TKT_MYCLE
ID TKT_MYCLE Reviewed; 699 AA.
AC P46708;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=ML0583; ORFNames=B1496_F1_26, MLCL536.38;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; U00013; AAA17139.1; -; Genomic_DNA.
DR EMBL; Z99125; CAB16182.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30091.1; -; Genomic_DNA.
DR PIR; S72772; S72772.
DR RefSeq; NP_301494.1; NC_002677.1.
DR RefSeq; WP_010907818.1; NC_002677.1.
DR AlphaFoldDB; P46708; -.
DR SMR; P46708; -.
DR STRING; 272631.ML0583; -.
DR EnsemblBacteria; CAC30091; CAC30091; CAC30091.
DR KEGG; mle:ML0583; -.
DR PATRIC; fig|272631.5.peg.1017; -.
DR Leproma; ML0583; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_11; -.
DR OMA; HHTEGIE; -.
DR Proteomes; UP000000806; 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; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..699
FT /note="Transketolase"
FT /id="PRO_0000191861"
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 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 699 AA; 75642 MW; 64900CFB9B4A4481 CRC64;
MTTLDQISTL TQPRHPDDWT EIDSAAVDTI RVLATDAVQK AGNGHPGTAM SLAPLAYTLF
QRTLRHDPND TAWLGRDRFV LSAGHSSLTL YIQLYLGGFG LELSDIESLR TWGSTTPGHP
EFRHTKGVEI TTGPLGQGLA SAVGMAMASR YERGLFDPDA EPGASPFDHY IYVIASDGDI
EEGVTSEASS LAAVQQLGNL IVFYDHNQIS IEGDTKITLC EDTAARYRAY GWHVQEVEGG
ENVVGIEEAI ANAKAATDRP SFISLRTIIG YPAPTLINTG KAHGAALGED EVAATKRILG
FDPDKTFAVR EDVITHTRGL IARGKEAHER WQLEFEAWAQ REPERKALLD RLLAQQLPDG
WDADLPNWEP RSKELATRAA SGAVLSAIGP KLPELWGGSA DLAGSNNTTI KDVDSFGPPS
ISTDEYTAHW YGRTLHFGVR EHAMGAILSG IVLHGPTRAY GGTFLQFSDY MRPSVRLASL
MDIDTIYVWT HDSVGLGEDG PTHQPIEHLA ALRAIPRLSV VRPADANETA YAWRTILARG
ANSGPVGLIL TRQSVPVLEG TNTEGVARGG YVLGDGGSSE AKEPDVILIA TGSEVQLAVA
AQKLLADKDI IVRVVSMPCV EWFESQPYEY RDSVLPPSVS ARVAVEAGVA QCWHKLVGDT
GKIVSIEHYG ESADYQTLFR EYGFTPEAVV AAAEQVLDN
