NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY.
STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400;
PubMed=7646819 [NCBI, ExPASy, EBI, Israel, Japan]
van den Brink H.J.M., van Zeijl C.M.J., Brons J.F., van den Hondel C.A.M.J.J., van Gorcom R.F.M.;
"Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger.";
DNA Cell Biol. 14:719-729(1995).

[2]

CHARACTERIZATION.
STRAIN=T18.5;
DOI=10.1006/abbi.2001.2534; PubMed=11594739 [NCBI, ExPASy, EBI, Israel, Japan]
Faber B.W., van Gorcom R.F.M., Duine J.A.;
"Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger.";
Arch. Biochem. Biophys. 394:245-254(2001).

Comments

FUNCTION: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein.
COFACTOR: FAD.
COFACTOR: FMN.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity).
INDUCTION: By benzoic acid (BA).
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z26938; CAA81550.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S38427; S38427.

3D structure databases

HSSP

P16435; 1B1C. [HSSP ENTRY / PDB]

ModBase

Q00141.

Ontologies

GO:0005792;	Cellular component: microsome (inferred from direct assay from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from direct assay from UniProtKB).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from direct assay from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 693`	`693`	`NADPH--cytochrome P450 reductase.`	`PRO_0000167604`
`TRANSMEM`	`9 31`	`23`	`Potential.`
`DOMAIN`	`66 220`	`155`	`Flavodoxin-like.`
`DOMAIN`	`276 522`	`247`	`FAD-binding FR-type.`
`NP_BIND`	`165 196`	`32`	`FMN (By similarity).`
`NP_BIND`	`316 327`	`12`	`FAD (By similarity).`
`NP_BIND`	`445 456`	`12`	`FAD (By similarity).`
`NP_BIND`	`545 563`	`19`	`NADP (By similarity).`
`NP_BIND`	`640 656`	`17`	`NADP (By similarity).`

Sequence information

Length: 693 AA [This is the length of the unprocessed precursor]

Molecular weight: 77073 Da [This is the MW of the unprocessed precursor]

CRC64: 1BEF35D4FC767674 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQLDTLDLV VLAVLLVGSV AYFTKGTYWA VAKTRMPLPA PRMNGAAKAG KTRNIIEKME 

        70         80         90        100        110        120 
ETGKNCVIFY GSQTGTAEDY ASRLAKEGSQ RFGLKTMVAD LEEYDYENLD QFPEDKVAFF 

       130        140        150        160        170        180 
VLATYGEGEP TDNAVEFYQF FTGDDVAFES ASADEKPLSK LKYVAFGLGN NTYEHYNAMV 

       190        200        210        220        230        240 
RQVDAAFQKL GPQRIGSAGE GDDGAGTMEE DFLAWKEPMW AALSESMDLE EREAVYEPVF 

       250        260        270        280        290        300 
CVTENESLSP EDETVYLGEP TQSHLQGTPK GPYSAHNPFI APIAESRELF TVKDRNCLHM 

       310        320        330        340        350        360 
EISIAGSNLS YQTGDHIAVW PTNAGAEVDR FLQVFGLEGK RDSVINIKGI DVTAKVPIPT 

       370        380        390        400        410        420 
PTTYDAAVRY YMEVCAPVSR QFVATLAAFA PMRKARQRLC VWVAQGLFPR EGHQPMLQHA 

       430        440        450        460        470        480 
QALQSITSKP FSAVPFSLLI EGITKLQPRY YSISSSSLVQ KDKISITAVV ESVRLPGASH 

       490        500        510        520        530        540 
MVKGVTTNYL LALKQKQNGR SLSRPSRLDL LHHGPRNKYD GIHVPVHVRH SNFKLPSDPS 

       550        560        570        580        590        600 
RPIIMVGPGT GVAPFRGFIQ ERAALAAKGE KVGPTVLFFG CRKSDEDFLY KDEWKTYQDQ 

       610        620        630        640        650        660 
LGDNLKIITA FSREGPQKVY VQHRLREHSE LVSDLLKQKA TFYVCGDAAN MAREVNLVLG 

       670        680        690 
QIIAAQRGLP AEKGEEMVKH MRRRGRYQED VWS

Q00141 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools