ILVB2_ORYSJ
ID ILVB2_ORYSJ Reviewed; 663 AA.
AC Q7XKQ8; A0A0P0W9Z1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable acetolactate synthase 2, chloroplastic;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase 2;
DE Flags: Precursor;
GN Name=ALS2; OrderedLocusNames=Os04g0389800, LOC_Os04g32010;
GN ORFNames=OSJNBa0053B21.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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; AL731599; CAE05539.2; -; Genomic_DNA.
DR EMBL; AP014960; BAS88952.1; -; Genomic_DNA.
DR EMBL; AK109628; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015634624.1; XM_015779138.1.
DR AlphaFoldDB; Q7XKQ8; -.
DR SMR; Q7XKQ8; -.
DR STRING; 4530.OS04T0389800-01; -.
DR PaxDb; Q7XKQ8; -.
DR PRIDE; Q7XKQ8; -.
DR EnsemblPlants; Os04t0389800-01; Os04t0389800-01; Os04g0389800.
DR GeneID; 4335672; -.
DR Gramene; Os04t0389800-01; Os04t0389800-01; Os04g0389800.
DR KEGG; osa:4335672; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_1_3_1; -.
DR InParanoid; Q7XKQ8; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
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 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XKQ8; OS.
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..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..663
FT /note="Probable acetolactate synthase 2, chloroplastic"
FT /id="PRO_0000235810"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..558
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 24..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 340..361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 383..402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT DISULFID 152..298
FT /evidence="ECO:0000250"
SQ SEQUENCE 663 AA; 71176 MW; 97AD4CE1D898C059 CRC64;
MAAAAAAASL SVSDAAAKLP KPGGQVQRRR DRDRPRVDAA ACTRDSRRPT RERCSTTVSL
AATATATTAT PVRAPVRTRA PMGQRKGADI VVEALERCGV RDVFEYPGGA SMEIHQALTR
SPVIRNHLLR HEQGEAFAAS GYARSSGRPG VCVATSGPGA TNLVSALADA HLDSVPLVAI
TGQAPRRMIG TDAFQETPIV EFTRSITKHN YLILDVDDIP RVINEAFFLA STGRPGPVLV
DIPKDIQQQM AVPSWDAPMR LPGYISRLPK PPAANLLDEV IRLVGDAERP VLYVGGGCSA
SGYELRRFVE LTGIPVTTTL MGIGNFPSDD PLSLRMLGMH GTVYANYAVD NADLLLALGV
RFDDRVTGKV EAFASRAKIV HVDIDPSELG KNKQPHVSIC ADVKLALQGM NAMLEEQSAA
AARKNLDFSA WRSELEKKKV EFPLGYRTFG EEIPPQYAIQ VLDEVTNGEA IVATGVGQHQ
MWATQHYTYR RPRQWLSSAG LGAMGFGLPA AAGAAVANPG ATVVDIDGDG SLLMNIQELA
MVRVEDLPVK VMVLNNQHLG MVVQWEDRFY DANRAHTYLG NPAANGGGEV YPDFVTIAGG
FGIPAARVTR KGEVRAAVEE MMAAPGPYLL DVVVPHQEHV LPMIPSNGAF KDIIVDGDGR
SSY
