ID A0A166EJT1_DAUCS Unreviewed; 648 AA.
AC A0A166EJT1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=DCAR_007493 {ECO:0000313|EMBL:KZN06656.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN06656.1};
RN [1] {ECO:0000313|EMBL:KZN06656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN06656.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN06656.1}.
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DR EMBL; LNRQ01000002; KZN06656.1; -; Genomic_DNA.
DR RefSeq; XP_017235857.1; XM_017380368.1.
DR AlphaFoldDB; A0A166EJT1; -.
DR STRING; 79200.A0A166EJT1; -.
DR EnsemblPlants; KZN06656; KZN06656; DCAR_007493.
DR GeneID; 108209456; -.
DR Gramene; KZN06656; KZN06656; DCAR_007493.
DR KEGG; dcr:108209456; -.
DR OMA; RMNCGEL; -.
DR OrthoDB; 1831659at2759; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000077755; Chromosome 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 76..187
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 267..400
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 462..617
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70745 MW; BB78E5DEA5696A5D CRC64;
MAATALKPSI AKPPPSLFPK SPQPFSRFSL PIRPPSQFHR PATLRITNVL SKPTPTTTTT
APQQFISRFS SDEPRKGSDV LVEALEREGV EHVFAYPGGA SMEIHQALTR SQTIQNILPR
HEQGGIFAAE GYARATGRPG ICIATSGPGA TNLVSGLADA LLDSTPLVAI TGQVPRRMIG
TDAFQETPIV EVTRSITKHN YLVLDVEDIP RIVKEAFFLA TSGRPGPVLI DIPKDIQQQL
VVPDWDQPMR LPGYLSRLPK FPNIGILEQI VRLISESKKP VLYVGGGCLN SGDELKRFVE
LTGIPVASTL MGLGAYPCSD DLSLQMLGMH GTVYANYAVD KSDLLLAFGV RFDDRVTGKL
EAFASRAKIV HIDIDSAEIG KNKTPHVSVC TDMKLALEGL NKILESKRGS LKADFSSWRE
ELKEQKTNNP LVFKTFGEAI PPQYAIQVLD ELTNGEAIIS TGVGQHQMWA AQYYKYNRPR
QWLTSGGLGA MGFGLPAAIG AAVGRPDCVV VDIDGDGSFM MNVQELATIR ASKLPIKILL
LNNQHLGMVV QWEDRFYKAN RAHTYLGDPA NESEIFPNML KFAEACNIKA ARVTKVGDLR
AAIQKMLDYP GPYLLDVIVP HQEHVLPMIP SGGAFKDVIT EGDGRSSY
//
