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 01-MAY-2013, entry version 107.
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; QPWYKYV; -.
DR ProtClustDB; PRK05899; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
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; Transketo_C_like; 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
//
