ID ILVI_HAEIN Reviewed; 573 AA.
AC P45261;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 01-MAY-2013, entry version 97.
DE RecName: Full=Acetolactate synthase large subunit;
DE Short=AHAS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase large subunit;
DE Short=ALS;
GN Name=ilvI; OrderedLocusNames=HI_1585;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 -!- SUBUNIT: Dimer of large and small chains (By similarity).
CC -!- MISCELLANEOUS: Contains 1 molecule of FAD per monomer. The role of
CC this cofactor is not clear considering that the reaction does not
CC involve redox chemistry (By similarity).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
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DR EMBL; L42023; AAC23233.1; -; Genomic_DNA.
DR PIR; C64131; C64131.
DR RefSeq; NP_439730.1; NC_000907.1.
DR ProteinModelPortal; P45261; -.
DR STRING; 71421.HI1585; -.
DR EnsemblBacteria; AAC23233; AAC23233; HI_1585.
DR GeneID; 950449; -.
DR KEGG; hin:HI1585; -.
DR PATRIC; 20191903; VBIHaeInf48452_1659.
DR eggNOG; COG0028; -.
DR KO; K01652; -.
DR OMA; GRYEANM; -.
DR ProtClustDB; PRK06882; -.
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; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1 573 Acetolactate synthase large subunit.
FT /FTId=PRO_0000090795.
FT NP_BIND 261 282 FAD (By similarity).
FT NP_BIND 304 323 FAD (By similarity).
FT REGION 396 476 Thiamine pyrophosphate binding.
FT METAL 447 447 Magnesium (By similarity).
FT METAL 474 474 Magnesium (By similarity).
FT BINDING 51 51 Thiamine pyrophosphate (By similarity).
FT BINDING 153 153 FAD (By similarity).
SQ SEQUENCE 573 AA; 62620 MW; CA055388605F60BE CRC64;
MKKLSGAEMV VQSLRDEGVE YVFGYPGGAV LDIYDAIHTL GGIEHILVRH EQAAVHMADG
YARSTGKVGC VLVTSGPGAT NAITGILTAY TDSVPMVIIS GQVMSNLIGS DAFQECDMLG
ISRPVVKHSF IVKKAEDIPS TLKKAFYIAS TGRPGPVVVD IPKDTVNPNF KYPYEYPEYV
ELRSYNPTVN GHKGQIKKAL KALLVAKKPI LFVGGGAITA ECSEQLIQFA QRLNLPVTSS
LMGLGAYPST DKQFLGMLGM HGTLEANTAM HESDLILGIG VRFDDRTTNN LEKYCPNAKV
IHIDIDPTSI SKNVPVAIPI VGNAKNVLEE FLGLLNEEGL KSQTDLESWW QEINQWKAKK
CLEFDRTSGV IKPQQVVEAV YRLTKGQAYV ASDVGQHQMF AALHYPFDEP RHWINSGGAG
TMGFGFPAAL GVKLAHPEGT VVCVTGDGSI QMNIQELSTA TQYGIPVVII CLNNHFLGMV
KQWQDLIYSG RHSQTYMNSL PDFAKLAESY GHVGIKIATP DELESKLQEA FSIKNKLVFV
DINVDESEHV YPMQIRGGAM NEMILSKPQE ETN
//
