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Entry: A0A099W979_9LIST
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ID   A0A099W979_9LIST        Unreviewed;       472 AA.
AC   A0A099W979;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=EP57_09005 {ECO:0000313|EMBL:KGL40685.1};
OS   Listeria booriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL40685.1, ECO:0000313|Proteomes:UP000029844};
RN   [1] {ECO:0000313|EMBL:KGL40685.1, ECO:0000313|Proteomes:UP000029844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL40685.1,
RC   ECO:0000313|Proteomes:UP000029844};
RA   den Bakker H.C.;
RT   "Novel Listeriaceae from food processing environments.";
RL   Submitted (MAY-2014) 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:KGL40685.1}.
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DR   EMBL; JNFA01000023; KGL40685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099W979; -.
DR   STRING; 1552123.EP57_09005; -.
DR   eggNOG; COG0028; Bacteria.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000029844; 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; 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   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:UP000029844};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:KGL40685.1}.
FT   DOMAIN          105..240
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          299..447
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   472 AA;  51839 MW;  7EB5AFA550C5D294 CRC64;
     MSDSIPLVVF TGQVATPGIG KDAFQEADMI GLTIPITKYN YQVRDVKDIP KIIKEAFHIA
     TTGRKGPVVI DLPKDISIAS TDKVNDDTIH LPGYQPTVMP NRMQLEKLMQ ALAEASKPVI
     LAGAGVNHAR ATAELLDFAE KYQIPVVNTL LGLGSFPQDH PLFLGMGGMH GSYAANMALT
     DPDLLINFGS RFDDRVVGVP KEFAKHAVIA HIDIDPAEIG KVLTTKIPIV ADIKETLTQL
     LDIEIPEKAD TSHWYKLNMT RKERHPFTYN REAKAEIKPQ KVIEIIGDIT AGKALVATDV
     GQHQMWVAQF YPFSHDHQIM TSGGLGTMGF GFPAAIGAQL AYPEQTVVAF VGDGGFQMTN
     QELAILNDYM INLKVVILNN STLGMVRQWQ EKFHNERYSH SIFQSQPDFV KLSEAYGVKA
     VRLTDPTTLE ADLAEAFAYP GPMVIDCVIS PNELVLPMIP PGKANHQMEG VE
//
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