TKTL2_BOVIN
ID TKTL2_BOVIN Reviewed; 626 AA.
AC Q2NKZ4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Transketolase-like protein 2;
DE EC=2.2.1.1;
GN Name=TKTL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in total transketolase activity and
CC cell proliferation in cancer cells; after transfection with anti-TKTL1
CC siRNA, total transketolase activity dramatically decreases and
CC proliferation was significantly inhibited in cancer cells. Plays a
CC pivotal role in carcinogenesis (By similarity). {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}.
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DR EMBL; BC111320; AAI11321.1; -; mRNA.
DR RefSeq; NP_001039490.1; NM_001046025.1.
DR AlphaFoldDB; Q2NKZ4; -.
DR SMR; Q2NKZ4; -.
DR STRING; 9913.ENSBTAP00000052271; -.
DR PaxDb; Q2NKZ4; -.
DR PRIDE; Q2NKZ4; -.
DR Ensembl; ENSBTAT00000011778; ENSBTAP00000052271; ENSBTAG00000008947.
DR GeneID; 509186; -.
DR KEGG; bta:509186; -.
DR CTD; 84076; -.
DR VEuPathDB; HostDB:ENSBTAG00000008947; -.
DR VGNC; VGNC:35886; TKTL2.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000161969; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; Q2NKZ4; -.
DR OMA; YAPHTPD; -.
DR OrthoDB; 354970at2759; -.
DR TreeFam; TF313097; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000008947; Expressed in spermatid and 71 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
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; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..626
FT /note="Transketolase-like protein 2"
FT /id="PRO_0000285199"
FT ACT_SITE 369
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 247
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 626 AA; 67501 MW; 5C63B165FE27B586 CRC64;
MADSATLDAT TVQVLQDLAN RLRVHSIRAT CASGSGHPTS CCSAAEIVSV LFFHTMRYRQ
TEPAHPDNDR FVLSKGHAAP LLYAAWVEAG SISEPDLLNL RTIHCDLEGH PTPRLSFVDV
ATGSLGQGLG AACGMAYTGK YLDKASYRVF CLLGDGESSE GSVWEALAFA SHYGLDNLVA
VFDVNRLGQS GVAPLKHCTD IYRNRCEAFG WNTYLVDGHD VEALCQAFSQ AAQGKNKPTA
IIAKTYKGRG IPNVEDAENW HGKPLPKERA DEIIRLIKSQ IKTNRNLLPK PPVEGSPPVS
ITNIKMTCLP DYKVGDKVAT QKAYGLALAK LGLANERVVV LDGDPKNSTF FEIFKKEHPE
RFIECFAAEQ NMVSVALGCA TRGRTITFVT TLGAFLTRAF DQIRMGAISQ SNINLIGSHC
GVSVGEDGPS QMALEDLAMF RSIPNCTVFL PSDAVSTEHA VYLAANSEGM CFIRTNRSET
AVIYTPQEHF EIGRAKVIRH SNNDKVTVIG AGVTLHEALA AADALSQQDI SICVIDPFTI
KPLDAATIIS CAKATDGRVV TVEDHYQEGG IGEAVCAAVS GEPAIHVHQL SVSGVSERNR
KPSELLSIFG VSARHIIAAV KYTLMN
