ID Q24XT7_DESHY Unreviewed; 561 AA.
AC Q24XT7;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 01-MAY-2013, entry version 59.
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; ERYEYVY; -.
DR ProtClustDB; CLSK2465803; -.
DR BioCyc; DHAF138119:GHT5-1367-MONOMER; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA: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 PANTHER; PTHR18968:SF13; PTHR18968:SF13; 1.
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
//
