A0R4S7 (ACDH2_MYCS2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 52.
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 2 EC=1.2.1.10 Alternative name(s): Acetaldehyde dehydrogenase [acetylating] 2 | ||||
| Gene names |
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| Organism | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 246196 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › ![]() |
Protein attributes
| Sequence length | 307 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. |
| Sequence caution | The sequence ABK73662.1 differs from that shown. Reason: Erroneous initiation. |
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 – 307 | 307 | Acetaldehyde dehydrogenase 2 HAMAP-Rule MF_01657 | PRO_0000387681 | |||||
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] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [2] | "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
| [3] | "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000480 Genomic DNA. Translation: ABK73662.1. Different initiation. CP001663 Genomic DNA. Translation: AFP42212.1. |
| RefSeq | YP_006570507.1. NC_018289.1. YP_890165.1. NC_008596.1. |
3D structure databases | |
| ProteinModelPortal | A0R4S7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 246196.MSMEG_5939. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK73662; ABK73662; MSMEG_5939. |
| GeneID | 13427109. 4531880. |
| KEGG | msg:MSMEI_5779. msm:MSMEG_5939. |
| PATRIC | 18084117. VBIMycSme59918_5778. |
Phylogenomic databases | |
| eggNOG | COG4569. |
| HOGENOM | HOG000052149. |
| KO | K04073. |
| ProtClustDB | PRK08300. |
Enzyme and pathway databases | |
| BioCyc | MSME246196:GJ4Y-5938-MONOMER. |
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 | ACDH2_MYCS2 | ||||||||
| Accession | Primary (citable) accession number: A0R4S7 Secondary accession number(s): I7G9C0 | ||||||||
| 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 |

Clusters with
