Reviewed, UniProtKB/Swiss-Prot Q00141 (NCPR_ASPNG)

Names and origin

Protein names

Recommended name:
    NADPH--cytochrome P450 reductase
      Short name=CPR
      Short name=P450R
    EC=1.6.2.4

Gene names

Name:

cprA

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1 Ref.2
Catalytic activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein. Ref.1
Cofactor	FAD. Ref.1 Ref.2 FMN. Ref.1 Ref.2
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. UniProtKB P50126
Induction	By benzoic acid (BA). Ref.1
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. UniProtKB P50126 Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Ref.1 Inferred from direct assay. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 693	693	NADPH--cytochrome P450 reductase		PRO_0000167604
Regions
	Transmembrane	9 – 31	23	Potential
	Domain	66 – 220	155	Flavodoxin-like
	Domain	276 – 522	247	FAD-binding FR-type
	Nucleotide binding	165 – 196	32	FMN By similarity UniProtKB P50126
	Nucleotide binding	316 – 327	12	FAD By similarity UniProtKB P50126
	Nucleotide binding	445 – 456	12	FAD By similarity UniProtKB P50126
	Nucleotide binding	545 – 563	19	NADP By similarity UniProtKB P50126
	Nucleotide binding	640 – 656	17	NADP By similarity UniProtKB P50126

Sequences

	Sequence		Length	Mass (Da)
	Q00141-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1BEF35D4FC767674	FASTA	693	77,073
	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

References

[1]

"Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger." 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. DNA Cell Biol. 14:719-729(1995) [PubMed: 7646819] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY. Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

[2]

"Purification and characterization of benzoate-para-hydroxylase, a cytochrome P450 (CYP53A1), from Aspergillus niger." Faber B.W., van Gorcom R.F.M., Duine J.A. Arch. Biochem. Biophys. 394:245-254(2001) [PubMed: 11594739] [Abstract] Cited for: CHARACTERIZATION. Strain: T18.5.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z26938 Genomic DNA. Translation: CAA81550.1.
PIR	S38427.
3D structure databases
HSSP	HSSP built from PDB template 1B1C based on UniProtKB P16435.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.2.4. 277.
Family and domain databases
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR015702. NADPH_Cyt_P450_Rdtase. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
PANTHER	PTHR19384:SF17. NADPH_Cyt_Red. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NCPR_ASPNG

Accession

Primary (citable) accession number: Q00141

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)