NSCC_ASPFU
ID NSCC_ASPFU Reviewed; 408 AA.
AC Q4WA60;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=AFUA_7G00150;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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: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:23368997}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000015; EAL84876.1; -; Genomic_DNA.
DR RefSeq; XP_746914.1; XM_741821.1.
DR AlphaFoldDB; Q4WA60; -.
DR SMR; Q4WA60; -.
DR STRING; 746128.CADAFUBP00008427; -.
DR EnsemblFungi; EAL84876; EAL84876; AFUA_7G00150.
DR GeneID; 3504089; -.
DR KEGG; afm:AFUA_7G00150; -.
DR VEuPathDB; FungiDB:Afu7g00150; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_040697_0_0_1; -.
DR InParanoid; Q4WA60; -.
DR OMA; WIADCGE; -.
DR OrthoDB; 1519546at2759; -.
DR Proteomes; UP000002530; Chromosome 7.
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; IGC:AspGD.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..408
FT /note="FAD-dependent monooxygenase nscC"
FT /id="PRO_0000437905"
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; 44994 MW; 02F1A2F9ED7C322C CRC64;
MASRLPILII GAGISGLTTA RLLTNSGIPN IVFEASSPDR RQGFAISLRE WGYTILLSAL
GDLPLRSLTR GVAPDREIGG SGWIDQAVWD NGTAKKLFVP DANSSTKELI VRANRNALRR
WIADCGEEEL DVRYGHRLKR VEGSLGDVRV EFENGAFYRG LMVVAADGVN STVRSQVLAH
VQPETVPAVL YHGEFQLPRA DFDRLFRPHT GESNILAGVG DGFNTPFAVC NMTKTHVHMD
WSYSRPVRGS GEDDPLYRPN LASEEAKRIP TALVEELASR DLAEPWSLFL NGEAIQHHRV
FHWAVRCVSV TREDMQRAVG RGVAFVGDSW HAMPIFGGEG GNHALADGIE LAGAIAAGAT
GDLGTAIGNY YDQAWKRSQD AVRRSKQRFY TLHRPMAEWR ELSKKKPL
