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Database: UniProt/TrEMBL
Entry: F2QGM3_STROU
LinkDB: F2QGM3_STROU
Original site: F2QGM3_STROU 
ID   F2QGM3_STROU            Unreviewed;       658 AA.
AC   F2QGM3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   26-NOV-2014, entry version 21.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   Name=tktA {ECO:0000313|EMBL:CBY99884.1};
GN   OrderedLocusNames=SOR_0183 {ECO:0000313|EMBL:CBY99884.1};
OS   Streptococcus oralis (strain Uo5).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=927666 {ECO:0000313|Proteomes:UP000008131};
RN   [1] {ECO:0000313|Proteomes:UP000008131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uo5 {ECO:0000313|Proteomes:UP000008131};
RX   PubMed=21460080; DOI=10.1128/JB.00321-11;
RA   Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B.,
RA   Maurer P., Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT   "Genome of Streptococcus oralis strain Uo5.";
RL   J. Bacteriol. 193:2888-2889(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.
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   -!- COFACTOR:
CC       Note=Binds 1 magnesium ion per subunit. Can also utilize other
CC       divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- COFACTOR:
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996}.
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DR   EMBL; FR720602; CBY99884.1; -; Genomic_DNA.
DR   RefSeq; YP_004325225.1; NC_015291.1.
DR   EnsemblBacteria; CBY99884; CBY99884; SOR_0183.
DR   GeneID; 10415465; -.
DR   KEGG; sor:SOR_0183; -.
DR   PATRIC; 54422970; VBIStrOra177080_0156.
DR   KO; K00615; -.
DR   BioCyc; SORA927666:GH8G-183-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 {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008131};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00021604};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00021567};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00021572};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00021577}.
SQ   SEQUENCE   658 AA;  70927 MW;  07932755C6C95AC4 CRC64;
     MSNLSVNAIR FLGIDAINKA NSGHPGVVMG AAPMAYSLFT KQLRINPAQP NWINRDRFIL
     SAGHGSMLLY ALLHLSGFED VSMDEIKSFR QWGSKTPGHP EFGHTAGVDA TTGPLGQGIS
     TATGFAQAER FLAAKYNREG FNIFDHYTYV ICGDGDLMEG VSSEAASYAG LQKLDKLVVL
     YDSNDINLDG ETKDSFTESV RDRYNAYGWY TALVEDGTDL EAIHAAIEAA KASGKPSLIE
     VKTVIGYGSP NKQGTNAVHG APLGADETAA TRQALGWDYE PFEIPEQVYA DFKENVADRG
     ASAYQAWTKL VADYKEAHPE LAAEVEAIID GRDPVKVTPA DFPALENGFS QATRNSSQDA
     LNVVAAKLPT FLGGSADLAH SNMTYIKTDG LQDDANRLNR NIQFGVREFA MGTILNGMAL
     HGGLRVYGGT FFVFSDYVKA AVRLSALQGL PVTYVFTHDS IAVGEDGPTH EPVEHLAGLR
     AMPNLNVFRP ADARETQAAW YLAVTSEKTP TALVLTRQNL TVEEGTDFDK VAKGAYVVYE
     NAADFDTILI ATGSEVNLVV AAAKELASQG AKVRVVSMPS TDVFDAQDAA YKEEILPNAV
     RRRVAVEMGA TQNWYKYVGL DGAVLGIDTF GASAPAPKVL AEYGFTVENL VKVVQNLK
//
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