ID Q67KX7_SYMTH Unreviewed; 571 AA.
AC Q67KX7;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 67.
DE RecName: Full=Acetolactate synthase;
DE EC=2.2.1.6;
GN OrderedLocusNames=STH2684;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Clostridiales;
OC Clostridiales Family XVIII. Incertae Sedis; Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T.,
RA Morimura K., Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable
RT bacterium that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AP006840; BAD41669.1; -; Genomic_DNA.
DR RefSeq; YP_076513.1; NC_006177.1.
DR ProteinModelPortal; Q67KX7; -.
DR STRING; 292459.STH2684; -.
DR EnsemblBacteria; BAD41669; BAD41669; STH2684.
DR GeneID; 2980169; -.
DR KEGG; sth:STH2684; -.
DR PATRIC; 23783544; VBISymThe116959_2677.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR OMA; RQWQKLF; -.
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 571 AA; 61492 MW; 07790DA1E096F98B CRC64;
MEMQAARALM RALEAEGVEV IFGYPGGASL YIYDALYDSP IHHVLTRHEQ GAIHAAEGYA
RATGKVGVVL ATSGPGATNL VTGLCDAMMD STPIVAITGQ VTRSLIGRDA FQEADVTGIT
MPVTKHNYLV TDPNDLLRVV REAFYIARTG RPGPVLIDIP KDVTNAQVRW EYPPRIHLPG
YRVPREASPE AVAAAAEAIR SARQPVLICG GGVVSSPDAT GPFRTLAERM DAPVVETLMG
LGGFPMDHPL CLGLVGMHGT FAANRAVANS DLVIACGMRF DDRVTGMASR FAPKARIIHI
DIDPAEMSKN LTAHIPLVGD CGLVLAQLNE ALGDWSQTLP EWRAQVQGWQ EQFPLWGVRR
GEEIATDPDG VPKPQQVIQA VQAAFGPEAV VATDVGQHQM WAAHYCTRTE PRTWLSSSGL
GTMGFGLPAA IGAAIGRPDR DVVLITGDGS FQMCIQELAT VVQERVPVKI VLLNNGYLGM
VRQWQEMFYK GRYKEVDLRP GMPDFVKLAE AYGIKGLRVR RLGELEGAVA EARAHQGPVL
LEVVVEEEEN VFPIVPPGGA NTEALLPGAG R
//
