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Database: UniProt/TrEMBL
Entry: Q8DW01_STRMU
LinkDB: Q8DW01_STRMU
Original site: Q8DW01_STRMU 
ID   Q8DW01_STRMU            Unreviewed;       658 AA.
AC   Q8DW01;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   22-JAN-2014, entry version 84.
DE   RecName: Full=Transketolase;
DE            EC=2.2.1.1;
GN   Name=tkt; OrderedLocusNames=SMU_291;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58055.1; -; Genomic_DNA.
DR   RefSeq; NP_720749.1; NC_004350.2.
DR   ProteinModelPortal; Q8DW01; -.
DR   SMR; Q8DW01; 2-657.
DR   STRING; 210007.SMU.291; -.
DR   EnsemblBacteria; AAN58055; AAN58055; SMU_291.
DR   GeneID; 1029437; -.
DR   KEGG; smu:SMU_291; -.
DR   PATRIC; 19662831; VBIStrMut61772_0251.
DR   KO; K00615; -.
DR   OMA; CWQLALK; -.
DR   OrthoDB; EOG6N3CRG; -.
DR   ProtClustDB; PRK05899; -.
DR   BioCyc; SMUT210007:GC7Z-301-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   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; 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   658 AA;  71076 MW;  0A996A8DAFCAB68C CRC64;
     MSDLSVNAIR FLGVDAIEKS KSGHPGVVMG AAPMAYSLYT KHLRVNPSQP NWINRDRFVL
     SAGHGSMLLY ALLHLSGFED ISIDEIKNFR QWGSKTPGHP EYGHTVGVDV TTGPLGQGIS
     MAVGLAQAER FLAAKYNREG YPIFDHYTYV IAGDGDFMEG VSGEASSYAA KQNLDKLIVL
     YDSNDICLDG ETNDAFTESV RARYDAYGWH TILVEDGNNI EAIGLAIEEA KAAGKPSLIE
     IKTVIGYGAP TKGGTNAVHG APLGAEEAAA TRKALNWGYA PFEVPQEVYD DFKENVADRG
     EAAYDAWSNL VGEYRQAYPK EAREVDAIID GKDPVEIKEA DFPVYENGFS QATRNSSQDA
     INAAADVLPN FLGGSADLAH SNMTYIKADG LQDADHPLNR NIQFGVREFA MGTVLNGMAL
     HGGLRVYGGT FFVFSDYLKA AVRLSALQGV PVTYVFTHDS IAVGEDGPTH EPIEHLAGLR
     ATPNLVVFRP ADARETQAAW HYALTSQNTP TALVLTRQNL DVEAGSSFTS VAKGAYVTYE
     TDSDFNTILL ASGSEVNLAV KAAKELEAQG EKVRVVSVPS TELFDEQSAA YKEAILPNSV
     RRRVAIEMAA SQPWYKYVGL DGAVIGIDKF GASAPAAQVI ENYGFTVDNV VKVVKELK
//
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