TKT_PONAB
ID TKT_PONAB Reviewed; 623 AA.
AC Q5R4C1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CR861331; CAH93395.1; -; mRNA.
DR RefSeq; NP_001126993.1; NM_001133521.1.
DR AlphaFoldDB; Q5R4C1; -.
DR SMR; Q5R4C1; -.
DR STRING; 9601.ENSPPYP00000023523; -.
DR GeneID; 100174016; -.
DR KEGG; pon:100174016; -.
DR CTD; 7086; -.
DR eggNOG; KOG0523; Eukaryota.
DR InParanoid; Q5R4C1; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Isopeptide bond; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome; Thiamine pyrophosphate; Transferase;
KW Ubl conjugation.
FT CHAIN 1..623
FT /note="Transketolase"
FT /id="PRO_0000236208"
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 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:0000250|UniProtKB:P29401"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29401"
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; 67897 MW; 99C73645C2CB91BB CRC64;
MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS
QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL RKISSDLDGH PVPKQAFTDV
ATGSLGQGLG VACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA
ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAVIVDGHS VEELCKAFGQ AKHQPTAIIA
KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN
IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNPTFSEI FKKEHPDRFI
ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
IGEDGPSQMA LENLAMFRSV PTSTVFYPSD GVVTEKAVEL AANTKGICFI RTSRPENAII
YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL
DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE
LLKMFGIDKD AIAQAVRGLI TKA
