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Protein

NADPH--cytochrome P450 reductase

Gene

ccr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.

Cofactori

Protein has several cofactor binding sites:

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi153 – 18432FMNPROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi306 – 31712FADBy similarityAdd
BLAST
Nucleotide bindingi437 – 44812FADBy similarityAdd
BLAST
Nucleotide bindingi535 – 55319NADPBy similarityAdd
BLAST
Nucleotide bindingi630 – 64617NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. NADPH-hemoprotein reductase activity Source: PomBase
  4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: GO_Central

GO - Biological processi

  1. ergosterol biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, FMN, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
NADPH--cytochrome P450 reductase (EC:1.6.2.4)
Short name:
CPR
Short name:
P450R
Gene namesi
Name:ccr1
ORF Names:SPBC29A10.01, SPBC365.17
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC29A10.01.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei6 – 2621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: GO_Central
  2. endoplasmic reticulum Source: PomBase
  3. endoplasmic reticulum membrane Source: PomBase
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 678678NADPH--cytochrome P450 reductasePRO_0000167609Add
BLAST

Proteomic databases

MaxQBiP36587.

Interactioni

Protein-protein interaction databases

BioGridi277553. 28 interactions.
MINTiMINT-4688783.
STRINGi4896.SPBC29A10.01-1.

Structurei

3D structure databases

ProteinModelPortaliP36587.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 208156Flavodoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini267 – 514248FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0369.
HOGENOMiHOG000282027.
InParanoidiP36587.
KOiK00327.
OMAiXINISRT.
OrthoDBiEOG744TKC.
PhylomeDBiP36587.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36587-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTYEYVLLV IILILSLCYF IYNNFLNKPK APERRVVATD SIVELMEAEK
60 70 80 90 100
LTAAVFFGSQ TGTAEDFAYR FSTEAKANFN LTNMVFDLEN YDLTDLDNFD
110 120 130 140 150
RSKLLVFFLA TYGEGEPTDN AEAFLQLLEG DDTVFSSGKG IEDTPFEGIR
160 170 180 190 200
YAIFGLGNHT YEYYNAMAKK VDAAMTRLGA TRVGNLGLGD DAAGMLEEDY
210 220 230 240 250
LQWKDDTLPE IGKLFHLQEV HKEYNPMFEV IEKPEISNTS STVFLGEPSR
260 270 280 290 300
QQLKGNVASK APRSQANPFF SSPVRSLELF KSGSRNCLHL ELDIADSGMR
310 320 330 340 350
YQTGDYASIC PMNPSQAVDD LLEVLGLKEK RDTVIIVKPI DTLDKAPVLS
360 370 380 390 400
PTTYDTVFRY YYEICGIVSR QLLSFIAPFA PTPESKQELE KLGNDYDYFK
410 420 430 440 450
KNVVDLHLNL AQVLRRVSPD APFTKLPFSM LLENMAHMKP RYYSISSSSV
460 470 480 490 500
VHPDKVHVTA VVDKKEWTDK NHIFYGLTTN YLLAHCRHMH GEKIPHPNGL
510 520 530 540 550
EYTLEGPRKN WTGKIPMFVK KSTFRLAPPD VPIIMVGPGT GVAPFRGFVM
560 570 580 590 600
ERANLASKGV KVAKTLLFYG CQYSDKDFLY KEEWQQYKDV LKDSFELITA
610 620 630 640 650
FSREQDHKIY VQHRLLEHSD TIAKLVEEGA AFYICGDADH MAKDVVNALA
660 670
SILTTVDVDG MKAVKALRDD NRFFEDTW
Length:678
Mass (Da):76,775
Last modified:June 1, 1994 - v1
Checksum:i6AEDDFBA6DE39C8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64702 mRNA. Translation: CAA45956.1.
CU329671 Genomic DNA. Translation: CAB44769.1.
AB027780 Genomic DNA. Translation: BAA87084.1.
PIRiS29123.
T40056.
RefSeqiNP_596046.1. NM_001021956.2.

Genome annotation databases

EnsemblFungiiSPBC29A10.01.1; SPBC29A10.01.1:pep; SPBC29A10.01.
GeneIDi2541038.
KEGGispo:SPBC29A10.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64702 mRNA. Translation: CAA45956.1.
CU329671 Genomic DNA. Translation: CAB44769.1.
AB027780 Genomic DNA. Translation: BAA87084.1.
PIRiS29123.
T40056.
RefSeqiNP_596046.1. NM_001021956.2.

3D structure databases

ProteinModelPortaliP36587.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277553. 28 interactions.
MINTiMINT-4688783.
STRINGi4896.SPBC29A10.01-1.

Proteomic databases

MaxQBiP36587.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC29A10.01.1; SPBC29A10.01.1:pep; SPBC29A10.01.
GeneIDi2541038.
KEGGispo:SPBC29A10.01.

Organism-specific databases

PomBaseiSPBC29A10.01.

Phylogenomic databases

eggNOGiCOG0369.
HOGENOMiHOG000282027.
InParanoidiP36587.
KOiK00327.
OMAiXINISRT.
OrthoDBiEOG744TKC.
PhylomeDBiP36587.

Miscellaneous databases

NextBioi20802152.
PROiP36587.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR023208. P450R.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000208. P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 128-276.
    Strain: ATCC 38364 / 968.

Entry informationi

Entry nameiNCPR_SCHPO
AccessioniPrimary (citable) accession number: P36587
Secondary accession number(s): Q9USU6, Q9UU68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 4, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.