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Database: UniProt
Entry: K3VIR0_FUSPC
LinkDB: K3VIR0_FUSPC
Original site: K3VIR0_FUSPC 
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
//
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