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Database: UniProt
Entry: E8NCS8_MICTS
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Original site: E8NCS8_MICTS 
ID   E8NCS8_MICTS            Unreviewed;       602 AA.
AC   E8NCS8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=ilvB {ECO:0000313|EMBL:BAJ76158.1};
GN   OrderedLocusNames=MTES_3194 {ECO:0000313|EMBL:BAJ76158.1};
OS   Microbacterium testaceum (strain StLB037).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ76158.1, ECO:0000313|Proteomes:UP000008975};
RN   [1] {ECO:0000313|EMBL:BAJ76158.1, ECO:0000313|Proteomes:UP000008975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StLB037 {ECO:0000313|EMBL:BAJ76158.1,
RC   ECO:0000313|Proteomes:UP000008975};
RX   PubMed=21357489; DOI=10.1128/JB.00180-11;
RA   Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT   lactone-degrading bacterium isolated from potato leaves.";
RL   J. Bacteriol. 193:2072-2073(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=StLB037;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Genome sequence of Microbacterium testaceum StLB037.";
RL   Submitted (FEB-2011) 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         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; AP012052; BAJ76158.1; -; Genomic_DNA.
DR   RefSeq; WP_013586280.1; NC_015125.1.
DR   AlphaFoldDB; E8NCS8; -.
DR   STRING; 979556.MTES_3194; -.
DR   KEGG; mts:MTES_3194; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_11; -.
DR   OMA; CFGTSGP; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000008975; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          23..139
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          213..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          411..566
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   602 AA;  64016 MW;  2251D6B71064D6F8 CRC64;
     MSIDSPTAAV PRPPARTAPA PVMTGAQAVV RSLDLLGVTD VFGLPGGAIM PVYDPLMDDE
     HVRHILVRHE QGAGHAAEGY AAASGKVGVA IATSGPGATN LVTAIADAYM DSVPLVCITG
     QVFSTLMGTD AFQEADIVGI TMPITKHSFL VKTADEIPGA IAAAFEIAST GRPGPVLVDI
     TKDAQQAEAP FVWPPKIDLP GYRPVTRAHG KQIQAAAQLL ATAKKPVLYV GGGTIRSSAS
     AELKVLAEAT GAPVVTTLMA RGAFPDSHEQ HLGMPGMHGT VPAVLALQES DLIVSLGARF
     DDRVTGKAAL FAPHAQVVHV DIDPAEISKI RTADVPIVGD LKEVLVDLDA AFRAADAEHP
     HDYTEWWTYL NGLREEFPLG YTPTTDGLLS PQHVIQRIGE LTGPEGVYAS GVGQHQMWAA
     QFIKYERPNA WLNSGGAGTM GYAVPAAMGA KVAQPDRAVW AIDGDGCFQM TNQELATCVI
     NDIPIKVAII NNSSLGMVRQ WQTLFFDGRH SNTDLNTGHG TRRIPDFVKL AEAYGCLAIR
     VEKEDEIDAA IQLALDTNDR PVVIDFVVSA DAMVWPMVPQ GVSNSYVQYA RDHSPAFNEQ
     ED
//
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