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
//