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Database: UniProt
Entry: D4ZCU4_SHEVD
LinkDB: D4ZCU4_SHEVD
Original site: D4ZCU4_SHEVD 
ID   D4ZCU4_SHEVD            Unreviewed;       551 AA.
AC   D4ZCU4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   25-APR-2018, entry version 57.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   Name=ilvG {ECO:0000313|EMBL:BAJ03839.1};
GN   OrderedLocusNames=SVI_3868 {ECO:0000313|EMBL:BAJ03839.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 /
OS   DSS12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ03839.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E.,
RA   Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M.,
RA   Kato C., Oshima T., Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella
RT   violacea, a psychrophilic and piezophilic bacterium from deep sea
RT   floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; AP011177; BAJ03839.1; -; Genomic_DNA.
DR   RefSeq; WP_013053131.1; NC_014012.1.
DR   STRING; 637905.SVI_3868; -.
DR   EnsemblBacteria; BAJ03839; BAJ03839; SVI_3868.
DR   KEGG; svo:SVI_3868; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; FRPLCKF; -.
DR   OrthoDB; POG091H02KO; -.
DR   BioCyc; SVIO637905:G1GKA-3698-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002350; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002350};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN        1    162       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      186    319       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      374    522       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   551 AA;  59701 MW;  ADC067E086170E0D CRC64;
     MRGADAVIKV LVDHGVTNIF GYPGGAIMPI YDALYGAPVE HLLSRHEQGA AFAALGYARA
     TGKTGVCFAT SGPGATNLVT SLADALLDSV AVVAITGQVS TAVIGTDAFQ EIDVLGMSLS
     CTKHSFMVTD IDQLVPTLYK AFEIAASGRP GPVLVDIPKD IQIAMFEYFT PIQEKYPQPE
     AEACKLDDAL TLLKQAKKPM LYVGGGVGMA RAVPQLREFI KLTGVPSVAT LKGLGTIEKE
     TSGYLGMLGM HGSKAANIAV QECDLLIVVG ARFDDRVTGR LASFAEHAKV IHLDIDAAEL
     GKLRLPEVAI AGDLRQILPV LATELNIAPW REEVAQLKAD HKWKYDRPGE LIFAPAMLNR
     LADKLPQDSV VTCDVGQHQM WVAQHMWFRN PEDHLSSSGL GTMGFGLPAG IGAKVSRPDA
     TVVVVSGDGS FMMNVQELTT IKRRKLAVKI LLIDNQKLGM VKQWQQLFFE ERYSETDLSD
     NPDFVTLASA FDIPGRTITT TAEVEEALDH LVNCEGPYLL HVRIDDAHNV WPLVPPGASN
     RDMMEEMDKQ T
//
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