ID TKTL1_MACFA Reviewed; 596 AA.
AC Q4R6M8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Transketolase-like protein 1;
DE EC=2.2.1.1 {ECO:0000250|UniProtKB:P51854};
DE AltName: Full=Transketolase 2;
DE Short=TK 2;
GN Name=TKTL1; ORFNames=QtsA-17611;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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|UniProtKB:P23254}.
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 Evidence={ECO:0000250|UniProtKB:P51854};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10510;
CC Evidence={ECO:0000250|UniProtKB:P51854};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P23254};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P23254};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P23254};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P23254};
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+).
CC {ECO:0000250|UniProtKB:P23254};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P23254};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P23254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51854}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AB169154; BAE01247.1; -; mRNA.
DR RefSeq; NP_001270056.1; NM_001283127.1.
DR RefSeq; XP_015299212.1; XM_015443726.1.
DR AlphaFoldDB; Q4R6M8; -.
DR SMR; Q4R6M8; -.
DR STRING; 9541.ENSMFAP00000015756; -.
DR Ensembl; ENSMFAT00000066283.2; ENSMFAP00000015756.1; ENSMFAG00000031072.2.
DR GeneID; 101865992; -.
DR KEGG; mcf:101865992; -.
DR CTD; 8277; -.
DR VEuPathDB; HostDB:ENSMFAG00000031072; -.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000162426; -.
DR OMA; EWTTGNL; -.
DR OrthoDB; 178912at2759; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000031072; Expressed in heart.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR PANTHER; PTHR43195:SF2; TRANSKETOLASE-LIKE PROTEIN 1; 1.
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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..596
FT /note="Transketolase-like protein 1"
FT /id="PRO_0000285198"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
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|UniProtKB:P23254"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 127
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27302"
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|UniProtKB:P27302"
FT BINDING 232
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 340
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT BINDING 366
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27302"
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|UniProtKB:P27302"
FT SITE 46
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P23254"
FT SITE 232
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P23254"
SQ SEQUENCE 596 AA; 65269 MW; 0E213AE55C06F7F8 CRC64;
MADAEASAEL PEEARPDGGT LRVLRDMASR LRIHSIRATC STSSGHPTSC SSSAEIMSVL
FFYIMRYKQS DPENPDNDRF VLAKRLSFVD VATGWLGQGL GVACGMAYTG KYFDRASYRV
FCLMSDGESS EGSVWEAMAF ASYYSLDNLV AIFDVNRLGH SGALPAEHCI DIYQRRCEAF
GWNTYVVDGR DVEALCQVFW QASQVKHKPT AVVAKTFKGR GTPSIEDAES WHGKPMPRER
ADAIIKLIES QIETSRNLDP QLPIEDSPEV NITDVRMTSP PDYRVGDKIA TRKACGLALA
KLGYANDRVI VLDGDTKYST FSEIFNKEYP ERFIECFMAE QNMVSVALGC ASRGRTIAFA
STFAAFLTRA FDQIRIGGLS ESNINIIGSH CGVSVGEDGA SQMALEDIAM FRTIPKCTIF
YPTDAVSTEH AVSLAANAKG MCFIRTTRPE TMVIYTPQER FEIGQAKVLR HCVSDKVTVI
GAGITVYEAL AAADELLKQD IFIRVIDLFT IKPLDVTTII SSAKATEGRI ITVEDHYPQG
GIGEAVCAAV SMDPDIQVHS LAVSGVPQSG KSEELLDMYG ISARHIIVAV KCMLLN
//
