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Database: UniProt
Entry: A0A0U2IQN1_9BACL
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ID   A0A0U2IQN1_9BACL        Unreviewed;       581 AA.
AC   A0A0U2IQN1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=IJ21_40170 {ECO:0000313|EMBL:ALS29403.1};
OS   Paenibacillus sp. 32O-W.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1695218 {ECO:0000313|EMBL:ALS29403.1, ECO:0000313|Proteomes:UP000059673};
RN   [1] {ECO:0000313|Proteomes:UP000059673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-W {ECO:0000313|Proteomes:UP000059673};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic Paenibacillus
RT   species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS29403.1, ECO:0000313|Proteomes:UP000059673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-W {ECO:0000313|EMBL:ALS29403.1,
RC   ECO:0000313|Proteomes:UP000059673};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(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}.
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DR   EMBL; CP013653; ALS29403.1; -; Genomic_DNA.
DR   RefSeq; WP_062494945.1; NZ_CP013653.1.
DR   AlphaFoldDB; A0A0U2IQN1; -.
DR   STRING; 1695218.IJ21_40170; -.
DR   KEGG; pow:IJ21_40170; -.
DR   PATRIC; fig|1695218.3.peg.4326; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000059673; Chromosome.
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: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, CHLOROPLASTIC; 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}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059673};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          25..139
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          406..554
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   581 AA;  63008 MW;  69E91A3FA0E7C374 CRC64;
     MVTQSATLKS KEEIIERMKK PEVITGSEML LRSLVLEGVE CVFGYPGGAV LYIYDAMHGF
     KDFHHVLTRH EQGAIHAADG YARASGKVGV CIATSGPGAT NLVTGIATAY MDSVPLVVIT
     GNVATSAIGT DAFQEADITG ITMPITKHSY LVRRVEDLPR IIHEAFHIAN TGRKGPVLID
     IPKDVSAAKA LFQPVTEVNI RGYNPTVAPH KPQIDKLLQA IAEAERPLIL AGGGVIYSGG
     HEELYEFVTK TNIPVTTTLL GLGGFPSGHE LWLGMPGMHG TYASNKAIQA ADLLINIGAR
     FDDRVTMKLS GFAPNAKIAH IDIDPAEIGK NVPTDIPIVG DIKTVLTIIN REAKPAAKAD
     AWRAQTQAWK KEVPLKYKDS DTELKPQWVI EMIHDTTGGD AIVTTDVGQH QMWAAQFYRF
     NKPRSWITSG GLGTMGFGFP SAIGAQMAHP DRLVVSINGD GGMQMCAQEL AVCAINNIPV
     KVAIINNQVL GMVRQWQEII YDNRYSHIDL AGSPDFVKLA EAYGVKGFRA TNKEEARSAW
     EAALRHPGPA VVEFVVRKEE NVYPMVTQGN TIDEMIMGDA E
//
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