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Database: UniProt
Entry: A0A161PWQ2_9FIRM
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ID   A0A161PWQ2_9FIRM        Unreviewed;       553 AA.
AC   A0A161PWQ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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_1 {ECO:0000313|EMBL:KYO68070.1};
GN   ORFNames=ATZ99_03810 {ECO:0000313|EMBL:KYO68070.1};
OS   Thermovenabulum gondwanense.
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermovenabulum.
OX   NCBI_TaxID=520767 {ECO:0000313|EMBL:KYO68070.1, ECO:0000313|Proteomes:UP000075737};
RN   [1] {ECO:0000313|EMBL:KYO68070.1, ECO:0000313|Proteomes:UP000075737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R270 {ECO:0000313|EMBL:KYO68070.1,
RC   ECO:0000313|Proteomes:UP000075737};
RA   Patel B.K.;
RT   "Draft genome of Thermovenabulum gondwanense isolated from a red
RT   thermophilic microbial mat colonisisng an outflow channel of a bore well.";
RL   Submitted (DEC-2015) 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}.
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:KYO68070.1}.
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DR   EMBL; LOHZ01000019; KYO68070.1; -; Genomic_DNA.
DR   RefSeq; WP_068747549.1; NZ_LOHZ01000019.1.
DR   AlphaFoldDB; A0A161PWQ2; -.
DR   STRING; 520767.ATZ99_03810; -.
DR   PATRIC; fig|520767.4.peg.386; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000075737; Unassembled WGS sequence.
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:UP000075737};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:KYO68070.1}.
FT   DOMAIN          4..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          382..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   553 AA;  59946 MW;  B7B9EB39F3C87786 CRC64;
     MKITAAEALI KALEAEGVDL IFGYPGGAIL PVYDSLYNSK KIKHVLTRSE QAAAHAASGF
     ARVSGKVGVC MATSGPGATN LVTGIATAYM DSVPIVAITG QVPTGVIGRD VFQEVDITGA
     TAPFTKHNYL VKRAEDIPRI VKEAFYIAST GRPGPVLIDL PKDVAETRIE FKMPGKINLR
     GYKPKVQGHP LQIERAVEEI KRAQRPVIIA GGGVNSAKAE KELMELVEKT GIPVATSLMG
     IGCFPQNHPL SLGMAGMHGS PRANIAITEA DLIIAAGVRF SDRMTGKVSG FAPKAKILHI
     DIDPAEIGKN VRVDIPIVGD LRVVLSEISK NSTKKDLYEW YDFIEKISKK GVYEKKGMLC
     PQEIIEVISQ KTKGEAIITT EVGSHQMWVA QFYEFIHPRS FITSGGLGTM GYGLPAAIGA
     KFANPGKTVI NFAGDGSFQM NLAEMATIVE NNLAVKMVLF NNGGLGLVRQ LQEFYCDGRY
     HQVNFKFTPD FVKLAESYGI KAERIESRKE LPQAVDRMLS EEGSFLLECM VDIRENVYPM
     VLNGSPINKM IGG
//
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