NSCC_TRIT1
ID NSCC_TRIT1 Reviewed; 412 AA.
AC F2S701;
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=TESG_06704;
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818;
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).
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: 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 PubMed:23368997). The non-reducing polyketide synthase nscA probably
CC synthesizes and cyclizes the decaketide backbone (By similarity). The
CC hydrolase nscB then mediates the product release through hydrolysis
CC followed by spontaneous decarboxylation (By similarity). The
CC prenyltransferase nscD catalyzes the addition of the dimethylallyl
CC group to the aromatic C5 (By similarity). The FAD-dependent
CC monooxygenase nscC is then responsible for the stereospecific
CC hydroxylation at C2 (By similarity). Neosartoricin B can be converted
CC into two additional compounds neosartoricins C and D (PubMed:23758576).
CC Neosartoricin C is a spirocyclic compound that is cyclized through the
CC attack of C3 hydroxyl on C14, followed by dehydration
CC (PubMed:23758576). On the other hand, neosartoricin D is a further
CC cyclized compound in which attack of C2 on C14 in neosartoricin C
CC results in the formation of the acetal-containing dioxabicyclo-octanone
CC ring (PubMed:23758576). Both of these compounds are novel and possibly
CC represent related metabolites of the gene cluster (PubMed:23758576).
CC {ECO:0000250|UniProtKB:A1D8J0, ECO:0000269|PubMed:23758576,
CC ECO:0000305|PubMed:23368997}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23758576}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; GG698521; EGD99350.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S701; -.
DR SMR; F2S701; -.
DR EnsemblFungi; EGD99350; EGD99350; TESG_06704.
DR HOGENOM; CLU_040697_0_0_1; -.
DR OrthoDB; 1519546at2759; -.
DR Proteomes; UP000009172; 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..412
FT /note="FAD-dependent monooxygenase nscC"
FT /id="PRO_0000437908"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 336..340
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"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 412 AA; 45269 MW; 3FFF11593EDE04FD CRC64;
MGKQQETILI IGAGISGLAT SRLLTNNGIP NIVFEASTPD RSQGFAISLQ EFGYSTLLAA
LGDLPLSSLI RAVAPDRQIG GTGWIDQALR DNRTGELLVA PDLTTTKQTI VRANRNALRH
WIADCGEDEL DVRYGHKLQS IKGKLGDVTA IFENGAKYKG SLIIAADGVN STSRSQILPD
VVPETIPLIH YHGEFQLSHS AFDELIRPHS GHSNILVGVG DSFNTPLSIC NITKTRVHLD
WSYSRTVKGE NDILYRPNVQ SEEAKQIPPA LLEELDALNL AEPWKTILNS ESLKTHRVFH
WTTRCVYITQ DDARRAGEQG VIFVGDSWHA MPIFGGEGGN HALLDGVELA DAIAASTASS
GNGDWDSVIK NYYGGAWKRS QEAVRRSTQR FFLLHRPATE WKEISEQKKK PA
