ID   NSCD_NEOFI              Reviewed;         454 AA.
AC   A1D8I8;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=NFIA_112230;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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:0000269|PubMed:23368997,
CC       ECO:0000305|PubMed:23758576}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:23368997}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; DS027692; EAW20699.1; -; Genomic_DNA.
DR   RefSeq; XP_001262596.1; XM_001262595.1.
DR   AlphaFoldDB; A1D8I8; -.
DR   SMR; A1D8I8; -.
DR   STRING; 36630.CADNFIAP00010297; -.
DR   EnsemblFungi; EAW20699; EAW20699; NFIA_112230.
DR   GeneID; 4589232; -.
DR   KEGG; nfi:NFIA_112230; -.
DR   VEuPathDB; FungiDB:NFIA_112230; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_2_2_1; -.
DR   OMA; TGIDCCK; -.
DR   OrthoDB; 1531660at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
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   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..454
FT                   /note="Prenyltransferase nscD"
FT                   /id="PRO_0000437915"
SQ   SEQUENCE   454 AA;  50940 MW;  537FCABDE5ADF5E7 CRC64;
     MSPLQLNGKS RGTSPGNAEP LPIFDALCRS LPVGTADEQF WWKLTGRHLA RMMLEAGYPE
     HRQVECLLFH RFKVVPTFGP QPQSAEPWYR SRVAASAGDG APISYSWRFG TADRKPYIRN
     YIEPLGPLTG TAADPNNDVA TRAFLQDLTT TLPNLDLSLF WTFEPHLVSR FSDKADREKY
     AGPSVLTGVE LSPDSDAIEI KMYLYPRIPE QISQLLSTII PKAMREAYGD DVCLDSLNLV
     KDFLSNHPDG RQLSPRGTTG IDCCKVQDSR VKFYVATNNT SFDHIATVMT IGGRRPLSTE
     VLDKLRELWY ELNGLPSDFP TSEQVPTDQG QEGPSGHHGV GFYYDIQPRL ALPDVKAFIN
     VRKHAKSDLA AAETVIGFLE RHGQGHHNPR AYLNVLRDIV PAEELETRVG AQAFYSVAVK
     KEELDITAYF IPQVYRRFAS VQVELNGQRR SRFE