ID A0A2I2GPQ4_9EURO Unreviewed; 656 AA.
AC A0A2I2GPQ4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=NADP/FAD dependent oxidoreductase {ECO:0000313|EMBL:PLB54843.1};
GN ORFNames=P170DRAFT_470281 {ECO:0000313|EMBL:PLB54843.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB54843.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB54843.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB54843.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:PLB54843.1}.
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DR EMBL; MSFO01000001; PLB54843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GPQ4; -.
DR STRING; 1392250.A0A2I2GPQ4; -.
DR VEuPathDB; FungiDB:P170DRAFT_470281; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT DOMAIN 236..495
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 23..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 72281 MW; 184DE98FFC4D7949 CRC64;
MIEIQWLTWT LKIVHAVLEP PVRTNAPRSS PVINGDHRNI PVSSTSHPDN PVPEEPRGVR
SLSVTDMTFN GFSADTETST NTESPSTPAT SLQSDTETLA RKQSVSDNDS GRERRASTVL
ISQNSEDMRR LLENVGIGGT QKVQPLCCGG GCCRSQPLRR TSEPVSGVNY ITAPDNKAYR
GLKLNVEYLT MDSELTNVAE LPEKTVSFSA IPASAVDMQL GPADHPPPFV QPHPPYNVFR
APLHHARELT KAGAEKRTYH FDIDVTDYPA ESGMVDFVVG GAIGVCPRNK DEEVDDIFNQ
LGVPKSIRDK KVSVRTAKGR WPTIWGDDKP RELITTRREL LNWCADIQSY APTKGLFRLL
AEYASDVNEK QILMFLSSAQ GQGAFCDLRT ASHVSVSQLL HAFPSAQPPL DHLLSVLNTL
MPRFYSLSQD PLLSCTKGAQ PRRLVEVAVS VAESDDWKGG MRTGVGSGYL ERLAQQVMQA
EKRGIDPRTL DLHVPMFRGL MANPLATRFA SDGPMLLIGA GVGIAPFRGF VQRRLQSANC
ANKVWVLQGV RDSLLDELYR GEWGVDEDKV RTVVQSRRGE SMYVQEEVRH QADLVWFVIN
ALDGRVFVCG SGKGMGEGVE AALVDVAMAK GNLNVEEAEQ FWANKKEAGQ YIAETW
//
