ID ILVB1_TOBAC Reviewed; 667 AA. AC P09342; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 153. 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; GN Name=ALS SURA; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-194. RX PubMed=16453837; DOI=10.1002/j.1460-2075.1988.tb02937.x; RA Lee K.Y., Townsend J., Tepperman J., Black M., Chui C.-F., Mazur B., RA Dunsmuir P., Bedbrook J.; RT "The molecular basis of sulfonylurea herbicide resistance in tobacco."; RL EMBO J. 7:1241-1248(1988). RN [2] RP SEQUENCE REVISION. RA Lee K.Y.; RL Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases. RN [3] RP DISULFIDE BOND. RX PubMed=10814542; DOI=10.1006/bbrc.2000.2706; RA Shin H.J., Chong C.K., Chang S.I., Choi J.D.; RT "Structural and functional role of cysteinyl residues in tobacco RT acetolactate synthase."; RL Biochem. Biophys. Res. Commun. 271:801-806(2000). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 pyruvate + H(+) = (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: There are two distinct ALS genes in tobacco. The enzyme CC shown here is derived from the ALS gene on locus SuRA. 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; X07644; CAA30484.1; -; Genomic_DNA. DR PIR; S00545; YCNT1. DR AlphaFoldDB; P09342; -. DR SMR; P09342; -. DR STRING; 4097.P09342; -. DR PaxDb; 4097-P09342; -. DR SABIO-RK; P09342; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000790787; Unplaced. DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0009099; P:L-valine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd02015; TPP_AHAS; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR FunFam; 3.40.50.1220:FF:000008; Acetolactate synthase; 1. DR FunFam; 3.40.50.970:FF:000007; Acetolactate synthase; 1. DR FunFam; 3.40.50.970:FF:000053; Acetolactate synthase, mitochondrial; 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 1: Evidence at protein level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Chloroplast; Disulfide bond; FAD; Flavoprotein; Herbicide resistance; KW Magnesium; Metal-binding; Plastid; Reference proteome; KW Thiamine pyrophosphate; Transferase; Transit peptide. FT TRANSIT 1..94 FT /note="Chloroplast" FT CHAIN 95..667 FT /note="Acetolactate synthase 1, chloroplastic" FT /id="PRO_0000035659" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 484..564 FT /note="Thiamine pyrophosphate binding" FT COMPBIAS 1..35 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 141 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250" FT BINDING 243 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 349..370 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 392..411 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 535 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 562 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT DISULFID 161..307 FT /evidence="ECO:0000269|PubMed:10814542" FT MUTAGEN 194 FT /note="P->Q: In C3; highly resistant to sulfonylurea FT herbicides." FT /evidence="ECO:0000269|PubMed:16453837" SQ SEQUENCE 667 AA; 72868 MW; DF2674EC6CA827C2 CRC64; MAAAAPSPSS SAFSKTLSPS SSTSSTLLPR STFPFPHHPH KTTPPPLHLT HTHIHIHSQR RRFTISNVIS TNQKVSQTEK TETFVSRFAP DEPRKGSDVL VEALEREGVT DVFAYPGGAS MEIHQALTRS SIIRNVLPRH EQGGVFAAEG YARATGFPGV CIATSGPGAT NLVSGLADAL LDSVPIVAIT GQVPRRMIGT DAFQETPIVE VTRSITKHNY LVMDVEDIPR VVREAFFLAR SGRPGPILID VPKDIQQQLV IPDWDQPMRL PGYMSRLPKL PNEMLLEQIV RLISESKKPV LYVGGGCSQS SEDLRRFVEL TGIPVASTLM GLGAFPTGDE LSLSMLGMHG TVYANYAVDS SDLLLAFGVR FDDRVTGKLE AFASRAKIVH IDIDSAEIGK NKQPHVSICA DIKLALQGLN SILESKEGKL KLDFSAWRQE LTEQKVKHPL NFKTFGDAIP PQYAIQVLDE LTNGNAIIST GVGQHQMWAA QYYKYRKPRQ WLTSGGLGAM GFGLPAAIGA AVGRPDEVVV DIDGDGSFIM NVQELATIKV ENLPVKIMLL NNQHLGMVVQ WEDRFYKANR AHTYLGNPSN EAEIFPNMLK FAEACGVPAA RVTHRDDLRA AIQKMLDTPG PYLLDVIVPH QEHVLPMIPS GGAFKDVITE GDGRSSY //