ID A0A397I4S7_9EURO Unreviewed; 609 AA.
AC A0A397I4S7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CDV55_103250 {ECO:0000313|EMBL:RHZ67850.1}, CFD26_107212
GN {ECO:0000313|EMBL:RLL97679.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ67850.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL97679.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ67850.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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 -!- 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:RHZ67850.1}.
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DR EMBL; NKHV02000050; RHZ67850.1; -; Genomic_DNA.
DR EMBL; NIDN02000071; RLL97679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397I4S7; -.
DR STRING; 1245748.A0A397I4S7; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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:UP000215289}.
FT DOMAIN 1..151
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 190..452
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 609 AA; 68017 MW; 9EAD5DDD8F56334A CRC64;
MVYWGSQSGR AERLAASFAR ECSARLGLRV AVADLDDHDH EHLFEVRSPK LVVFVVSTFG
EGDPTDNAST FCSMLKALRD TDNRQLLKDL RYAAFGLGNR NYRHYNKIVD LVDRTLQDLG
ARRVGTVGKA DEAKGGTATD EDFLEWKESM FERLSEMFGV EERPMVYSPE LNIIPANPKT
NVILTREAMS NILPALMVVA RTLTDSVDRR CLHLELDLSG NRSMKYQTGD HLLIWPHNSV
AETQRLCQLV GLSEVERTQP VKIKSPIQGK STGFPSPTTK ETILRHYLDI SGPVSRDVLR
QLAVFSPTKA AQEYLLALAK DKAKFETTVS LKLLSLGKVM QLAAGDKVWN QLPFTFLLEC
LGKLQPRYYS IASSPSVSPF QPAITLAITR KFLEAPAQFA HFHGVASNYL LAVKRSQKSN
SNQQQPLDQG PDYGPTTSKV LVQIRRSTFK LPANPQRPIV MIAAGTGVAP FRAFVQERAA
LASRGLPVGE AVLLFGCRSP TEDYLYADEW RDHAARLPGF EVINAFSRYG ERKVYVQDKV
LEVKDKIAGL LDKDAAVYIC GSADMAKEVR RALIKVLKAT RSWTEQEAEQ YVMGEMKKAK
RLQEDVWSG
//