ID A0A0D2FEX1_9EURO Unreviewed; 541 AA.
AC A0A0D2FEX1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z518_09617 {ECO:0000313|EMBL:KIX00552.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX00552.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX00552.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX00552.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847482; KIX00552.1; -; Genomic_DNA.
DR RefSeq; XP_013267688.1; XM_013412234.1.
DR AlphaFoldDB; A0A0D2FEX1; -.
DR STRING; 1442369.A0A0D2FEX1; -.
DR GeneID; 25297688; -.
DR VEuPathDB; FungiDB:Z518_09617; -.
DR HOGENOM; CLU_022195_9_2_1; -.
DR OrthoDB; 1351063at2759; -.
DR Proteomes; UP000053617; 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 CDD; cd11041; CYP503A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
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|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..541
FT /note="Cytochrome P450"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002253023"
FT BINDING 471
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 541 AA; 60600 MW; 423C531A059274A4 CRC64;
MGIPYGMLTG AVLLCYMAWR ISSSSGPRLP KGLPIIGARK GDWFPFFQAT LRNSLDVKKA
ALEGYQQYPD QAAILPVAGP GGASFIVLPA SETQFVSEQP ESVLNLRAVI KEGLLYRYTV
ADNFIILNAA HQHLITTTLT NQIGNLLSAL NEETAFCFEE IWGSDTETFR DVGVWDTLGR
VVGEVTNRAF VGLPYCRDPA LLNAGLGFAR CLPLSARFLS FVWEPLRPLA SPLFTLPNHF
FERRFTNILL PEIEGRLRDR IDNMKEDKDK FAAAKNDFLQ WSIEQAIASG DPRMWKPRTL
AGRILLLNLV SIHTSSLTIT NLVLDLISSK AEVLDELRTE ITSVLAETQG VWTKNSMYKM
EKLDSVFRES ARLNTLTAVA LRRVVVAKDG LTTPLGVHIP HGNFVAVPSL AVLTDANKYP
SPEFFHPFRF VDLRRDVNSG ERLPDHVERS RMSFAATSND YLAFGNGRQA CPGRFFAAAE
LKLMLAYILL HYDFEMLPNR PSDSWVGILR IPSPSAKIRV KKRKPSEIPE FRFPTHDEAW
T
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