ID A0A0A0KBL8_CUCSA Unreviewed; 745 AA.
AC A0A0A0KBL8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=Csa_6G077460 {ECO:0000313|EMBL:KGN46249.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN46249.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN46249.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
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=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; CM002927; KGN46249.1; -; Genomic_DNA.
DR RefSeq; XP_004145002.1; XM_004144954.2.
DR AlphaFoldDB; A0A0A0KBL8; -.
DR STRING; 3659.A0A0A0KBL8; -.
DR EnsemblPlants; KGN46249; KGN46249; Csa_6G077460.
DR GeneID; 101206943; -.
DR Gramene; KGN46249; KGN46249; Csa_6G077460.
DR KEGG; csv:101206943; -.
DR eggNOG; KOG0523; Eukaryota.
DR OMA; YEARNIW; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000029981; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; 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; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 435..607
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 745 AA; 80564 MW; DE5496A3D720DAD8 CRC64;
MASTSSAALS QAVLPRTISH HASNPSADRV SLSTRSLPTF SGLKSTNSAA VVASSRRNRS
SRSRCGVVRA SVAETVDKTT DTSLIEKSVN TIRFLSIDAV EKANSGHPGL PMGCAPMGHV
LYDEVMRYNP KNPYWFNRDR FVLSAGHGCM LQYALLHLAG YDSVKEEDLK NFRQWESRTP
GHPENFETPG IEVTTGPLGQ GVANAVGLAL AEKHLAARFN KPDNEIVDHY TYVILGDGCQ
MEGIANEACS LAGHWGLGKL IAFYDDNHIS IDGHTEIAFT ENVDKRFEAL GWHVIWVKNG
NNGYDEIRAA IREAKAVKDK PTLIKVTTTI GYGSPNKANS YSVHGSALGA KEVDATRQNL
GWPYEPFHVP EDVKKHWSRH TPQGAALEAE WNAKFAEYEK KYAEEAAELK GIISGELPAG
WEKALPTYTP ESPADATRNL SQQNLNALAK VLPGFLGGSA DLASSNMTLL KSFGNFQKDT
PEERNLRFGV REHGMGAICN GIALHSPGLI PYCATFFVFT DYMRAAIRIS ALSQAGVIYV
MTHDSIGLGE DGPTHQPIEH LASFRAMPNI LMLRPADGNE TAGAYKVAVL NQKRPSILAL
SRQKLPNLPG TSIEGVEKGG YILSDNSSGN KPDVILIGTG SELEIAAKAA EELRKEGKAV
RLVSFVSWEL FNEQSDAYKE SVLPAAVSAR VSIEAGTTFG WEKIVGSKGK AIGIDRFGAS
APAGKIYKEF GITVEAVIAA AKQVI
//
