EPAE_ASPNC
ID EPAE_ASPNC Reviewed; 488 AA.
AC A2QTE8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cytochrome P450 monooxygenase orf2 {ECO:0000303|PubMed:30384904};
DE EC=1.-.-.- {ECO:0000305|PubMed:30384904};
DE AltName: Full=Pestalamide A biosynthesis cluster protein orf2 {ECO:0000303|PubMed:30384904};
GN Name=orf2 {ECO:0000303|PubMed:30384904}; ORFNames=An09g01850;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=30384904; DOI=10.1016/j.micres.2018.10.004;
RA Wang B., Li X., Yu D., Chen X., Tabudravu J., Deng H., Pan L.;
RT "Deletion of the epigenetic regulator GcnE in Aspergillus niger FGSC A1279
RT activates the production of multiple polyketide metabolites.";
RL Microbiol. Res. 217:101-107(2018).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of nigerpyrone and its derivatives
CC carbonarone A and pestalamide A (PubMed:30384904). The biosynthesis
CC pathway begins with the polyketide assembly by epaA to form
CC phenylacetyl triketide precursor from successive condensation of two
CC malonyl-CoA, presumably with one phenylacetyl-CoA starter unit produced
CC by the phenylacetyl-CoA ligase epaB (PubMed:30384904). For the
CC nigerpyrone biosynthesis, the reactive polyketide chain is released as
CC an aldehyde through the R-domain. A nonenzymatic cyclization and
CC dehydration may create nigerpyrone (PubMed:30384904). For the
CC biosynthesis of carbonarone A and pestalamide A, an extra methyl group
CC is added through the C-methyltransferase domain. Several further steps
CC involving the dehydrogenase orf1, the cytochrome P450 monooxygenase
CC orf2 and the FAD-dependent monooxygenase orf3 are required to form a
CC carbonarone A precursor which is converted to carbonarone A via
CC cyclization (PubMed:30384904). The O-acetyltransferase epaC could
CC catalyze the transfer of 2-methylsuccinyl-CoA, a common intermediate in
CC the ethylmalonyl-CoA pathway, to generate the final product pestalamide
CC A (Probable). {ECO:0000269|PubMed:30384904,
CC ECO:0000305|PubMed:30384904}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30384904}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AM270194; CAK40123.1; -; Genomic_DNA.
DR RefSeq; XP_001393500.1; XM_001393463.1.
DR AlphaFoldDB; A2QTE8; -.
DR SMR; A2QTE8; -.
DR PaxDb; A2QTE8; -.
DR EnsemblFungi; CAK40123; CAK40123; An09g01850.
DR GeneID; 4983716; -.
DR KEGG; ang:ANI_1_1130084; -.
DR VEuPathDB; FungiDB:An09g01850; -.
DR HOGENOM; CLU_001570_14_2_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..488
FT /note="Cytochrome P450 monooxygenase orf2"
FT /id="PRO_0000446158"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 432
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 488 AA; 55371 MW; 664E1629A8F003DF CRC64;
MESLAHLPGI FLPLAGCVLA LSLTTIVYRT VTNPLSHIPG PQISKWSSLI EQYYWFAGTK
VEYVDYLHRK YGPIVRVTPT EVDICDLPAV REIHRVRGGY LKSEWYKSLT PPGVTSLLTL
IEPAQYSEWR RLLAGPLSDT SLGKVEPMVT NHVHATIDRI ASDLQSQGVS DLYKWWTYMA
TDVVSELSFG EPIGLLARPK ETAWVMDYLD KVGIMHAWRT TFPFVFVLGR FMPVHPFKHA
IQAIGLLGKW ARQSIQQYRQ HIQEQPESPK PTLFTKLFKT GKFDDFQLTY LAGSYITAGS
HTTAVTLLYL IYAICSDNEV RQKLLAEIRT LPENFRHDEL RHLPYLNQVI TETLRKYAVV
SSALPRVVPA GGATLAGYYL PGGTTVSTQA YTLHRNEAIF PNPEKFDPSR WESPTQDMKD
AYMPFGGASR MCIGNSLALM EIRLTTTLFL RRFPEVHMSR QNGMRDEDLA QEQYLIMAPR
GQRLLVEA
