TKTL1_BOVIN
ID TKTL1_BOVIN Reviewed; 596 AA.
AC Q2NL26;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Transketolase-like protein 1;
DE EC=2.2.1.1;
DE AltName: Full=Transketolase 2;
DE Short=TK 2;
GN Name=TKTL1;
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: 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51854}. Nucleus
CC {ECO:0000250|UniProtKB:P51854}. Note=Predominantly cytoplasmic and to a
CC lesser extent also nuclear. {ECO:0000250|UniProtKB:P51854}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; BC111166; AAI11167.1; -; mRNA.
DR RefSeq; NP_001039437.1; NM_001045972.1.
DR AlphaFoldDB; Q2NL26; -.
DR SMR; Q2NL26; -.
DR STRING; 9913.ENSBTAP00000036249; -.
DR PaxDb; Q2NL26; -.
DR PRIDE; Q2NL26; -.
DR Ensembl; ENSBTAT00000036390; ENSBTAP00000036249; ENSBTAG00000020127.
DR GeneID; 507517; -.
DR KEGG; bta:507517; -.
DR CTD; 8277; -.
DR VEuPathDB; HostDB:ENSBTAG00000020127; -.
DR VGNC; VGNC:35885; TKTL1.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000162426; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; Q2NL26; -.
DR OMA; LTRAHDF; -.
DR OrthoDB; 354970at2759; -.
DR TreeFam; TF313097; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000020127; Expressed in spermatid and 61 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 2.
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; Cytoplasm; Magnesium; Metal-binding; Nucleus; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..596
FT /note="Transketolase-like protein 1"
FT /id="PRO_0000285197"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 94..96
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
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 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 46
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 596 AA; 64966 MW; 0C4335E6FCEBADA6 CRC64;
MADAEASATM ADEAKPDSKT LQILRDMANR LRIHSIRATC ASSSGHPISC SSAAEIMSVL
FFHVMRYKQA DPKNPDNDRF ILSKRLSFVD VATGWLGQGL GAACGMAYTG KYFDKASYRV
FCLVGDVESW EGSVWEALAF ASHYSLDNLV AIFDVNRLTH STTLPLEHSI DVYQKRCEAF
GWNTLVVDGR DVEALCQVFW QAAQMKNKPT AVVAKTFKGR GIPSVEDAEN WHGKPMPKER
ADAIIKLIES QIETNKSLEP KAPIEDSPQI NISVIEMTSP PDYEISDVIA TRKACGLALA
KLGHANDRVI VLDGDTKNST FSDIFKREHP ERFIECFIAE QNMVSVALGC VTRGRTVAFA
CTFAAFLTRA FDQIRMGGIS QTNINLIGSH CGVSIGEDGP SQMALEDLAM FRAIPNCTIF
YPSDAISTEH AVFLAANIKG MCYIRTSRPE TAIIYTPQES FEIGQAKVIR QSVNDKITVV
GAGITLHEAL AAADDLSKQG ISLRVIDLFT VKPLDAATII SNAKATGGQI ITVEDHYPEG
GIGEAVSAAV SMEPDIVVHH LAVSGIPRSG KPSDLLDMFG ISSKHIIWAV ERILMK
