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Database: UniProt
Entry: P45261
LinkDB: P45261
Original site: P45261 
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-OCT-2014, entry version 103.
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. {ECO:0000250}.
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000250}.
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. {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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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; EETVICV; -.
DR   OrthoDB; EOG6KT2NW; -.
DR   PhylomeDB; P45261; -.
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   Gene3D; 3.40.50.1220; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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; 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. {ECO:0000250}.
FT   NP_BIND     304    323       FAD. {ECO:0000250}.
FT   REGION      396    476       Thiamine pyrophosphate binding.
FT   METAL       447    447       Magnesium. {ECO:0000250}.
FT   METAL       474    474       Magnesium. {ECO:0000250}.
FT   BINDING      51     51       Thiamine pyrophosphate. {ECO:0000250}.
FT   BINDING     153    153       FAD. {ECO:0000250}.
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
//
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