P57253 (NUOB_BUCAI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 76.
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-quinone oxidoreductase subunit B EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit B NDH-1 subunit B | ||||
| Gene names |
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| Organism | Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 107806 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › ![]() |
Protein attributes
| Sequence length | 224 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. HAMAP-Rule MF_01356 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01356 |
| Cofactor | Binds 1 4Fe-4S cluster By similarity. HAMAP-Rule MF_01356 |
| Subunit structure | NDH-1 is composed of 13 different subunits. Subunits NuoB, CD, E, F, and G constitute the peripheral sector of the complex By similarity. |
| Subcellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP-Rule MF_01356. |
| Sequence similarities | Belongs to the complex I 20 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell membrane Membrane |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: HAMAP quinone 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 224 | 224 | NADH-quinone oxidoreductase subunit B HAMAP-Rule MF_01356 | PRO_0000118769 | |||||
Sites | |||||||||
| Metal binding | 67 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 68 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 133 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 162 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000003 Genomic DNA. Translation: BAB12873.1. |
| RefSeq | NP_239987.1. NC_002528.1. |
3D structure databases | |
| ProteinModelPortal | P57253. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB12873; BAB12873; BAB12873. |
| GeneID | 1109599. |
| KEGG | buc:BU155. |
| PATRIC | 21243826. VBIBucAph127364_0165. |
Phylogenomic databases | |
| eggNOG | COG0377. |
| HOGENOM | HOG000228249. |
| KO | K00331. |
| OMA | PRPEAYI. |
| ProtClustDB | PRK06411. |
Enzyme and pathway databases | |
| BioCyc | BAPH107806:GBZJ-155-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.700. 1 hit. |
| HAMAP | MF_01356. NDH1_NuoB. |
| InterPro | IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view] |
| PANTHER | PTHR11995. PTHR11995. 1 hit. |
| Pfam | PF01058. Oxidored_q6. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01957. nuoB_fam. 1 hit. |
| PROSITE | PS01150. COMPLEX1_20K. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOB_BUCAI | ||||||||
| Accession | Primary (citable) accession number: P57253 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Buchnera aphidicola (subsp. Acyrthosiphon pisum) Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
