ID K3VIR0_FUSPC Unreviewed; 727 AA.
AC K3VIR0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN ORFNames=FPSE_05207 {ECO:0000313|EMBL:EKJ74457.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ74457.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ74457.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ74457.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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 -!- 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:EKJ74457.1}.
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DR EMBL; AFNW01000108; EKJ74457.1; -; Genomic_DNA.
DR RefSeq; XP_009256600.1; XM_009258325.1.
DR AlphaFoldDB; K3VIR0; -.
DR EnsemblFungi; EKJ74457; EKJ74457; FPSE_05207.
DR GeneID; 20363825; -.
DR KEGG; fpu:FPSE_05207; -.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_0_0_1; -.
DR OrthoDB; 5399939at2759; -.
DR Proteomes; UP000007978; Chromosome 2.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF6; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 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:UP000007978};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 384..567
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 727 AA; 80857 MW; 055A3C811C799ED4 CRC64;
MAPSAITPET QYEHTALSNV VKLIKNDDAQ TIDLALRQFR CLIADLCEQF KGGHPGGAMG
MAAIGLALWK YIMQYSPNDP DYFNRDRFVL SNGHTCLFQY TFLHLVGYKA MTFDHLKSYH
SSNYDSLAPG HPEIEHEGIE VTTGPLGQGI ANAVGLAMAT KNLAAIYNKP NFELVNNMTY
CMIGDACLQE GVALEAIQLA GHWKLNNLVV MYDNNQITCD GSVDLCNTED VNAKMRACGW
DVIEVEDGCY DVEGIVKALI KAKASTDKPT FINIHTVIGV GSKVAGDAKA HGAAFSPEGV
KAIKEHFGMD TDKQYFVSDE VYTFFRDRKA RGDRLVEDWK ILVDSYAKEY PDLHQEFIKR
VEGRFTEDWR SIIPAKESLP TTPTPSRKSA GIICNPLAAK LKNFMVGTAD LSPSVNMIWK
DKVDFQHPEL RTTCGINGDY SGRYIHWGIR EHAMASISNG LAAYRKGTIL PVTSSFFMFY
IYAAPGVRMG ALQNLQAIHI ATHDSIGTGE DGPTHQPIAL PALYRSMPNI LYIRPCDTEE
TAGAFITALE AKDTPSIISL SRQNLEQYPQ HSSREGTQKG AYVFIEEDNA DVTLIGVGAE
MVFAVKTREV LKDKFGIRAR IVSFPCQRLF NSQPLEYKRQ VLQYRSNAPR VVIEAYAVNG
WERYADAGYS MSTFGKSLPG RDAYKYFGFD ETVIAPAVAR LVEEVKEEGI ESLRGEFRDL
NNVTHEH
//