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Protein

Probable NADPH:adrenodoxin oxidoreductase, mitochondrial

Gene

arh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

2 reduced adrenodoxin + NADP+ = 2 oxidized adrenodoxin + NADPH.

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271FAD; via amide nitrogenBy similarity
Binding sitei48 – 481FADBy similarity
Binding sitei56 – 561FAD; via amide nitrogenBy similarity
Binding sitei92 – 921FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei220 – 2201NADPBy similarity
Binding sitei375 – 3751FAD; via amide nitrogenBy similarity
Binding sitei382 – 3821NADP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi164 – 1674NADPBy similarity
Nucleotide bindingi208 – 2092NADPBy similarity
Nucleotide bindingi382 – 3843FADBy similarity

GO - Molecular functioni

  • ferredoxin-NADP+ reductase activity Source: PomBase
  • flavin adenine dinucleotide binding Source: PomBase
  • NADP binding Source: PomBase
  • NADPH-adrenodoxin reductase activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiR-SPO-2395516. Electron transport from NADPH to Ferredoxin.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable NADPH:adrenodoxin oxidoreductase, mitochondrial (EC:1.18.1.6)
Short name:
AR
Short name:
Adrenodoxin reductase
Alternative name(s):
Ferredoxin--NADP(+) reductase
Short name:
Ferredoxin reductase
Gene namesi
Name:arh1
ORF Names:SPBC3B8.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3B8.01c.
PomBaseiSPBC3B8.01c. arh1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: PomBase
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionSequence analysisAdd
BLAST
Chaini39 – 469431Probable NADPH:adrenodoxin oxidoreductase, mitochondrialPRO_0000337259Add
BLAST

Proteomic databases

MaxQBiO59710.

PTM databases

SwissPalmiO59710.

Interactioni

Protein-protein interaction databases

MINTiMINT-4675583.

Structurei

3D structure databases

ProteinModelPortaliO59710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000249250.
InParanoidiO59710.
KOiK18914.
OMAiWFCHTST.
OrthoDBiEOG7HTHTK.
PhylomeDBiO59710.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59710-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRFIKRTY STQTSSPVVG IIGSGPAAFY TAHRLLRNDP NVKIDMFESR
60 70 80 90 100
PVPFGLVRYG VAPDHPEVKH VEHKFSEIAE STQFRFLGNV NVGTDVSLRD
110 120 130 140 150
LTKNYDCLVL AYGAAGDKRL GIPGEDLSGV YSAREVVGWY NSDPRNQNLE
160 170 180 190 200
LDLSQVEDAV VIGHGNVSLD VARILLSNPA QLSPTDINPL FLKSLERSNL
210 220 230 240 250
KRLHIVGRRN IFSVSFTIKE LRELFALSSA VFFAPSFNYS TKWMNETDAS
260 270 280 290 300
GLDRPRKRLL KLLVSEIQKA VSEKRVAPYS KDKKCWNLEF GLTPVEILGH
310 320 330 340 350
KGNVENVRFQ ITDSIRTDAE SKFTTIPAQL FIRSIGYKSM PLPGMKDVGV
360 370 380 390 400
PFDDAKGIVK NVNGFVRPGI YTSGWVKHGP IGVIATTMMD AFATADTITK
410 420 430 440 450
DWKSKKEFLK NSKLGWDGLK KNIKTPVIHW KDWKVIRNAE IERGLRHESL
460
SEKFRSNEDM IKLIYPGKK
Length:469
Mass (Da):52,716
Last modified:August 1, 1998 - v1
Checksum:i2AFBDBCF86C57291
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18290.1.
PIRiT40339.
RefSeqiNP_596413.1. NM_001022332.2.

Genome annotation databases

EnsemblFungiiSPBC3B8.01c.1; SPBC3B8.01c.1:pep; SPBC3B8.01c.
GeneIDi2541049.
KEGGispo:SPBC3B8.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18290.1.
PIRiT40339.
RefSeqiNP_596413.1. NM_001022332.2.

3D structure databases

ProteinModelPortaliO59710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4675583.

PTM databases

SwissPalmiO59710.

Proteomic databases

MaxQBiO59710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3B8.01c.1; SPBC3B8.01c.1:pep; SPBC3B8.01c.
GeneIDi2541049.
KEGGispo:SPBC3B8.01c.

Organism-specific databases

EuPathDBiFungiDB:SPBC3B8.01c.
PomBaseiSPBC3B8.01c. arh1.

Phylogenomic databases

HOGENOMiHOG000249250.
InParanoidiO59710.
KOiK18914.
OMAiWFCHTST.
OrthoDBiEOG7HTHTK.
PhylomeDBiO59710.

Enzyme and pathway databases

ReactomeiR-SPO-2395516. Electron transport from NADPH to Ferredoxin.

Miscellaneous databases

NextBioi20802163.
PROiO59710.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
3.50.50.60. 1 hit.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR021163. Ferredox_Rdtase_adrenod.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000362. FNR. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.
  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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADRO_SCHPO
AccessioniPrimary (citable) accession number: O59710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 1, 1998
Last modified: February 17, 2016
This is version 103 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

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 one 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.