P10127 (ADH4_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alcohol dehydrogenase 4 EC=1.1.1.1 Alternative name(s): Alcohol dehydrogenase IV Short name=ADHIV | ||||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | ||||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 382 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all. Ref.13 |
| Catalytic activity | An alcohol + NAD+ = an aldehyde or ketone + NADH. |
| Cofactor | Zinc. May bind iron when zinc levels are limiting. Ref.5 |
| Enzyme regulation | Inhibited by EDTA. Ref.5 |
| Subunit structure | Homodimer. Ref.5 |
| Subcellular location | |
| Induction | Induced by transcription factor ZAP1 in response to zinc deficiency. Ref.5 Ref.6 Ref.7 Ref.10 Ref.12 Ref.13 |
| Miscellaneous | While ADH4 is expressed at only low levels in laboratory strains, it is often highly expressed in brewing strains. Present with 125 molecules/cell in log phase SD medium. Ref.9 |
| Sequence similarities | Belongs to the iron-containing alcohol dehydrogenase family. |
| Biophysicochemical properties | Kinetic parameters: KM=59 mM for NAD Ref.5 KM=122 µM for NADH KM=2.83 mM for acetaldehyde KM=16.7 mM for ethanol pH dependence: Optimum pH is 8.3. |
| Sequence caution | The sequence CAA64131.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA96976.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Ligand | Metal-binding NAD Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | fermentation Inferred from mutant phenotype. Source: SGD |
| Cellular component | mitochondrion Inferred from direct assay Ref.8. Source: SGD |
| Molecular function | alcohol dehydrogenase (NAD) activity Inferred from direct assay Ref.5. Source: SGD metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ERJ5 | P43613 | 1 | EBI-2233,EBI-23020 | |
| SWI6 | P09959 | 1 | EBI-2233,EBI-18641 | |
| TAF6 | P53040 | 1 | EBI-2233,EBI-18876 | |
| UIP3 | P39547 | 1 | EBI-2233,EBI-20760 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 382 | 382 | Alcohol dehydrogenase 4 | PRO_0000087817 | |||||
Experimental info | |||||||||
| Sequence conflict | 60 | 1 | D → G in CAA29410. Ref.1 | ||||||
| Sequence conflict | 88 | 1 | Q → E in CAA29410. Ref.1 | ||||||
| Sequence conflict | 310 | 1 | F → C in CAA29410. Ref.1 | ||||||
| Sequence conflict | 339 | 1 | E → D in CAA29410. Ref.1 | ||||||
| Sequence conflict | 348 | 1 | E → D in CAA29410. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis." Williamson V.M., Paquin C.E. Mol. Gen. Genet. 209:374-381(1987) [PubMed: 2823079] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae." Coissac E., Maillier E., Robineau S., Netter P. Yeast 12:1555-1562(1996) [PubMed: 8972578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K.Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [4] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [5] | "Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces cerevisiae." Drewke C., Ciriacy M. Biochim. Biophys. Acta 950:54-60(1988) [PubMed: 3282541] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, ENZYME REGULATION. |
| [6] | "Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon tagging." Yuan D.S. Genetics 156:45-58(2000) [PubMed: 10978274] [Abstract] Cited for: INDUCTION. |
| [7] | "Genome-wide characterization of the Zap1p zinc-responsive regulon in yeast." Lyons T.J., Gasch A.P., Gaither L.A., Botstein D., Brown P.O., Eide D.J. Proc. Natl. Acad. Sci. U.S.A. 97:7957-7962(2000) [PubMed: 10884426] [Abstract] Cited for: INDUCTION, IDENTIFICATION OF PROBABLE INITIATION SITE. |
| [8] | "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]. |
| [9] | "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]. |
| [10] | "Repression of ADH1 and ADH3 during zinc deficiency by Zap1-induced intergenic RNA transcripts." Bird A.J., Gordon M., Eide D.J., Winge D.R. EMBO J. 25:5726-5734(2006) [PubMed: 17139254] [Abstract] Cited for: INDUCTION. |
| [11] | "Characterization of low-acetic-acid-producing yeast isolated from 2-deoxyglucose-resistant mutants and its application to high-gravity brewing." Mizuno A., Tabei H., Iwahuti M. J. Biosci. Bioeng. 101:31-37(2006) [PubMed: 16503288] [Abstract] Cited for: EXPRESSION LEVEL IN BREWING STRAINS. |
| [12] | "Physiological and transcriptional responses of Saccharomyces cerevisiae to zinc limitation in chemostat cultures." De Nicola R., Hazelwood L.A., De Hulster E.A.F., Walsh M.C., Knijnenburg T.A., Reinders M.J.T., Walker G.M., Pronk J.T., Daran J.-M., Daran-Lapujade P. Appl. Environ. Microbiol. 73:7680-7692(2007) [PubMed: 17933919] [Abstract] Cited for: INDUCTION. |
| [13] | "Acetaldehyde addition throughout the growth phase alleviates the phenotypic effect of zinc deficiency in Saccharomyces cerevisiae." Cheraiti N., Sauvage F.-X., Salmon J.-M. Appl. Microbiol. Biotechnol. 77:1093-1109(2008) [PubMed: 17938904] [Abstract] Cited for: FUNCTION, INDUCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X05992 Genomic DNA. Translation: CAA29410.1. X94357 Genomic DNA. Translation: CAA64131.1. Different initiation. Z72778 Genomic DNA. Translation: CAA96976.1. Different initiation. BK006941 Genomic DNA. Translation: DAA07863.1. |
| PIR | DEBY4. S61605. |
| RefSeq | NP_011258.2. NM_001181122.1. |
3D structure databases | |
| ProteinModelPortal | P10127. |
| SMR | P10127. Positions 5-380. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-4812N. |
| IntAct | P10127. 11 interactions. |
| MINT | MINT-475922. |
| STRING | P10127. |
Proteomic databases | |
| PeptideAtlas | P10127. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | YGL256W; YGL256W; YGL256W. |
| GeneID | 852636. |
| KEGG | sce:YGL256W. |
| NMPDR | fig|4932.3.peg.2361. |
Organism-specific databases | |
| CYGD | YGL256w. |
| SGD | S000003225. ADH4. |
Phylogenomic databases | |
| eggNOG | fuNOG07707. |
| GeneTree | EFGT00050000001042. |
| HOGENOM | HBG742415. |
| OMA | SAHDNAK. |
| OrthoDB | EOG4SXRN9. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MONOMER-11725. |
Gene expression databases | |
| ArrayExpress | P10127. |
| Genevestigator | P10127. |
| GermOnline | YGL256W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view] |
| KO | K13954. |
| Pfam | PF00465. Fe-ADH. 1 hit. [Graphical view] |
| PROSITE | PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ADH4_YEAST | ||||||||
| Accession | Primary (citable) accession number: P10127 Secondary accession number(s): D6VV79 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome VII Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with