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Database: UniProt
Entry: H0EDJ6_GLAL7
LinkDB: H0EDJ6_GLAL7
Original site: H0EDJ6_GLAL7 
ID   H0EDJ6_GLAL7            Unreviewed;       774 AA.
AC   H0EDJ6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative Bifunctional P-450:NADPH-P450 reductase {ECO:0000313|EMBL:EHL03422.1};
GN   ORFNames=M7I_0645 {ECO:0000313|EMBL:EHL03422.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHL03422.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHL03422.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC       family. {ECO:0000256|ARBA:ARBA00010018}.
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:EHL03422.1}.
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DR   EMBL; AGUE01000010; EHL03422.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EDJ6; -.
DR   HOGENOM; CLU_001570_7_0_1; -.
DR   InParanoid; H0EDJ6; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; cd06206; bifunctional_CYPOR; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450_NADPH--P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          221..362
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          395..612
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   774 AA;  84999 MW;  E124DB0CD8101F61 CRC64;
     MVSVLEESQT RGSLPTVLNM FRRSAQRKYD EEIAWMRGIC EEMIAHRRKN PLEKKDLLNA
     MIHGKDPKTG CYMTDESIVD NILTFLVAGH ETTSGLLSFV FYLLIKNPAI MNLAREEVDK
     VLGTGPITPQ HMNQFPYLEA ILKETLRLYP TAPAIAMAPV PETTEYPIFL AGGKYQLNKG
     DNLLALLVKI QKDPLAFGDD AEEWKPERML EENFAKLPPN SWKPFGNGAR TCEALAQSLA
     RVAGTRGFEV RVDPLDSATD DVPKSQPLII ICPSYEGQPP DNAAQFFGWL EKLKDGKSLQ
     NVEFTVFGVG NRDWTSTFHK VPMNLDRLLA ANGGTRIAAL GLGDVAKGDI FNDFDYWQDN
     VLWPAIQGSG SSTKNVVAEL DLEIDTSARS QTLRQDLQGA VVLSNKILTA LGVPEKRHIE
     IQLPKGMNYT AGEYLAILPT NSQTNVRRVL KRFGLPADAM ITIRNVNAGS TLPATHPVSV
     TDLLSSYVEL NQPATKRNIQ VLASLPTTPS TRTALLALTT NTTTKNTPPP SLLTLLETHP
     TLPIPFQTYI SLLPPLRTRQ YSISSSPLAT PDVVSITFSI LPSGVASTYL ATLEPDDIMH
     IAVKPTILFT LPEHMGKTPI IMIGAGAGIA PFLGFLQERA ALLNRNSELS LAPAWLFLGC
     RAPEQDALFA DELRAYEDAG VVRVYYAYSQ EEGKSRGCRY VQDRVWAERG EIGGLIRGEG
     KILVCGGQEL GEGVKGVVRR IYGEGRRGDG KADGIGEEDV ERWFDGLKGK GRGI
//
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