TKT_MYCTO
ID TKT_MYCTO Reviewed; 700 AA.
AC P9WG24; L0T9N4; O06811;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=MT1496;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group
CC from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing
CC xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of
CC a two-carbon ketol group from a ketose donor to an aldose acceptor, via
CC a covalent intermediate with the cofactor thiamine pyrophosphate (By
CC similarity). {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 Note=Binds 1 Mg(2+) ion per subunit. {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=AAK45759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45759.1; ALT_INIT; Genomic_DNA.
DR PIR; D70917; D70917.
DR RefSeq; WP_003407451.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WG24; -.
DR SMR; P9WG24; -.
DR EnsemblBacteria; AAK45759; AAK45759; MT1496.
DR KEGG; mtc:MT1496; -.
DR PATRIC; fig|83331.31.peg.1608; -.
DR HOGENOM; CLU_009227_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; Magnesium; Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..700
FT /note="Transketolase"
FT /id="PRO_0000428436"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 133..135
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 45
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 283
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 700 AA; 75541 MW; 6591502AAFBA905C CRC64;
MTTLEEISAL TRPRHPDDWT EIDSAAVDTI RVLAADAVQK VGNGHPGTAM SLAPLAYTLF
QRTMRHDPSD THWLGRDRFV LSAGHSSLTL YIQLYLGGFG LELSDIESLR TWGSKTPGHP
EFRHTPGVEI TTGPLGQGLA SAVGMAMASR YERGLFDPDA EPGASPFDHY IYVIASDGDI
EEGVTSEASS LAAVQQLGNL IVFYDRNQIS IEDDTNIALC EDTAARYRAY GWHVQEVEGG
ENVVGIEEAI ANAQAVTDRP SFIALRTVIG YPAPNLMDTG KAHGAALGDD EVAAVKKIVG
FDPDKTFQVR EDVLTHTRGL VARGKQAHER WQLEFDAWAR REPERKALLD RLLAQKLPDG
WDADLPHWEP GSKALATRAA SGAVLSALGP KLPELWGGSA DLAGSNNTTI KGADSFGPPS
ISTKEYTAHW YGRTLHFGVR EHAMGAILSG IVLHGPTRAY GGTFLQFSDY MRPAVRLAAL
MDIDTIYVWT HDSIGLGEDG PTHQPIEHLS ALRAIPRLSV VRPADANETA YAWRTILARR
NGSGPVGLIL TRQGVPVLDG TDAEGVARGG YVLSDAGGLQ PGEEPDVILI ATGSEVQLAV
AAQTLLADND ILARVVSMPC LEWFEAQPYE YRDAVLPPTV SARVAVEAGV AQCWHQLVGD
TGEIVSIEHY GESADHKTLF REYGFTAEAV AAAAERALDN
