NADPH--cytochrome P450 reductase

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Q00141 (NCPR_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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	694 AA.
Sequence status	Complete.
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. Involved in ergosterol biosynthesis. Ref.1 Ref.2
Catalytic activity	NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein. Ref.1 Ref.2
Cofactor	FAD. Ref.1 Ref.2 FMN. Ref.1 Ref.2
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Cell membrane; Single-pass membrane protein By similarity. Microsome 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.
Sequence caution	The sequence CAA81550.1 differs from that shown. Reason: Frameshift at positions 34, 43, 392, 405, 421, 501 and 515.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Cell membrane Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane Transmembrane helix
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular membrane-bounded organelle Inferred from direct assay Ref.2. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from direct assay Ref.1. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 694

694

NADPH--cytochrome P450 reductase

PRO_0000167604

Regions

Transmembrane

9 – 31

Helical; Potential

Domain

66 – 220

155

Flavodoxin-like

Domain

276 – 537

262

FAD-binding FR-type

Nucleotide binding

72 – 76

FMN By similarity

Nucleotide binding

165 – 196

FMN By similarity UniProtKB P50126

Nucleotide binding

316 – 327

FAD By similarity UniProtKB P50126

Nucleotide binding

446 – 457

FAD By similarity

Nucleotide binding

546 – 564

NADP By similarity

Nucleotide binding

641 – 657

NADP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q00141 [UniParc].

Last modified February 8, 2011. Version 2.
Checksum: BA3E7867ACB1D810
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FASTA

694

76,807

        10         20         30         40         50         60 
MAQLDTLDLV VLAVLLVGSV AYFTKGTYWA VAKDPYASTG PAMNGAAKAG 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 PDEESKAEIV RLGSHKDYFH EKVTNQCFNM 

       430        440        450        460        470        480 
AQALQSITSK PFSAVPFSLL IEGITKLQPR YYSISSSSLV QKDKISITAV VESVRLPGAS 

       490        500        510        520        530        540 
HMVKGVTTNY LLALKQKQNG DPSPDPHGLT YSITGPRNKY DGIHVPVHVR HSNFKLPSDP 

       550        560        570        580        590        600 
SRPIIMVGPG TGVAPFRGFI QERAALAAKG EKVGPTVLFF GCRKSDEDFL YKDEWKTYQD 

       610        620        630        640        650        660 
QLGDNLKIIT AFSREGPQKV YVQHRLREHS ELVSDLLKQK ATFYVCGDAA NMAREVNLVL 

       670        680        690 
GQIIAAQRGL PAEKGEEMVK HMRRRGRYQE DVWS

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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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, INDUCTION.
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] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
Strain: T18.5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z26938 Genomic DNA. Translation: CAA81550.1. Frameshift.
PIR	S38427.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG0369.
Family and domain databases
Gene3D	1.20.990.10. 1 hit.
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR001433. OxRdtase_FAD/NAD-bd. IPR023208. P450R. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF000208. P450R. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
SUPFAM	SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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:	February 8, 2011
Last modified:	April 3, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents