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Database: UniProt
Entry: A0A3M2T548_9EURO
LinkDB: A0A3M2T548_9EURO
Original site: A0A3M2T548_9EURO 
ID   A0A3M2T548_9EURO        Unreviewed;      1115 AA.
AC   A0A3M2T548;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE   Includes:
DE     RecName: Full=Cytochrome P450 {ECO:0000256|PIRNR:PIRNR000209};
DE              EC=1.14.14.1 {ECO:0000256|PIRNR:PIRNR000209};
DE   Includes:
DE     RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE              EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000209};
GN   ORFNames=PHISP_04201 {ECO:0000313|EMBL:RMJ24927.1};
OS   Aspergillus sp. HF37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ24927.1, ECO:0000313|Proteomes:UP000272442};
RN   [1] {ECO:0000313|EMBL:RMJ24927.1, ECO:0000313|Proteomes:UP000272442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HF37 {ECO:0000313|EMBL:RMJ24927.1,
RC   ECO:0000313|Proteomes:UP000272442};
RA   Tafer H., Lopandic K.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00036596,
CC         ECO:0000256|PIRNR:PIRNR000209};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001025,
CC         ECO:0000256|PIRNR:PIRNR000209};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC       family. {ECO:0000256|ARBA:ARBA00010018, ECO:0000256|PIRNR:PIRNR000209}.
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:RMJ24927.1}.
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DR   EMBL; RAQS01000148; RMJ24927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2T548; -.
DR   STRING; 1960876.A0A3M2T548; -.
DR   Proteomes; UP000272442; Unassembled WGS sequence.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd06206; bifunctional_CYPOR; 1.
DR   CDD; cd11068; CYP120A1; 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; IPR023206; Bifunctional_P450_P450_red.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
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   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
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   PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
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; PS00086; CYTOCHROME_P450; 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   ECO:0000256|PIRNR:PIRNR000209};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000209};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000209};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000209};
KW   Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW   Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000209};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|PIRNR:PIRNR000209};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000209};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272442};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT   DOMAIN          506..646
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          684..929
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          481..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         413
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:PIRSR000209-1"
SQ   SEQUENCE   1115 AA;  123826 MW;  1F2782CDAE524060 CRC64;
     MTSTESPIPG PKGVPFLGNI YDVDREVPIH SLELLADNYG PIYRLTNFGI SRVFISSHEL
     ADEVFNEERF TKVVAGGLKE IRNGVHDGLF TANYPGEENW AVAHRVLVPA FGPLSIRAMF
     DEMYDIATQL VMKWARQGPK APIMVTDDFT RLTLDTIALC AMGTRFNSFY HEEMHPFVEA
     MLGLLQGSSD RTRRPALFNN LPTTENTKFW SDITFLRNLS QEMVDARKEN PQDKKDLLNA
     LILGRDSQTG QGLTDDSIAN NMITFLIAGH ETTSGMLSFL FYFLLKNPQA YKKAQEEVDT
     VIGRRKITVE DLSKLPYITA VMRETLRLRP TAPLIAVHAH PDKNKEHPVT LGDGEYTLND
     DETIALILSK IHRDPHVYGP DADEFKPERM LDENFNKLPK NAWKPFGNGM RACIGRPFAW
     QEALLVVAIL LQNFNFQMDN PSYDLRIKQS LTLKPKDFHM RATLREGLDA TTLGAFLNAG
     EAPSQAGADR SRKAKASPAP DKMKPMHIFF GSNTGTCEAF ARRMADDAAG YGYAAEVGSL
     DSAMQNVPKN GPVVFITASY EGQPPDNAAH FFEWLSAAKG KELEGVNYAV FGCGHHDWHA
     TFHRIPKAIN QSVEACGGSR LCGIGLTDAA NSDMFTDFDS WGESTFWPAL ATKFGAVQPQ
     DGPKSKSAFQ VEVSSGTRAS TLGLQLQEGY VLENRLLSQP DAPAKRMIRF KLPSDMTYQC
     GDYLAVLPVN PSSVVRRAIR RFHLPWDAVL RIQKQITNTT TSIPLDTPIS AFELLSTYVE
     LSQPASKRDL NMLADAAVAD ADVQAELRYF ASSPSRFSDE VVKKRLSPLD LLMRYHSVDL
     SIGDFLAMLP PMRVRQYSIS SSPLADSSEC SITFSVLNAR SLAASSLSPN ERAEEEQYLG
     VASTYLSDLR DGERAHVVVR PSHSGFKPPA DLKTPMIMAC AGSGLAPFRG FVMDRAEKIR
     GRRSSSSVTS AAQSEVEQPA KAILYAGCRT QGKDDIHAEE LAEWERLGAV QVRWTYSRPS
     DGSPGRHVQD RMLEDRKDLV ELFEQGARIY VCGSTGVGNG VREACKKIYL EQRQEKIGQA
     KERGEEVPEK DEQAAAEEFL EGLRTKERYA TDVFT
//
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