NSCC_TRIRC
ID NSCC_TRIRC Reviewed; 412 AA.
AC F2T0M2;
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=TERG_08359;
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892;
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; GG700661; EGD92144.1; -; Genomic_DNA.
DR RefSeq; XP_003231061.1; XM_003231013.1.
DR AlphaFoldDB; F2T0M2; -.
DR SMR; F2T0M2; -.
DR EnsemblFungi; EGD92144; EGD92144; TERG_08359.
DR GeneID; 10377339; -.
DR VEuPathDB; FungiDB:TERG_08359; -.
DR eggNOG; ENOG502SIVG; Eukaryota.
DR HOGENOM; CLU_040697_0_0_1; -.
DR InParanoid; F2T0M2; -.
DR Proteomes; UP000008864; 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_0000437913"
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 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
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"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 412 AA; 45536 MW; E6EC37A1E9C3354C CRC64;
MGKPQETILI IGAGIAGLTA SRLPTNNGIP NIVFEASTPE RNQGFAISLQ EFGYSSLLAA
LGDLPLSNLT RGVAPDRQIG GTGWIDQALR DNRTGELLVA PDLTTMKQTI VRANRNALRH
WIADCGEDEL DVRYGHKLRR IEGKLGDITA VFENHAKYKG SLVIAADGVN STTRSQILPN
VIPETIPLIH YHGEFQVSHS AFDKLIRPHS GHSNILVGVG DRFNTPLSIC NVTKTKVHLD
WSYSRPVKGE NDTLYRPNVP SEEAKQIPPA LLEELDALSL AEPWKNFLNS ESLKTHRVFH
WTTRCVYITQ DDARRAGEQG VVFVGDSWHA MPIFGGEGGN HALLDGVELA NAIIKSTASG
GKDGWDNVVK SYYAGAWKRS QEAVRRSTQR FFLLHRPAKE WKEISEKKKK PA
