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Database: UniProt
Entry: A0A117DZ50_ASPNG
LinkDB: A0A117DZ50_ASPNG
Original site: A0A117DZ50_ASPNG 
ID   A0A117DZ50_ASPNG        Unreviewed;       470 AA.
AC   A0A117DZ50;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ABL_03648 {ECO:0000313|EMBL:GAQ40492.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ40492.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ40492.1}.
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DR   EMBL; BCMY01000005; GAQ40492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117DZ50; -.
DR   VEuPathDB; FungiDB:An04g02950; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1159092; -.
DR   VEuPathDB; FungiDB:ATCC64974_68680; -.
DR   VEuPathDB; FungiDB:M747DRAFT_257734; -.
DR   OMA; HTIWRRI; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
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   Gene3D; 1.10.630.10; Cytochrome P450; 2.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF156; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   BINDING         441
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:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   470 AA;  52812 MW;  D2F816921DFC47E6 CRC64;
     MATAELATAA AAITLQTFLS PIPEVSTIKI LSTYILVNLA AVAWSLRASI LADIPPPPSI
     AWLNLVFLST ATSWTVIHRL YFSPLASLPG PKRAAVSRLW VANQCRLGRS AAYLEEIHEE
     YNADIVRVGP NEVSIIDVEA IQEIYKGQYP RGYFYELRAS MGERNLNSER DYTHHGEWRR
     LWEKALSAKE LVNYDGRLQH HVEKFLRLLK NSEGRDVNTI KLTERFQVDV IMDVFFSKDS
     QIQDSEEDTF LSNFVHKYLG VAGVIACLRN VGEILSCLPS PPEAKAFERE IEEIISERRM
     KVAPQKDFIH HFITGGPAGR HLVQAKLRAE LDTTYNAGAE LTVESTRKLP YLNGVLNEGL
     RLGNPAPVGV PVKTPPGGLQ FGDTYVPGNV EVKVPFRVTL TDSRWFPKGD RFIPERWTGE
     MPELVRDRRA FTPFGYSVHS CVGKQLVTNE LKILIAKTVH EFNIFARGSV
//
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