ID PTF_BOTFB Reviewed; 309 AA. AC A0A384JK99; DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2018, sequence version 1. DT 12-OCT-2022, entry version 14. DE RecName: Full=Aromatic prenyltransferase {ECO:0000303|PubMed:20351110}; DE EC=2.5.1.- {ECO:0000269|PubMed:20351110}; GN Name=ptf {ECO:0000303|PubMed:20351110}; ORFNames=BCIN_06g02600; OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis OS cinerea). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Botrytis. OX NCBI_TaxID=332648; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230; RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A., RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E., RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M., RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P., RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I., RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P., RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C., RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C., RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E., RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N., RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O., RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.; RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia RT sclerotiorum and Botrytis cinerea."; RL PLoS Genet. 7:E1002230-E1002230(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=23104368; DOI=10.1128/ec.00164-12; RA Staats M., van Kan J.A.L.; RT "Genome update of Botrytis cinerea strains B05.10 and T4."; RL Eukaryot. Cell 11:1413-1414(2012). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B05.10; RX PubMed=26913498; DOI=10.1111/mpp.12384; RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L., RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D., RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.; RT "A gapless genome sequence of the fungus Botrytis cinerea."; RL Mol. Plant Pathol. 18:75-89(2017). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE RP SPECIFICITY. RX PubMed=20351110; DOI=10.1074/jbc.m110.113720; RA Haug-Schifferdecker E., Arican D., Brueckner R., Heide L.; RT "A new group of aromatic prenyltransferases in fungi, catalyzing a 2,7- RT dihydroxynaphthalene 3-dimethylallyl-transferase reaction."; RL J. Biol. Chem. 285:16487-16494(2010). CC -!- FUNCTION: Prenyltransferase that attaches isoprenoid moieties to carbon CC atoms of aromatic substrates in an enzyme-catalyzed Friedel-Crafts CC reaction (PubMed:20351110). Shows specificity for dimethylallyl CC diphosphate (DMAPP) and does not accept geranyl diphosphate (GPP) or CC isopentenyl diphosphate (IPP) (PubMed:20351110). Prenylates the CC artificial substrate 2,7-dihydroxynaphthalene (2,7-DHN), as well as CC dihydrophenazine-1-carboxylic acid and 4-hydroxybenzoic acid at lower CC levels (PubMed:20351110). Only traces of products are detected with CC aspulvinone E or flaviolin as substrates; and no product is formed with CC L-tryptophan, L-tyrosine, or 4-hydroxyphenylpyruvate (PubMed:20351110). CC Ptf seems no to be involved in the prenylation reaction in the CC biosynthesis of aspulvinone H and J and the physiological function of CC ptf remains unknown (PubMed:20351110). {ECO:0000269|PubMed:20351110}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1010 uM for DMAPP {ECO:0000269|PubMed:20351110}; CC KM=996 uM for 2,7-dihydroxynaphthalene {ECO:0000269|PubMed:20351110}; CC -!- MISCELLANEOUS: The gene is not located within a recognizable secondary CC metabolic gene cluster. {ECO:0000269|PubMed:20351110}. CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase 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; CP009810; ATZ50774.1; -; Genomic_DNA. DR RefSeq; XP_001560463.1; XM_001560413.1. DR EnsemblFungi; Bcin06g02600.1; Bcin06p02600.1; Bcin06g02600. DR GeneID; 5441104; -. DR KEGG; bfu:BCIN_06g02600; -. DR VEuPathDB; FungiDB:Bcin06g02600; -. DR OMA; ALNYRFY; -. DR Proteomes; UP000001798; Chromosome bcin06. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt. DR CDD; cd13931; PT-CloQ_NphB; 1. DR InterPro; IPR033964; Aro_prenylTrfase. DR InterPro; IPR020965; Prenyltransferase_CloQ. DR InterPro; IPR036239; PrenylTrfase-like_sf. DR Pfam; PF11468; PTase_Orf2; 1. DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1. DR SFLD; SFLDG01163; II; 1. DR SUPFAM; SSF143492; SSF143492; 1. PE 1: Evidence at protein level; KW Prenyltransferase; Reference proteome; Transferase. FT CHAIN 1..309 FT /note="Aromatic prenyltransferase" FT /id="PRO_0000455462" SQ SEQUENCE 309 AA; 34474 MW; 434F9267B029F90A CRC64; MVVQAVSESL KFDQSRFLND IQILSAAINA PYSESTTKKV LSVFSDSFHD GVVLWRATDR VGDALNYRFY SRRPIDTVTI ASSAGLLSPD VVSNLGRLVT SWSSLYDGLP EESCDFDAEK GLVKAWVYMR GMRPLGDILS AEGVPESLKQ HEERFKALEL EKVRHVAVDY QKATVNLYFR AQGPISLQQA TSFNALAGAG PPSQTQFLEM QEFLNAVGYT FAVTIRVDSG DIERVGYYAL KLPDRATKNW PVINAQLEKF AQFAPSYDRE EMNAVAWSFG GTKRYVKFER SYCGELVPLI KGWGTTLSS //