Reviewed,
UniProtKB/Swiss-Prot Q72GC9 (NUOB_THET2)
Last modified
February 9, 2010.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names 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 | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 262724 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 181 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. |
| Subunit structure | NDH-1 is composed of 14 different subunits. Subunits nuoB, C, D, 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. |
| Sequence similarities | Belongs to the complex I 20 kDa subunit family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reactionInferred from electronic annotation. Source: HAMAP |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 181 | 181 | NADH-quinone oxidoreductase subunit B | PRO_0000358501 | |||||
Sites | |||||||||
| Metal binding | 45 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 46 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 111 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 140 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017221 Genomic DNA. Translation: AAS82261.1. |
| RefSeq | YP_005888.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 2FUG based on UniProtKB Q56218. |
| SMR | Q72GC9. Positions 15-175. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q72GC9. |
Genome annotation databases | |
| GeneID | 2775039. |
| GenomeReviews | Gene locus TT_C1919 in contig AE017221_GR. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0377. |
| HOGENOM | HBG553221. |
| OMA | TDELINW. |
| PhylomeDB | Q72GC9. |
Enzyme and pathway databases | |
| BioCyc | TTHE262724:TT_C1919-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01356. NDH1_NuoB. [Tree] |
| InterPro | IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_20kDa_su. IPR014406. NiFe_hyd_3_ssu/Q_oxred_NuoB. [Graphical view] |
| PANTHER | PTHR11995:SF2. NADH_DH_20kDa. 1 hit. 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_THET2 | ||||||||
| Accession | Primary (citable) accession number: Q72GC9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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