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Database: UniProt/TrEMBL
Entry: Q24XT7_DESHY
LinkDB: Q24XT7_DESHY
Original site: Q24XT7_DESHY 
ID   Q24XT7_DESHY            Unreviewed;       561 AA.
AC   Q24XT7;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   13-NOV-2013, entry version 62.
DE   RecName: Full=Acetolactate synthase;
DE            EC=2.2.1.6;
GN   OrderedLocusNames=DSY1366;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
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DR   EMBL; AP008230; BAE83155.1; -; Genomic_DNA.
DR   RefSeq; YP_517599.1; NC_007907.1.
DR   ProteinModelPortal; Q24XT7; -.
DR   STRING; 138119.DSY1366; -.
DR   EnsemblBacteria; BAE83155; BAE83155; DSY1366.
DR   GeneID; 3953996; -.
DR   KEGG; dsy:DSY1366; -.
DR   PATRIC; 21671117; VBIDesHaf65307_1523.
DR   eggNOG; COG0028; -.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; PGPCLIH; -.
DR   OrthoDB; EOG6KT2NW; -.
DR   ProtClustDB; CLSK2465803; -.
DR   BioCyc; DHAF138119:GHT5-1395-MONOMER; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
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:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; 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   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW   Transferase.
SQ   SEQUENCE   561 AA;  60138 MW;  94ACC0EB4289EF5B CRC64;
     MGNEKESTTY ATGAALLLDS LVQEGVEVMF GYPGGAVLPI YDALINSPIR HLLPRHEQTA
     IHAADAFARV SGKVGVCLAT SGPGATNLVT GIANAYMDSI PVVILTGQVP TSLLGTDSFQ
     EVDITGITLP ITKHSYLVKD PRQIPRIVKE AFYIASTGRP GPVLIDLPKN VLAATDVRPA
     PAELNLKSYK YFTKGNAGQI EEAARVIAQS QRPVLYAGGG VITAGASEIL QQVVERANLP
     VVTTLMGIGS LPTNHPNVLG MVGMHGTVTA NYAVDDCDLL IAIGVRFDDR VTSGLGHRFA
     TKAKIIHIDI DPAEIGKVAR TKVPIVGNAK LVLEELLSKV SKPEISPWWE QIRLWQEEKL
     KTDNPNLNPQ VIIETLGEIA GEETIVTTDV GQHQMWAAQG YPVPAPRHFI TSGGLGTMGF
     GLPAALGAQV AAPESTVFLV TGDGSFQMSI QELATAVQYQ LPVKIILMNN GVLGMVRQLQ
     MVFCDERYSQ IQLTANPDFI KIAEAYGIRG IRVTETSEVR NALLEAINHP GPVLMDFIIS
     EDEVVSPMVP PGKGLTEMLG W
//
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