ID   FCK3_FUSPC              Reviewed;         394 AA.
AC   K3VJJ1;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Probable glycosyltransferase FCK3 {ECO:0000303|PubMed:28802024};
DE            EC=2.4.1.- {ECO:0000305|PubMed:28802024};
DE   AltName: Full=Cytokinin biosynthesis protein 3 {ECO:0000303|PubMed:28802024};
GN   Name=FCK3 {ECO:0000303|PubMed:28802024}; ORFNames=FPSE_06371;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS3096;
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).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RC   STRAIN=CS3096;
RX   PubMed=28802024; DOI=10.1111/mpp.12593;
RA   Soerensen J.L., Benfield A.H., Wollenberg R.D., Westphal K., Wimmer R.,
RA   Nielsen M.R., Nielsen K.F., Carere J., Covarelli L., Beccari G., Powell J.,
RA   Yamashino T., Kogler H., Sondergaard T.E., Gardiner D.M.;
RT   "The cereal pathogen Fusarium pseudograminearum produces a new class of
RT   active cytokinins during infection.";
RL   Mol. Plant Pathol. 19:1140-1154(2018).
CC   -!- FUNCTION: Probable glycosyl transferase; part of the gene cluster that
CC       mediates the biosynthesis of cytokinins such as fusatin, fusatinic
CC       acids or 8-oxofusatin, known for their growth promoting and anti-
CC       senescence activities toward host plants (PubMed:28802024). FCK1 is a
CC       bifunctional enzyme that performs the first steps in the biosynthesis
CC       of Fusarium cytokinins (PubMed:28802024). It first condenses adenosine
CC       monophosphate (AMP) with dimethylallyl diphosphate (DMAPP) to yield
CC       isoprenyl adenosine monophosphate (PubMed:28802024). It then catalyzes
CC       the removal of the phosphoribose to produce isopentenylaldehyde
CC       (PubMed:28802024). The cytochrome P450 monooxygenase then converts
CC       isopentenylaldehyde to trans-zeatin (PubMed:28802024). A condensation
CC       step converts trans-zeatin to fusatin which is further modified to
CC       produce fusatinic acid (PubMed:28802024). The mechanism for oxidation
CC       of fusatin to fusatinic acid remains unknown (PubMed:28802024). 8-
CC       oxofusatin could be produced through several pathways, via direct
CC       oxygenation of fusatin, or via the 8-oxo-pentenyladenine intermediate
CC       which itself must arise from either the prenylation of 8-oxo-AMP by
CC       FCK1 and/or oxygenation of isopentenylaldehyde (PubMed:28802024). Both
CC       the FCK3 and FCK4 enzymes act downstream of the identified cytokinins
CC       to produce yet unidentified compounds (PubMed:28802024).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:28802024}.
CC   -!- INDUCTION: Expressed during infection of barley and Brachypodium
CC       (PubMed:28802024). {ECO:0000269|PubMed:28802024}.
CC   -!- DISRUPTION PHENOTYPE: Results in enhanced production of cytokinins,
CC       including a compound which could be 8-oxo-trans-zeatin, an obvious
CC       intermediate for the parallel biosynthesis of 8-oxo-fusatin
CC       (PubMed:28802024). {ECO:0000269|PubMed:28802024}.
CC   -!- SIMILARITY: Belongs to the afumC glycosyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFNW01000149; EKJ73453.1; -; Genomic_DNA.
DR   RefSeq; XP_009257764.1; XM_009259489.1.
DR   AlphaFoldDB; K3VJJ1; -.
DR   EnsemblFungi; EKJ73453; EKJ73453; FPSE_06371.
DR   GeneID; 20364989; -.
DR   KEGG; fpu:FPSE_06371; -.
DR   eggNOG; ENOG502RHHQ; Eukaryota.
DR   HOGENOM; CLU_061936_0_0_1; -.
DR   InParanoid; K3VJJ1; -.
DR   Proteomes; UP000007978; Chromosome 3.
DR   Proteomes; UP000007978; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008441; AfumC-like_glycosyl_Trfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF05704; Caps_synth; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..394
FT                   /note="Probable glycosyltransferase FCK3"
FT                   /id="PRO_0000442154"
SQ   SEQUENCE   394 AA;  45451 MW;  A9470D793D072692 CRC64;
     MHFAIPLEYQ SELEATEPVD VGTDEEIISS IEQYRPVTSE KNIWAFWDSG ILSMPSWCKR
     NVIGWARICG ADWTIRVLDM KPNSPNHVLK FIDRDMLPEA FLSGTMDGHH TGQHSADFIR
     GPLLHHYGGV SMDVGCLLIR HIDRICWDLL ADPDSPYEIA VPVLYDQTIA NHFIAARKNN
     IFIEKWHQLF LHLWNGRTHQ QGISDSPLLG FIKDIRYDDA TDFHWDWSVP VPQFLEYIAQ
     VLCWQRLCLI RDTGDGFKSS EYWQRNVLCI DSLNEVWGGE KTLGFDGIGP RMYNLLTTRL
     DADPDSTAYK DAYKLVWRLL TRSSFQKVTR AKNLTYTPHL GTLWDQNEGK DCIPGSFGEL
     LRYGPVHFRQ KRENIEQLEA SEPRTLIEKG LLEV