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Database: UniProt
Entry: A0A0G3WM54_9BACT
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ID   A0A0G3WM54_9BACT        Unreviewed;       578 AA.
AC   A0A0G3WM54;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:AKL98549.1};
GN   ORFNames=Epro_1170 {ECO:0000313|EMBL:AKL98549.1};
OS   Endomicrobium proavitum.
OC   Bacteria; Elusimicrobiota; Endomicrobiia; Endomicrobiales;
OC   Endomicrobiaceae; Endomicrobium.
OX   NCBI_TaxID=1408281 {ECO:0000313|EMBL:AKL98549.1, ECO:0000313|Proteomes:UP000035337};
RN   [1] {ECO:0000313|EMBL:AKL98549.1, ECO:0000313|Proteomes:UP000035337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rsa215 {ECO:0000313|EMBL:AKL98549.1,
RC   ECO:0000313|Proteomes:UP000035337};
RA   Zheng H.;
RT   "Complete genome sequence of Endomicrobium proavitum.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP009498; AKL98549.1; -; Genomic_DNA.
DR   RefSeq; WP_052571188.1; NZ_CP009498.1.
DR   AlphaFoldDB; A0A0G3WM54; -.
DR   STRING; 1408281.Epro_1170; -.
DR   KEGG; epo:Epro_1170; -.
DR   PATRIC; fig|1408281.3.peg.1207; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000035337; 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:UP000035337};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          5..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          385..551
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   578 AA;  62669 MW;  7C7BE0A6DD7ED656 CRC64;
     MAELTGAQIL IECLLKENVE VVFGLPGGQA LPIFDAIHGS KLNFILARHE QAAGHMADGY
     ARSTGKPGVC IVTSGPGATN IVTPLATAYM DSVPLVAFSG QVSTAVIGQD AFQEADITGI
     TRPVTKHNFL VKDVKDLART IKEAFYIAST GRPGPVLVDI PVDVQRGICE LVYPEKVSIR
     SYKPNYNGHP GQIKKAASII NESKNPVFYI GTGVVVSNAE KEILEISKKA DIPVTNTLLA
     VGAYPHDTNL SLGMLGMHGT YAANKAVQAA DVIIAVGARF DDRCTGKVCD FAKAAKIIHV
     DIDPTAISKV VETDIPVVGD AKKVLEEMSG LVESKKRADW IKKIDAWKAE HPLGYERNDD
     KLHPQYVIEK ISELTKGEAV ITTEVGQHQM WSAQYYKAAN PRLFVSSGGL GTMGFGFPAA
     IGAKFGNPTK EVIAVAGDGS FQMNMQEMAI AILNDVNVKV VILNNQYLGN VRQWQEMFYG
     KRYSHTCLAK RPACPSWCNS PDRSKCPVYV PDFVKWAESY GALGIRVTHK KDVEGAIKKM
     LEAKNSVVLD VWVEIEENIF PMVPAGKSLD EIITRIGG
//
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