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 27-MAR-2024, entry version 124. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; 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: CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {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 from CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z11524; CAA77613.1; -; Genomic_DNA. DR PIR; S17691; S17691. DR RefSeq; XP_013648961.1; XM_013793507.1. DR RefSeq; XP_013648962.1; XM_013793508.1. DR RefSeq; XP_013661739.1; XM_013806285.1. DR RefSeq; XP_013661740.1; XM_013806286.1. DR AlphaFoldDB; P27818; -. DR SMR; P27818; -. DR GeneID; 106353715; -. DR GeneID; 106353716; -. DR KEGG; bna:106353715; -. DR KEGG; bna:106353716; -. DR OrthoDB; 1831659at2759; -. 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 CDD; cd02015; TPP_AHAS; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR012846; Acetolactate_synth_lsu. DR InterPro; IPR039368; AHAS_TPP. 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; IPR045229; TPP_enz. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR NCBIfam; TIGR00118; acolac_lg; 1. DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. 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 FT /note="Chloroplast" FT /evidence="ECO:0000250" FT CHAIN 83..655 FT /note="Acetolactate synthase 1, chloroplastic" FT /id="PRO_0000035656" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 472..552 FT /note="Thiamine pyrophosphate binding" FT BINDING 129 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 337..358 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 380..399 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 523 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 550 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="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 //