TKT_STRPN
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 03-AUG-2022, entry version 148.
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; DOI=10.1128/jb.172.7.3669-3674.1990;
RA Radnis B.A., Rhee D.-K., Morrison D.A.;
RT "Genetic transformation in Streptococcus pneumoniae: nucleotide sequence
RT 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., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA 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 recombination.";
RL Res. Microbiol. 144:341-347(1993).
CC -!- FUNCTION: Necessary for high-efficiency recombination chromosomal DNA
CC during genetic transformation. {ECO:0000269|PubMed:2361942}.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26967.1; Type=Frameshift; Evidence={ECO:0000305};
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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; WP_000067853.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P22976; -.
DR SMR; P22976; -.
DR STRING; 170187.SP_2030; -.
DR EnsemblBacteria; AAK76095; AAK76095; SP_2030.
DR KEGG; spn:SP_2030; -.
DR eggNOG; COG0021; Bacteria.
DR OMA; NSGHSGM; -.
DR PhylomeDB; P22976; -.
DR BioCyc; SPNE170187:G1FZB-2100-MON; -.
DR Proteomes; UP000000585; Chromosome.
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 CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
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; DNA recombination; Magnesium; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..658
FT /note="Probable transketolase"
FT /id="PRO_0000191878"
FT ACT_SITE 408
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 113..115
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 24
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 491..497
FT /note="ADARETQ -> SRCAWNE (in Ref. 1; AAA26967)"
FT /evidence="ECO:0000305"
FT CONFLICT 541..548
FT /note="NAADFDTI -> MQRPTLIPS (in Ref. 1; AAA26967)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="I -> S (in Ref. 1; AAA26967)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="V -> I (in Ref. 1; AAA26967)"
FT /evidence="ECO:0000305"
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
