TKT_MYCTU
ID TKT_MYCTU Reviewed; 700 AA.
AC P9WG25; L0T9N4; O06811;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=Rv1449c; ORFNames=MTCY493.05;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP THIAMINE DIPHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22645655; DOI=10.1098/rsob.110026;
RA Fullam E., Pojer F., Bergfors T., Jones T.A., Cole S.T.;
RT "Structure and function of the transketolase from Mycobacterium
RT tuberculosis and comparison with the human enzyme.";
RL Open Biol. 2:E10026-E10026(2012).
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.
CC {ECO:0000269|PubMed:22645655}.
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 Evidence={ECO:0000269|PubMed:22645655};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22645655};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:22645655};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22645655};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:22645655};
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+).
CC {ECO:0000269|PubMed:22645655};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:22645655};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000269|PubMed:22645655};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for ribose 5-phosphate {ECO:0000269|PubMed:22645655};
CC KM=0.6 mM for fructose 6-phosphate {ECO:0000269|PubMed:22645655};
CC KM=0.35 mM for xylulose 5-phosphate {ECO:0000269|PubMed:22645655};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22645655}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44208.1; -; Genomic_DNA.
DR PIR; D70917; D70917.
DR RefSeq; NP_215965.1; NC_000962.3.
DR RefSeq; WP_003916819.1; NZ_NVQJ01000071.1.
DR PDB; 3RIM; X-ray; 2.49 A; A/B/C/D=1-700.
DR PDBsum; 3RIM; -.
DR AlphaFoldDB; P9WG25; -.
DR SMR; P9WG25; -.
DR STRING; 83332.Rv1449c; -.
DR iPTMnet; P9WG25; -.
DR PaxDb; P9WG25; -.
DR DNASU; 886638; -.
DR GeneID; 886638; -.
DR KEGG; mtu:Rv1449c; -.
DR TubercuList; Rv1449c; -.
DR eggNOG; COG0021; Bacteria.
DR OMA; HHTEGIE; -.
DR PhylomeDB; P9WG25; -.
DR BRENDA; 2.2.1.1; 3445.
DR SABIO-RK; P9WG25; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..700
FT /note="Transketolase"
FT /id="PRO_0000191863"
FT ACT_SITE 441
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 85
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 133..135
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 135
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22645655"
FT BINDING 178
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22645655"
FT BINDING 207
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:22645655"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
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 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"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 21..41
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 319..341
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 441..454
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 465..471
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 526..537
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 538..541
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 552..555
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 586..591
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:3RIM"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 621..626
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 629..635
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:3RIM"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 676..682
FT /evidence="ECO:0007829|PDB:3RIM"
FT HELIX 687..698
FT /evidence="ECO:0007829|PDB:3RIM"
SQ SEQUENCE 700 AA; 75589 MW; CF357AC84837B98D CRC64;
MTTLEEISAL TRPRHPDYWT 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
