GenomeNet

Database: UniProt
Entry: Q58094
LinkDB: Q58094
Original site: Q58094 
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   27-MAR-2024, entry version 117.
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}.
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; 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   PaxDb; 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   OrthoDB; 25494at2157; -.
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   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 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
//
DBGET integrated database retrieval system