UniProt: G3N9U2

Database: UniProt
Entry: G3N9U2_GASAC

LinkDB:  G3N9U2_GASAC 
Original site:  G3N9U2_GASAC

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (11)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

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ID   G3N9U2_GASAC            Unreviewed;       628 AA.
AC   G3N9U2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   Name=TKT {ECO:0000313|Ensembl:ENSGACP00000002083.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000002083.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000002083.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000002083.1}
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; G3N9U2; -.
DR   Ensembl; ENSGACT00000002088.1; ENSGACP00000002083.1; ENSGACG00000001593.1.
DR   GeneTree; ENSGT00940000155552; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000001593; Expressed in camera-type eye and 4 other cell types or tissues.
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; 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.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          320..484
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   628 AA;  69277 MW;  7BF50F778D7AE406 CRC64;
     MEDYHKPDQQ TVQALRNIAN RLRINSIKAT TAAGSGHPTS CCSVAEIMSV LYFHTMKYRP
     EDPRNFNSDR FILSKGHAAP ALYSMWVETG FLKENELLSL CQVDSALEGH PNPKQQIVDV
     ATGSLGQGLG VACGMAYTGK YFDKSSYRVY CLLGDGEMSE GAVWEAMSFA SYYQLDNLVA
     IMDINRLGQS DPAPLQHHVE KYQKRCEAFG KCVLMHSFIV DGHSVEELCK ALSQPRHQPT
     AIIAKTIKGK GIPAAEDKLG WHAKTLPKDM AEMVMKDLQS RIMNSSKHLY PPAPVEDSPP
     VSLRNIRMPS APSYKTGEKI ATRKAYGMAL AKLGRYNERV IALDGDTNNL TYSEIFKNEH
     PNRFVECYIA QQNMVSVAVG CAARERNVVF ASTLASFFTR AYDQLRMAAI SDSNINLCGS
     HCGLSTGEEG PSLMGLEDVA MFRALPTATI FYPCDGVSTE KAVELAASTK GVCYIRTSRQ
     DCSIIYNSNE DFHVGQAKVV YQSKEDQVTI VAAGVTLHEA LAAAEHLKKE RISVRVIDPF
     TIKPLDVKTI IDHTRATRGR ILTVEDHYYE GGLGEAVSSA MVNESGFNLH RLAVSHVPRS
     GKPHELLKIY GIDRDSITQA VRKMLSSS
//

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