TKTN_METJA
ID TKTN_METJA Reviewed; 274 AA.
AC Q58094;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative transketolase N-terminal section;
DE Short=TK;
DE EC=2.2.1.1;
GN OrderedLocusNames=MJ0681;
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=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {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 -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. Corresponds to the N-
CC terminal of members of this family. {ECO:0000305}.
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DR EMBL; L77117; AAB98676.1; -; Genomic_DNA.
DR PIR; A64385; A64385.
DR RefSeq; WP_010870186.1; NC_000909.1.
DR AlphaFoldDB; Q58094; -.
DR SMR; Q58094; -.
DR STRING; 243232.MJ_0681; -.
DR EnsemblBacteria; AAB98676; AAB98676; MJ_0681.
DR GeneID; 1451547; -.
DR KEGG; mja:MJ_0681; -.
DR eggNOG; arCOG01053; Archaea.
DR HOGENOM; CLU_009227_4_1_2; -.
DR InParanoid; Q58094; -.
DR OMA; MVHAVNS; -.
DR OrthoDB; 73908at2157; -.
DR PhylomeDB; Q58094; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd02012; TPP_TK; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005474; Transketolase_N.
DR Pfam; PF00456; Transketolase_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 5: Uncertain;
KW Calcium; Metal-binding; Reference proteome; Thiamine pyrophosphate;
KW Transferase.
FT CHAIN 1..274
FT /note="Putative transketolase N-terminal section"
FT /id="PRO_0000191914"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 30336 MW; FE3C053AC09F0A4E CRC64;
MDNNLEIKDL EKIAKKVRYN IVKMVGLAKS GHPGGSLSAT DIIVALYFKL MNYSPDNPYK
KDRDRFVLSK GHAAPALYAV LSELGIIEEE ELWKLRRLEG KLQGHPSMDT PGVEICTGSL
GQGFSAAVGM ALGCRLDKLN NYVYVLLGDG ECQEGIVWEA AMAAAHYKLD NLIAFIDRNK
LQIDGCTEDV MSLGDIKAKF EAFGWDVFEI DGHNFEEIIN TVEKAKSMKN GKPKMIIAYT
VKGKGVSFME NNVAFHGKAP NEEQLKQALE ELSE