ILVB1_TOBAC
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 03-AUG-2022, entry version 140.
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=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: 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 SABIO-RK; P09342; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000084051; 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; IBA:GO_Central.
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:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd02015; TPP_AHAS; 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-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00118; acolac_lg; 1.
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 7..31
FT /note="Polar residues"
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
