TKT_SCHPO
ID TKT_SCHPO Reviewed; 685 AA.
AC Q9URM2; P78824;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN ORFNames=SPBC2G5.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-685.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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; CU329671; CAA21881.1; -; Genomic_DNA.
DR EMBL; D89172; BAA13834.1; -; mRNA.
DR PIR; T40162; T40162.
DR PIR; T42537; T42537.
DR RefSeq; NP_596066.1; NM_001021977.2.
DR AlphaFoldDB; Q9URM2; -.
DR SMR; Q9URM2; -.
DR BioGRID; 276969; 5.
DR STRING; 4896.SPBC2G5.05.1; -.
DR iPTMnet; Q9URM2; -.
DR MaxQB; Q9URM2; -.
DR PaxDb; Q9URM2; -.
DR PRIDE; Q9URM2; -.
DR EnsemblFungi; SPBC2G5.05.1; SPBC2G5.05.1:pep; SPBC2G5.05.
DR GeneID; 2540441; -.
DR KEGG; spo:SPBC2G5.05; -.
DR PomBase; SPBC2G5.05; -.
DR VEuPathDB; FungiDB:SPBC2G5.05; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; Q9URM2; -.
DR OMA; HHTEGIE; -.
DR PhylomeDB; Q9URM2; -.
DR PRO; PR:Q9URM2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IDA:PomBase.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; EXP:PomBase.
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 2: Evidence at transcript level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..685
FT /note="Probable transketolase"
FT /id="PRO_0000191903"
FT ACT_SITE 422
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 121..123
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 268
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 685 AA; 75182 MW; 1749F5A28770A408 CRC64;
MTSSSYTDID TLAINTIRTL AVDTTAHAKS GHPGAPMGLA PAAHVLFSRI MKFNPAHPKW
LNRDRFILSN GHACVLQYIM CHLLGYKLTI EDLKQFRQVG SKTPGHPETH NPDLNIETGA
GPLGQGIASA VGLAIGKAHS AAVYNKPGFD LFSNYTFCFL GDGCLQEGVS SEACSLAGHL
KLSNLIAVWD NNKITIDGAT SMSFDEDVEK RFEAYGWNIV RVANGDTDLD GIEKGFREAM
SCTDKPTLIN LKTTIGYGSE LQGTHSVHGS PLKPEDCVHV KKLFGFDPTK TFQVPPEVYA
YYKERVAIAS SAEEEYKKMY ASYKQSYPDL SNQLERILSR KFPEGWEKHL PVYKPGDKAV
ATRKLSEIVL DALCPVLPEL VGGSADLTPS NLTRWEGAAD FQPPSSKLGT YAGRYIRYGI
REHGMAGIMN GLAVYGPIIP YGGTFLNFVS YAAGAVRMAA LNNSRVIYVA THDSIGLGED
GPTHQPIETF AHFRAMPNIN CWRPADGNET SAAYYSALTS DSTPSILALT RQNLPQLENS
TIENALKGGY VMLENKEADI TLVGTGSEVS LCIDTVKTLE TEYNLKARVV SLPCWEVFEQ
QPESYRLSVI PDGIPAMSVE VWATNGWRRY VHEAFGMHTF GDSGPAPKLY EKFHFTTSGV
AQRAKKTVDA YKDIPYIRSP VRRAF
