ILVB1_ORYSJ
ID ILVB1_ORYSJ Reviewed; 644 AA.
AC Q6K2E8; Q5D6B1; Q5D6B2; Q5D6B3; Q9FRV2; Q9FRV3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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; OrderedLocusNames=Os02g0510200, LOC_Os02g30630;
GN ORFNames=OSJNBa0052M16.38;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Kinmaze;
RA Shimizu T., Kato Y., Nakayama I., Nakayama K., Fukuda A., Tanaka Y.;
RT "Isolation and Expression of acetolactate synthase genes from Oryza
RT sativa.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Bengal, and cv. Strawhull;
RX AGRICOLA=IND43755071; DOI=10.1614/WS-04-111R1.1;
RA Rajguru S.N., Burgos N.R., Shivrain V.K., Stewart J.M.;
RT "Mutations in the red rice ALS gene associated with resistance to
RT imazethapyr.";
RL Weed Sci. 53:567-577(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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; AB049822; BAB20812.1; -; mRNA.
DR EMBL; AB049823; BAB20813.1; -; mRNA.
DR EMBL; AY885674; AAX14282.1; -; Genomic_DNA.
DR EMBL; AY885673; AAX14281.1; -; Genomic_DNA.
DR EMBL; AY885675; AAX14283.1; -; Genomic_DNA.
DR EMBL; AP005841; BAD23668.1; -; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015626459.1; XM_015770973.1.
DR AlphaFoldDB; Q6K2E8; -.
DR SMR; Q6K2E8; -.
DR BioGRID; 798487; 1.
DR STRING; 4530.OS02T0510200-01; -.
DR PaxDb; Q6K2E8; -.
DR PRIDE; Q6K2E8; -.
DR EnsemblPlants; Os02t0510200-01; Os02t0510200-01; Os02g0510200.
DR GeneID; 4329450; -.
DR Gramene; Os02t0510200-01; Os02t0510200-01; Os02g0510200.
DR KEGG; osa:4329450; -.
DR eggNOG; KOG4166; Eukaryota.
DR InParanoid; Q6K2E8; -.
DR OrthoDB; 1132247at2759; -.
DR BRENDA; 2.2.1.6; 4460.
DR PlantReactome; R-OSA-1119460; Isoleucine biosynthesis from threonine.
DR PlantReactome; R-OSA-1119600; Valine biosynthesis.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6K2E8; baseline and differential.
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 2: Evidence at transcript 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..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..644
FT /note="Acetolactate synthase 1, chloroplastic"
FT /id="PRO_0000235809"
FT REGION 47..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..541
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 326..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 369..388
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 138..284
FT /evidence="ECO:0000250"
FT VARIANT 11
FT /note="A -> T (in strain: cv. Bengal and cv. Strawhull)"
FT VARIANT 160
FT /note="S -> P (in strain: cv. Strawhull; resistant to
FT imidazolinone and sulfonylurea herbicides; when associated
FT with T-11; R-293; E-390; D-401; D-604; N-627 and P-636)"
FT VARIANT 293
FT /note="W -> R (in strain: cv. Bengal and cv. Strawhull)"
FT VARIANT 390
FT /note="K -> E (in strain: cv. Strawhull; resistant to
FT imidazolinone and sulfonylurea herbicides; when associated
FT with T-11; P-160; R-293; D-401, D-604; N-627 and P-636)"
FT VARIANT 401
FT /note="Q -> D (in strain: cv. Bengal and cv. Strawhull)"
FT VARIANT 548
FT /note="W -> L (in strain: cv. Japonica /Kinmaze; resistant
FT to imidazolinone and sulfonylurea herbicides; when
FT associated with I-627)"
FT VARIANT 604
FT /note="E -> D (in strain: cv. Strawhull)"
FT VARIANT 627
FT /note="S -> I (in strain: cv. Japonica /Kinmaze; resistant
FT to imidazolinone and sulfonylurea herbicides; when
FT associated with L-548)"
FT VARIANT 627
FT /note="S -> N (in strain: cv. Strawhull; resistant to
FT imidazolinone and sulfonylurea herbicides; when associated
FT with T-11; P-160; R-293; E-390; D-401; D-604 and P-636)"
FT VARIANT 636
FT /note="L -> P (in strain: cv. Strawhull; resistant to
FT imidazolinone and sulfonylurea herbicides; when associated
FT with T-11, P-160; R-293; E-390; D-401; D-604 and N-627)"
SQ SEQUENCE 644 AA; 69393 MW; ED626E55F8B89EC9 CRC64;
MATTAAAAAA ALSAAATAKT GRKNHQRHHV LPARGRVGAA AVRCSAVSPV TPPSPAPPAT
PLRPWGPAEP RKGADILVEA LERCGVSDVF AYPGGASMEI HQALTRSPVI TNHLFRHEQG
EAFAASGYAR ASGRVGVCVA TSGPGATNLV SALADALLDS VPMVAITGQV PRRMIGTDAF
QETPIVEVTR SITKHNYLVL DVEDIPRVIQ EAFFLASSGR PGPVLVDIPK DIQQQMAVPV
WDTSMNLPGY IARLPKPPAT ELLEQVLRLV GESRRPILYV GGGCSASGDE LRWFVELTGI
PVTTTLMGLG NFPSDDPLSL RMLGMHGTVY ANYAVDKADL LLAFGVRFDD RVTGKIEAFA
SRAKIVHIDI DPAEIGKNKQ PHVSICADVK LALQGLNALL QQSTTKTSSD FSAWHNELDQ
QKREFPLGYK TFGEEIPPQY AIQVLDELTK GEAIIATGVG QHQMWAAQYY TYKRPRQWLS
SAGLGAMGFG LPAAAGASVA NPGVTVVDID GDGSFLMNIQ ELALIRIENL PVKVMVLNNQ
HLGMVVQWED RFYKANRAHT YLGNPECESE IYPDFVTIAK GFNIPAVRVT KKSEVRAAIK
KMLETPGPYL LDIIVPHQEH VLPMIPSGGA FKDMILDGDG RTVY
