ILVB3_BRANA
ID ILVB3_BRANA Reviewed; 652 AA.
AC P27819;
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 3, chloroplastic;
DE EC=2.2.1.6;
DE AltName: Full=ALS III;
DE AltName: Full=Acetohydroxy-acid synthase III;
DE AltName: Full=Acetolactate synthase III;
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).
RN [2]
RP SEQUENCE REVISION.
RA Miki B.L.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
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; Z11526; CAA77615.1; -; Genomic_DNA.
DR PIR; S29838; S29838.
DR AlphaFoldDB; P27819; -.
DR SMR; P27819; -.
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..69
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 70..652
FT /note="Acetolactate synthase 3, chloroplastic"
FT /id="PRO_0000035658"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..549
FT /note="Thiamine pyrophosphate binding"
FT BINDING 126
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 334..355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 377..396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 652 AA; 70988 MW; B12534C50CC5AE0D CRC64;
MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKPSS RLHRPLAISA VLNSPVNVAP
EKTDKIKTFI SRYAPDEPRK GADILVEALE RQGVETVFAY PGGASMEIHQ ALTRSSTIRN
VLPRHEQGGV FAAEGYARSS GKPGICIATS GPGATNLVSG LADAMLDSVP LVAITGQVPR
RMIGTDAFQE TPIVEVTRSI TKHNYLVMDV DDIPRIVQEA FFLATSGRPG PVLVDVPKDI
QQQLAIPNWD QPMRLPGYMS RLPQPPEVSQ LGQIVRLISE SKRPVLYVGG GSLNSSEELG
RFVELTGIPV ASTLMGLGSY PCNDELSLQM LGMHGTVYAN YAVEHSDLLL AFGVRFDDRV
TGKLEAFASR AKIVHIDIDS AEIGKNKTPH VSVCGDVKLA LQGMNKVLEN RAEELKLDFG
VWRSELSEQK QKFPLSFKTF GEAIPPQYAI QVLDELTQGK AIISTGVGQH QMWAAQFYKY
RKPRQWLSSS GLGAMGFGLP AAIGASVANP DAIVVDIDGD GSFIMNVQEL ATIRVENLPV
KILLLNNQHL GMVMQWEDRF YKANRAHTYL GDPARENEIF PNMLQFAGAC GIPAARVTKK
EELREAIQTM LDTPGPYLLD VICPHQEHVL PMIPSGGTFK DVITEGDGRT KY
