Q2RJU7 (NUOA_MOOTA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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 A EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit A NDH-1 subunit A NUO1 | ||||
| Gene names |
| ||||
| Organism | Moorella thermoacetica (strain ATCC 39073) | ||||
| Taxonomic identifier | 264732 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Moorella group › Moorella |
Protein attributes
| Sequence length | 120 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 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 MF_01394 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01394 |
| 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. |
| Subcellular location | Cell membrane; Multi-pass membrane protein By similarity HAMAP MF_01394. |
| Sequence similarities | Belongs to the complex I subunit 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | transport Inferred 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 120 | 120 | NADH-quinone oxidoreductase subunit A HAMAP MF_01394 | PRO_5000105751 | |||||
Regions | |||||||||
| Transmembrane | 6 – 26 | 21 | Helical; Potential | ||||||
| Transmembrane | 63 – 83 | 21 | Helical; Potential | ||||||
| Transmembrane | 89 – 109 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)." Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W. Environ. Microbiol. 10:2550-2573(2008) [PubMed: 18631365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39073. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000232 Genomic DNA. Translation: ABC19292.1. |
| RefSeq | YP_429835.1. NC_007644.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2RJU7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3831253. |
| GenomeReviews | Gene locus Moth_0977 in contig CP000232_GR. |
| KEGG | mta:Moth_0977. |
| NMPDR | fig|264732.9.peg.957. |
| PATRIC | 22639128. VBIMooThe6753_1051. |
Phylogenomic databases | |
| eggNOG | COG0838. |
| HOGENOM | HBG605540. |
| OMA | GERELTY. |
| PhylomeDB | Q2RJU7. |
| ProtClustDB | CLSK943542. |
Enzyme and pathway databases | |
| BioCyc | MTHE264732:MOTH_0977-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01394. NDH1_NuoA. [Tree] |
| InterPro | IPR023043. NAD(P)H_OxRDtase_bac/plastid. IPR000440. NADH_UbQ/plastoQ_OxRdtase_su3. [Graphical view] |
| KO | K00330. |
| PANTHER | PTHR11058. Oxidored_q4. 1 hit. |
| Pfam | PF00507. Oxidored_q4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOA_MOOTA | ||||||||
| Accession | Primary (citable) accession number: Q2RJU7 | ||||||||
| 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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