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Database: UniProt/TrEMBL
Entry: D6XU56_BACIE
LinkDB: D6XU56_BACIE
Original site: D6XU56_BACIE 
ID   D6XU56_BACIE            Unreviewed;       665 AA.
AC   D6XU56;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   02-NOV-2016, entry version 46.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   OrderedLocusNames=Bsel_1836 {ECO:0000313|EMBL:ADH99342.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99342.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH99342.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS00570687}.
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DR   EMBL; CP001791; ADH99342.1; -; Genomic_DNA.
DR   RefSeq; WP_013172764.1; NC_014219.1.
DR   ProteinModelPortal; D6XU56; -.
DR   STRING; 439292.Bsel_1836; -.
DR   EnsemblBacteria; ADH99342; ADH99342; Bsel_1836.
DR   KEGG; bse:Bsel_1836; -.
DR   PATRIC; 38123009; VBIBacSel78655_1948.
DR   eggNOG; ENOG4105CV1; Bacteria.
DR   eggNOG; COG0021; LUCA.
DR   HOGENOM; HOG000225954; -.
DR   KO; K00615; -.
DR   OMA; GDLINHY; -.
DR   OrthoDB; POG091H02B4; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR11624; PTHR11624; 2.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460037};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00459980};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460013}.
FT   DOMAIN       14     34       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   665 AA;  72287 MW;  8CE6F2007A657A0A CRC64;
     MSTEIHEKAI NTIRTLSIDA IEKANSGHPG LPMGAAPMAY KVFTDFMNHN PKNPDWFNRD
     RFVLSAGHGS MLLYSLLHLH GYDLSLDELK NFRQWGSKTP GHPEYGHTAG VEATTGPLGQ
     GIAMAVGMAM AEQHLSGKYN TDDFNIVDHY TYALCGDGDL MEGVSAEAAS LAGHLKLGKL
     VLLYDSNDIS LDGDLHQSFS EDVRKRFDAY GWHTLYVEDG NDLDAIGKAI EEGRNDDRPT
     MIEIKTVIGY GSPNKGGKNA AHGAPLGADE VKLAKEAYKW PSEEPFHIPE DVKAHYEQYK
     QQGAEAEEAW NSLFEKYKAA YPEQGKELAL AIEGKLPEGW AEELPVYEEG SKAATRATGG
     EVLNAVAKSV PSLFGGSADL ASSNKTMLNG EEDFSRDQHS GRNIWFGVRE FAMAAAANGM
     ALHGGVRPYA ATFFVFSDYL RPAVRLSALM GVPVTYVFTH DSIAVGEDGP THEPVEQLAA
     MRAIPNLSLI RPADGNETQA AWRLAMETTD QPTALVLTRQ NLPVLKGTKE NAYEGVKKGA
     YVVSDANGNK DGLLLATGSE VSLAVEAQKL LEKDGIHVAV VSMPSWDRFE AQDQAYKDEV
     LPPALTKRLA VEVANPLGWD RYTTSDGSIL GIDGYGASAP GDLIMEKYGF IAENVVARFK
     QMLNK
//
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