LLPPPEPKNE
     WRALMDILSE ISCNAYRKVV RGEPDFVPYF RQATPELELG KLPLGSRPAK RNPTGGVESL
     RAIPWIFSWS QNRLILPAWL GAGEAIQIAI NEGHQALLEE MCREWPFFST RLGMLEMVYT
     KCSVSIACHY DERLVEPTLR PLGEKLRAQL QQDIKVVLNV ENNENLMQSD PWGQESIRLR
     NIYIEPLNML QAELLYRTRQ SELPAPELEE ALMVTIAGIA AGMRNTG
//
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