ID L5MEI3_MYODS Unreviewed; 598 AA.
AC L5MEI3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=MDA_GLEAN10016596 {ECO:0000313|EMBL:ELK36999.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK36999.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB100898; ELK36999.1; -; Genomic_DNA.
DR RefSeq; XP_006754735.1; XM_006754672.2.
DR AlphaFoldDB; L5MEI3; -.
DR GeneID; 102760871; -.
DR KEGG; myd:102760871; -.
DR CTD; 7086; -.
DR eggNOG; KOG0523; Eukaryota.
DR OrthoDB; 178912at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 290..454
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 64990 MW; 7AA0F09BD2E3FF3C CRC64;
MHVSVSLLGH SHPTSCCSAA EIMSVLFFHT MRYKSQDPRN AHNDRFVLSK GHAAPILYAV
WAEAGFLPEA ELLNLRKISS DLDGHPVPKQ AFTDVATGSL GQGLGAACGM AYTGKYFDKA
SYRVYCLLGD GELSEGSVWE AMAFAGIYKL DNLVAILDIN RLGQSEPAPL QHQLDVYQKR
CEAFGWHTVI VNGHSVEELC KAFSQAKHQP TAIIAKTFKG RGISGVEDKE SWHGKPLPKN
MADQVIQEIQ SQIQSKKKIL ATPPQEDAPS VDITNIRMPT PPSYKVGDKI ATRKAYGQAL
AKLGHASDRI IALDGDTKNS TFSDLFKKEH PDRFIECYIA EQNMVSIAVG CATRNRTVPF
CSTFAAFYTR AFDQIRMAAI SESNINLCGS HCGVSIGEDG PSQMALEDLA MFRAVPMSTV
FYPSDGVSTE KAVELAANTK GICFIRTSRP ENAIIYSNNE DFQIGQAKVV LKSQDDQVTV
IGAGVTLHEA LAAADLLKKE KINIRVLDPF TIKPLDRKLI LDSARATKGR ILTVEDHYYE
GGIGEAVSSA VVGEPGVTVT RLAVSQVPRS GKPAELLKMF GIDKDAIVQA VKGLVSKA
//
