ID PTF_SCLS1 Reviewed; 309 AA. AC A7EVV6; A0A1D9QLA6; DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 22-FEB-2023, entry version 56. 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=SS1G_09465; OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold) OS (Whetzelinia sclerotiorum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Helotiales; Sclerotiniaceae; Sclerotinia. OX NCBI_TaxID=665079; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 18683 / 1980 / Ss-1; 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=ATCC 18683 / 1980 / Ss-1; RX PubMed=28204478; DOI=10.1093/gbe/evx030; RA Derbyshire M., Denton-Giles M., Hegedus D., Seifbarghy S., Rollins J., RA van Kan J., Seidl M.F., Faino L., Mbengue M., Navaud O., Raffaele S., RA Hammond-Kosack K., Heard S., Oliver R.; RT "The complete genome sequence of the phytopathogenic fungus Sclerotinia RT sclerotiorum reveals insights into the genome architecture of broad host RT range pathogens."; RL Genome Biol. Evol. 9:593-618(2017). RN [3] 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=1232 uM for DMAPP {ECO:0000269|PubMed:20351110}; CC KM=590 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; CH476633; EDN93598.1; -; Genomic_DNA. DR EMBL; CP017828; APA15717.1; -; Genomic_DNA. DR RefSeq; XP_001589743.1; XM_001589693.1. DR AlphaFoldDB; A7EVV6; -. DR EnsemblFungi; EDN93598; EDN93598; SS1G_09465. DR GeneID; 5485694; -. DR KEGG; ssl:SS1G_09465; -. DR VEuPathDB; FungiDB:sscle_15g104870; -. DR eggNOG; ENOG502SMTG; Eukaryota. DR HOGENOM; CLU_057184_0_0_1; -. DR InParanoid; A7EVV6; -. DR OMA; ALNYRFY; -. DR OrthoDB; 2686367at2759; -. DR Proteomes; UP000001312; Unassembled WGS sequence. DR Proteomes; UP000177798; Chromosome 15. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic 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; Prenyltransferase-like; 1. PE 1: Evidence at protein level; KW Prenyltransferase; Reference proteome; Transferase. FT CHAIN 1..309 FT /note="Aromatic prenyltransferase" FT /id="PRO_0000455463" SQ SEQUENCE 309 AA; 34721 MW; 75E5439230B5AAD1 CRC64; MVVQLISKPS KFSQSRFLDD IRNLSAAINA PYSERTTIEA LSVYSHSFHN GVVLWRVTDR PGDALNYRFY SREPIDTVSI AASAGLLSPD IANTLGKLVT SWSSLYDGTP EESCDFDAEK GLVKAWVYFG GMRPLDDILG AEGVPESVRQ HEKRFKELGL QKVRHVAVDY HKQTVNLYFR AQGPISFQQA TAFNALAGAE PPSQSQFIEM REFLNAVGYT FAVTINIDSG DIERVGYYAL KLPERSAKKW PAINAQLERF VQFAPSYDRE EMNAVAWSFG ERKTYVKFER SYCGELIPLI KGWGTTLSS //