ID A0A078HWK8_BRANA Unreviewed; 738 AA.
AC A0A078HWK8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=BnaA09g38720D {ECO:0000313|EMBL:CDY41143.1};
GN ORFNames=DARMORV10_A09P52910.1 {ECO:0000313|EMBL:CAF2048871.1},
GN GSBRNA2T00072539001 {ECO:0000313|EMBL:CDY41143.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY41143.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY41143.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
RN [2] {ECO:0000313|EMBL:CDY41143.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAF2048871.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope - CEA;
RA William W.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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; HG994363; CAF2048871.1; -; Genomic_DNA.
DR EMBL; LK032492; CDY41143.1; -; Genomic_DNA.
DR STRING; 3708.A0A078HWK8; -.
DR PaxDb; 3708-A0A078HWK8; -.
DR EnsemblPlants; CDY41143; CDY41143; GSBRNA2T00072539001.
DR Gramene; CDY41143; CDY41143; GSBRNA2T00072539001.
DR OMA; EWTTGNL; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
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:SF14; TRANSKETOLASE-1, CHLOROPLASTIC; 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:UP000028999};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 428..600
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 24..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 79515 MW; AAEDE795E6D3500F CRC64;
MASTSSLALS QALLARAISH HGSDQRISLP SPFSRASASA SSRRRSNAAT TKPRSLRPLV
VRAAAVDTLE PTTDASIVDK SVNTIRFLAI DAVEKAKSGH PGLPMGCAPM AHILYDEVMR
YNPKNPYWFN RDRFVLSAGH GCMLLYALLH LAGYDSVLEE DLKSFRQWGS KTPGHPENFE
TPGIEVTTGP LGQGIANAVG LALAEKHLAA RFNKPDAEVV DHYTYVILGD GCQMEGISNE
AASLAGHWGL GKLIAFYDDN HISIDGDTEI AFTENVDQRF EALGWHVIWV KNGNTGYDEI
RAAIKEAKSV TDKPTLIKVT TTIGYGSPNK ANSYSVHGAA LGEKEVEATR NNLGWPYEPF
KVPDEVKSHW SRHTPDGKAL ESDWNASFAA YEKKYPEEAA ELKSIITGEL PAGWEKALPT
YTPESPGDAT RNLSQQCLNA LAKVVPGFLG GSADLASSNM TLLKAFGDFQ KATPEERNLR
FGVREHGMGA ICNGIALHSP GLIPYCATFF VFTDYMRGAM RISALSEAGV IYVMTHDSIG
LGEDGPTHQP VEHLASFRAM PNTLMFRPAD GNETAGAYKI AVTKRKTPSI LALSRQKLPQ
LPGTSIEGVE KGGYTISDNS SGNKPDVILV GTGSELEIAA QAAEVLRKEG KTVRVVSFVC
WELFDEQTDE YKESVLPSGV SARVSIEAAS TFGWGKIVGG EGKSIGINSF GASAPAPLLY
KEFGITVEAV VDAAKSFF
//
