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Database: UniProt
Entry: I0BBL3_9BACL
LinkDB: I0BBL3_9BACL
Original site: I0BBL3_9BACL 
ID   I0BBL3_9BACL            Unreviewed;       580 AA.
AC   I0BBL3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=B2K_03300 {ECO:0000313|EMBL:AFH59760.1};
OS   Paenibacillus mucilaginosus K02.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH59760.1, ECO:0000313|Proteomes:UP000007392};
RN   [1] {ECO:0000313|EMBL:AFH59760.1, ECO:0000313|Proteomes:UP000007392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K02 {ECO:0000313|EMBL:AFH59760.1,
RC   ECO:0000313|Proteomes:UP000007392};
RA   Xiao B., Sun L., Xiao L., Lian B.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL   Submitted (JUN-2013) 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; CP003422; AFH59760.1; -; Genomic_DNA.
DR   RefSeq; WP_014368421.1; NC_017672.3.
DR   AlphaFoldDB; I0BBL3; -.
DR   KEGG; pmw:B2K_03300; -.
DR   PATRIC; fig|997761.3.peg.657; -.
DR   HOGENOM; CLU_013748_1_2_9; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000007392; 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, ECO:0000313|EMBL:AFH59760.1}.
FT   DOMAIN          24..138
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          405..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   580 AA;  63151 MW;  B3D80BB254B6666F CRC64;
     MIVQTTQKSK EQLREELLKP DVITGSEALL RSLLLEDVDC VFGYPGGAVL YIYDAMHGNP
     DFNHLLTRHE QGAIHAADGY ARSTGKVGVC IATSGPGATN LVTGIATAYM DSVPLVVITG
     NVATTVIGTD AFQEADITGI TMPITKHSYL VRDVRDLPRI IKEAFHIAST GRKGPVLIDI
     PKDVSNDASP FYYPEKVEIR GYNPTVQPNR LQVDRMLEAI AEAERPVILA GGGVVYSGAA
     DELIKFVNAT RIPVTTTLLG LGGFPSAHEL WLGMPGMHGT HTANHALQNC DLLIGIGARF
     DDRVTMKVNG FAPKAKKIVH IDVDPAEIGK IVETAIPVVG DVKIVLEMAN QKVKAGDTSA
     WVDWVKENKA KYPLTYKDSD TELKPQYVIE MLHETTNGEA IVTTDVGQHQ MWSAQYYKFN
     KPRSWITSGG LGTMGFGFPS AIGAQVANPD RLVISINGDG GMQMCSQELA ICAINKIPVK
     IVVINNQVLG MVRQWQEIIY DNRYSHIDLA GSPDFVKLAE AYGVKGLRAT NKDEARTAWK
     EALDTPGPVL VEFVVRKHEN VFPMVTQGST IDQMIMGDSE
//
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