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Database: UniProt
Entry: P22976
LinkDB: P22976
Original site: P22976 
ID   TKT_STRPN               Reviewed;         658 AA.
AC   P22976;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   11-JUN-2014, entry version 112.
DE   RecName: Full=Probable transketolase;
DE            Short=TK;
DE            EC=2.2.1.1;
GN   Name=tkt; Synonyms=recP; OrderedLocusNames=SP_2030;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Rx / CP1200;
RX   PubMed=2361942;
RA   Radnis B.A., Rhee D.-K., Morrison D.A.;
RT   "Genetic transformation in Streptococcus pneumoniae: nucleotide
RT   sequence and predicted amino acid sequence of recP.";
RL   J. Bacteriol. 172:3669-3674(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [3]
RP   POSSIBLE FUNCTION.
RX   PubMed=8248627; DOI=10.1016/0923-2508(93)90191-4;
RA   Reizer J., Reizer A., Bairoch A., Saier M.H. Jr.;
RT   "A diverse transketolase family that includes the RecP protein of
RT   Streptococcus pneumoniae, a protein implicated in genetic
RT   recombination.";
RL   Res. Microbiol. 144:341-347(1993).
CC   -!- FUNCTION: Necessary for high-efficiency recombination chromosomal
CC       DNA during genetic transformation (PubMed:2361942).
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.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26967.1; Type=Frameshift; Positions=38, 103, 117, 129, 173, 209;
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DR   EMBL; M31296; AAA26967.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE005672; AAK76095.1; -; Genomic_DNA.
DR   PIR; A43018; XJSOKP.
DR   PIR; F95237; F95237.
DR   RefSeq; NP_346455.1; NC_003028.3.
DR   ProteinModelPortal; P22976; -.
DR   SMR; P22976; 1-657.
DR   STRING; 170187.SP_2030; -.
DR   EnsemblBacteria; AAK76095; AAK76095; SP_2030.
DR   GeneID; 932029; -.
DR   KEGG; spn:SP_2030; -.
DR   PATRIC; 19708609; VBIStrPne105772_2111.
DR   eggNOG; COG0021; -.
DR   HOGENOM; HOG000225954; -.
DR   KO; K00615; -.
DR   OMA; METVECW; -.
DR   OrthoDB; EOG6N3CRG; -.
DR   BioCyc; SPNE170187:GHGN-2075-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
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; DNA recombination; Magnesium;
KW   Metal-binding; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    658       Probable transketolase.
FT                                /FTId=PRO_0000191878.
FT   NP_BIND     113    115       Thiamine pyrophosphate (By similarity).
FT   ACT_SITE    408    408       Proton donor (By similarity).
FT   METAL       154    154       Magnesium (By similarity).
FT   METAL       184    184       Magnesium (By similarity).
FT   METAL       186    186       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING      24     24       Substrate (By similarity).
FT   BINDING      64     64       Thiamine pyrophosphate (By similarity).
FT   BINDING     155    155       Thiamine pyrophosphate; via amide
FT                                nitrogen (By similarity).
FT   BINDING     184    184       Thiamine pyrophosphate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     259    259       Thiamine pyrophosphate (By similarity).
FT   BINDING     354    354       Substrate (By similarity).
FT   BINDING     381    381       Substrate (By similarity).
FT   BINDING     434    434       Thiamine pyrophosphate (By similarity).
FT   BINDING     458    458       Substrate (By similarity).
FT   BINDING     466    466       Substrate (By similarity).
FT   BINDING     517    517       Substrate (By similarity).
FT   SITE         24     24       Important for catalytic activity (By
FT                                similarity).
FT   SITE        259    259       Important for catalytic activity (By
FT                                similarity).
FT   CONFLICT    491    497       ADARETQ -> SRCAWNE (in Ref. 1; AAA26967).
FT   CONFLICT    541    548       NAADFDTI -> MQRPTLIPS (in Ref. 1;
FT                                AAA26967).
FT   CONFLICT    573    573       I -> S (in Ref. 1; AAA26967).
FT   CONFLICT    653    653       V -> I (in Ref. 1; AAA26967).
SQ   SEQUENCE   658 AA;  71098 MW;  A0A95D17643C9C65 CRC64;
     MSNLSVNAIR FLGIDAINKA NSGHPGVVMG AAPMAYSLFT KQLHINPAQP NWINRDRFIL
     SAGHGSMLLY ALLHLSGFED VSMDEIKSFR QWGSKTPGHP EFGHTAGIDA TTGPLGQGIS
     TATGFAQAER FLAAKYNREG YNIFDHYTYV ICGDGDLMEG VSSEAASYAG LQKLDKLVVL
     YDSNDINLDG ETKDSFTESV RDRYNAYGWH TALVENGTDL EAIHAAIETA KASGKPSLIE
     VKTVIGYGSP NKQGTNAVHG APLGADETAS TRQALGWDYE PFEIPEQVYA DFKEHVADRG
     ASAYQAWTKL VADYKEAHPE LAAEVEAIID GRDPVEVTPA DFPALENGFS QATRNSSQDA
     LNVVAAKLPT FLGGSADLAH SNMTYIKTDG LQDDANRLNR NIQFGVREFA MGTILNGMAL
     HGGLRVYGGT FFVFSDYVKA AVRLSALQGL PVTYVFTHDS IAVGEDGPTH EPVEHLAGLR
     AMPNLNVFRP ADARETQAAW YLAVTSEKTP TALVLTRQNL TVEDGTDFDK VAKGAYVVYE
     NAADFDTILI ATGSEVNLAV SAAKELASQG EKIRVVSMPS TDVFDKQDAA YKEEILPNAV
     RRRVAVEMGA SQNWYKYVGL DGAVLGIDTF GASAPAPKVL AEYGFTVENL VKVVRNLK
//
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