Reviewed,
UniProtKB/Swiss-Prot O59710 (ADRO_SCHPO)
Last modified
November 3, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||
| 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 | 469 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 process | Electron transport Transport |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from direct assay. Source: GeneDB_SPombe NADP or NADPH bindingInferred from direct assay. Source: GeneDB_SPombe NADPH-adrenodoxin reductase activityInferred from direct assay. Source: GeneDB_SPombe electron carrier activityInferred from electronic annotation. Source: InterPro ferredoxin-NADP+ reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 38 | 38 | Mitochondrion Potential | ||||||
| Chain | 39 – 469 | 431 | Probable NADPH:adrenodoxin oxidoreductase, mitochondrial | PRO_0000337259 | |||||
Regions | |||||||||
| Nucleotide binding | 164 – 167 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 208 – 209 | 2 | NADP By similarity | ||||||
| Nucleotide binding | 382 – 384 | 3 | FAD By similarity | ||||||
Sites | |||||||||
| Binding site | 27 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 48 | 1 | FAD By similarity | ||||||
| Binding site | 56 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 92 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 220 | 1 | NADP By similarity | ||||||
| Binding site | 375 | 1 | FAD; via amide nitrogen By similarity | ||||||
| Binding site | 382 | 1 | NADP; via amide nitrogen By similarity | ||||||
Sequences
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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. 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. | |
| PIR | T40339. |
| RefSeq | NP_596413.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LQT based on UniProtKB O05783. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O59710. |
Genome annotation databases | |
| GeneID | 2541049. |
| GenomeReviews | Gene locus arh1 in contig CU329671_GR. |
| KEGG | spo:SPBC3B8.01c. |
| NMPDR | fig|4896.1.peg.2279. |
Organism-specific databases | |
| GeneDB_Spombe | SPBC3B8.01c. |
Phylogenomic databases | |
| OMA | YHAVLLT. |
Gene expression databases | |
| ArrayExpress | O59710. |
Family and domain databases | |
| InterPro | IPR000759. Adrndx_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. [Graphical view] |
| Pfam | PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00419. ADXRDTASE. |
| ProtoNet | Search... |
Entry information
| Entry name | ADRO_SCHPO | ||||||||
| Accession | Primary (citable) accession number: O59710 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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