Reviewed,
UniProtKB/Swiss-Prot B0BZW2 (NU1C_ACAM1)
Last modified
June 16, 2009.
Version 10.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NAD(P)H-quinone oxidoreductase subunit 1 EC=1.6.5.- Alternative name(s): NAD(P)H dehydrogenase I subunit 1 NDH-1 subunit 1 NDH-A | ||||
| Gene names |
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| Organism | Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 329726 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Acaryochloris |
Protein attributes
| Sequence length | 372 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 an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient By similarity. |
| Catalytic activity | NAD(P)H + plastoquinone = NAD(P)+ + plastoquinol. HAMAP MF_01350 |
| Subunit structure | NDH-1 is composed of at least 11 different subunits By similarity. |
| Subcellular location | Cellular thylakoid membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the complex I subunit 1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Thylakoid |
| Domain | Transmembrane |
| Ligand | NAD NADP Plastoquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: HAMAP |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW thylakoid membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | oxidoreductase activity Inferred 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 – 372 | 372 | NAD(P)H-quinone oxidoreductase subunit 1 HAMAP MF_01350 | PRO_1000086932 | |||||
Regions | |||||||||
| Transmembrane | 27 – 47 | 21 | Potential | ||||||
| Transmembrane | 65 – 85 | 21 | Potential | ||||||
| Transmembrane | 97 – 117 | 21 | Potential | ||||||
| Transmembrane | 128 – 148 | 21 | Potential | ||||||
| Transmembrane | 176 – 196 | 21 | Potential | ||||||
| Transmembrane | 204 – 224 | 21 | Potential | ||||||
| Transmembrane | 249 – 269 | 21 | Potential | ||||||
| Transmembrane | 308 – 328 | 21 | Potential | ||||||
| Transmembrane | 351 – 371 | 21 | Potential | ||||||
Sequences
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References
| [1] | "Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. Touchman J.W.Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000828 Genomic DNA. Translation: ABW27172.1. | |
| RefSeq | YP_001516486.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5680972. |
| GenomeReviews | Gene locus AM1_2158 in contig CP000828_GR. |
| KEGG | amr:AM1_2158. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | B0BZW2. LYLGGWE. |
Family and domain databases | |
| HAMAP | MF_01350. [Tree] |
| InterPro | IPR001694. NADH_UbQ_OxRdtase_su1. IPR018086. NADH_UbQ_OxRdtase_su1_CS. [Graphical view] |
| PANTHER | PTHR11432. Resp_NADH_DH_1. 1 hit. |
| Pfam | PF00146. NADHdh. 1 hit. [Graphical view] |
| PROSITE | PS00667. COMPLEX1_ND1_1. 1 hit. PS00668. COMPLEX1_ND1_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NU1C_ACAM1 | ||||||||
| Accession | Primary (citable) accession number: B0BZW2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


