Reviewed,
UniProtKB/Swiss-Prot P65575 (NUOB_MYCTU)
Last modified
June 16, 2009.
Version 28.
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 | Mycobacterium tuberculosis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 184 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 a menaquinone. 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. |
| 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 membrane; Peripheral membrane protein; Cytoplasmic side By similarity. |
| 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 |
| 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 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 – 184 | 184 | NADH-quinone oxidoreductase subunit B HAMAP MF_01356 | PRO_0000118773 | |||||
Sites | |||||||||
| Metal binding | 37 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 38 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 103 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 132 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| BX842582 Genomic DNA. Translation: CAB06270.1. AE000516 Genomic DNA. Translation: AAK47573.1. | |
| PIR | C70647. |
| RefSeq | NP_217662.1. NP_337759.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 888791. 923386. |
| GenomeReviews | Gene locus MT3234 in contig AE000516_GR. Gene locus Rv3146 in contig AL123456_GR. |
| KEGG | mtc:MT3234. mtu:Rv3146. |
| TIGR | MT3234. |
Organism-specific databases | |
| TubercuList | Rv3146. |
Phylogenomic databases | |
| HOGENOM | P65575. |
| OMA | P65575. LINWART. |
Enzyme and pathway databases | |
| BRENDA | 1.6.99.5. 809. |
Family and domain databases | |
| HAMAP | MF_01356. [Tree] |
| InterPro | IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR006138. NADH_UbQ_OxRdtase_su-20kDa. 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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65575 Secondary accession number(s): P95180 | ||||||||
| 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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