ILVB1_BRANA
ID ILVB1_BRANA Reviewed; 655 AA.
AC P27818;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Topas;
RX PubMed=1896019; DOI=10.1007/bf00264210;
RA Rutledge R.G., Ouellet T., Hattori J., Miki B.L.A.;
RT "Molecular characterization and genetic origin of the Brassica napus
RT acetohydroxyacid synthase multigene family.";
RL Mol. Gen. Genet. 229:31-40(1991).
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: 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; Z11524; CAA77613.1; -; Genomic_DNA.
DR PIR; S17691; S17691.
DR RefSeq; XP_013648961.1; XM_013793507.1.
DR RefSeq; XP_013648962.1; XM_013793508.1.
DR RefSeq; XP_013661739.1; XM_013806285.1.
DR RefSeq; XP_013661740.1; XM_013806286.1.
DR AlphaFoldDB; P27818; -.
DR SMR; P27818; -.
DR GeneID; 106353715; -.
DR GeneID; 106353716; -.
DR GeneID; 106366633; -.
DR GeneID; 106366634; -.
DR KEGG; bna:106353715; -.
DR KEGG; bna:106353716; -.
DR KEGG; bna:106366633; -.
DR KEGG; bna:106366634; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
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; IEA:InterPro.
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; IEA:UniProtKB-UniPathway.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Chloroplast; FAD; Flavoprotein; Herbicide resistance; Magnesium;
KW Metal-binding; Plastid; Thiamine pyrophosphate; Transferase;
KW Transit peptide.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 83..655
FT /note="Acetolactate synthase 1, chloroplastic"
FT /id="PRO_0000035656"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..552
FT /note="Thiamine pyrophosphate binding"
FT BINDING 129
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 337..358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 380..399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 71289 MW; 1BEAD7D7A0DAD91A CRC64;
MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKDSS RLHRPLAISA VLNSPVNVAP
PSPEKTDKNK TFVSRYAPDE PRKGADILVE ALERQGVETV FAYPGGASME IHQALTRSST
IRNVLPRHEQ GGVFAAEGYA RSSGKPGICI ATSGPGATNL VSGLADAMLD SVPLVAITGQ
VPRRMIGTDA FQETPIVEVT RSITKHNYLV MDVDDIPRIV QEAFFLATSG RPGPVLVDVP
KDIQQQLAIP NWDQPMRLPG YMSRLPQPPE VSQLGQIVRL ISESKRPVLY VGGGSLNSSE
ELGRFVELTG IPVASTLMGL GSYPCNDELS LQMLGMHGTV YANYAVEHSD LLLAFGVRFD
DRVTGKLEAF ASRAKIVHID IDSAEIGKNK TPHVSVCGDV KLALQGMNKV LENRAEELKL
DFGVWRSELS EQKQKFPLSF KTFGEAIPPQ YAIQILDELT EGKAIISTGV GQHQMWAAQF
YKYRKPRQWL SSSGLGAMGF GLPAAIGASV ANPDAIVVDI DGDGSFIMNV QELATIRVEN
LPVKILLLNN QHLGMVMQWE DRFYKANRAH TYLGDPAREN EIFPNMLQFA GACGIPAARV
TKKEELREAI QTMLDTPGPY LLDVICPHQE HVLPMIPSGG TFKDVITEGD GRTKY
