Reviewed, UniProtKB/Swiss-Prot P36587 (NCPR_SCHPO)

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:	ccr1
ORF Names:	SPBC29A10.01, SPBC365.17

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	678 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
Cofactor	FAD. FMN.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein.
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
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Traceable author statement. Source: GeneDB_SPombe electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 678	678	NADPH--cytochrome P450 reductase		PRO_0000167609
Regions
	Transmembrane	6 – 26	21	Potential
	Domain	53 – 208	156	Flavodoxin-like
	Domain	267 – 514	248	FAD-binding FR-type
	Nucleotide binding	153 – 184	32	FMN By similarity
	Nucleotide binding	306 – 317	12	FAD By similarity
	Nucleotide binding	437 – 448	12	FAD By similarity
	Nucleotide binding	535 – 553	19	NADP By similarity
	Nucleotide binding	630 – 646	17	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P36587-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 6AEDDFBA6DE39C8F	FASTA	678	76,775
	10 20 30 40 50 60 MKTYEYVLLV IILILSLCYF IYNNFLNKPK APERRVVATD SIVELMEAEK LTAAVFFGSQ 70 80 90 100 110 120 TGTAEDFAYR FSTEAKANFN LTNMVFDLEN YDLTDLDNFD RSKLLVFFLA TYGEGEPTDN 130 140 150 160 170 180 AEAFLQLLEG DDTVFSSGKG IEDTPFEGIR YAIFGLGNHT YEYYNAMAKK VDAAMTRLGA 190 200 210 220 230 240 TRVGNLGLGD DAAGMLEEDY LQWKDDTLPE IGKLFHLQEV HKEYNPMFEV IEKPEISNTS 250 260 270 280 290 300 STVFLGEPSR QQLKGNVASK APRSQANPFF SSPVRSLELF KSGSRNCLHL ELDIADSGMR 310 320 330 340 350 360 YQTGDYASIC PMNPSQAVDD LLEVLGLKEK RDTVIIVKPI DTLDKAPVLS PTTYDTVFRY 370 380 390 400 410 420 YYEICGIVSR QLLSFIAPFA PTPESKQELE KLGNDYDYFK KNVVDLHLNL AQVLRRVSPD 430 440 450 460 470 480 APFTKLPFSM LLENMAHMKP RYYSISSSSV VHPDKVHVTA VVDKKEWTDK NHIFYGLTTN 490 500 510 520 530 540 YLLAHCRHMH GEKIPHPNGL EYTLEGPRKN WTGKIPMFVK KSTFRLAPPD VPIIMVGPGT 550 560 570 580 590 600 GVAPFRGFVM ERANLASKGV KVAKTLLFYG CQYSDKDFLY KEEWQQYKDV LKDSFELITA 610 620 630 640 650 660 FSREQDHKIY VQHRLLEHSD TIAKLVEEGA AFYICGDADH MAKDVVNALA SILTTVDVDG 670 MKAVKALRDD NRFFEDTW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structurally and functionally conserved regions of cytochrome P-450 reductase as targets for DNA amplification by the polymerase chain reaction. Cloning and nucleotide sequence of the Schizosaccharomyces pombe cDNA." Miles J.S. Biochem. J. 287:195-200(1992) [PubMed: 1417773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library." Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y. Genes Cells 5:169-190(2000) [PubMed: 10759889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 128-276. Strain: ATCC 38364 / 968.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64702 mRNA. Translation: CAA45956.1. CU329671 Genomic DNA. Translation: CAB44769.1. AB027780 Genomic DNA. Translation: BAA87084.1.
PIR	S29123. T40056.
RefSeq	NP_596046.1.
3D structure databases
HSSP	HSSP built from PDB template 1AMO based on UniProtKB P00388.
ModBase	Search...
Protein-protein interaction databases
STRING	P36587.
Genome annotation databases
GeneID	2541038.
GenomeReviews	Gene locus ccr1 in contig CU329671_GR.
KEGG	spo:SPBC29A10.01.
NMPDR	fig|4896.1.peg.1912.
Organism-specific databases
GeneDB_Spombe	SPBC29A10.01.
Phylogenomic databases
OMA	ATEIWNI.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004880-MON.
BRENDA	1.6.2.4. 653.
Gene expression databases
ArrayExpress	P36587.
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_SCHPO

Accession

Primary (citable) accession number: P36587
Secondary accession number(s): Q9USU6, Q9UU68

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)