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Database: UniProt
Entry: A0A0M2SRI9_9BACI
LinkDB: A0A0M2SRI9_9BACI
Original site: A0A0M2SRI9_9BACI 
ID   A0A0M2SRI9_9BACI        Unreviewed;       545 AA.
AC   A0A0M2SRI9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-DEC-2017, entry version 11.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KKK36291.1};
GN   ORFNames=WQ57_19965 {ECO:0000313|EMBL:KKK36291.1};
OS   Bacillus campisalis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK36291.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK36291.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK36291.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar
RT   saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK36291.1}.
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DR   EMBL; LAYY01000034; KKK36291.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKK36291; KKK36291; WQ57_19965.
DR   PATRIC; fig|1408103.3.peg.4420; -.
DR   Proteomes; UP000034166; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034166};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN        4    170       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      188    322       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      380    526       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
FT   COILED      312    332       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   545 AA;  59662 MW;  716ED4E9E5F59665 CRC64;
     MKVKAAQLLI KCLEQEGVEY IFGVPGEENL DIMDALLDSE IEFIVTRHEA NAAFMAGTYG
     RLTGKPGVCL ATLGPGATNL LTGVANANMD HSPIVAITGQ AGLDRQHKIS HQYYDLVSVY
     EPVTKWNTQV KKAEIIPEVV RKAFEVAKGE KPGAAHIDLP EDIAAQDVDA TPIEVRKPTK
     FEAGERVIKE AATMIEKAKH PLILAGMGVE RGHAEGSLRK LVEKVDIPVV HTFMGKGAIS
     WRNDLSLLTA GLSGKDYISC GFEEADLIIA VGFDMAEYPP KNWNPGGQTP VLHVDTREAE
     TDAHYPVEHS VIGDLAENLK QLESAMSAAK RNNDWVSHVR EQALQESDAF SGDESFPVKP
     QKIISDLRSV MREEDIVISD VGAHKMWMAR MYHAYEPNTC LISNGLASMG IAVPGAIAAK
     MVHPEKNVVA VCGDGAFQMS SADLETAVRL KLPIVILLWR DEGYGLIEWK QLNEFKRASN
     VKFGNPDFIQ LAKSYGFEAI GIREGGQLKD ALQEAIDLNK PVLIDCPVDY SENTKLTERL
     GKLLC
//
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