P71866 (ACDH_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
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: Acetaldehyde dehydrogenase EC=1.2.1.10 Alternative name(s): Acetaldehyde dehydrogenase [acetylating] | ||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 1773 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex![]() |
Protein attributes
| Sequence length | 303 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds By similarity. HAMAP-Rule MF_01657 |
| Catalytic activity | Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657 |
| Sequence similarities | Belongs to the acetaldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP cellular amino acid metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular_function | NAD binding Inferred from electronic annotation. Source: HAMAP acetaldehyde dehydrogenase (acetylating) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 303 | 303 | Acetaldehyde dehydrogenase HAMAP-Rule MF_01657 | PRO_0000387688 | |||||
Regions | |||||||||
| Nucleotide binding | 12 – 15 | 4 | NAD By similarity | ||||||
| Nucleotide binding | 158 – 166 | 9 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 127 | 1 | Acyl-thioester intermediate By similarity | ||||||
| Binding site | 277 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842583 Genomic DNA. Translation: CAB05043.1. AE000516 Genomic DNA. Translation: AAK47998.1. AL123456 Genomic DNA. Translation: CCP46357.1. |
| PIR | H70675. |
| RefSeq | NP_218052.1. NC_000962.3. NP_338184.1. NC_002755.2. YP_006517024.1. NC_018143.1. |
3D structure databases | |
| ProteinModelPortal | P71866. |
| SMR | P71866. Positions 4-297. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 83332.Rv3535c. |
Proteomic databases | |
| PRIDE | P71866. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAK47998; AAK47998; MT3639. |
| GeneID | 13317143. 888396. 926564. |
| KEGG | mtc:MT3639. mtu:Rv3535c. mtv:RVBD_3535c. |
| PATRIC | 18129762. VBIMycTub22151_3976. |
Organism-specific databases | |
| TubercuList | Rv3535c. |
Phylogenomic databases | |
| eggNOG | COG4569. |
| HOGENOM | HOG000052149. |
| KO | K04073. |
| OMA | TSAYVHK. |
| ProtClustDB | PRK08300. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-16959. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| HAMAP | MF_01657. Ac_ald_DH_ac. |
| InterPro | IPR003361. Acetaldehyde_dehydrogenase. IPR015426. Acetylaldehyde_DH_C. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. [Graphical view] |
| PANTHER | PTHR21123. PTHR21123. 1 hit. |
| Pfam | PF09290. AcetDehyd-dimer. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view] |
| PIRSF | PIRSF015689. Actaldh_dh_actl. 1 hit. |
| SMART | SM00859. Semialdhyde_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03215. ac_ald_DH_ac. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ACDH_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P71866 Secondary accession number(s): L0TEF0, Q7D5C3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
