GenomeNet

Database: UniProt
Entry: U3C6H9_9VIBR
LinkDB: U3C6H9_9VIBR
Original site: U3C6H9_9VIBR 
ID   U3C6H9_9VIBR            Unreviewed;       879 AA.
AC   U3C6H9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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:GAD77004.1};
GN   ORFNames=VAZ01S_057_00390 {ECO:0000313|EMBL:GAD77004.1};
OS   Vibrio azureus NBRC 104587.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219077 {ECO:0000313|EMBL:GAD77004.1, ECO:0000313|Proteomes:UP000016567};
RN   [1] {ECO:0000313|EMBL:GAD77004.1, ECO:0000313|Proteomes:UP000016567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 104587 {ECO:0000313|EMBL:GAD77004.1,
RC   ECO:0000313|Proteomes:UP000016567};
RA   Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA   Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT   "Whole genome shotgun sequence of Vibrio azureus NBRC 104587.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD77004.1}.
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; BATL01000057; GAD77004.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3C6H9; -.
DR   STRING; 1219077.VAZ01S_057_00390; -.
DR   eggNOG; COG2352; Bacteria.
DR   Proteomes; UP000016567; Unassembled WGS sequence.
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};
KW   Pyruvate {ECO:0000313|EMBL:GAD77004.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016567}.
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   879 AA;  99609 MW;  3E73AD949EB209D5 CRC64;
     MTMNEKYAAL KSNVRMLGHL LGNTIRDAHG EEIFEKVETI RTLSKSAQAG NQADRESLIE
     EIKSLPDEQL TPVTRAFNQF LNLTNIAEQY HTISRHCEEH VCEPDAMNTL FSKLVQNKVS
     KLDTAQAVKD LNIELVLTAH PTEITRRTMI NKLVKINECL SKLELSDLSF KERKKTERRL
     EQLIAESWHS DVIRQQRPTP LDEAKWGFAV VENSLWEAVP EFLREMNDRL KPYLGEGLPI
     DARPVHFSSW MGGDRDGNPF VTHSITREVL LLSRWKAADL YLNDINELIS ELSMTVCNEN
     VRQLAGEDAH EPYRAILKQL RSLLIESKDI LDAKIHGQQL AVKAPLRNVQ QLWEPLYACY
     KSLTECGMTV IANGSLLDTL RRVKAFGVHL VRLDIRQEST RHADALSELT RYLGIGDYEQ
     WSEQDKVAFL TNELASKRPL LPRDWEPSEP VKEVLDTCKI IAAQPREAFG AYVISMARTA
     SDVLAVHLLL QEAGCPYRMD VCPLFETLDD LNNAESVIQQ LMGIDLYRGF IQNHQMVMIG
     YSDSAKDAGV MSAGWAQYHA MESLVKVAEN EGIELTLFHG RGGTIGRGGA PAHAALLSQP
     PKSLKGGLRV TEQGEMIRFK LGLPDVAVNS FNLYASAILE ANLLPPPEPK QEWRELMEVL
     SQVSCEAYRR VVRDEPDFVP YFRQATPELE LGKLPLGSRP AKRNPNGGVE SLRAIPWIFS
     WSQNRLVLPA WLGAGEAIQY SINQGHQALL EEMCREWPFF STRLGMLEMV YSKCNIDISR
     YYDQRLADES LLPLGERLRE QLQQDIKAVL NVENNENLMQ RNPWGLESIR LRNIYVEPLN
     MLQAELLYRT RQTEQPSTHL EEALMVTIAG IAAGMRNTG
//
DBGET integrated database retrieval system