Q92406 (NDUV1_ASPNG) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial EC=1.6.5.3 EC=1.6.99.3 Alternative name(s): Complex I-51kD Short name=CI-51kD | ||
| Gene names |
| ||
| Organism | Aspergillus niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 496 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone By similarity. |
| Catalytic activity | NADH + ubiquinone = NAD+ + ubiquinol. NADH + acceptor = NAD+ + reduced acceptor. |
| Cofactor | Binds 1 FMN Potential. Binds 1 4Fe-4S cluster Potential. |
| Subunit structure | Complex I is composed of about 40 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme By similarity. |
| Subcellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. |
| Sequence similarities | Belongs to the complex I 51 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Respiratory chain Transport |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide |
| Ligand | 4Fe-4S FMN Flavoprotein Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chainInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FMN bindingInferred from electronic annotation. Source: InterPro NAD bindingInferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 30 | 30 | Mitochondrion By similarity | ||||||
| Chain | 31 – 496 | 466 | NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial | PRO_0000019979 | |||||
Regions | |||||||||
| Nucleotide binding | 98 – 107 | 10 | NAD By similarity | ||||||
| Nucleotide binding | 214 – 261 | 48 | FMN By similarity | ||||||
Sites | |||||||||
| Metal binding | 393 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 396 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 399 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 439 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "The role of the proton-pumping and alternative respiratory chain NADH:ubiquinone oxidoreductases in overflow catabolism of Aspergillus niger." Proemper C., Schneider R., Weiss H. Eur. J. Biochem. 216:223-230(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FGSC 732. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X64402 Genomic DNA. Translation: CAA45744.1. |
3D structure databases | |
| ProteinModelPortal | Q92406. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | COG1894. |
Family and domain databases | |
| InterPro | IPR001949. NADH-UbQ_OxRdtase_51kDa_CS. IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd. IPR011537. NADH-UbQ_OxRdtase_suF. IPR011538. NADH_UbQ_OxRdtase_51kDa_su. IPR019554. Soluble_ligand-bd. [Graphical view] |
| Pfam | PF01512. Complex1_51K. 1 hit. PF10589. NADH_4Fe-4S. 1 hit. PF10531. SLBB. 1 hit. [Graphical view] |
| SMART | SM00928. NADH_4Fe-4S. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01959. nuoF_fam. 1 hit. |
| PROSITE | PS00644. COMPLEX1_51K_1. 1 hit. PS00645. COMPLEX1_51K_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NDUV1_ASPNG | ||||||||
| Accession | Primary (citable) accession number: Q92406 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
