TKT_MYCGE
ID TKT_MYCGE Reviewed; 648 AA.
AC P47312; Q49280;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; Synonyms=tktA; OrderedLocusNames=MG066;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71284.1; -; Genomic_DNA.
DR EMBL; U02154; AAD12435.1; -; Genomic_DNA.
DR PIR; C64207; C64207.
DR RefSeq; WP_010869316.1; NC_000908.2.
DR AlphaFoldDB; P47312; -.
DR SMR; P47312; -.
DR STRING; 243273.MG_066; -.
DR EnsemblBacteria; AAC71284; AAC71284; MG_066.
DR KEGG; mge:MG_066; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_14; -.
DR OMA; YALQQTD; -.
DR OrthoDB; 188169at2; -.
DR BioCyc; MGEN243273:G1GJ2-71-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..648
FT /note="Transketolase"
FT /id="PRO_0000191859"
FT ACT_SITE 397
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 109..111
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 22
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 252
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="G -> C (in Ref. 2; AAD12435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 73785 MW; 0252E8DDD2BFB453 CRC64;
MKYLYATQHL TLNAIKHAKG GHVGMAIGAS PILFSLFTKH FHFDPDQPKW INRDRFVLSA
GHGSMALYSI FHFAGLISKQ EILQHKHGQI NTSSHPEYAP NNFIDASTGP LGQGFGMAVG
MVLAQKLLAN EFKELSDKLF DHYTYVVVGD GDLQEGVSYE VSQIAGLYKL NKLIVLHDSN
RVQMDSEVKK VANENLKVRF ENVGWNYIHT DDQLENIDQA IIKAKQSDKP TFIEVRTTIA
KNTHLEDQYG GHWFIPNEVD FQLFEKRTNT NFNFFNYPDS IYHWFKQTVI ERQKQIKEDY
NNLLISLKDK PLFKKFTNWI DSDFQALYLN QLDEKKVAKK DSATRNYLKD FLNQINNPNS
NLYCLNADVS RSCFIKIGDD NLHENPCSRN IQIGIREFAM ATIMNGMALH GGIKVMGGTF
LAFADYSKPA IRLGALMNLP VFYVYTHDSY QVGGDGPTHQ PYDQLPMLRA IENVCVFRPC
DEKETCAGFN YGLLSQDQTT VLVLTRQPLK SIDNTDSLKT LKGGYILLDR KQPDLIIAAS
GSEVQLAIEF EKVLTKQNVK VRILSVPNIT LLLKQDEKYL KSLFDANSSL ITIEASSSYE
WFCFKKYVKN HAHLGAFSFG ESDDGDKVYQ QKGFNLERLM KIFTSLRN
