ID A0A0D0AWP9_9AGAR Unreviewed; 457 AA.
AC A0A0D0AWP9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_48174 {ECO:0000313|EMBL:KIK54975.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK54975.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK54975.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK54975.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN834810; KIK54975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0AWP9; -.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OrthoDB; 1776156at2759; -.
DR Proteomes; UP000053593; 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:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11062; CYP58-like; 1.
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:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT BINDING 440
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 457 AA; 52296 MW; 4166E40100A7974F CRC64;
MIYLVLASLL FSYLAALALY RIFFHPLHKF RGPVLAALTD WYEIYYNIVH DGGLVVEIER
LHDLYGPVVR TGPNTLHFND RRAYHDIYTY GTTLTKEPRF YHGFLAQATE SSTVFTDPQQ
ARNRRSLLAP SFSRQAVMKL EYLIQKKVDQ LIAILEEYYN SPDSNAKISL AYRSLTTDVI
TEYCFASSIN TLADPNFSHP FVLETQKFLK RVWTQVYFPF IIRLVARLPK TFVLWLFPNF
TTILEVQEKF EIQIDSLLNN PEDLSTSDHE TVYHHLLAPK DPELRPSRIS LVHEAFTLLT
AGSDTVGHTC TVGTYFALQD HLIRGRLAEE LRDAWLDKGR PLSFTTLEKL PYLTAFIKES
LRMAIGAIHP MPRIVSSETP EIAGLKIPPG TIVGMSPYFM HMNPGVFSDP FTFNPDRWLV
EDTSEMMLDF VPFSKGPRQC VGLKCGITCS NTNPYEN
//
