TKTC_METJA
ID TKTC_METJA Reviewed; 316 AA.
AC Q58092;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative transketolase C-terminal section;
DE Short=TK;
DE EC=2.2.1.1;
GN OrderedLocusNames=MJ0679;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Corresponds to the C-
CC terminal of members of this family. {ECO:0000305}.
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DR EMBL; L77117; AAB98674.1; -; Genomic_DNA.
DR PIR; G64384; G64384.
DR RefSeq; WP_010870184.1; NC_000909.1.
DR AlphaFoldDB; Q58092; -.
DR SMR; Q58092; -.
DR STRING; 243232.MJ_0679; -.
DR EnsemblBacteria; AAB98674; AAB98674; MJ_0679.
DR GeneID; 1451545; -.
DR KEGG; mja:MJ_0679; -.
DR eggNOG; arCOG01051; Archaea.
DR HOGENOM; CLU_009227_1_1_2; -.
DR InParanoid; Q58092; -.
DR OMA; VINTCDY; -.
DR OrthoDB; 56448at2157; -.
DR PhylomeDB; Q58092; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 5: Uncertain;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..316
FT /note="Putative transketolase C-terminal section"
FT /id="PRO_0000191915"
SQ SEQUENCE 316 AA; 34580 MW; ABAB04A6DBB35199 CRC64;
MVKLSGVYKG MRKGYGETLI ELGKKYENLV VLDADLSGST QTAMFAKEFP ERFFNAGVAE
QNMIGMAAGL ATTGKIVFAS SFSMFASGRA WEIIRNLVAY PKLNVKIVAT HAGITVGEDG
ASHQMCEDIA IMRAIPNMVV IAPTDYYHTK NVIRTIAEYK GPVYVRMPRR DTEIIYENEE
EATFEIGKGK ILVDGEDLTI IATGEEVPEA LRAGEILKEN GISAEIVEMA TIKPIDEEII
KKSKDFVVTV EDHSIIGGLG GAVAEVIASN GLNKKLLRIG INDVFGRSGK ADELLKYYGL
DGESIAKRIM EEMKKE