ID   PTF_ASPTN               Reviewed;         336 AA.
AC   Q0CZR3;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
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=ATEG_00821;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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 at a lower level (PubMed:20351110).
CC       Only traces of products are detected with aspulvinone E, flaviolin, or
CC       4-hydroxybenzoic acid as substrates; and no product is formed with L-
CC       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=325 uM for DMAPP {ECO:0000269|PubMed:20351110};
CC         KM=324 uM for 2,7-dihydroxynaphthalene {ECO:0000269|PubMed:20351110};
CC       pH dependence:
CC         Optimum pH is 8.7. {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}.
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DR   EMBL; CH476594; EAU39467.1; -; Genomic_DNA.
DR   RefSeq; XP_001210907.1; XM_001210907.1.
DR   EnsemblFungi; EAU39467; EAU39467; ATEG_00821.
DR   GeneID; 4355582; -.
DR   VEuPathDB; FungiDB:ATEG_00821; -.
DR   eggNOG; ENOG502SMTG; Eukaryota.
DR   HOGENOM; CLU_826338_0_0_1; -.
DR   OMA; ALNYRFY; -.
DR   OrthoDB; 971902at2759; -.
DR   BRENDA; 2.5.1.B25; 536.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
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..336
FT                   /note="Aromatic prenyltransferase"
FT                   /id="PRO_0000455461"
SQ   SEQUENCE   336 AA;  37289 MW;  5E7739F2313FAF18 CRC64;
     MIQQVQQAVF DPERFLVDIE ETCRAIGAPY SQEKTLKVLE GFQASFARGA VLWRITNRPG
     DALNYRFYER VSIDAVSCAV EAKLFQPNHP LSELIVSWTA LYPGAAQQSC DFDAEQGFSK
     IWVYLGDMRP LSDILSAPHV PLSIRKHATT FYNLGLELVR HVAADFTSNT INIYFRVQGL
     LTLERARSLV RLSDPAYLLE CGEVEEMRRL LNPVGFTFAV TMDYSTGDIK RVGIYALKLA
     PGTYPAMDER LKATRAIPLE KQAYILLSQG VLMAKEVAAA FPVPSETAAV NRPREVDVEV
     GVGVASFMFQ PTTPIAPTVD VRDNVVVAVF HAVESP