ID   A2QDQ5_ASPNC            Unreviewed;      1110 AA.
AC   A2QDQ5;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Contig An02c0240, genomic contig {ECO:0000313|EMBL:CAK37756.1};
DE            EC=1.14.-.- {ECO:0000313|EMBL:CAK37756.1};
GN   ORFNames=An02g07930 {ECO:0000313|EMBL:CAK37756.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / 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 {ECO:0000313|EMBL:CAK37756.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK37756.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
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., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.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).
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DR   EMBL; AM270019; CAK37756.1; -; Genomic_DNA.
DR   RefSeq; XP_001399926.1; XM_001399889.2.
DR   AlphaFoldDB; A2QDQ5; -.
DR   PeroxiBase; 5306; AnLDS03.
DR   EnsemblFungi; CAK37756; CAK37756; An02g07930.
DR   GeneID; 4979282; -.
DR   KEGG; ang:An02g07930; -.
DR   VEuPathDB; FungiDB:An02g07930; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000006706; Chromosome 4R.
DR   GO; GO:0051213; F:dioxygenase activity; ISA:AspGD.
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:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd20612; CYP_LDS-like_C; 1.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo-like_N.
DR   PANTHER; PTHR11903:SF13; LINOLEATE 10R-LIPOXYGENASE; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAK37756.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         423
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   1110 AA;  125110 MW;  ABDB7FCF9D4142C8 CRC64;
     MLRRFSSTFK RSSKGDRDSK PNGTQVNGQK RQSKVPAPRK SSSDESHSDH GVESDDGVSV
     FEKYAQVLHA SRRPLPNQNG DGTYLEQEHS GSLFKDLRAL GFKDIGTLKD LIKTKAKGEY
     IDDKTMLMER IIQLVSSLPG NSKTRVDLTN AFLDELWGSL PHPPLSYMGE EYAYRSADGS
     NNNPTLPWLG AAGTPYARSI APLTIQPGGL PDAGLVFDCL FAREKFTPHP NKVSSLFFDW
     ASLVIHDIFQ TDYTNSHVNK TSAYLDLSIL YGDDQEDQNL VRTFKDGKLK PDTFSEQRLQ
     AFPPACSVLM VMLSRFHNWV VEELAAINEN GRFNKPDPRL DEEKARKAWE KYDNDLFQTG
     RLVTCGLFIN ITLYDYLRTI VNLNRSNSTW CLDPRVQMEG TKSTPSGLGN QCSVEFNLAY
     RWHSAISAND EKWTEEIYEE LMGKPASEVS MRELLVGLGK YEREIPKDPS KRTFAGLKRQ
     EDGTFKDEDL VRILANAIED VASSFGARNV PKVLRSVEIL GIEQGRKWNV GSLNEFRKFF
     DLKPYETFEE INSDPDVADS LRHLYEHPDY VELYPGIVAE EAKEPMIPGV GIAPTYTISR
     AVLSDAVALV RGDRYYTIDY NPRNLTNWGY NEVRYDLNIN QGCVFYKLAM RAFPNYFKPD
     SIYAHYPMTI PSENRNIMKN LGRESHYSYD RPRYTEPVPN LLSYANAKLV LNNQKDFTVP
     WGGLSSIHAG KGGADFWSKS FDNEQWRNSV KEFYEDATLK LLNEKSCKLA GNKQVDIARD
     VGNLVPVHFV SKVFSLPLKT KSNPRGIFTE HEMFMIMAVV FNSTFFDVDP TKSFPLQHAA
     RAVSQELGKV VEAHVKSINH PGFLHGIIDS FRDDHNALKD YGDQLIKRLL ESGLGVSDVT
     WGQILPAAVE MVHTQSQMFT QIIHFYLTEG QKYLPEINRL ANENTAEAND RLTRFCLEAV
     RLNGNLGIYR EAQADINVSD ETGQYSVKSG EKVFVGSSKA NRDPQAFPSP DEVRLDRPLD
     SYLHYGLGPQ SGLGKDATLA AVTAMVRVVA RLDTLRPAPG AQGQLKKIPQ EAGFSVYMRE
     DYGSYSPFPT TYKVHYNGDV PAPKRQVTTA
//