A2QS05 (NCPR_ASPNC) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	An08g07840

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
Cofactor	FAD By similarity. FMN By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Cell membrane; Single-pass membrane protein By similarity. Microsome By similarity.
Sequence similarities	In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

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
Technical term	Complete proteome
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 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 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 – 695	695	NADPH--cytochrome P450 reductase		PRO_5000220324
Regions
	Transmembrane	9 – 31	23	Helical; Potential
	Domain	66 – 221	156	Flavodoxin-like
	Domain	277 – 538	262	FAD-binding FR-type
	Nucleotide binding	72 – 76	5	FMN By similarity
	Nucleotide binding	166 – 197	32	FMN By similarity
	Nucleotide binding	317 – 328	12	FAD By similarity
	Nucleotide binding	447 – 458	12	FAD By similarity
	Nucleotide binding	547 – 565	19	NADP By similarity
	Nucleotide binding	642 – 658	17	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2QS05 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 835324930A8A62F3	FASTA	695	76,589
	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 GASADEKPLS KLKYVAFGLG NNTYEHYNAM 190 200 210 220 230 240 VRQVDAAFQK LGAQRIGSAG EGDDGAGTME EDFLAWKEPM WAALSESMDL QEREAVYEPV 250 260 270 280 290 300 FCVTENESLS PEDETVYLGE PTQSHLQGTP KGPYSAHNPF IAPIAESREL FTVKDRNCLH 310 320 330 340 350 360 MEISIAGSNL SYQTGDHIAV WPTNAGAEVD RFLQVFGLEG KRDSVINIKG IDVTAKVPIP 370 380 390 400 410 420 TPTTYDAAVR YYMEVCAPVS RQFVATLAAF APDEESKAEI VRLGSDKDYF HEKVTNQCFN 430 440 450 460 470 480 IAQALQSITS KPFSAVPFSL LIEGITKLQP RYYSISSSSL VQKDKISITA VVESVRLPGA 490 500 510 520 530 540 SHMVKGVTTN YLLALKQKQN GDPSPDPHGL TYSITGPRNK YDGIHVPVHV RHSNFKLPSD 550 560 570 580 590 600 PSRPIIMVGP GTGVAPFRGF IQERAALAAK GEKVGPTVLF FGCRKSDEDF LYKDEWKTYQ 610 620 630 640 650 660 DQLGDNLKII TAFSREGPQK VYVQHRLREH SELVSDLLKQ KATFYVCGDA ANMAREVNLV 670 680 690 LGQIIAAQRG LPAEKGEEMV KHMRSSGSYQ EDVWS

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270176 Genomic DNA. Translation: CAK45677.1.
RefSeq	XP_001392901.1. XM_001392864.2.
3D structure databases
ProteinModelPortal	A2QS05.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00006979.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00007108; CADANGAP00006979; CADANGAG00007108.
GeneID	4983103.
KEGG	ang:ANI_1_1104074.
Phylogenomic databases
HOGENOM	HOG000282027.
KO	K00327.
OrthoDB	EOG47SWP5.
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_ASPNC

Accession

Primary (citable) accession number: A2QS05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program