ID M3XER1_FELCA Unreviewed; 626 AA.
AC M3XER1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=TKTL2 {ECO:0000313|Ensembl:ENSFCAP00000025120.3,
GN ECO:0000313|VGNC:VGNC:66205};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000025120.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000025120.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025120.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000025120.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025120.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000025120.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025120.3};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XER1; -.
DR STRING; 9685.ENSFCAP00000025120; -.
DR PaxDb; 9685-ENSFCAP00000025120; -.
DR Ensembl; ENSFCAT00000023882.4; ENSFCAP00000025120.3; ENSFCAG00000027909.4.
DR VGNC; VGNC:66205; TKTL2.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000161969; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR InParanoid; M3XER1; -.
DR OMA; HKVYCLC; -.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000027909; Expressed in testis and 1 other cell type or tissue.
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; 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:SF4; TRANSKETOLASE-LIKE PROTEIN 2; 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 319..483
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 626 AA; 67933 MW; 58FCAD53EC3C1B79 CRC64;
VMANDCKPDG NTVQVLRDVA NRLRIHSIRA TCASGSGHPT SCCSAAEIMS VLFFHTMRYK
QTDPGHPDND RFILSKGHAA PILYAAWAEV GNIRESDLLN LRKIHSDLEG HPTPRVLFVD
VATGSLGQGL GAACGMAYTG KYFDKASYRV FCLIGDGESS EGSVWEALAF ASHYNLDNLV
AVFDVNRLGQ SGATPLEHCT DIYQNRCEVF GWNTYLVDGH DVEALCQAFW QVAQVKNKPT
AIVAKTFKGR GIPDIEDAEN WHGKPMPKER VDTIIKLIES QIQTNRNLIP KPPIEDSPQI
SISNIKMTCL PEYIVGDTIA TRKACGLALA KLGHANERVI VLDGDTKNAT FSEIFNKEHP
EHFIECFIAE QNMVSVALGC ATRGRTIAFV STFAAFLARA FDQIRMGAIS QTNINLIGSH
CGVSIGDDGP SQVALEDLAM FRSIPNCTVF YPSDAISTEY AVYLAANTKG MCFIRTSQPE
TAVIYTPQEN FEIGQAKVIR QSVNDKVTVI GAGVTLHEAL AAADSLSQQG ISIRVIDPFT
IKPLDAANII SNARATGGRV ITVEDHYREG GIGEAVCAAV SREPDILVHQ LAVSEVPQSG
KPGELLDKFG ISARHIIAAV KNTLMN
//
