ID   NSCD_ASPFU              Reviewed;         453 AA.
AC   Q4WA62;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Prenyltransferase nscD {ECO:0000303|PubMed:23368997};
DE            EC=2.5.1.- {ECO:0000305|PubMed:23368997};
DE   AltName: Full=Neosartoricin biosynthesis protein D {ECO:0000303|PubMed:23368997};
GN   Name=nscD {ECO:0000303|PubMed:23368997}; ORFNames=AFUA_7G00170;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION.
RX   PubMed=23758576; DOI=10.1021/sb400048b;
RA   Yin W.B., Chooi Y.H., Smith A.R., Cacho R.A., Hu Y., White T.C., Tang Y.;
RT   "Discovery of cryptic polyketide metabolites from dermatophytes using
RT   heterologous expression in Aspergillus nidulans.";
RL   ACS Synth. Biol. 2:629-634(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=23368997; DOI=10.1021/ol303435y;
RA   Chooi Y.H., Fang J., Liu H., Filler S.G., Wang P., Tang Y.;
RT   "Genome mining of a prenylated and immunosuppressive polyketide from
RT   pathogenic fungi.";
RL   Org. Lett. 15:780-783(2013).
CC   -!- FUNCTION: Prenyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of neosartoricin, a prenylated anthracenone that exhibits
CC       T-cell antiproliferative activity, suggestive of a physiological role
CC       as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The
CC       non-reducing polyketide synthase nscA probably synthesizes and cyclizes
CC       the decaketide backbone (PubMed:23368997). The hydrolase nscB then
CC       mediates the product release through hydrolysis followed by spontaneous
CC       decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes
CC       the addition of the dimethylallyl group to the aromatic C5
CC       (PubMed:23368997). The FAD-dependent monooxygenase nscC is then
CC       responsible for the stereospecific hydroxylation at C2
CC       (PubMed:23368997). There is no gene encoding O-acetyltransferase in the
CC       nsc gene cluster; thus, the last step of 2-O-acetylation leading to
CC       neosartoricin may be catalyzed by an unidentified O-acetyltransferase
CC       (PubMed:23368997). {ECO:0000305|PubMed:23368997,
CC       ECO:0000305|PubMed:23758576}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23368997}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000015; EAL84874.1; -; Genomic_DNA.
DR   RefSeq; XP_746912.1; XM_741819.1.
DR   AlphaFoldDB; Q4WA62; -.
DR   SMR; Q4WA62; -.
DR   STRING; 746128.CADAFUBP00008429; -.
DR   EnsemblFungi; EAL84874; EAL84874; AFUA_7G00170.
DR   GeneID; 3504087; -.
DR   KEGG; afm:AFUA_7G00170; -.
DR   VEuPathDB; FungiDB:Afu7g00170; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   InParanoid; Q4WA62; -.
DR   OMA; TGIDCCK; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IGC:AspGD.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR012148; DMATS-type_fun.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..453
FT                   /note="Prenyltransferase nscD"
FT                   /id="PRO_0000437914"
SQ   SEQUENCE   453 AA;  50911 MW;  0C6AD4943AEA2E5C CRC64;
     MSLQLNGKSR GTSPGNAQPL PIFDALCRSL PVGTADEQFW WKLTGRHLAR MMLEAGYPEH
     RQVECLVFHR FKVVPTFGPQ PRSAEPWYRS RVAASAGDGA PISYSWRFGT ADRKPYIRNY
     IEPLGPLTGT AADPNNDVAT RAFLQDLTTT LPNLDLSLFW TFEPHLVSRF SDKADREKYA
     GPSVLTGVEL SPDSDAIDIK MYLYPRNPEQ ISQLLSTIIP KAMRDAYGED VCLDSLNIVK
     DFLTNHPDGR QLKPRGTTGI DCCKVQDSRV KFYVATDNTS FDHIATVMTI GGRRPLSTEV
     LDKLRELWYE LNGLPSDFPT SEQVPTGQGQ ELPAGHHGVG FYYDIQPRLA LPDVKAFINV
     RKHAKSDLAA AETVISFLER HGQGHHNPRA YLNVLRDIVP AEELETRVGA QAFYSVAVKK
     EELDITAYFI PQVYRRFASV QVELNGQRRS RFE