ID I3J0J0_ORENI Unreviewed; 594 AA.
AC I3J0J0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=TKT {ECO:0000313|Ensembl:ENSONIP00000002380.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000002380.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000002380.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; I3J0J0; -.
DR STRING; 8128.ENSONIP00000035314; -.
DR Ensembl; ENSONIT00000002381.2; ENSONIP00000002380.2; ENSONIG00000001900.2.
DR eggNOG; KOG0523; Eukaryota.
DR GeneTree; ENSGT00940000155552; -.
DR HOGENOM; CLU_009227_3_0_1; -.
DR TreeFam; TF313097; -.
DR Proteomes; UP000005207; Linkage group LG20.
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:UP000005207};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 283..447
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 594 AA; 65347 MW; 95A28E6ACA532DF4 CRC64;
MCLLHPTSCS SVAEIMSVLF FHSMKYRPED PRNPNNDRFV LSKGHAAPVL YAVWAETGYL
KENELLNLRK VDSILEGHPV PKQQFVDVAT GSLGQGLGAA CGMAYTGKYF DKASYRVFCL
LGDGELSEGS VWEAMAFASY YQLDNLVAIL DINRLGQSDP TPLQHHVEKY QRRCESFGWH
AIIVDGHSVE ELCKVLSQPR HQPLAIIAKT IKGKGIPGID KMGWHGKPLP KDMAESVIKE
LQNRIISCNK RLYPAAPNED TSPVSLRNIR MPSAPSYKPG DKIATRKAYG MALAKLGRYN
ERVVVLDGDT KNSTFSELFK NEHPNRYVEC YIAEQNMVSV AIGCAVRDRN VVFASTFATF
FTRAYDQLRM AAISESNINL CGSHCGVSIG EDGPSQMGLE DLAMFRAIPA ATVFYPSDGV
STEKAVELAA NTKGLCFIRT SRPENNIIYN CNEDFHVGQA KVAYKTNDDY VTVVGAGVTL
HEALAAAEML KKERINIRVI DPFTVKPLDS KTIIDNARAT RGRIITVEDH YYEGGLGEAV
CSAVVNETSF TVHRLAVSQV PRSGKPHELL RIFGIDRDAI AQAAAGVTAA GTTW
//
