ID   NSCC_TRIEC              Reviewed;         179 AA.
AC   F2PWS7;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=FAD-dependent monooxygenase nscC {ECO:0000303|PubMed:23758576};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23758576};
DE   AltName: Full=Neosartoricin B biosynthesis protein C {ECO:0000303|PubMed:23758576};
DE   Flags: Precursor;
GN   Name=nscC {ECO:0000303|PubMed:23758576}; ORFNames=TEQG_05348;
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of neosartoricin B, a prenylated anthracenone
CC       that probably exhibits T-cell antiproliferative activity, suggestive of
CC       a physiological role as an immunosuppressive agent (PubMed:23758576).
CC       The non-reducing polyketide synthase nscA probably synthesizes and
CC       cyclizes the decaketide backbone (By similarity). The hydrolase nscB
CC       then mediates the product release through hydrolysis followed by
CC       spontaneous decarboxylation (By similarity). The prenyltransferase nscD
CC       catalyzes the addition of the dimethylallyl group to the aromatic C5
CC       (By similarity). The FAD-dependent monooxygenase nscC is then
CC       responsible for the stereospecific hydroxylation at C2 (By similarity).
CC       Neosartoricin B can be converted into two additional compounds
CC       neosartoricins C and D (By similarity). Neosartoricin C is a
CC       spirocyclic compound that is cyclized through the attack of C3 hydroxyl
CC       on C14, followed by dehydration (By similarity). On the other hand,
CC       neosartoricin D is a further cyclized compound in which attack of C2 on
CC       C14 in neosartoricin C results in the formation of the acetal-
CC       containing dioxabicyclo-octanone ring (By similarity). Both of these
CC       compounds are novel and possibly represent related metabolites of the
CC       gene cluster (By similarity). {ECO:0000250|UniProtKB:A1D8J0,
CC       ECO:0000250|UniProtKB:F2S701, ECO:0000269|PubMed:23758576}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:23758576}.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; DS995747; EGE06345.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PWS7; -.
DR   SMR; F2PWS7; -.
DR   EnsemblFungi; EGE06345; EGE06345; TEQG_05348.
DR   eggNOG; ENOG502SIVG; Eukaryota.
DR   HOGENOM; CLU_1504514_0_0_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..179
FT                   /note="FAD-dependent monooxygenase nscC"
FT                   /id="PRO_0000437909"
FT   BINDING         36..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   179 AA;  19166 MW;  75EB7AFA48041796 CRC64;
     MGKQQETILI IGAGISGLAT SRLLTNNGIP NIVFEASTPD RSQGFAISLQ EFGYSTLLAA
     LGDLPLSSLI RAVAPDRQIG GTGWIDQALR DNRTGELLVA PDLTTTKQTI VRANRNALRH
     WIADCGEDEL DVRYGHKLQS IKGKLGDVTA IFENGAKYKG SLIIAADGVN STYSPRRGS