ID ILVB3_BRANA Reviewed; 652 AA. AC P27819; 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 3, chloroplastic; DE EC=2.2.1.6; DE AltName: Full=ALS III; DE AltName: Full=Acetohydroxy-acid synthase III; DE AltName: Full=Acetolactate synthase III; 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). RN [2] RP SEQUENCE REVISION. RA Miki B.L.; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. 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; Z11526; CAA77615.1; -; Genomic_DNA. DR PIR; S29838; S29838. DR AlphaFoldDB; P27819; -. DR SMR; P27819; -. 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..69 FT /note="Chloroplast" FT /evidence="ECO:0000250" FT CHAIN 70..652 FT /note="Acetolactate synthase 3, chloroplastic" FT /id="PRO_0000035658" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..549 FT /note="Thiamine pyrophosphate binding" FT BINDING 126 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250" FT BINDING 228 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 334..355 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 377..396 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 520 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 547 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" SQ SEQUENCE 652 AA; 70988 MW; B12534C50CC5AE0D CRC64; MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKPSS RLHRPLAISA VLNSPVNVAP EKTDKIKTFI SRYAPDEPRK GADILVEALE RQGVETVFAY PGGASMEIHQ ALTRSSTIRN VLPRHEQGGV FAAEGYARSS GKPGICIATS GPGATNLVSG LADAMLDSVP LVAITGQVPR RMIGTDAFQE TPIVEVTRSI TKHNYLVMDV DDIPRIVQEA FFLATSGRPG PVLVDVPKDI QQQLAIPNWD QPMRLPGYMS RLPQPPEVSQ LGQIVRLISE SKRPVLYVGG GSLNSSEELG RFVELTGIPV ASTLMGLGSY PCNDELSLQM LGMHGTVYAN YAVEHSDLLL AFGVRFDDRV TGKLEAFASR AKIVHIDIDS AEIGKNKTPH VSVCGDVKLA LQGMNKVLEN RAEELKLDFG VWRSELSEQK QKFPLSFKTF GEAIPPQYAI QVLDELTQGK AIISTGVGQH QMWAAQFYKY RKPRQWLSSS GLGAMGFGLP AAIGASVANP DAIVVDIDGD GSFIMNVQEL ATIRVENLPV KILLLNNQHL GMVMQWEDRF YKANRAHTYL GDPARENEIF PNMLQFAGAC GIPAARVTKK EELREAIQTM LDTPGPYLLD VICPHQEHVL PMIPSGGTFK DVITEGDGRT KY //