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Database: UniProt
Entry: A0A0P6WWB6_9CHLR
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ID   A0A0P6WWB6_9CHLR        Unreviewed;       574 AA.
AC   A0A0P6WWB6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ADM99_02790 {ECO:0000313|EMBL:KPL73184.1};
OS   Leptolinea tardivitalis.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Leptolinea.
OX   NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL73184.1, ECO:0000313|Proteomes:UP000050430};
RN   [1] {ECO:0000313|EMBL:KPL73184.1, ECO:0000313|Proteomes:UP000050430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL73184.1,
RC   ECO:0000313|Proteomes:UP000050430};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL   Submitted (JUL-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:KPL73184.1}.
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DR   EMBL; LGCK01000006; KPL73184.1; -; Genomic_DNA.
DR   RefSeq; WP_062421572.1; NZ_LGCK01000006.1.
DR   AlphaFoldDB; A0A0P6WWB6; -.
DR   STRING; 229920.ADM99_02790; -.
DR   PATRIC; fig|229920.5.peg.2185; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000050430; 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:UP000050430};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:KPL73184.1}.
FT   DOMAIN          4..117
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          387..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  62746 MW;  3D86B5B474F932F3 CRC64;
     MKLTGAQIVW ECLQREGVEV VFGYPGGASL PIYDALHDYN IHHVLVRHEQ GAAHMADGYA
     RASGKVGVAL ATSGPGATNL VTGIATAMMD SVPVVFITAQ VHSKLIGYDA FQEVDVTGIT
     LPITKHNYLV TDVKDIAHTL REAFYIARTG RPGPVLVDIT KDAQQNSIEY DPDSEPIHLR
     GYRPTALPVE DDIQKAVTMI HSAKRPVILA GHGVLQSGAM KEVLEFAERT QTPVAMTLLG
     ISGFPASHPL NLGMMGMHGE AWVNHAIQDA DLLLAFGMRF DDRVTGDVRR YATHARKIHI
     DIDPAEINKN VRVDLALVGD LSQTLEQILK HVKPGRHDEW LASINEMKGS SSVRDIQNLP
     DNGHLYAAHV INDLWNITKG NAVIVTDVGQ NQMWTAQYYR QDNPSQFITS GGLGTMGFGL
     PAGIGAKFGQ PDKEVWVICG DGGFQMTQAE LATAAQEGIK VNIAILNNGY LGMVRQWQEF
     FYDRRYSATP MKSPDFIKIA DAHGLTGMRV TTRADVETAI QTARETEGTV VIDFRVEKED
     SVYPMVPTGS ELKEMIRRPL PAAVAVNEAV KVEA
//
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