ID A0A2S6CKB4_9PEZI Unreviewed; 510 AA.
AC A0A2S6CKB4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_03150 {ECO:0000313|EMBL:PPJ60143.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ60143.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ60143.1}.
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DR EMBL; PNEN01000313; PPJ60143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CKB4; -.
DR STRING; 357750.A0A2S6CKB4; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000237631; 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:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Heme {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 Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 451
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 510 AA; 58444 MW; 5E10E3B4EEA2B5C3 CRC64;
MDLNFLYEAT STQIIAAAFA AYIVLGSIYR LYLHPLRHIP GPKLAALTWW YEVYYDVIQS
GQYNFKIQKL HKQYGPILRV NPEEVHIGDP DFLGEIYNAR KRDKPPEPSL DIAGSVAGTD
DWDLHKKRRQ AMTSFFSPKA VRELEPLLAR KRDKLVKVVE KKAKDDDGIP LNLSDLYFAY
CWDLIQEYAF AFDSTVLRDD LSESAQLRAN SQDLLLQVNF TRHFGWINSL AAYLPASIGE
KLIPPGVMDL KRVAARVAKT VQSVVQDKTT TKEEIQNSNQ HRSIFYTIRD DEQLPDVEKE
PLRLSREGNF LVVAASDSPA RAIHITHFYL MYEPKCMQKL RDELRPLGPT PSMEQVTELP
YLNAVFLEGT RLMFGLARRI FRVAPDDPIV YGKYIIPAGI NVATSTYCVH SDERIFPEPF
KFRPERWLGS NSKELRSKYH MTFGSKSPRS CLGIHLAEAE MKFAIAAVVR FEMELFETGL
KDVEYRHDFQ MAHGDLNSKG VRAVVKNSLW
//
