ILVB1_MAIZE
ID ILVB1_MAIZE Reviewed; 638 AA.
AC Q41768;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Acetolactate synthase 1, chloroplastic;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase 1;
DE Flags: Precursor;
GN Name=ALS1; Synonyms=AHAS108;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1600154; DOI=10.1007/bf00047723;
RA Fang L.Y., Gross P.R., Chen C.-H., Lillis M.;
RT "Sequence of two acetohydroxyacid synthase genes from Zea mays.";
RL Plant Mol. Biol. 18:1185-1187(1992).
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 {ECO:0000250}.
CC -!- MISCELLANEOUS: Acetolactate synthase is the target enzyme for
CC sulfonylurea and imidazolinone herbicides.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; X63553; CAA45116.1; -; Genomic_DNA.
DR PIR; S22490; S22490.
DR RefSeq; NP_001151761.1; NM_001158289.1.
DR AlphaFoldDB; Q41768; -.
DR SMR; Q41768; -.
DR STRING; 4577.GRMZM2G143008_P01; -.
DR ChEMBL; CHEMBL2366574; -.
DR PaxDb; Q41768; -.
DR PRIDE; Q41768; -.
DR EnsemblPlants; Zm00001eb241810_T001; Zm00001eb241810_P001; Zm00001eb241810.
DR GeneID; 100285396; -.
DR Gramene; Zm00001eb241810_T001; Zm00001eb241810_P001; Zm00001eb241810.
DR KEGG; zma:100285396; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_1_2_1; -.
DR OMA; GFATCDL; -.
DR OrthoDB; 1132247at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000007305; Chromosome 5.
DR ExpressionAtlas; Q41768; baseline and differential.
DR Genevisible; Q41768; ZM.
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; 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.
PE 3: Inferred from homology;
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..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..638
FT /note="Acetolactate synthase 1, chloroplastic"
FT /id="PRO_0000235807"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..535
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 320..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363..382
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 132..278
FT /evidence="ECO:0000250"
SQ SEQUENCE 638 AA; 68930 MW; DF1BF3120BC84972 CRC64;
MATAAAASTA LTGATTAAPK ARRRAHLLAT RRALAAPIRC SAASPAMPMA PPATPLRPWG
PTDPRKGADI LVESLERCGV RDVFAYPGGA SMEIHQALTR SPVIANHLFR HEQGEAFAAS
GYARSSGRVG VCIATSGPGA TNLVSALADA LLDSVPMVAI TGQVPRRMIG TDAFQETPIV
EVTRSITKHN YLVLDVDDIP RVVQEAFFLA SSGRPGPVLV DIPKDIQQQM AVPVWDKPMS
LPGYIARLPK PPATELLEQV LRLVGESRRP VLYVGGGCAA SGEELRRFVE LTGIPVTTTL
MGLGNFPSDD PLSLRMLGMH GTVYANYAVD KADLLLALGV RFDDRVTGKI EAFASRAKIV
HVDIDPAEIG KNKQPHVSIC ADVKLALQGM NALLEGSTSK KSFDFGSWND ELDQQKREFP
LGYKTSNEEI QPQYAIQVLD ELTKGEAIIG TGVGQHQMWA AQYYTYKRPR QWLSSAGLGA
MGFGLPAAAG ASVANPGVTV VDIDGDGSFL MNVQELAMIR IENLPVKVFV LNNQHLGMVV
QWEDRFYKAN RAHTYLGNPE NESEIYPDFV TIAKGFNIPA VRVTKKNEVR AAIKKMLETP
GPYLLDIIVP HQEHVLPMIP SGGAFKDMIL DGDGRTVY
