Reviewed,
UniProtKB/Swiss-Prot Q06099 (FADH_CANMA)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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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: S-(hydroxymethyl)glutathione dehydrogenase EC=1.1.1.284 Alternative name(s): Glutathione-dependent formaldehyde dehydrogenase Short name=GSH-FDH Short name=FALDH Short name=FDH Short name=FLD EC=1.1.1.- | ||||
| Gene names |
| ||||
| Organism | Candida maltosa (Yeast) | ||||
| Taxonomic identifier | 5479 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida |
Protein attributes
| Sequence length | 381 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Confers resistance to formaldehyde. |
| Catalytic activity | S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Sequence similarities | Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | ethanol oxidation Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | S-(hydroxymethyl)glutathione 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 – 381 | 381 | S-(hydroxymethyl)glutathione dehydrogenase | PRO_0000160781 | |||||
Sites | |||||||||
| Metal binding | 49 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 71 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 101 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 104 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 107 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 115 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 178 | 1 | Zinc 1; catalytic By similarity | ||||||
Sequences
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References
| [1] | "Cloning and analysis of a Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cerevisiae." Sasnauskas K., Jomantiene R., Januska A., Lebediene E., Lebedys J., Janulaitis A. Gene 122:207-211(1992) [PubMed: 1339376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 899. |
Cross-references
Sequence databases | |
|---|---|
| M58332 Genomic DNA. Translation: AAA34344.1. | |
| PIR | JN0447. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M6H based on UniProtKB P11766. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.284. 3846. |
Family and domain databases | |
| InterPro | IPR014183. ADH_3. 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] |
| TIGRFAMs | TIGR02818. adh_III_F_hyde. 1 hit. |
| PROSITE | PS00059. ADH_ZINC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FADH_CANMA | ||||||||
| Accession | Primary (citable) accession number: Q06099 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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