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Database: UniProt
Entry: A0A0M1JFH9_9GAMM
LinkDB: A0A0M1JFH9_9GAMM
Original site: A0A0M1JFH9_9GAMM 
ID   A0A0M1JFH9_9GAMM        Unreviewed;       572 AA.
AC   A0A0M1JFH9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JAN-2018, entry version 17.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=TI04_00570 {ECO:0000313|EMBL:KOR31480.1};
OS   Achromatium sp. WMS2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Achromatium.
OX   NCBI_TaxID=1604835 {ECO:0000313|EMBL:KOR31480.1, ECO:0000313|Proteomes:UP000037003};
RN   [1] {ECO:0000313|EMBL:KOR31480.1, ECO:0000313|Proteomes:UP000037003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMS2 {ECO:0000313|EMBL:KOR31480.1};
RX   PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA   Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT   "Metabolic diversity and ecological niches of Achromatium populations
RT   revealed with single-cell genomic sequencing.";
RL   Front. Microbiol. 6:822-822(2015).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
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.
CC       {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|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KOR31480.1}.
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DR   EMBL; JXSN01000004; KOR31480.1; -; Genomic_DNA.
DR   EnsemblBacteria; KOR31480; KOR31480; TI04_00570.
DR   PATRIC; fig|1604835.3.peg.1515; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000037003; 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   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037003};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037003};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:KOR31480.1}.
FT   DOMAIN        4    169       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      195    328       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      393    542       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   572 AA;  63299 MW;  D52D364AAE6EE92A CRC64;
     MELSGAEIVV QALQDEGVEY VFGYPGGAVL HIYDAIFKSQ AFKHVLVRHE QGAVHAADGY
     SRSTGKPGVA LVTSGPGATN AVTGLATAYM DSVPLIVISG QVPTPVIGSD AFQEVDTVGI
     TRPCTKHNFL VKDPRLLAET FKRAFHIATT GRPGPVLIDI PKDVTDPNVT VSYEYPKSIK
     LRSYNPAQAG HLGQIKKAVE LVTKAERPMV YTGGGVIHGE ASKELTELVK HMNLPITQTL
     MGLGSYPGTD KQFLGMLGMH GTYEANMAMH ECDVLLAIGV RFDDRVTGKL DQFCPDAAII
     HIDIDPSSIS KNVRVDVPIV GPVKSVLRDF LRLVKEESWT GNNQLQQLWW QQIETWRSRL
     CLNYDRNSSK IKPQFAIETL YNITNGELYL TSDVGQHQMF AAQFYKFNEP RRWINSGGLG
     TMGFGLPSAM GVQLAHPGKP VACISGEASI LMCIQELATC KQHDLPIKIV LLNNGYMGMV
     RQWQEMFYDK RYSHSYVEAL PDFVKLAESF GHVGMNLERP QDLEPAMREA FAMKDRLVFM
     NVIVDPEENV YPMIAMGQGH HNMHLAPERE LA
//
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