Reviewed,
UniProtKB/Swiss-Prot P0A6J5 (DADA_ECOLI)
Last modified
November 3, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: D-amino acid dehydrogenase small subunit EC=1.4.99.1 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 432 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Oxidative deamination of D-amino acids. HAMAP MF_01202 |
| Catalytic activity | A D-amino acid + H2O + acceptor = a 2-oxo acid + NH3 + reduced acceptor. HAMAP MF_01202 |
| Cofactor | FAD. HAMAP MF_01202 Nonheme iron. HAMAP MF_01202 |
| Pathway | Amino-acid degradation; D-alanine degradation; NH(3) and pyruvate from D-alanine: step 1/1. HAMAP MF_01202 |
| Subunit structure | Heterodimer of a small and a large subunit. HAMAP MF_01202 |
| Subcellular location | Cell inner membrane; Peripheral membrane protein. HAMAP MF_01202 |
| Induction | By alanine. HAMAP MF_01202 |
| Sequence similarities | Belongs to the dadA oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Ligand | FAD Flavoprotein Iron |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine catabolic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | D-amino-acid dehydrogenase activity Inferred from electronic annotation. Source: HAMAP iron ion 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 – 432 | 432 | D-amino acid dehydrogenase small subunit HAMAP MF_01202 | PRO_0000166131 | ||||
Regions | ||||||||
| Nucleotide binding | 3 – 17 | 15 | FAD Potential | |||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Organization and expression of the Escherichia coli K-12 dad operon encoding the smaller subunit of D-amino acid dehydrogenase and the catabolic alanine racemase." Lobocka M., Hennig J., Wild J., Klopotowski T. J. Bacteriol. 176:1500-1510(1994) [PubMed: 7906689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T.DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [3] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
Cross-references
Sequence databases | |
|---|---|
| L02948 Unassigned DNA. Translation: AAC36880.1. U00096 Genomic DNA. Translation: AAC74273.1. AP009048 Genomic DNA. Translation: BAA36044.1. | |
| PIR | B53383. |
| RefSeq | AP_001814.1. NP_415707.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P0A6J5. |
Genome annotation databases | |
| GeneID | 945752. |
| GenomeReviews | Gene locus JW1178 in contig AP009048_GR. Gene locus b1189 in contig U00096_GR. |
| KEGG | ecj:JW1178. eco:b1189. |
Organism-specific databases | |
| EchoBASE | EB1379. |
| EcoGene | EG11407. dadA. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A6J5. |
| OMA | MFQKHAP. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:DALADEHYDROGA-MON. MetaCyc:DALADEHYDROGA-MON. |
Gene expression databases | |
| Genevestigator | P0A6J5. |
Family and domain databases | |
| HAMAP | MF_01202. [Tree] |
| InterPro | IPR006076. FAD-dep_OxRdtase. [Graphical view] |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | DADA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P0A6J5 Secondary accession number(s): P29011 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


