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Reviewed, UniProtKB/Swiss-Prot O59710 (ADRO_SCHPO)

Last modified November 3, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
      Short name=Adrenodoxin reductase
      Short name=AR
    EC=1.18.1.2
Alternative name(s):
    Ferredoxin--NADP(+) reductase
      Short name=Ferredoxin reductase
Gene names
Name: arh1
ORF Names: SPBC3B8.01c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Serves as the first electron transfer protein in all the mitochondrial P450 systems By similarity.

Catalytic activity

2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.

Cofactor

FAD By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the ferredoxin--NADP reductase type 1 family.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from direct assay. Source: GeneDB_SPombe

NADP or NADPH binding

Inferred from direct assay. Source: GeneDB_SPombe

NADPH-adrenodoxin reductase activity

Inferred from direct assay. Source: GeneDB_SPombe

electron carrier activity

Inferred from electronic annotation. Source: InterPro

ferredoxin-NADP+ reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion Potential
Chain39 – 469431Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
PRO_0000337259

Regions

Nucleotide binding164 – 1674NADP By similarity
Nucleotide binding208 – 2092NADP By similarity
Nucleotide binding382 – 3843FAD By similarity

Sites

Binding site271FAD; via amide nitrogen By similarity
Binding site481FAD By similarity
Binding site561FAD; via amide nitrogen By similarity
Binding site921FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2201NADP By similarity
Binding site3751FAD; via amide nitrogen By similarity
Binding site3821NADP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O59710-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 2AFBDBCF86C57291

FASTA46952,716
        10         20         30         40         50         60 
MLSRFIKRTY STQTSSPVVG IIGSGPAAFY TAHRLLRNDP NVKIDMFESR PVPFGLVRYG 

        70         80         90        100        110        120 
VAPDHPEVKH VEHKFSEIAE STQFRFLGNV NVGTDVSLRD LTKNYDCLVL AYGAAGDKRL 

       130        140        150        160        170        180 
GIPGEDLSGV YSAREVVGWY NSDPRNQNLE LDLSQVEDAV VIGHGNVSLD VARILLSNPA 

       190        200        210        220        230        240 
QLSPTDINPL FLKSLERSNL KRLHIVGRRN IFSVSFTIKE LRELFALSSA VFFAPSFNYS 

       250        260        270        280        290        300 
TKWMNETDAS GLDRPRKRLL KLLVSEIQKA VSEKRVAPYS KDKKCWNLEF GLTPVEILGH 

       310        320        330        340        350        360 
KGNVENVRFQ ITDSIRTDAE SKFTTIPAQL FIRSIGYKSM PLPGMKDVGV PFDDAKGIVK 

       370        380        390        400        410        420 
NVNGFVRPGI YTSGWVKHGP IGVIATTMMD AFATADTITK DWKSKKEFLK NSKLGWDGLK 

       430        440        450        460 
KNIKTPVIHW KDWKVIRNAE IERGLRHESL SEKFRSNEDM IKLIYPGKK 

« Hide

References

[1]"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. expand/collapse author list , 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.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAA18290.1.
PIRT40339.
RefSeqNP_596413.1.

3D structure databases

HSSPHSSP built from PDB template 1LQT based on UniProtKB O05783.
ModBaseSearch...

Protein-protein interaction databases

STRINGO59710.

Genome annotation databases

GeneID2541049.
GenomeReviewsGene locus arh1 in contig CU329671_GR.
KEGGspo:SPBC3B8.01c.
NMPDRfig|4896.1.peg.2279.

Organism-specific databases

GeneDB_SpombeSPBC3B8.01c.

Phylogenomic databases

OMAYHAVLLT.

Gene expression databases

ArrayExpressO59710.

Family and domain databases

InterProIPR000759. Adrndx_reductase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]
PfamPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00419. ADXRDTASE.
ProtoNetSearch...

Entry information

Entry nameADRO_SCHPO
AccessionPrimary (citable) accession number: O59710
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents