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Database: UniProt
Entry: P27818
LinkDB: P27818
Original site: P27818 
ID   ILVB1_BRANA             Reviewed;         655 AA.
AC   P27818;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   01-OCT-2014, entry version 95.
DE   RecName: Full=Acetolactate synthase 1, chloroplastic;
DE            EC=2.2.1.6;
DE   AltName: Full=ALS I;
DE   AltName: Full=Acetohydroxy-acid synthase I;
DE   AltName: Full=Acetolactate synthase I;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae;
OC   Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Topas;
RX   PubMed=1896019; DOI=10.1007/BF00264210;
RA   Rutledge R.G., Ouellet T., Hattori J., Miki B.L.A.;
RT   "Molecular characterization and genetic origin of the Brassica napus
RT   acetohydroxyacid synthase multigene family.";
RL   Mol. Gen. Genet. 229:31-40(1991).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: Acetolactate synthase is the target enzyme for
CC       sulfonylurea and imidazolinone herbicides.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; Z11524; CAA77613.1; -; Genomic_DNA.
DR   PIR; S17691; S17691.
DR   ProteinModelPortal; P27818; -.
DR   SMR; P27818; 71-652.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0009635; P:response to herbicide; IEA:UniProtKB-KW.
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   Chloroplast; FAD; Flavoprotein; Herbicide resistance; Magnesium;
KW   Metal-binding; Plastid; Thiamine pyrophosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     82       Chloroplast. {ECO:0000250}.
FT   CHAIN        83    655       Acetolactate synthase 1, chloroplastic.
FT                                /FTId=PRO_0000035656.
FT   NP_BIND     337    358       FAD. {ECO:0000250}.
FT   NP_BIND     380    399       FAD. {ECO:0000250}.
FT   REGION      472    552       Thiamine pyrophosphate binding.
FT   METAL       523    523       Magnesium. {ECO:0000250}.
FT   METAL       550    550       Magnesium. {ECO:0000250}.
FT   BINDING     129    129       Thiamine pyrophosphate. {ECO:0000250}.
FT   BINDING     231    231       FAD. {ECO:0000250}.
SQ   SEQUENCE   655 AA;  71289 MW;  1BEAD7D7A0DAD91A CRC64;
     MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKDSS RLHRPLAISA VLNSPVNVAP
     PSPEKTDKNK TFVSRYAPDE PRKGADILVE ALERQGVETV FAYPGGASME IHQALTRSST
     IRNVLPRHEQ GGVFAAEGYA RSSGKPGICI ATSGPGATNL VSGLADAMLD SVPLVAITGQ
     VPRRMIGTDA FQETPIVEVT RSITKHNYLV MDVDDIPRIV QEAFFLATSG RPGPVLVDVP
     KDIQQQLAIP NWDQPMRLPG YMSRLPQPPE VSQLGQIVRL ISESKRPVLY VGGGSLNSSE
     ELGRFVELTG IPVASTLMGL GSYPCNDELS LQMLGMHGTV YANYAVEHSD LLLAFGVRFD
     DRVTGKLEAF ASRAKIVHID IDSAEIGKNK TPHVSVCGDV KLALQGMNKV LENRAEELKL
     DFGVWRSELS EQKQKFPLSF KTFGEAIPPQ YAIQILDELT EGKAIISTGV GQHQMWAAQF
     YKYRKPRQWL SSSGLGAMGF GLPAAIGASV ANPDAIVVDI DGDGSFIMNV QELATIRVEN
     LPVKILLLNN QHLGMVMQWE DRFYKANRAH TYLGDPAREN EIFPNMLQFA GACGIPAARV
     TKKEELREAI QTMLDTPGPY LLDVICPHQE HVLPMIPSGG TFKDVITEGD GRTKY
//
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