TKT_MYCBO
ID TKT_MYCBO Reviewed; 700 AA.
AC P59956; A0A1R3XYE3; X2BHN3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; OrderedLocusNames=BQ2027_MB1484C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT708304; SIU00087.1; -; Genomic_DNA.
DR RefSeq; NP_855136.1; NC_002945.3.
DR RefSeq; WP_003407451.1; NC_002945.4.
DR AlphaFoldDB; P59956; -.
DR SMR; P59956; -.
DR EnsemblBacteria; SIU00087; SIU00087; BQ2027_MB1484C.
DR PATRIC; fig|233413.5.peg.1623; -.
DR OMA; HHTEGIE; -.
DR Proteomes; UP000001419; 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_0000191860"
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 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
