ID N1JHD2_BLUG1 Unreviewed; 1242 AA.
AC N1JHD2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BGHDH14_bgh06302 {ECO:0000313|EMBL:CCU77292.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU77292.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU77292.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU77292.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU77292.1}.
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DR EMBL; CAUH01003497; CCU77292.1; -; Genomic_DNA.
DR AlphaFoldDB; N1JHD2; -.
DR STRING; 546991.N1JHD2; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; N1JHD2; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 2.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 4.
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; 2.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 2.
DR Pfam; PF02780; Transketolase_C; 2.
DR Pfam; PF00456; Transketolase_N; 2.
DR SMART; SM00861; Transket_pyr; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 4.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 2.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 2.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 364..540
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT DOMAIN 917..1093
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1242 AA; 135766 MW; 1A77E2C8B6B69D32 CRC64;
MGYSAVDQEA INTIRLLAVD ATIKCNSGHP GAPMGMAPVA HVLFNKIMNF NPKSSSWINR
DRFVLSYSNL ISFRNGHGCM LQYALLHLAG FKLSIDDIKD FRKIGSLTPG HPESHETDGV
EVTTGPLGQG FSNAVGLAIA QQHAAGLYNK PDFELFNNYT FTFLGDGCMM EGVASEAASL
AGHLQLGNLI AIYDDNGISI DGNVNCTLTE DVVKRFEAYG WHTLTIEDGD NNLEAIEAAI
RECQSVKNKP SMIKLRTTIG FGSLLAGTHN VHGSPLKPDD AKQLKAKFGF DPEQSFVVRQ
SVYDLYNKRG AEGAAREQEW CKLFEKYCST HESEAKDLKR RLSGELPEGW EKNLPTYSAK
DPAIATRKLS ETVLQKIYSS VPELVGGSAD LTGSNLTRWK EAVDFQPPSL GIGNWSGRYI
RYGVREHAMG AIMNGLAAYG LFIPYAGTFL NFVSYASGAV RLSALSQVRT IWVATHDSIG
LGEDGPTHQP IEVLAHFRAL PNCMVWRPAD GNEVSAAYYV ALTSKNTPSI LALSRQNLPQ
LENSSIGNAI KGGYVACEDE NADITIVSSG SEVGICIESV KYLKEHHNLR ARVVSIPCFE
VFDAQSKEYR LSVIPDGIPS LSVEVMSTLG WERYSHEQFG LNRFGASGAY LDVYKKIGSL
TPGHPESHET DGVEVTTGPL GQGFSNAVGL AIAQQHAAGL YNKPDFELFN NYTFTFLGDG
CMMEGVASEA ASLAGHLQLG NLIAIYDDNG ISIDGNVNCT LTEDVVKRFE AYGWHTLTIE
DGDNNLEAIE AAIRECQSVK NKPSMIKLRT TIGFGSLLAG THNVHGSPLK PDDAKQLKAK
FGFDPEQSFV VRQSVYDLYN KRGAEGAARE QEWCKLFEKY CSTHESEAKD LKRRLSGELP
EGWEKNLPTY SAKDPAIATR KLSETVLQKI YSSVPELVGG SADLTGSNLT RWKEAVDFQP
PSLGIGNWSG RYIRYGVREH AMGAIMNGLA AYGLFIPYAG TFLNFVSYAS GAVRLSALSQ
VRTIWVATHD SIGLGEDGPT HQPIEVLAHF RALPNCMVWR PADGNEVSAA YYVALTSKNT
PSILALSRQN LPQLENSSIG NAIKGGYVAC EDENADITIV SSGSEVGICI ESVKYLKEHH
NLRARVVSIP CFEVFDAQSK EYRLSVIPDG IPSLSVEVMS TLGWERYSHE QFGLNRFGAS
GAYLDVYKVK QAFIPYMKAS NKGFTEVRVY TRGYIQACLG YG
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