TKT_RAT
ID TKT_RAT Reviewed; 623 AA.
AC P50137;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=Tkt;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Kim S., Kim B., Jeng J., Song B.J.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 175-186; 284-302; 382-395; 472-493 AND 556-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18026.1; Type=Erroneous initiation; Evidence={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; U09256; AAA18026.1; ALT_INIT; mRNA.
DR RefSeq; NP_072114.1; NM_022592.1.
DR AlphaFoldDB; P50137; -.
DR SMR; P50137; -.
DR BioGRID; 249108; 2.
DR IntAct; P50137; 2.
DR MINT; P50137; -.
DR STRING; 10116.ENSRNOP00000021862; -.
DR CarbonylDB; P50137; -.
DR iPTMnet; P50137; -.
DR PhosphoSitePlus; P50137; -.
DR World-2DPAGE; 0004:P50137; -.
DR jPOST; P50137; -.
DR PaxDb; P50137; -.
DR PeptideAtlas; P50137; -.
DR PRIDE; P50137; -.
DR GeneID; 64524; -.
DR KEGG; rno:64524; -.
DR UCSC; RGD:621036; rat.
DR CTD; 7086; -.
DR RGD; 621036; Tkt.
DR eggNOG; KOG0523; Eukaryota.
DR InParanoid; P50137; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; P50137; -.
DR Reactome; R-RNO-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-RNO-71336; Pentose phosphate pathway.
DR SABIO-RK; P50137; -.
DR PRO; PR:P50137; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:RGD.
DR GO; GO:0004802; F:transketolase activity; IDA:RGD.
DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISO:RGD.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:RGD.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:0046390; P:ribose phosphate biosynthetic process; IDA:RGD.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
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 PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Isopeptide bond;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Thiamine pyrophosphate; Transferase; Ubl conjugation.
FT CHAIN 1..623
FT /note="Transketolase"
FT /id="PRO_0000191898"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 123..125
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 258
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40142"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 275
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40142"
FT MOD_RES 603
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29401"
SQ SEQUENCE 623 AA; 67644 MW; A198AB56A73C23CE CRC64;
MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKA
LDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG AACGMAYTGK YFDKASYRVY CMLGDGEVSE GSVWEAMAFA GIYKLDNLVA
IFDINRLGQS DPAPLQHQVD VYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG IEDKEAWHGK PLPKNMAEQI IQEIYSQVQS KKKILATPPQ EDAPSVDIAN
IRMPTPPNYK VGDKIATRKA YGLALAKLGH ASDRIIALDG DTKNSTFSEL FKKEHPDRFI
ECYIAEQNMV SIAVGCATRD RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LEDLAMFRSV PMSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
YSNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE MLKKEKIGVR VLDPFTIKPL
DKKLILDCAR ATKGRILTVE DHYYEGGIGE AVSAVVVGEP GVTVTRLAVS QVPRSGKPAE
LLKMFGIDKD AIVQAVKGLV TKG
