Reviewed,
UniProtKB/Swiss-Prot A3LT66 (MCR1_PICST)
Last modified
January 19, 2010.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADH-cytochrome b5 reductase 2 EC=1.6.2.2 Alternative name(s): Mitochondrial cytochrome b reductase | ||||
| Gene names |
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| Organism | Pichia stipitis (Yeast) [Complete proteome] | ||||
| Taxonomic identifier | 4924 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia |
Protein attributes
| Sequence length | 298 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | May mediate the reduction of outer membrane cytochrome b5 By similarity. |
| Catalytic activity | NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5. |
| Cofactor | FAD By similarity. |
| Subcellular location | Mitochondrion outer membrane; Single-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion Mitochondrion outer membrane |
| Domain | Transmembrane |
| Ligand | FAD Flavoprotein NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis." Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M. Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000498 Genomic DNA. Translation: ABN66017.2. |
| RefSeq | XP_001384046.2. |
3D structure databases | |
| SMR | A3LT66. Positions 49-298. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A3LT66. |
Genome annotation databases | |
| GeneID | 4838868. |
| GenomeReviews | Gene locus MCR1 in contig CP000498_GR. |
| KEGG | pic:PICST_44816. |
Phylogenomic databases | |
| eggNOG | fuNOG07850. |
| HOGENOM | HBG591994. |
| OMA | PVASCIT. |
| OrthoDB | EOG9TB5TC. |
Family and domain databases | |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view] |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00406. CYTB5RDTASE. PR00371. FPNCR. |
| PROSITE | PS51384. FAD_FR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MCR1_PICST | ||||||||
| Accession | Primary (citable) accession number: A3LT66 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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