UniProt: C6WUC9

Database: UniProt
Entry: C6WUC9_METML

LinkDB:  C6WUC9_METML 
Original site:  C6WUC9_METML

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (8)   
   Pfam (3)   
Literature (1)   
   PubMed (1)   
All databases (22)   

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ID   C6WUC9_METML            Unreviewed;       574 AA.
AC   C6WUC9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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   OrderedLocusNames=Mmol_0618 {ECO:0000313|EMBL:ACT47528.1};
OS   Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT47528.1, ECO:0000313|Proteomes:UP000002742};
RN   [1] {ECO:0000313|Proteomes:UP000002742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC   {ECO:0000313|Proteomes:UP000002742};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT   "Complete sequence of Methylotenera mobilis JLW8.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACT47528.1, ECO:0000313|Proteomes:UP000002742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC   {ECO:0000313|Proteomes:UP000002742};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
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|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; CP001672; ACT47528.1; -; Genomic_DNA.
DR   RefSeq; WP_015831565.1; NC_012968.1.
DR   AlphaFoldDB; C6WUC9; -.
DR   STRING; 583345.Mmol_0618; -.
DR   KEGG; mmb:Mmol_0618; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_4; -.
DR   OrthoDB; 2254214at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002742; 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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
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}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002742};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          11..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          200..335
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          398..546
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  63293 MW;  827A697897F97ED3 CRC64;
     MAETTHPQQI TGAEIVIRCL EQESVKFLFG YPGGAVLHIY DAIYKQGHFK HILVRHEQAA
     VHAADAFARA TGEVGVALVT SGPGATNAIT GIATAYMDSI PLVVISGQVP VPAIGLDAFQ
     EVDMVGVTRP CVKHNFLVKD VKDIATTLKK AFHIARTGRP GPVVVDIPKD ITAHFADFVY
     PESVEMRSYN PVTKGHSGQI KKAVKLLLEA ERPMVYTGGG LVLGDASEAL VKLVRALGVP
     VTNTLMGLGG YPSTDKQFLG MLGMHGTYEA NMAMQNCDVL LAVGARFDDR VIGNTDHFYS
     KDRTIIHVDI DPSSISKRVK VHVPIVGDVK SVLAEMNELV ALEKPTPSPA LKAWWAQIDS
     WRSKLCLDYS NNNGLIKPQY VIEKLWEVTK GEAYVTSDVG QHQMWAAQYY KFDKPRRWIN
     SGGLGTMGVG LPYAMGCQFA DPTAQVACVT GEGSIQMNIQ ELSTCKQYSL PIKVILLNNR
     YLGMVRQWQE FFYENRYSES YMESLPDFVK LAESYGHVGM QITKPEDVEG ALKEAFDMKS
     RFVFMDFITD QKENVFPMIP NGKGLSEMIL AEDL
//

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