FCK1_FUSPC
ID FCK1_FUSPC Reviewed; 487 AA.
AC K3VH30;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Bifunctional cytokinin biosynthesis protein {ECO:0000303|PubMed:28802024};
DE AltName: Full=IPT-LOG {ECO:0000303|PubMed:28802024};
DE Includes:
DE RecName: Full=Adenylate isopentenyltransferase {ECO:0000303|PubMed:28802024};
DE EC=2.5.1.27 {ECO:0000269|PubMed:28802024};
DE Includes:
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000303|PubMed:28802024};
DE EC=3.2.2.n1 {ECO:0000269|PubMed:28802024};
GN Name=FCK1 {ECO:0000303|PubMed:28802024}; ORFNames=FPSE_06372;
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, CATALYTIC ACTIVITY, 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: Bifunctional cytokinine synthesis protein; part of the gene
CC cluster that mediates the biosynthesis of cytokinins such as fusatin,
CC fusatinic acids or 8-oxofusatin, known for their growth promoting and
CC anti-senescence activities toward host plants (PubMed:28802024). FCK1
CC is a bifunctional enzyme that performs the first steps in the
CC biosynthesis of Fusarium cytokinins (PubMed:28802024). It first
CC condenses adenosine monophosphate (AMP) with dimethylallyl diphosphate
CC (DMAPP) to yield isoprenyl adenosine monophosphate (PubMed:28802024).
CC It then catalyzes the removal of the phosphoribose to produce
CC isopentenylaldehyde (PubMed:28802024). The cytochrome P450
CC monooxygenase then converts isopentenylaldehyde to trans-zeatin
CC (PubMed:28802024). A condensation step converts trans-zeatin to fusatin
CC which is further modified to produce fusatinic acid (PubMed:28802024).
CC The mechanism for oxidation of fusatin to fusatinic acid remains
CC unknown (PubMed:28802024). 8-oxofusatin could be produced through
CC several pathways, via direct oxygenation of fusatin, or via the 8-oxo-
CC pentenyladenine intermediate which itself must arise from either the
CC prenylation of 8-oxo-AMP by FCK1 and/or oxygenation of
CC isopentenylaldehyde (PubMed:28802024). Both the FCK3 and FCK4 enzymes
CC act downstream of the identified cytokinins to produce yet unidentified
CC compounds (PubMed:28802024).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + dimethylallyl diphosphate = diphosphate + N(6)-
CC (dimethylallyl)adenosine 5'-phosphate; Xref=Rhea:RHEA:15285,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57526, ChEBI:CHEBI:57623,
CC ChEBI:CHEBI:456215; EC=2.5.1.27;
CC Evidence={ECO:0000269|PubMed:28802024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-
CC phosphate + N(6)-dimethylallyladenine; Xref=Rhea:RHEA:48560,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17660, ChEBI:CHEBI:57526,
CC ChEBI:CHEBI:78346; EC=3.2.2.n1;
CC Evidence={ECO:0000269|PubMed:28802024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-
CC phosphate + trans-zeatin; Xref=Rhea:RHEA:48564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16522, ChEBI:CHEBI:78346, ChEBI:CHEBI:87947; EC=3.2.2.n1;
CC Evidence={ECO:0000269|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: Impairs the production of cytokinins,
CC isopentenylaldehyde, trans-zeatin and cis-zeatin (PubMed:28802024).
CC {ECO:0000269|PubMed:28802024}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the IPP transferase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the LOG family.
CC {ECO:0000305}.
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DR EMBL; AFNW01000149; EKJ73454.1; -; Genomic_DNA.
DR RefSeq; XP_009257765.1; XM_009259490.1.
DR AlphaFoldDB; K3VH30; -.
DR SMR; K3VH30; -.
DR STRING; 101028.EKJ73454; -.
DR EnsemblFungi; EKJ73454; EKJ73454; FPSE_06372.
DR GeneID; 20364990; -.
DR KEGG; fpu:FPSE_06372; -.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_047145_0_0_1; -.
DR InParanoid; K3VH30; -.
DR Proteomes; UP000007978; Chromosome 3.
DR Proteomes; UP000007978; Unassembled WGS sequence.
DR GO; GO:0009824; F:AMP dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005269; LOG.
DR InterPro; IPR031100; LOG_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03641; Lysine_decarbox; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00730; TIGR00730; 1.
PE 1: Evidence at protein level;
KW Cytokinin biosynthesis; Hydrolase; Multifunctional enzyme; Transferase.
FT CHAIN 1..487
FT /note="Bifunctional cytokinin biosynthesis protein"
FT /id="PRO_0000442150"
FT REGION 1..266
FT /note="Adenylate isopentenyltransferase"
FT /evidence="ECO:0000303|PubMed:28802024"
FT REGION 267..487
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase"
FT /evidence="ECO:0000303|PubMed:28802024"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 380..381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 403..409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ SEQUENCE 487 AA; 52919 MW; 7A6476A761A6B96B CRC64;
MESTNRFMIG VFGPTGVGKT KLGVSIAKSV HGQVISVDSL QCYSPGGIVT AKPTPEEMDG
IEHHMIGYLE AEEEPTNFVA EAVERLEKLC DHGAIPVVVG GSTSLTLPLL RGALNRGWRM
AAITLLPHQS TYLGNIESRV DDMLEAGLLE ELSGLKSLED RNLNGKPNFH KGIWKTIGYQ
ELYPYLEAQR SDGHCDELLK SGLASMKENT FQYGNTQLEW IRQALSPFLH AEKIANMSLT
VVDKTSWTRG VEKPAIRMAS DFCYASTSIS FHPINEPKPR VICIFGGSSS GNDPAHMEAA
KSLGRVCHEN SIKLVYGGGT TGVMGAIAST LVELSGPNAV HGIIPEALLK YEAKESGRHA
QDSAFARYGR RTVVKDMHTR KRLMIQEVID GGDGSGFVGL SGGYGTLEEL FEVITWHQLG
IHDRGVCLLN MDGFFDGLVN WLGNVVKKGF IGLQDAAILS IASTAEGVVK CLDQKPGFSR
KGELEWV
