NSCC_NEOFI
ID NSCC_NEOFI Reviewed; 408 AA.
AC A1D8J0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=FAD-dependent monooxygenase nscC {ECO:0000303|PubMed:23368997};
DE EC=1.-.-.- {ECO:0000305|PubMed:23368997};
DE AltName: Full=Neosartoricin biosynthesis protein C {ECO:0000303|PubMed:23368997};
DE Flags: Precursor;
GN Name=nscC {ECO:0000303|PubMed:23368997}; ORFNames=NFIA_112250;
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: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of neosartoricin, a prenylated anthracenone
CC that exhibits T-cell antiproliferative activity, suggestive of a
CC 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 (PubMed:23368997). The
CC hydrolase nscB then mediates the product release through hydrolysis
CC followed by spontaneous decarboxylation (PubMed:23368997). The
CC prenyltransferase nscD catalyzes the addition of the dimethylallyl
CC group to the aromatic C5 (PubMed:23368997). The FAD-dependent
CC monooxygenase nscC is then responsible for the stereospecific
CC hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-
CC acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-
CC acetylation leading to neosartoricin may be catalyzed by an
CC unidentified O-acetyltransferase (PubMed:23368997).
CC {ECO:0000269|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:0000269|PubMed:23368997}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; DS027692; EAW20701.1; -; Genomic_DNA.
DR RefSeq; XP_001262598.1; XM_001262597.1.
DR AlphaFoldDB; A1D8J0; -.
DR SMR; A1D8J0; -.
DR STRING; 36630.CADNFIAP00010116; -.
DR EnsemblFungi; EAW20701; EAW20701; NFIA_112250.
DR GeneID; 4589234; -.
DR KEGG; nfi:NFIA_112250; -.
DR VEuPathDB; FungiDB:NFIA_112250; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_040697_0_0_1; -.
DR OMA; WIADCGE; -.
DR OrthoDB; 735852at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..408
FT /note="FAD-dependent monooxygenase nscC"
FT /evidence="ECO:0000255"
FT /id="PRO_0000437906"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 338..342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
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 408 AA; 44828 MW; 2264ED4ABC8A37E1 CRC64;
MAPPLPILII GAGISGLTTA RLLTNSGIPN IVFEASSPDR RQGFAISLRE WGYATLLSAL
GDLPLRSLTR GVAPDREIGG SGWIDQAVWD NGTAKKLFVP DANSSTKEQI VRANRNALRR
WIADCGEEEL DVRYGHRLKR VEGSLGDVQV EFENGAFYRG LMVVAADGVN STVRSQVLAD
VQPEIVPAVL YHGEFQLPRA DFDRLFRPHT GESNILAGVG DGFNTPFAVC NMTKTHVHMD
WSYSRPAWGS GENDPLYRPN LASEEAKRIP PALVEELASR DLAEPWSLFL NGEAIQHHRV
FHWAVRCVSV TQEDMQRAVG RGIAFVGDSW HAMPIFGGEG GNHALADGVE LAAAVAAGVA
GDLGVAIGNY YDRAWKRSQD AVRRSKQRFY ALHRPMAQWR ELSQKKPV
