ID A0A395MHU3_9HYPO Unreviewed; 527 AA.
AC A0A395MHU3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cytochrome p450 oxidoreductase {ECO:0000313|EMBL:RFN47488.1};
GN ORFNames=FIE12Z_8283 {ECO:0000313|EMBL:RFN47488.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN47488.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN47488.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN47488.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN47488.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXXK01000252; RFN47488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MHU3; -.
DR STRING; 2594813.A0A395MHU3; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000265631; 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; cd11062; CYP58-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; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF147; P450, PUTATIVE (EUROFUNG)-RELATED; 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:UP000265631}.
SQ SEQUENCE 527 AA; 58604 MW; 15C8575D00685EA8 CRC64;
MADTIQSAVA ALSAREWAGV AVLSWLAFKV LQALYNISPL HPLSGVPGPK LAGATYLPEF
YYDVILVGRY THAIKKMHEK YGPIVRINPN ETHCADMAFS DEIYAVGGRK RDKPFHQVHG
SAAGTGNAFS TPDHDVHRLR RAPVAKFFSR AMIARLEQEV HELAQTLCNK LLAEASGKKS
QPIDVAHAYS CFTSDAISGY CFGEPFGLLS RDTWRPTFRE ATLAVLKPVF IFRFFPFLVG
TVKFGKYFVD YLPADAAMLV RTLQIDIPER VTKTKTDLNS GIVYDRPTIF ADLLNSELDE
SEKGTDRLVE EAVTIVNAGT ETTSWALAVI TYFLLSQPET MSKLQAELAT VVDDPRHLPS
WTTLEQLPYL GSVINEGLRL SYGVSSRSAR VPTTEDLVYR GEFNKKPATV VLPRGYAIGM
SAAISHHDEG VFPDSYGFIP ERWIGDDGAI KKNLERSMLA FSKGSRGCLG KNLALCELYL
SLTALVMRVM PHMRLYETTE RDVRYDHDMF IPVTVDDSEG VRVTIET
//
