Reviewed,
UniProtKB/Swiss-Prot P25405 (ADH1A_UROHA)
Last modified
September 2, 2008.
Version 53.
History...
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90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase 1A EC=1.1.1.1 Alternative name(s): Alcohol dehydrogenase I-A Short name=ADH IA |
| Organism | Uromastyx hardwickii (Indian spiny-tailed lizard) |
| Taxonomic identifier | 40250 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Iguania › Acrodonta › Agamidae › Uromastycinae › Uromastyx |
Protein attributes
| Sequence length | 375 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | An alcohol + NAD(+) = an aldehyde or ketone + NADH. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subunit structure | Multimeric (with different ratios of monomers). |
| Subcellular location | |
| Miscellaneous | In U.hardwickii there are two isozymes of alcohol dehydrogenase I. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| None. [Check GOA] | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 375 | 375 | Alcohol dehydrogenase 1A | |||||
Sites | ||||||||
| Metal binding | 46 | 1 | Zinc 1; catalytic By similarity | |||||
| Metal binding | 67 | 1 | Zinc 1; catalytic By similarity | |||||
| Metal binding | 97 | 1 | Zinc 2 By similarity | |||||
| Metal binding | 100 | 1 | Zinc 2 By similarity | |||||
| Metal binding | 103 | 1 | Zinc 2 By similarity | |||||
| Metal binding | 111 | 1 | Zinc 2 By similarity | |||||
| Metal binding | 174 | 1 | Zinc 1; catalytic By similarity | |||||
Amino acid modifications | ||||||||
| Modified residue | 1 | 1 | N-acetylglycine | |||||
Sequences
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References
| [1] | "Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization of isozymes in Uromastix hardwickii." Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H. Eur. J. Biochem. 236:563-570(1996) [PubMed: 8612630] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [2] | "Reptilian alcohol dehydrogenase. Heterogeneity relevant to class multiplicity of the mammalian enzyme." Hjelmqvist L., Ericsson M., Shafqat J., Carlquist M., Siddiqi A.R., Hoeoeg J.-O., Joernvall H. FEBS Lett. 298:297-300(1992) [PubMed: 1544464] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S62638. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EE2 based on UniProtKB P00328. |
| SMR | P25405. Positions 2-375. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P25405. |
Family and domain databases | |
| InterPro | IPR013154. AlcDHase_GroES-like. IPR002085. AlcDHase_SF_Zn. IPR013149. AlcDHase_Zn-bd. IPR002328. AlcDHase_Zn_CS. [Graphical view] |
| PANTHER | PTHR11695. ADH_Sf_Zn. 1 hit. |
| Pfam | PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view] |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProDom | P25405. [Graphical view] [Entries sharing at least one domain] |
| BLOCKS | Search... |
Other Resources | |
| ProtoNet | Search... |
Entry information
| Entry name | ADH1A_UROHA | ||||||||
| Accession | Primary (citable) accession number: P25405 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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