ID   G3V826_RAT              Unreviewed;       661 AA.
AC   G3V826;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   Name=Tkt {ECO:0000313|Ensembl:ENSRNOP00000021862.4,
GN   ECO:0000313|RGD:621036};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000021862.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000021862.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021862.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000021862.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021862.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00002931}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   AlphaFoldDB; G3V826; -.
DR   Ensembl; ENSRNOT00000021862.7; ENSRNOP00000021862.4; ENSRNOG00000016064.7.
DR   RGD; 621036; Tkt.
DR   VEuPathDB; HostDB:ENSRNOG00000016064; -.
DR   GeneTree; ENSGT00940000155552; -.
DR   HOGENOM; CLU_009227_3_0_1; -.
DR   OMA; ADYMRGS; -.
DR   OrthoDB; 178912at2759; -.
DR   TreeFam; TF313097; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000016064; Expressed in ovary and 19 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0004802; F:transketolase activity; IEA:Ensembl.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:Ensembl.
DR   GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR   GO; GO:1901159; P:xylulose 5-phosphate biosynthetic process; IEA:Ensembl.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
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   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43195:SF3; TRANSKETOLASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          353..517
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   661 AA;  71792 MW;  FA262F4A497AC6DA CRC64;
     MDPVRQIQCD REGKRFPFLS APPASTSSPD RAMEGYHKPD QQKLQALKDT ANRLRISSIQ
     ATTAAGSGHP TSCCSAAEIM AVLFFHTMRY KALDPRNPHN DRFVLSKGHA APILYAVWAE
     AGFLPEAELL NLRKISSDLD GHPVPKQAFT DVATGSLGQG LGAACGMAYT GFLGKPYSLP
     FVHSYRVYCM LGDGEVSEGS VWEAMAFAGI YKLDNLVAIF DINRLGQSDP APLQHQVDVY
     QKRCEAFGWH AIIVDGHSVE ELCKAFGQAK HQPTAIIAKT FKGRGITGIE DKEAWHGKPL
     PKNMAEQIIQ EIYSQVQSKK KILATPPQED APSVDIANIR MPTPPNYKVG DKIATRKAYG
     LALAKLGHAS DRIIALDGDT KNSTFSELFK KEHPDRFIEC YIAEQNMVSI AVGCATRDRT
     VPFCSTFAAF FTRAFDQIRM AAISESNINL CGSHCGVSIG EDGPSQMALE DLAMFRSVPM
     STVFYPSDGV ATEKAVELAA NTKGICFIRT SRPENAIIYS NNEDFQVGQA KVVLKSKDDQ
     VTVIGAGVTL HEALAAAEML KKEKIGVRVL DPFTIKPLDK KLILDCARAT KGRILTVEDH
     YYEGGIGEAV SAAVVGEPGV TVTRLAVSQV PRSGKPAELL KMFGIDKDAI VQAVKGLVTK
     G
//