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 03-APR-2013, entry version 91.
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; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; 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 (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 -!- 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.
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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: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 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 Chloroplast; FAD; Flavoprotein; Herbicide resistance; Magnesium;
KW Metal-binding; Plastid; Thiamine pyrophosphate; Transferase;
KW Transit peptide.
FT TRANSIT 1 82 Chloroplast (By similarity).
FT CHAIN 83 655 Acetolactate synthase 1, chloroplastic.
FT /FTId=PRO_0000035656.
FT NP_BIND 337 358 FAD (By similarity).
FT NP_BIND 380 399 FAD (By similarity).
FT REGION 472 552 Thiamine pyrophosphate binding.
FT METAL 523 523 Magnesium (By similarity).
FT METAL 550 550 Magnesium (By similarity).
FT BINDING 129 129 Thiamine pyrophosphate (By similarity).
FT BINDING 231 231 FAD (By similarity).
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
//
