ID   FCK2_FUSPC              Reviewed;         551 AA.
AC   P0DPA4;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Cytochrome P450 monooxygenase FCK2 {ECO:0000303|PubMed:28802024};
DE            EC=1.-.-.- {ECO:0000305|PubMed:28802024};
DE   AltName: Full=Cytokinin biosynthesis protein 2 {ECO:0000303|PubMed:28802024};
GN   Name=FCK2 {ECO:0000303|PubMed:28802024};
GN   ORFNames=FPSE_20001 {ECO:0000303|PubMed:28802024};
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   GENOME REANNOTATION, FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND
RP   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: Cytochrome P450 monooxygenase; 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:28802024}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expressed during infection of barley and Brachypodium
CC       (PubMed:28802024). {ECO:0000269|PubMed:28802024}.
CC   -!- DISRUPTION PHENOTYPE: Results in the production of only two cytokinins,
CC       isopentenylaldehyde and 8-oxo-isopentenyladenine (PubMed:28802024).
CC       {ECO:0000269|PubMed:28802024}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AFNW01000149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DPA4; -.
DR   SMR; P0DPA4; -.
DR   Proteomes; UP000007978; Chromosome 3.
DR   Proteomes; UP000007978; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..551
FT                   /note="Cytochrome P450 monooxygenase FCK2"
FT                   /id="PRO_0000442155"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         493
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   551 AA;  63076 MW;  667399AA13B13C2F CRC64;
     MATLHAYFDP ANYSLFFVLG VLTHVFIFRR GEWDLHVFNI LQAFAVLESS LVYIVTRAVQ
     AQGLSLWKVT TISSCFTLST LMGLLISILM YRSWFHRLRR FPGPFCARLS NLYITFRAFK
     KNRLYEEVQQ LHRRYGDIVR IGPNELSIID PHALRALHSN SSPCTKGPWY SVEHPIKALQ
     MTRDKEEHAY RRKAWDLAFS SKALREYEAR VAGYTTQLVD QIEASQSTPI DASLWFNFYS
     FDVMGDLAFG RTFDMLKNGT AHPFMELVHS NMLTAGSLSH LPWIFPLLKR IPLLNQKTLE
     FQGWLKQQVD WRQKNNPDLP DVFSWILSDY DALDKPTAQD TINLRGDAQL IAVAGSDTTA
     ASLSCLFSEL AVNPETCLNL QRELDQYHAE HDKPDHLSLS KLRYLQACID ESMRLYPAIP
     SGLQRMTPPE GLDIGNTYLP GDTIVTIPTY TFNRDERLFT HADKFIPERW TTKKELTKDP
     SNFVPFSIGQ YSCVGKQLGL METRFVASQI LVKYNVRLAH EDVARDFVAG LRDGFTLAMP
     SLSLVFTQRT T