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Database: UniProt/TrEMBL
Entry: B9KY20_THERP
LinkDB: B9KY20_THERP
Original site: B9KY20_THERP 
ID   B9KY20_THERP            Unreviewed;       536 AA.
AC   B9KY20;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   01-OCT-2014, entry version 36.
DE   SubName: Full=Probable acetolactate synthase large subunit {ECO:0000313|EMBL:ACM04855.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:ACM04855.1};
GN   OrderedLocusNames=trd_0363 {ECO:0000313|EMBL:ACM04855.1};
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC   Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC   Thermomicrobium.
OX   NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM04855.1, ECO:0000313|Proteomes:UP000000447};
RN   [1] {ECO:0000313|EMBL:ACM04855.1, ECO:0000313|Proteomes:UP000000447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2
RC   {ECO:0000313|Proteomes:UP000000447};
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E.,
RA   Bryant D.A., Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R.,
RA   Ward N.L., Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003702}.
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DR   EMBL; CP001275; ACM04855.1; -; Genomic_DNA.
DR   RefSeq; YP_002521612.1; NC_011959.1.
DR   ProteinModelPortal; B9KY20; -.
DR   STRING; 309801.trd_0363; -.
DR   EnsemblBacteria; ACM04855; ACM04855; trd_0363.
DR   GeneID; 7354730; -.
DR   KEGG; tro:trd_0363; -.
DR   PATRIC; 23911946; VBITheRos91376_0357.
DR   eggNOG; COG0028; -.
DR   HOGENOM; HOG000258446; -.
DR   KO; K01652; -.
DR   OMA; PCAIALQ; -.
DR   OrthoDB; EOG6DJXX1; -.
DR   BioCyc; TROS309801:GI0S-361-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 {ECO:0000313|Proteomes:UP000000447};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000447};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004476};
KW   Transferase {ECO:0000313|EMBL:ACM04855.1}.
SQ   SEQUENCE   536 AA;  57601 MW;  187D1631B895EE47 CRC64;
     MRVTGGEAVV RTLERLGVEV VFGIPGVHTL AIYDALYSSP IRHVLARHEQ GAGFMADGYA
     RVSGKPGVAI VITGPGVTNI ATAIGEAYAD SSPVVVIASN VEQAWQGQML GHLHDCKDQL
     GIMRVVTKWA DRARSVEDVP RLLRTAFAEA ISGRRRPTHL EVPLDVLHGS GDIELAHLAP
     LSMERSQPRR SAIELAARMI EEAERVVLYC GGGVVASGAT AELSALAERL GAAVITSLQG
     KGAIPEDHPR CLGNLWEPEN AVERVLRESD LVIVIGSKLG AQDTANGRLP LPDRRIRIDI
     DAQEILRNYP PTLPIVADAR ETVRALLSEL TSRGITKQGW PVDVLQATKR EALATAWGAG
     QAEWLRAIRA VLPRDGILVS DMTMMAYVGN RHYPVYEPGT YLFPTGYGTL GFALPAAIGA
     KIARPEAAVV ALVGDGGYQF TMQELATAVQ FRIGIPIILF NDASYTAVKD EQARSFGGRF
     IAVDLVNPDF QKLAAAYGIP SEYVTSPQTL EGAIARALER DLPTLIEVPI DFPLGA
//
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