Reviewed,
UniProtKB/Swiss-Prot P40047 (ALDH5_YEAST)
Last modified
November 25, 2008.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aldehyde dehydrogenase 5, mitochondrial EC=1.2.1.3 EC=1.2.1.4 | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 520 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose. |
| Catalytic activity | An aldehyde + NAD(+) + H(2)O = an acid + NADH. An aldehyde + NADP(+) + H(2)O = an acid + NADPH. |
| Enzyme regulation | Induced by potassium ions. |
| Pathway | Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. |
| Subcellular location | |
| Miscellaneous | Present with 23300 molecules/cell in log phase SD medium. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.64 mM for NADP (with acetaldehyde as cosubstrate) KM=3.47 mM for NADP (with propionaldehyde as cosubstrate) KM=6.43 mM for NAD (with propionaldehyde as cosubstrate) KM=0.058 mM for acetaldehyde (with NADP as cosubstrate) KM=0.39 mM for propionaldehyde (with NADP as cosubstrate) KM=0.83 mM for propionaldehyde (with NAD as cosubstrate) Vmax=1.1 µmol/min/mg enzyme with acetaldehyde and NADP as substrates Vmax=0.45 µmol/min/mg enzyme with propionaldehyde and NADP as substrates Vmax=0.011 µmol/min/mg enzyme with propionaldehyde and NAD as substrates |
Ontologies
Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | acetate biosynthetic process Ref.8 Inferred from mutant phenotype. Source: SGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NADP+) activityInferred from electronic annotation. Source: EC aldehyde dehydrogenase [NAD(P)+] activity Ref.3Inferred from direct assay. Source: SGD protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 23 | 23 | Mitochondrion Potential | ||||||
| Chain | 24 – 520 | 497 | Aldehyde dehydrogenase 5, mitochondrial | PRO_0000007166 | |||||
Regions | |||||||||
| Nucleotide binding | 266 – 271 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 288 | 1 | Proton acceptor By similarity | ||||||
| Active site | 322 | 1 | Nucleophile By similarity | ||||||
| Site | 190 | 1 | Transition state stabilizer By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 48 | 1 | I → T in AAB01220. Ref.1 | ||||||
| Sequence conflict | 90 | 1 | A → L in AAB01220. Ref.1 | ||||||
| Sequence conflict | 93 – 104 | 12 | AFETK…IVEPE → LLKRSVYCRAG in AAB01220. Ref.1 | ||||||
| Sequence conflict | 411 | 1 | G → E in AAB01220. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Saccharomyces cerevisiae aldehyde dehydrogenases. Identification and expression." Wang X., Bai Y., Ni L., Weiner H. Adv. Exp. Med. Biol. 414:277-280(1997) [PubMed: 9059631] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W.Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972. |
| [3] | "Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae." Wang X., Mann C.J., Bai Y., Ni L., Weiner H. J. Bacteriol. 180:822-830(1998) [PubMed: 9473035] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. |
| [4] | "Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae." Kurita O., Nishida Y. FEMS Microbiol. Lett. 181:281-287(1999) [PubMed: 10585550] [Abstract] Cited for: FUNCTION. |
| [5] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [6] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [7] | "The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [8] | "Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation." Saint-Prix F., Boenquist L., Dequin S. Microbiology 150:2209-2220(2004) [PubMed: 15256563] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U56605 Genomic DNA. Translation: AAB01220.1. U18814 Genomic DNA. Translation: AAB64612.1. | |
| PIR | S50576. |
| RefSeq | NP_010996.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1BI9 based on UniProtKB Q63639. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:3872N. |
| IntAct | P40047. |
Proteomic databases | |
| PeptideAtlas | P40047. |
Genome annotation databases | |
| Ensembl | YER073W. Saccharomyces cerevisiae. [Contig view] |
| GeneID | 856804. |
| GenomeReviews | Gene locus YER073W in contig U00092_GR. |
| KEGG | sce:YER073W. |
Organism-specific databases | |
| CYGD | YER073w. |
| SGD | S000000875. ALD5. |
| Yeast-GFP | Search... |
Phylogenomic databases | |
| HOGENOM | P40047. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-13665. |
Gene expression databases | |
| ArrayExpress | P40047. |
| GermOnline | YER073W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR016160. Ald_DHase_CS. IPR015590. Aldehyde_DHase. [Graphical view] |
| PANTHER | PTHR11699. Aldehyde_dehyd. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| LinkHub | P40047. |
| NextBio | 983056. |
Entry information
| Entry name | ALDH5_YEAST | ||||||||
| Accession | Primary (citable) accession number: P40047 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome V Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names |

Clusters with


