P42974 (DHNA_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 116.
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 dehydrogenase EC=1.6.99.3 Alternative name(s): Alkyl hydroperoxide reductase | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 509 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone By similarity. |
| Catalytic activity | NADH + acceptor = NAD+ + reduced acceptor. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cell membrane; Peripheral membrane protein By similarity. |
| Sequence similarities | Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 509 | 509 | NADH dehydrogenase | PRO_0000166789 | |||||||
Regions | |||||||||||
| Nucleotide binding | 210 – 241 | 32 | FAD By similarity | ||||||||
| Nucleotide binding | 349 – 379 | 31 | NAD By similarity | ||||||||
| Nucleotide binding | 469 – 479 | 11 | FAD By similarity | ||||||||
| Region | 1 – ?183 | 183 | Membrane-binding | ||||||||
| Region | ?184 – 509 | 326 | Catalytic | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 337 ↔ 340 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 29 | 1 | G → E AA sequence Ref.4 | ||||||||
| Sequence conflict | 227 | 1 | T → D Ref.3 | ||||||||
| Sequence conflict | 393 | 1 | Y → I Ref.3 | ||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome." Kasahara Y., Nakai S., Ogasawara N. DNA Res. 4:155-159(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene." Zhang J., Aronson A.I. Gene 140:85-90(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-509. Strain: 168 / JH642. |
| [4] | "Isolation and characterization of a hydrogen peroxide resistant mutant of Bacillus subtilis." Hartford O.M., Dowds B.C.A. Microbiology 140:297-304(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-29. Strain: 168 / YB886 / BG214. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D78193 Genomic DNA. Translation: BAA11269.1. AL009126 Genomic DNA. Translation: CAB16047.1. L19710 Genomic DNA. No translation available. |
| PIR | G69583. |
| RefSeq | NP_391890.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P42974. |
| SMR | P42974. Positions 2-509. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU40100. |
PTM databases | |
| PhosSite | P0803268. |
Proteomic databases | |
| PaxDb | P42974. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB16047; CAB16047; BSU40100. |
| GeneID | 937717. |
| KEGG | bsu:BSU40100. |
| PATRIC | 18980090. VBIBacSub10457_4207. |
Organism-specific databases | |
| GenoList | BSU40100. [Micado] |
Phylogenomic databases | |
| eggNOG | COG3634. |
| HOGENOM | HOG000169462. |
| KO | K03387. |
| OMA | DQGPRFA. |
| ProtClustDB | PRK15317. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU40100-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.30.10. 2 hits. |
| InterPro | IPR012081. Alkyl_hydroperoxide_Rdtase_suF. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR002109. Glutaredoxin. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF13192. Thioredoxin_3. 1 hit. [Graphical view] |
| PIRSF | PIRSF000238. AhpF. 1 hit. |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 2 hits. |
| TIGRFAMs | TIGR03140. AhpF. 1 hit. |
| PROSITE | PS51354. GLUTAREDOXIN_2. 1 hit. PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHNA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P42974 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
