SDGC_EMENI
ID SDGC_EMENI Reviewed; 475 AA.
AC A0A1U8QHS4; C8VPE4; Q5BCE4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=FAD-dependent monooxygenase sdgC {ECO:0000303|PubMed:30302871};
DE EC=1.-.-.- {ECO:0000269|PubMed:30302871};
DE AltName: Full=Aspernidgulenes biosynthesis cluster protein C {ECO:0000303|PubMed:30302871};
DE Flags: Precursor;
GN Name=sdgC {ECO:0000303|PubMed:30302871}; ORFNames=AN1786, ANIA_01786;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BN001307; CBF85559.1; -; Genomic_DNA.
DR EMBL; AACD01000028; EAA63962.1; -; Genomic_DNA.
DR RefSeq; XP_659390.1; XM_654298.1.
DR AlphaFoldDB; A0A1U8QHS4; -.
DR SMR; A0A1U8QHS4; -.
DR STRING; 162425.CADANIAP00008433; -.
DR EnsemblFungi; CBF85559; CBF85559; ANIA_01786.
DR EnsemblFungi; EAA63962; EAA63962; AN1786.2.
DR GeneID; 2875010; -.
DR KEGG; ani:AN1786.2; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_12_2_1; -.
DR OMA; VPGLVFW; -.
DR OrthoDB; 462247at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..475
FT /note="FAD-dependent monooxygenase sdgC"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451915"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 149
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 327..331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 475 AA; 52305 MW; 68F8DCD2F0BB4022 CRC64;
MDKRSFKVIV VGGSIAGLTL AHSLDLAGID YIVLEKHSDP LATVGGSVGL LPNGWRILHQ
LGLRHQLEQE ACPVKVAHMT YPDGFVFSDN FPAAIQERQV PEIQFPIGYM PANDERFGYS
LSVLTRQQLI EVLYLGLRDK SKIKVGQRVI KIQHHQNRRG VSVFTESGQE HVGDLVAGAD
GVHSITRSQM WLQLGQKLDA EKERRQLVAE YSCVFGISSP LKGIPPGEQL IACHDNATVL
AFPGKDAHIG WGLIQKLNRP CNSPATTQSS DGETALIMAK SAAGLGLCKD LKFHDLWVNT
PKYSFTILEE GLFQIWHHGR IMTPNMAQGA NTAIEGAAAL ANTLRRISQI DKPSEDDINR
LLQGYTVRQQ KRLRAVHAIS RSVTRVHARQ GRIKKIIGRY VYPYTPGAAL HTFSRIIAPA
PCLDYVPMPF PGPGWTRALV SGWSPISGVL LLVIPIIALV YGYSVINFGR DSINN
