ID A0A1F8ACW3_9EURO Unreviewed; 691 AA.
AC A0A1F8ACW3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ABOM_001640 {ECO:0000313|EMBL:OGM49542.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM49542.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM49542.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OGM49542.1}.
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DR EMBL; LYCR01000008; OGM49542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8ACW3; -.
DR STRING; 109264.A0A1F8ACW3; -.
DR OrthoDB; 2290257at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
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:SF108; NADPH--CYTOCHROME 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 PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
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 4: Predicted;
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:UP000179179}.
FT DOMAIN 85..236
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 287..537
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 691 AA; 78041 MW; EBFA420DA99347CA CRC64;
MEILRHPVNT LSGSHYAWSA AEWDDFLALT LFSLIAATLL LDSSLFNKDP LQHIWYEYPQ
GAKAQEKSST DINITQVLKD QGKDIIIFYG TQSGTAYELA RYLSRTIFQR FSKAALVADI
SDYNYDCLST VPSDVIVLFI LSTYGEGDPP DNAIRFDEWL DKELPKQQPT RASLANLRFA
ILGLGNRNYK YYNQFAKKVQ NALEKAGGTA IMDLSLADDS NGQTRGDYSE WAAQLQQAFV
DRCQIEEQPR PYESALEIVA CESFTDNLPT TQPIDLRHRS KLRASASAIY SANIVSITDL
TPQAQTKALH IEVDISHLPR VKYNVGDHLL IWPENRAEGV QRLGRILGID DAEMHRPLEI
RSKDSEIKAL WPHPITIHTL FKHHLDIAGL ASRDMILALK EFADSKTSEA ALDEMARNYR
RLSLMRRLDL ESILLAAAGP RGTWKIPLSF LLENLNPLKP RYYSVSSAPA VSPRKITLTV
AMKEVTLSAE ESILGLTSRF FLEMQQSLSS SSNARDNAGP LNTSVWCALR KSKFKPPTSN
MQPIIMVANG TGIAPFMGFL RHRLRKFEID GKVGKMLLFY GCKNETTHLY RDEIQRIQSA
FGDQLRLVTA YSQKGDGYVQ DQVRSYGEET EDLLCDGKAN VYMCGSVNMA GSVREELLMI
IQKRENWSET QAHEFEGTQL RMRKWQLDVW G
//
