Reviewed,
UniProtKB/Swiss-Prot P00333 (ADH1_MAIZE)
Last modified
June 16, 2009.
Version 81.
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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 1 EC=1.1.1.1 | ||
| Gene names |
| ||
| Organism | Zea mays (Maize) | ||
| Taxonomic identifier | 4577 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea |
Protein attributes
| Sequence length | 379 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | An alcohol + NAD+ = an aldehyde or ketone + NADH. |
| Cofactor | Binds 2 zinc ions per subunit. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Polymorphism | The sequence shown is that of allele ADH1-F. |
| Miscellaneous | In maize there are two isozymes. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Polymorphism |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc 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 – 379 | 379 | Alcohol dehydrogenase 1 | PRO_0000160703 | |||||
Regions | |||||||||
| Nucleotide binding | 202 – 207 | 6 | NAD By similarity | ||||||
| Nucleotide binding | 295 – 297 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Metal binding | 47 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 69 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 99 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 102 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 105 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 113 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 177 | 1 | Zinc 1; catalytic By similarity | ||||||
| Binding site | 226 | 1 | NAD By similarity | ||||||
| Binding site | 231 | 1 | NAD By similarity | ||||||
| Binding site | 372 | 1 | NAD By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 52 | 1 | Y → D in allele ADH1-Cm. | ||||||
| Natural variant | 127 | 1 | A → G in allele ADH1-S. | ||||||
| Natural variant | 179 | 1 | Y → I in allele ADH1-Cm and allele ADH1-S. | ||||||
| Natural variant | 363 | 1 | D → N in allele ADH1-S. | ||||||
Sequences
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References
| [1] | "Molecular analysis of the alcohol dehydrogenase (Adh1) gene of maize." Dennis E.S., Gerlach W.L., Pryor A.J., Bennetzen J.L., Inglis A., Llewellyn D.J., Sachs M.M., Ferl R.J., Peacock W.J. Nucleic Acids Res. 12:3983-4000(1984) [PubMed: 6328449] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize." Dennis E.S., Sachs M.M., Gerlach W.L., Finnegan E.J., Peacock W.J. Nucleic Acids Res. 13:727-743(1985) [PubMed: 2987807] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [3] | "Correlation of exons with structural domains in alcohol dehydrogenase." Braenden C.-I., Eklund H., Cambillau C., Pryor A.J. EMBO J. 3:1307-1310(1984) [PubMed: 6378620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [4] | "Two alleles of maize alcohol dehydrogenase 1 have 3'-structural and poly(A) addition polymorphisms." Sachs M.M., Dennis E.S., Gerlach W.L., Peacock W.J. Genetics 113:449-467(1986) [PubMed: 17246333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ALLELE ADH1-F). Strain: cv. Berkeley Fast. |
| [5] | "Molecular analysis of the ADH1-Cm allele of maize." Osterman J.C., Dennis E.S. Plant Mol. Biol. 13:203-212(1989) [PubMed: 2577507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ALLELE ADH1-CM). |
| [6] | "cDNA cloning and induction of the alcohol dehydrogenase gene (Adh1) of maize." Gerlach W.L., Pryor A.J., Dennis E.S., Ferl R.J., Sachs M.M., Peacock W.J. Proc. Natl. Acad. Sci. U.S.A. 79:2981-2985(1982) [PubMed: 16593188] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 212-379. |
Cross-references
Sequence databases | |
|---|---|
| X04049 Genomic DNA. Translation: CAA27681.1. X00580 mRNA. Translation: CAA25239.1. X04050 Genomic DNA. Translation: CAA27682.1. M32984 Genomic DNA. Translation: AAA33434.1. | |
| PIR | S04571. |
| RefSeq | NP_001105409.1. |
| UniGene | Zm.1540 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M6H based on UniProtKB P11766. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 542363. |
Organism-specific databases | |
| Gramene | P00333. |
| MaizeGDB | 13844. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.1. 289. |
Family and domain databases | |
| InterPro | IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_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] |
| ProtoNet | Search... |
Entry information
| Entry name | ADH1_MAIZE | ||||||||
| Accession | Primary (citable) accession number: P00333 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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