Reviewed,
UniProtKB/Swiss-Prot P20368 (ADH1_ZYMMO)
Last modified
June 16, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase 1 EC=1.1.1.1 Alternative name(s): Alcohol dehydrogenase I Short name=ADH I | ||||
| Gene names |
| ||||
| Organism | Zymomonas mobilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 542 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Sphingomonadaceae › Zymomonas |
Protein attributes
| Sequence length | 337 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. |
| Enzyme regulation | Inhibited by ethanol. |
| Pathway | Alcohol metabolism; ethanol biosynthesis via fermentation pathway. |
| Subunit structure | Multimeric (with different ratios of monomers). |
| Miscellaneous | In Z.mobilis there are two isozymes of alcohol dehydrogenase. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 337 | 337 | Alcohol dehydrogenase 1 | PRO_0000160750 | |||||
Sites | |||||||||
| Metal binding | 37 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 58 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 89 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 92 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 95 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 103 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 145 | 1 | Zinc 1; catalytic By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 17 | 1 | T → I AA sequence Ref.5 | ||||||
| Sequence conflict | 26 | 1 | E → F AA sequence Ref.5 | ||||||
| Sequence conflict | 28 | 1 | L → H AA sequence Ref.5 | ||||||
| Sequence conflict | 30 | 1 | E → P AA sequence Ref.5 | ||||||
| Sequence conflict | 76 | 1 | V → A in AAA27682. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): sequence comparison and expression in Escherichia coli." Keshav K.F., Yomano L.P., An H., Ingram L.O. J. Bacteriol. 172:2491-2497(1990) [PubMed: 2185223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4. |
| [2] | "Mannitol dehydrogenase from Zymomonas mobilis." O'Mullan P.J., Stein D., Chase T. Jr., Eveleigh D.E. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4. |
| [3] | "The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4." Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y. Kang H.S.Nat. Biotechnol. 23:63-68(2005) [PubMed: 15592456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31821 / ZM4 / CP4. |
| [4] | "Cloning, sequencing, and expression of the Zymomonas mobilis phosphoglycerate mutase gene (pgm) in Escherichia coli." Yomano L.P., Scopes R.K., Ingram L.O. J. Bacteriol. 175:3926-3933(1993) [PubMed: 8320209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. Strain: ATCC 31821 / ZM4 / CP4. |
| [5] | "The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles." Neale A.D., Scopes R.K., Kelly J.M., Wettenhall R.E.H. Eur. J. Biochem. 154:119-124(1986) [PubMed: 2935393] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-31. |
Cross-references
Sequence databases | |
|---|---|
| M32100 Genomic DNA. Translation: AAA27682.1. AY170008 Genomic DNA. Translation: AAO38758.1. AE008692 Genomic DNA. Translation: AAV89860.1. L09650 Genomic DNA. Translation: AAA71935.2. | |
| PIR | A35260. |
| RefSeq | YP_162971.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JVB based on UniProtKB P39462. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3188393. |
| GenomeReviews | Gene locus ZMO1236 in contig AE008692_GR. |
| KEGG | zmo:ZMO1236. |
| NMPDR | fig|264203.3.peg.428. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P20368. |
| OMA | P20368. VRPGQWI. |
Enzyme and pathway databases | |
| BioCyc | ZMOB264203:ZMO1236-MON. |
| BRENDA | 1.1.1.1. 1658. |
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_ZYMMO | ||||||||
| Accession | Primary (citable) accession number: P20368 Secondary accession number(s): Q5NN50, Q6Y8J4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


