ID A0A0P7AX28_9HYPO Unreviewed; 443 AA.
AC A0A0P7AX28;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Isotrichodermin C-15 hydroxylase {ECO:0000313|EMBL:KPM37985.1};
GN ORFNames=AK830_g8582 {ECO:0000313|EMBL:KPM37985.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM37985.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM37985.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM37985.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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:KPM37985.1}.
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DR EMBL; LKCW01000148; KPM37985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7AX28; -.
DR STRING; 78410.A0A0P7AX28; -.
DR OrthoDB; 928042at2759; -.
DR Proteomes; UP000050424; 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; cd11058; CYP60B-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305:SF29; BENZOATE-PARA-HYDROXYLASE; 1.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
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|RuleBase:RU000461};
KW Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424}.
SQ SEQUENCE 443 AA; 50344 MW; AD49C63C3F2D4177 CRC64;
MWTGYHHRAV QELHAKYGPV VRIAPNNLSY INPQAWKDIY AHKKTREQEM IKDPEFYVRN
PDAPTIVNGN HEEHARYRRL YSPGFSARSL REQEPLIQGY VDMFINGLAR ACEHGETPVD
MVQWFNWVTF DIIGDLAFGE PFGCLADGAT DWLLKLNQIE EAQMHFRIIQ HIPLLGRYAR
QIVNTMLPSD AVKGSEGHRK LTQEKVTRRV NNNASRPDFM EHILRQPPGK GFTMGEMLSN
SATLIQAGSE TTATLLSGAL HLLVNHPDKM QKLVDELTTS FASDDMMTIE NTDRLPYLAA
VLEESLRLYS PAVPGFPRQV PKGGAMIDGD YVPGGTSVAV NHYAAYHSPL NFSRPNEFIP
ERFIDTAAFP DDRRDVLQPF SVGPRNCIGK SLAYAEGRLI LGRAVWKFDM RLSEKSHGWM
SDQKGYVTWM RPEMEVYVKM RHG
//
