ID A0A0L1JGH3_ASPNO Unreviewed; 512 AA.
AC A0A0L1JGH3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Benzoate 4-monooxygenase cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ANOM_000942 {ECO:0000313|EMBL:KNG90869.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG90869.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG90869.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG90869.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU000461}.
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:KNG90869.1}.
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DR EMBL; JNOM01000008; KNG90869.1; -; Genomic_DNA.
DR RefSeq; XP_015411792.1; XM_015546200.1.
DR AlphaFoldDB; A0A0L1JGH3; -.
DR STRING; 1509407.A0A0L1JGH3; -.
DR GeneID; 26802746; -.
DR OrthoDB; 509202at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF164; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 455
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 512 AA; 58744 MW; 0B47F9D9FBA3FE4A CRC64;
MIVDFLSQNL FYSPVTLSVI LSIFVIAWLV IQPLYFGPLS HIPGPWINKI SSIYLTYYDV
RLQRNDKIMQ WHRQYGPVIC ISPGEVSAAT LSATREIYGS SGRCAKSNYF HHFTAYNEQS
IFATLCYKEH REKRKLTSGF YQASMIYKRP DIEGYTRRCV QKVLQQLRQQ RHSGKYCDIY
ALSDWYGFDI ITYLTLGKAH GTQTIERDCT ERRILRDLKT LQLWGPFRLR FPKAFELLSS
CLRYWMPMFT YLKSDTHLAE WAYNRVSDAA QYSDSQDPCS LFQRLMALTD GSKSTGGGRQ
NYIAAEILDN INAAEATVSV TVAYFFYHLS QEVKWQEEIR KELLKLPPQS DGLPSFTQLN
EAPILEACLN ETYRLYPASS GRAERVVPDE GKFLSGTFVP ADTIVTTSLT AMHRDKEIFP
SPESFLPQRW LNSDPVQREA LERHIIPFGY GARICLGKPL ATLEIKLLIA GIFLQYRTIP
APSCLAESMR QSSTHDAVPW GLKCELEFHP LI
//
