B2HGE8 (B2HGE8_MYCMM) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 32.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit A HAMAP-Rule MF_01394 EC=1.6.99.5 HAMAP-Rule MF_01394 Alternative name(s): NADH dehydrogenase I subunit A HAMAP-Rule MF_01394 NDH-1 subunit A HAMAP-Rule MF_01394 NUO1 HAMAP-Rule MF_01394 | ||||
| Gene names |
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| Organism | Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] EMBL ACC39934.1 | ||||
| Taxonomic identifier | 216594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 162 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 By similarity. RuleBase RU003639 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. HAMAP-Rule MF_01394 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01394 RuleBase RU003639 |
| Subunit structure | NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. HAMAP-Rule MF_01394 |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01394. Membrane; Multi-pass membrane protein By similarity RuleBase RU003639. |
| Sequence similarities | Belongs to the complex I subunit 3 family. HAMAP-Rule MF_01394 RuleBase RU003639 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport HAMAP-Rule MF_01394 |
| Cellular component | Cell inner membrane HAMAP-Rule MF_01394 Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix HAMAP-Rule MF_01394 |
| Ligand | NAD HAMAP-Rule MF_01394 RuleBase RU003639 Ubiquinone EMBL ACC39934.1 |
| Molecular function | Oxidoreductase HAMAP-Rule MF_01394 RuleBase RU003639 |
| PTM | Quinone HAMAP-Rule MF_01394 RuleBase RU003639 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro quinone bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transmembrane | 40 – 60 | 21 | Helical; By similarity HAMAP-Rule MF_01394 | ||||||
| Transmembrane | 106 – 126 | 21 | Helical; By similarity HAMAP-Rule MF_01394 | ||||||
| Transmembrane | 134 – 154 | 21 | Helical; By similarity HAMAP-Rule MF_01394 | ||||||
Sequences
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References
| [1] | "Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T.Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000854 Genomic DNA. Translation: ACC39934.1. |
| RefSeq | YP_001849789.1. NC_010612.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 216594.MMAR_1483. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACC39934; ACC39934; MMAR_1483. |
| GeneID | 6225738. |
| KEGG | mmi:MMAR_1483. |
| PATRIC | 18063787. VBIMycMar75906_1581. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0838. |
| HOGENOM | HOG000100120. |
| KO | K00330. |
| OMA | IGMFGFW. |
| ProtClustDB | PRK07928. |
Enzyme and pathway databases | |
| BioCyc | MMAR216594:GJOB-1489-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01394. NDH1_NuoA. |
| InterPro | IPR023043. NAD(P)H_OxRDtase_bac/plastid. IPR000440. NADH_UbQ/plastoQ_OxRdtase_su3. [Graphical view] |
| PANTHER | PTHR11058. PTHR11058. 1 hit. |
| Pfam | PF00507. Oxidored_q4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | B2HGE8_MYCMM | ||||||||
| Accession | Primary (citable) accession number: B2HGE8 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
