ID   SDCF_EMENI              Reviewed;         479 AA.
AC   C8VPE5; Q5BCE3;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=FAD-dependent monooxygenase sdcF {ECO:0000303|PubMed:30302871};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30302871};
DE   AltName: Full=Aspernidgulenes biosynthesis cluster protein F {ECO:0000303|PubMed:30302871};
GN   Name=sdcF {ECO:0000303|PubMed:30302871}; ORFNames=AN1787, ANIA_01787;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30302871; DOI=10.1002/cbic.201800486;
RA   Lin T.S., Chen B., Chiang Y.M., Wang C.C.C.;
RT   "Discovery and elucidation of the biosynthesis of aspernidgulenes: novel
RT   polyenes from Aspergillus nidulans by using serial promoter replacement.";
RL   ChemBioChem 20:329-334(2019).
CC   -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the polyenes aspernidgulenes
CC       (PubMed:30302871). The carbon backbone of aspernidgulenes is
CC       synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter
CC       unit and performs malonyl-CoA extensions as well as regioselective
CC       methylation and reduction (PubMed:30302871). The resulting nonaketide
CC       offloads the HR-PKS by intramolecular lactonization to yield the 5,6-
CC       dihydro-alpha-pyrone-containing hexaenoic acids preaspernidgulene A1
CC       and A2 (PubMed:30302871). The FAD-dependent monooxygenase sdgC then
CC       installs the first epoxide on the penultimate double bond
CC       (PubMed:30302871). Subsequently, the FAD-dependent monooxygenase sdgF
CC       presumably generates a ketone intermediate through Meinwald
CC       rearrangement involving a hydride shift (PubMed:30302871). Next, sdgC
CC       introduces another epoxide on the last olefin of the ketone
CC       intermediate after E/Z isomerization (PubMed:30302871). The epoxide
CC       hydrolase sdgD then catalyzes stereospecific cyclization of the 5,6-
CC       dihydro-alpha-pyrone and opening of the epoxide ring to form an
CC       oxygenated trimethylcyclopentanone and an oxabicyclo[2.2.1]heptane unit
CC       (PubMed:30302871). Finally, the bicyclic unit undergoes hydrolytic
CC       cleavage, either spontaneously or catalyzed by sdgD, to assemble the
CC       dimethyl-gamma-lactone moiety in aspernidgulene A1 (PubMed:30302871).
CC       {ECO:0000269|PubMed:30302871}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30302871}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA63963.1; Type=Erroneous gene model prediction; Evidence={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; AACD01000028; EAA63963.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF85560.1; -; Genomic_DNA.
DR   RefSeq; XP_659391.1; XM_654299.1.
DR   AlphaFoldDB; C8VPE5; -.
DR   SMR; C8VPE5; -.
DR   STRING; 162425.CADANIAP00008434; -.
DR   EnsemblFungi; CBF85560; CBF85560; ANIA_01787.
DR   EnsemblFungi; EAA63963; EAA63963; AN1787.2.
DR   GeneID; 2875166; -.
DR   KEGG; ani:AN1787.2; -.
DR   VEuPathDB; FungiDB:AN1787; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_018354_1_2_1; -.
DR   InParanoid; C8VPE5; -.
DR   OMA; LCLYQPY; -.
DR   OrthoDB; 733611at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..479
FT                   /note="FAD-dependent monooxygenase sdcF"
FT                   /id="PRO_0000451916"
FT   DOMAIN          40..213
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   MOD_RES         79
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:P08159"
SQ   SEQUENCE   479 AA;  52411 MW;  E732797F0C7C6E10 CRC64;
     MATVSELCCA ALNTSIGNRI AFPGSTAYNE SLSSYFGVNA QLPPSCFVLP LSAQDVSVAV
     QTLTSQPDPC FFAIRSGGHT TSLGASAIEA GVTMDLSGMN TTTYDSSTNT AFIQPGARWG
     SVYETLLRDN VLVPGGRTAS VGVGGYLTGG RNSFHAARVG LACLSIKGYE IVLADGEVAK
     VDQDSHPNLF RALKGGSNNF GIVTLFDMEA FSTEGTIWGG TVLYDISTKD QYIAAGTAFT
     DNIPNDPYAS WVGMFAYNST TDQTAIFTSL AYTRPVQSWP QAFSEFYAIP NITHTLRSAT
     VLDLAVENSF PYGYRNVLQT GTYSNNAEII QKAVIILNNQ VKMAKLRARG KDYALFAIVQ
     PWVPLFWEHS EARGGDVLGL ERFETNLLNI AWDYSWDNSA DDELLYELAQ SAREQLDEYA
     RSTGAYNEYI YLNYAGRTQD PLRGYGLENL EFLRRVSEKF DPDGVFQRLV RGGFKIDRA