ID Q5VB45_HELAN Unreviewed; 652 AA.
AC Q5VB45;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN Name=AHAS1 {ECO:0000313|EMBL:AAT07326.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:AAT07326.1};
RN [1] {ECO:0000313|EMBL:AAT07326.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15309298; DOI=10.1007/s00122-004-1716-7;
RA Kolkman J.M., Slabaugh M.B., Bruniard J.M., Berry S., Bushman B.S.,
RA Olungu C., Maes N., Abratti G., Zambelli A., Miller J.F., Leon A.,
RA Knapp S.J.;
RT "Acetohydroxyacid synthase mutations conferring resistance to imidazolinone
RT or sulfonylurea herbicides in sunflower.";
RL Theor. Appl. Genet. 109:1147-1159(2004).
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 Evidence={ECO:0000256|ARBA:ARBA00000673,
CC ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; AY541455; AAT07326.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5VB45; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
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:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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 CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 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_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Herbicide resistance {ECO:0000256|ARBA:ARBA00022646};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:AAT07326.1}.
FT DOMAIN 80..190
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 272..404
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 466..621
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 652 AA; 70972 MW; 0848063B0E656EA8 CRC64;
MAAPPNPSIS FKPPSPAAAL PPRSAFLPRF ALPITSTTQK RHRLHISNVL SDSKSTTTTT
QPPLQAQPFV SRYAPDQPRK GADVLVEALE REGVTDVFAY PGGASMEIHQ ALTRSNTIRN
VLPRHEQGGV FAAEGYARAS GLPGVCIATS GPGATNLVSG LADALLDSVP MVAITGQVPR
RMIGTDVFQE TPIVEVTRSI TKHNYLVLDV EDIPRIVREA FYLASSGRPG PVLIDVPKDI
QQQLVVPKWD EPMRLPGYLS RMPKPQYDGH LEQIVRLVGE AKRPVLYVGG GCLNSDDELR
RFVELTGIPV ASTLMGLGAY PASSDLSLHM LGMHGTVYAN YAVDKSDLLL AFGVRFDDRV
TGKLEAFASR AKIVHIDIDP AEIGKNKQPH VSICGDIKVA LQGLNKILEE KNSVTNLDFS
NWRKELDEQK VKFPLSFKTF GEAIPPQHAI QVLDELTGGN AIISTGVGQH QMWAAQFYKY
NKPRQWLTSG GLGAMGFGLP AAIGAAVARP DAVVVDIDGD GSFMMNVQEL ATIRVENLPV
KILLLNNQHL GMVVQWEDRF YKANRAHTYL GNPSKESEIF PNMVKFAEAC DIPAARVTQK
ADLRAAIQKM LDTPGPYLLD VIVPHQEHVL PMIPAGGGFS DVITEGDGRT KY
//
