ID F1SYI0_9APHY Unreviewed; 547 AA.
AC F1SYI0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:BAK09524.1};
GN Name=PpCYP218 {ECO:0000313|EMBL:BAK09524.1};
GN ORFNames=IEO21_05548 {ECO:0000313|EMBL:KAF9813511.1};
OS Postia placenta.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=104341 {ECO:0000313|EMBL:BAK09524.1};
RN [1] {ECO:0000313|EMBL:BAK09524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MAD-698-R {ECO:0000313|EMBL:BAK09524.1};
RX PubMed=21938516; DOI=10.1007/s00203-011-0753-2;
RA Ide M., Ichinose H., Wariishi H.;
RT "Molecular identification and functional characterization of cytochrome
RT P450 monooxygenases from the brown-rot basidiomycete Postia placenta.";
RL Arch. Microbiol. 194:243-253(2012).
RN [2] {ECO:0000313|EMBL:KAF9813511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FPRL280 {ECO:0000313|EMBL:KAF9813511.1};
RA Koelle M., Horta M.A.C., Nowrousian M., Ohm R.A., Benz P., Pilgard A.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9813511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FPRL280 {ECO:0000313|EMBL:KAF9813511.1};
RX PubMed=32625194;
RA Kolle M., Horta M.A.C., Nowrousian M., Ohm R.A., Benz J.P., Pilgard A.;
RT "Degradative Capacity of Two Strains of Rhodonia placenta: From Phenotype
RT to Genotype.";
RL Front. Microbiol. 11:0-0(0).
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; AB573391; BAK09524.1; -; mRNA.
DR EMBL; JADOXO010000103; KAF9813511.1; -; Genomic_DNA.
DR Proteomes; UP000639403; 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 CDD; cd11042; CYP51-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; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 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 2: Evidence at transcript level;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
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|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000639403};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 492
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 547 AA; 62020 MW; 2191833DC0697D44 CRC64;
MANANFSEPW AGYLVQAQSQ LASTSIPRLL LLLVVNIPVI AVVLNVLSQM LPRDRSLPPL
VFHWIPWFGS AAQYGQDPVE FFKSCREKHG NVFTFILLGR RVTVTLGPKG NDFVFGGKHT
VVAAEEVYGP LTTPVFGKDV VYDCPNEVLM EQKKFVKVSL TTDKFRDYIG MVDDEVTQFL
STDPAFRTYQ MDDINEWGSF SVYKTLAEMT ILTAARTLQG KEIRENMTKG FAELYADLDH
GLTPLHWMFS NLPLPSYRKR DVAHEKMSQF YQNILRNRRN NNVGYEDDVM ASLMNQTYRD
GRPIPDHEIA HMMIALLMAG QHTSSSTTSW VLLHLADRPD IAEQLYQEQV KHFGLPGGGF
REMTYDELKK LPILDAVIRE TLRCHAPIHS IMRYIRDDLP VPQSLGAPSE DSVYVVPKGY
TVLASPALSQ MDPLIWKDAN TWDTTRWLDA AGMAAQAKRE YDEDTKVDFG FGLVSKGTES
PYLPFGAGRH RCIGEQFAIV QIGTIISTIV RKIEMRLEGP FPKPDYSSMM VVPQQPCQIA
YRRRKFD
//