P0AFC5 (NUOA_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 45.
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 | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 147 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_01394 |
| Catalytic activity | NADH + quinone = NAD+ + quinol. HAMAP MF_01394 |
| Subunit structure | NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. |
| Subcellular location | Cell inner 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 inner membrane Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete 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 – 147 | 147 | NADH-quinone oxidoreductase subunit A HAMAP MF_01394 | PRO_0000117863 | |||||
Regions | |||||||||
| Transmembrane | 16 – 36 | 21 | Helical; Potential | ||||||
| Transmembrane | 68 – 88 | 21 | Helical; Potential | ||||||
| Transmembrane | 98 – 118 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG57417.1. BA000007 Genomic DNA. Translation: BAB36595.1. |
| PIR | D91025. |
| RefSeq | NP_288862.1. NC_002655.2. NP_311199.2. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0AFC5. |
| SMR | P0AFC5. Positions 15-126. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000023894; EBESCP00000022787; EBESCG00000022948. EBESCT00000059474; EBESCP00000057302; EBESCG00000058521. |
| GeneID | 916880. 957052. |
| GenomeReviews | Gene locus Z3547 in contig AE005174_GR. Gene locus ECs3172 in contig BA000007_GR. |
| KEGG | ece:Z3547. ecs:ECs3172. |
| PATRIC | 18355730. VBIEscCol44059_3066. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009192. |
| HOGENOM | HBG605540. |
| OMA | FIEATIF. |
| ProtClustDB | PRK06602. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS3172-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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0AFC5 Secondary accession number(s): P33597, P77159 | ||||||||
| 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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