ID   A8WH37_XENLA            Unreviewed;       656 AA.
AC   A8WH37;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
DE   Flags: Fragment;
GN   Name=LOC780759 {ECO:0000313|EMBL:AAI54960.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI54960.1};
RN   [1] {ECO:0000313|EMBL:AAI54960.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Forelimbs and hindlimbs {ECO:0000313|EMBL:AAI54960.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2007) 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:0000256|ARBA:ARBA00002931}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; BC154959; AAI54960.1; -; mRNA.
DR   AlphaFoldDB; A8WH37; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR049557; Transketolase_CS.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43195:SF3; TRANSKETOLASE; 1.
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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          344..508
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAI54960.1"
SQ   SEQUENCE   656 AA;  70732 MW;  2F761F017B14AC85 CRC64;
     ASLSPVTGPR APAAARIPRS LSRSNCANPM AEYHKPDQQT LQSLRDTANR LRVLSINSTT
     AAGSGHPTSC CSAAEIMSVL FFHSMKYKPQ DPRNPNNDRF VMSKGHAAPI LYAAWAEAGF
     VQESELLNLR KLDSILEGHP VPKQEFVDVA TGSLGQGLGA ACGMAYTGKF FDKASYRVFC
     LLGDGEVSEG SVWEAMAFAG FYKLDNLVAI FDVNRLGQSE PAPLQHKVEV YQKRCEAFGW
     HSLVVDGHSV EELCKALCHV KNQPTAIIAK TFKGKGISGV EDKENWHGKP LPKELAEKSI
     KEIEGKIQSK KKLSPTLPVE DAPVISIKNI KMPSPPGYKL GEKIATRKAY GQALAKLGHA
     SDRVIALDGD TKNSTFAELF KKEHPGRYIE CYIAEQNMVS VAIGCATRDR TVAFASAFAT
     FFTRAFDQIR MAAISESNIN LCGSHCGVSI GEDGASQMAL EDLAMFRAVP TATVFYPSDA
     VSTEKAVELA ANTKGICFIR TSRPENAVIY SSTEGFNIGQ AKVVLQNKDD QVTVIGAGVT
     LHEALAAAEQ LKKEKIHIRV IDPFTIKPLD KQTIVENAKA TNGRIITVED HYHEGGIGEA
     VAAAVVGVPG ICLKSLAVSH VPRSGKPAEL LRMFEIDTEA IVAAVKGLVS PAKNAK
//