NSCC_ARTOC
ID NSCC_ARTOC Reviewed; 412 AA.
AC C5FM59;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=MCYG_03600;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
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 (By similarity).
CC Neosartoricin C is a spirocyclic compound that is cyclized through the
CC attack of C3 hydroxyl on C14, followed by dehydration (By similarity).
CC On the other hand, neosartoricin D is a further cyclized compound in
CC which attack of C2 on C14 in neosartoricin C results in the formation
CC of the acetal-containing dioxabicyclo-octanone ring (By similarity).
CC Both of these compounds are novel and possibly represent related
CC metabolites of the gene cluster (By similarity).
CC {ECO:0000250|UniProtKB:A1D8J0, ECO:0000250|UniProtKB:F2S701,
CC ECO:0000305|PubMed:23368997, ECO:0000305|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; DS995703; EEQ30781.1; -; Genomic_DNA.
DR RefSeq; XP_002848094.1; XM_002848048.1.
DR AlphaFoldDB; C5FM59; -.
DR SMR; C5FM59; -.
DR EnsemblFungi; EEQ30781; EEQ30781; MCYG_03600.
DR GeneID; 9229416; -.
DR eggNOG; ENOG502SIVG; Eukaryota.
DR HOGENOM; CLU_040697_0_0_1; -.
DR OMA; WIADCGE; -.
DR OrthoDB; 1519546at2759; -.
DR Proteomes; UP000002035; 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;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..412
FT /note="FAD-dependent monooxygenase nscC"
FT /id="PRO_0000437907"
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; 44983 MW; BD17A83A615BE403 CRC64;
MAKPQATVLI IGAGISGLTT SRLLTNSGIP NIVFEASTPD RSQGFAISLQ EFGYSALLSA
LGDLPLSSLI RGVAPDREIG GTGWIDQALR DNCTGELLVA PDLTTAKQTV VRANRNALRR
WIADCGEEEL DVRYGHKLQS VEGTVGDITA VFENKARYRG SLVVAADGVN STIRSQVLPG
VVPETIPLIH YHGEFQLSRT AFDELIRPHS GHSNILVGVG DGFNTPLSIC NMTKTQVHLD
WSYSRTVTGD DDLLYRPNLP SEEAKQIPPA LVKELAALAL AEPWKRFLNP ESLKSHRVFH
WTTRCVYMTQ DDARRAGEQG VVFVGDSWHA MPIFGGEGGN HALLDGVELA DAVVKVVASP
GKDHLSKAVA SYYAGAWKRS QEAVRRSTQR FFLLHRPAAE WKEIAEKKKK AV
