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Database: UniProt/TrEMBL
Entry: B8DG22_LISMH
LinkDB: B8DG22_LISMH
Original site: B8DG22_LISMH 
ID   B8DG22_LISMH            Unreviewed;       664 AA.
AC   B8DG22;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JUN-2014, entry version 36.
DE   RecName: Full=Transketolase;
DE            EC=2.2.1.1;
GN   Name=tkt; OrderedLocusNames=LMHCC_1265;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/JB.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T.,
RA   Bridges S.M., Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. Can also utilize
CC       other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)
CC       (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the transketolase family.
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DR   EMBL; CP001175; ACK39612.1; -; Genomic_DNA.
DR   RefSeq; YP_002350226.1; NC_011660.1.
DR   STRING; 552536.LMHCC_1265; -.
DR   EnsemblBacteria; ACK39612; ACK39612; LMHCC_1265.
DR   GeneID; 7080197; -.
DR   KEGG; lmh:LMHCC_1265; -.
DR   PATRIC; 20317645; VBILisMon86872_1253.
DR   eggNOG; COG0021; -.
DR   HOGENOM; HOG000225954; -.
DR   KO; K00615; -.
DR   OMA; CKTHIGK; -.
DR   OrthoDB; EOG6N3CRG; -.
DR   BioCyc; LMON552536:GIW4-1300-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
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; Complete proteome; Magnesium; Metal-binding;
KW   Thiamine pyrophosphate; Transferase.
SQ   SEQUENCE   664 AA;  71871 MW;  0DF58DA07BFB2DBF CRC64;
     MFDNTDSLAV NTIRTLSMDA IQKANSGHPG LPMGAAPMAY ALWSRVLNTN PKNSHWFNRD
     RFVLSAGHGS MLLYSLLHLS GFKLELEDLK NFRQWESKTP GHPEYRYTDG VDATTGPLGQ
     GIAMAVGMAM AERHLEAKYN KDGFPVVDHY TYALCGDGDL MEGVASEAAS YAGHQQLGRL
     VVLYDSNDIS LDGDLDKSFS ENVKQRFEAY GWEHLLVKDG NDTAEILAAI EKAKQNTSQP
     TMIEVKTVIG FGAPNAGTSK VHGAPLGDEG ILEAKKAYGW NYEEKFFVPE EVTARFKETI
     GERGEKAETA WNELFASYKA EYPELAKQLE DSLNNKLPAD WDEDLPVYDE SKALASRASS
     GEVINALAGK IPTIFGGSAD LAGSNNTTIK TDGEFTKATP AERNIWFGVR EFAMGAALNG
     MALHGGLQVY GGTFFVFSDY VRAAIRLSAI QHLPVTYVMT HDSIAVGEDG PTHEPIEQLA
     SLRAMPGLSV IRPADGNEVV EAWKLAITST STPHVLVLTR QGLPTLPNSA KLTAEGVKKG
     AYVISPAKGE VPEAIILASG SEVNLAIEAQ KELQAQGTDV SVVSVPSFDL FEQQSAEYKE
     SVLPNAVRKR VAVEMGASFG WERYVGLDGK VIGIDKFGAS APGETVIKNY GFTVENVVNT
     VKSL
//
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