P0AFC8 (NUOB_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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 NUO2 | ||||
| Gene names |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 220 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. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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 MF_01356 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01356 |
| Cofactor | Binds 1 4Fe-4S cluster By similarity. HAMAP 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 inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_01356. |
| Sequence similarities | Belongs to the complex I 20 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | transport Inferred 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 metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 220 | 220 | NADH-quinone oxidoreductase subunit B HAMAP MF_01356 | PRO_0000118767 | |||||
Sites | |||||||||
| Metal binding | 63 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 64 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 129 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 158 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN81282.1. |
| RefSeq | NP_754714.1. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | P0AFC8. |
| SMR | P0AFC8. Positions 34-181. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000041790; EBESCP00000040139; EBESCG00000040840. |
| GeneID | 1038369. |
| GenomeReviews | Gene locus c2828 in contig AE014075_GR. |
| KEGG | ecc:c2828. |
| PATRIC | 18283518. VBIEscCol75197_2666. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009829. |
| HOGENOM | HBG553221. |
| OMA | PRPEAYI. |
| PhylomeDB | P0AFC8. |
| ProtClustDB | PRK06411. |
Family and domain databases | |
| HAMAP | MF_01356. NDH1_NuoB. [Tree] |
| InterPro | IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UQ_OxRdtase_20Kd_su. IPR014406. NiFe-hyd_3_ssu/Q_oxred_NuoB. [Graphical view] |
| Gene3D | G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit. |
| KO | K00331. |
| PANTHER | PTHR11995. NiFe_hyd_3_ssu/Q_oxred_NuoB. 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_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0AFC8 Secondary accession number(s): P33598 P78187 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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