ID A0A074WJE9_9PEZI Unreviewed; 682 AA.
AC A0A074WJE9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000208};
DE EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000208};
GN ORFNames=M436DRAFT_47588 {ECO:0000313|EMBL:KEQ73148.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73148.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ73148.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73148.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC cytochrome P450. {ECO:0000256|PIRNR:PIRNR000208}.
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|PIRNR:PIRNR000208};
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|PIRNR:PIRNR000208}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family.
CC {ECO:0000256|PIRNR:PIRNR000208}.
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DR EMBL; KL584710; KEQ73148.1; -; Genomic_DNA.
DR RefSeq; XP_013427069.1; XM_013571615.1.
DR AlphaFoldDB; A0A074WJE9; -.
DR STRING; 1043004.A0A074WJE9; -.
DR GeneID; 25410741; -.
DR HOGENOM; CLU_001570_17_3_1; -.
DR OrthoDB; 2786000at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016126; P:sterol biosynthetic process; 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; IPR023208; P450R.
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 PIRSF; PIRSF000208; P450R; 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|PIRNR:PIRNR000208}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000208};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000208};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000208};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..217
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 266..525
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 682 AA; 76341 MW; 02E4B4ADC438502F CRC64;
MLNKPSGYAD YAAITAFSLA WGTYLLKGKA WDRPDPYHHV WFEKPQVSDA AASDGVKETR
DISQKLQETN NQIVIFWGSQ SGTAEGFAHR LGRECHSRFR LHALVADLSD YDMETIEHIT
KETLVVFIVS TFGEGDPSDN TAGLWHWIRS AKASLNNMRY IAFGLGNSNY KYYNKVVDVV
AESLNAHGAQ QLMPIGKADD AKGATEEDFI TWKENLFDYF KRNLGHQEYD MVYEPSLLVE
PDTSLELIDL HQGEPVLEAK ALAGSSAIRP LLIKDMRDLF DTTADRNCLH VELDLSDFPE
IGYKTGDHLS IWPSNPNAEV ERVLDQLGRL HEADVPVLIK SLDGSKVKIP TPTTLSALLQ
YYLEICAPVS RETAAQLARF APTKTSRLFL EDVSRNRSRY SAFLAATHIT VGRLLEISTR
SEPTTWSSLP LAFLLDVFPV MRPRHYSISS SSVVSPRTPS ITAVVSQATI PDSIGGQITI
PGLATNYLLA HHVKDKNGYS LLGPDAALEG RRVYAQIRKS KFKLPALASQ AIIMVAAGTG
IAPFRGFIQE RARMQRVGKA CGKMILYFGC RSLEEDFIYR EELAQLQRVL EDQLSIVTAF
SRHEGKKIYV QERILEDSER ISSMLIEGNA NLYICGSAAM AREVNNTISS MIQNVKGWTD
GEMKDWNETK KKTRKFQEDV WG
//
