ID A0A2K0WBY2_GIBNY Unreviewed; 449 AA.
AC A0A2K0WBY2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cytochrome P450 oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FNYG_06844 {ECO:0000313|EMBL:PNP79751.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP79751.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP79751.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP79751.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) 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:PNP79751.1}.
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DR EMBL; MTQA01000088; PNP79751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WBY2; -.
DR STRING; 42673.A0A2K0WBY2; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000236664; 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; cd11061; CYP67-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 2.
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:SF172; P450, PUTATIVE (EUROFUNG)-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 Heme {ECO:0000256|ARBA:ARBA00022617, 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000236664}.
FT BINDING 394
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 449 AA; 51097 MW; F54A4AD353A07582 CRC64;
MSTFSGMSNL PFMILAHGGA RSTHLAKLHK TKPIIRTGPN SLSFAGGQAI KDIYGHGTPC
IKDESYIVGA GTHFHLADVV DKHEHARKRK VLSSAYALKN LEGWEYKVAD KVQRMMNHFD
KVYTAPLPKG AKFPDPQDVN LDFRAWSNFF SLDAIADIGL SEKLGLLDQG HDRVEAQQTC
GTVYKANLRE CLYPTARKQS YLLWTYYHYK LLNKISNIIP FYRKMSESAK GWDDIVLRRA
QIRLDRYQKG EKLDDFFQAL MEDKNGNSHE LEWGRLVMEL LRQELDSILE PDEVVAPYEK
VKHLPYLRAC LDESLRLWPP TPQNLGRQTP PEGLTIMGQY IPGNTSVGVS ALVAHRDESI
YPESEKFIPE RFLGEKGKEL QSHFITFSAG ARGCIGRNIS YLEQAVCLAS IVHRYDFALP
AGFELKREET MNHILGPMPV KVWKRNLEE
//