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Database: UniProt
Entry: G7LQR9_9GAMM
LinkDB: G7LQR9_9GAMM
Original site: G7LQR9_9GAMM 
ID   G7LQR9_9GAMM            Unreviewed;       559 AA.
AC   G7LQR9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   07-JUN-2017, entry version 19.
DE   SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:EHD23116.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:EHD23116.1};
GN   ORFNames=BrE312_3767 {ECO:0000313|EMBL:EHD23116.1};
OS   Brenneria sp. EniD312.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD23116.1, ECO:0000313|Proteomes:UP000002759};
RN   [1] {ECO:0000313|EMBL:EHD23116.1, ECO:0000313|Proteomes:UP000002759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EniD312 {ECO:0000313|EMBL:EHD23116.1,
RC   ECO:0000313|Proteomes:UP000002759};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Balakrishnan V., Glasner J., Perna N., Woyke T.;
RT   "Complete sequence of Brenneria sp. EniD312.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CM001230; EHD23116.1; -; Genomic_DNA.
DR   RefSeq; WP_009114414.1; NZ_CM001230.1.
DR   EnsemblBacteria; EHD23116; EHD23116; BrE312_3767.
DR   OrthoDB; POG091H02KO; -.
DR   Proteomes; UP000002759; Chromosome.
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   GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012782; Acetolactate_synth_catblc.
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   TIGRFAMs; TIGR02418; acolac_catab; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002759};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002759};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:EHD23116.1}.
FT   DOMAIN       13    178       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      197    331       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      393    538       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   559 AA;  60225 MW;  8651B863CD0007EF CRC64;
     MENSTGQQSW NCGAALVVKH LEQQGVQYVF GIPGAKIDRV FDALEDSPIQ TIPVRHEANG
     AFMAAAIGRL SGKAGVTLVT SGPGCCNLVT GLATATSEGD PLVAIGGAVK RAESLKLTHQ
     SLDTVSLFQP VTKFSAEVRA SSAISEVLAN AFRAAETGHP GASFISLPQD IINDPVTSAV
     LVRPDLPALN GAPQAEIDKV ARMIQRAKNP VLLLGLMASQ PKTAEALRRL LHQSQLPVTS
     TYQAAGAVDQ QSFDHFAGRV GLFNNQTGDK LLQQADLIIT VGYSPVEYDP VLWNSGKAAL
     VHIDVLPASI DSAYLPDVEL IGDITTTVDA LAGCIRAPLA LSPQTQAILR DLCQQRRDLA
     TRGMNMRGFA IHPLRLVRAM QDIVNHDVTL CVDMGSFHIW LARYLYSFRA RQVLMTNGQQ
     TMGVALPWAI AASLIHPGQK VISVSGDGGF MQSSMELETA VRLNSNVLHI IWVDNAYNMV
     EIQEEKKYHR SSGVKFGPID FKAYADAFGA QGFAVEAEDE LVSKLRQAMD VQGPAVIAIP
     VDYSDNQRLM EDLNISQLI
//
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