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Database: UniProt/TrEMBL
Entry: Q022M2_SOLUE
LinkDB: Q022M2_SOLUE
Original site: Q022M2_SOLUE 
ID   Q022M2_SOLUE            Unreviewed;       588 AA.
AC   Q022M2;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   11-JUN-2014, entry version 51.
DE   SubName: Full=Acetolactate synthase, large subunit;
DE            EC=2.2.1.6;
GN   OrderedLocusNames=Acid_3099;
OS   Solibacter usitatus (strain Ellin6076).
OC   Bacteria; Acidobacteria; Solibacteres; Solibacterales;
OC   Solibacteraceae; Candidatus Solibacter.
OX   NCBI_TaxID=234267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin6076;
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B.,
RA   Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J.,
RA   Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D.,
RA   Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C.,
RA   Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S.,
RA   Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C.,
RA   Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D.,
RA   Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L.,
RA   Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
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DR   EMBL; CP000473; ABJ84078.1; -; Genomic_DNA.
DR   RefSeq; YP_824363.1; NC_008536.1.
DR   ProteinModelPortal; Q022M2; -.
DR   STRING; 234267.Acid_3099; -.
DR   EnsemblBacteria; ABJ84078; ABJ84078; Acid_3099.
DR   GeneID; 4428677; -.
DR   KEGG; sus:Acid_3099; -.
DR   PATRIC; 32008552; VBICanSol30224_3246.
DR   eggNOG; COG0028; -.
DR   HOGENOM; HOG000258449; -.
DR   KO; K01652; -.
DR   OMA; TAFGCNE; -.
DR   OrthoDB; EOG6MH5BB; -.
DR   BioCyc; SUSI234267:GHSK-3127-MONOMER; -.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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; 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   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Thiamine pyrophosphate; Transferase.
SQ   SEQUENCE   588 AA;  62986 MW;  1157CD9CD6159247 CRC64;
     MKTADLIVRT HISEGEKRIA AYQLVDYLER LGVEVIFGLC GHTVIAFLDA LRGSRIKFIS
     TRHEQVAAHA ADGYARASGK PGVLMTHLGP GLTNAATGVA NAALDSIPMV VIAGDVPSHY
     FGRHPHQEVN LHMDADQYEI YRPFCKRIYR VDRVADLPRI VERAFHLSQA GRPGPVLVDV
     PMDIFSADLP AGAFSQMPAP IVRPTIDAST AERIAQALAE AERPVLYVGG GVLGGNATNE
     LLALAEALEV PVAHTLMGKG CMREDHPLLL GMTGFWGTPI ANETCRTADL IVAVGTRLAE
     ANSSSWDPRF TFDIPPTRLI HIDIDAAEIG RNFATELGVV ADSRMALGAI AHAARGKYRS
     ERGDLRERIA AGRAAFASTW ADQWSSDQYP MRPERILSEL KKAIPEDGFI VTDVGWNKNG
     VGQQYPITVP GTFVTPSGLA TMGFGPSAVL GVKMAQPQRA AVALIGDGGF GSNPSVVATA
     MEAELAVVWL VMDNSAYGTI AGLEKAHYGT SFGCLFERQG RPYSVDYAAL ARSYGAGGIR
     ISAADELGPA LREALASGMP TVIQAEMENA PTPTPGHWNI NDIYRRGD
//
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