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Database: UniProt
Entry: A0BK57_PARTE
LinkDB: A0BK57_PARTE
Original site: A0BK57_PARTE 
ID   A0BK57_PARTE            Unreviewed;       644 AA.
AC   A0BK57;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=GSPATT00029554001 {ECO:0000313|EMBL:CAK58924.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK58924.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK58924.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK58924.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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; CT867999; CAK58924.1; -; Genomic_DNA.
DR   RefSeq; XP_001426322.1; XM_001426285.1.
DR   AlphaFoldDB; A0BK57; -.
DR   STRING; 5888.A0BK57; -.
DR   EnsemblProtists; CAK58924; CAK58924; GSPATT00029554001.
DR   GeneID; 5012106; -.
DR   KEGG; ptm:GSPATT00029554001; -.
DR   eggNOG; KOG0523; Eukaryota.
DR   HOGENOM; CLU_009227_3_0_1; -.
DR   InParanoid; A0BK57; -.
DR   OMA; HKVYCLC; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF1; FI06132P-RELATED; 1.
DR   PANTHER; PTHR43195; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          335..500
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   644 AA;  70806 MW;  D2821302A2EE8619 CRC64;
     MSDRVTRKGK SQPQKEEPKQ AKKQKVQKES YDVVQLQDIA HQLRIHSIEM TIASNSGHPT
     SCASMAEIMA VLFFTKAGMH FNPKDPGNFG NDRFVLSKGH AAPILYAAWS MVGYIDKAEL
     LNLRKIDSLL EGHPVPKLPF VDVATGSLGQ GLSVAGGMAY SSKFLDKIDN RYWVLMGDGE
     TAEGSVWEAA HLASHYKLDN LTAIVDVNRL GQSEETSIGH DTNVYKKRWE AFGWKTIVVD
     GHNLNSLTDA FEQCRNVKNQ PQVIIAKTFK GKHLEMENKE DWHGKPVPQA QVDFVKKQMK
     QQDGFTLAPE VPTSIDRPQQ SHFTVEVNYA VDGKQSTREA YGKALVGLSK SDANQQIVAV
     DGDTKNSTFS IKYKEAVPTN FVECFIAEQN MVGWAQGFSC RGKVAFASTF AAFFARAFDQ
     IRMGGISESQ VKYVGSHAGV SIGEDGPSQM GLEDIALFRT IPNCVVLYPS DGVSAERAIE
     LVANHKSACY VRMSRPSLPI LYPNNEVFEI GKSKILKQND DDKILLIGGG VTTHEIFKAA
     KQLSEQDKVH VTVLDLFSVK PLDHDGILNA ANKTALKTIL VVEDHYSEGG LFEAVSSALS
     LDKQIKIHSI HVDKVAKSGT PAQMLSLYHL DAAGIIAKVK SIIQ
//
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