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A6ZTT5 (ADH4_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 4

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase IV
Short name=ADHIV
Gene names
Name:ADH4
Synonyms:ZRG5
ORF Names:SCY_1818
OrganismSaccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]
Taxonomic identifier307796 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Zinc. May bind iron when zinc levels are limiting By similarity.

Enzyme regulation

Inhibited by EDTA By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion By similarity.

Induction

Induced by transcription factor ZAP1 in response to zinc deficiency By similarity.

Miscellaneous

While ADH4 is expressed at only low levels in laboratory strains, it is often highly expressed in brewing strains.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Sequence caution

The sequence EDN61873.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Alcohol dehydrogenase 4
PRO_0000345089

Sequences

Sequence LengthMass (Da)Tools
A6ZTT5 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: AC6E77B78D6B9AA8

FASTA38241,084
        10         20         30         40         50         60 
MSSVTGFYIP PISFFGEGAL EETADYIKNK DYKKALIVTD PGIAAIGLSG RVQKMLEERG 

        70         80         90        100        110        120 
LNVAIYDKTQ PNPNIANVTA GLKVLKEQNS EIVVSIGGGS AHDNAKAIAL LATNGGEIGD 

       130        140        150        160        170        180 
YEGVNQSKKA ALPLFAINTT AGTASEMTRF TIISNEEKKI KMAIIDNNVT PAVAVNDPST 

       190        200        210        220        230        240 
MFGLPPALTA ATGLDALTHC IEAYVSTASN PITDACALKG IDLINESLVA AYKDGKDKKA 

       250        260        270        280        290        300 
RTDMCYAEYL AGMAFNNASL GYVHALAHQL GGFYHLPHGV CNAVLLPHVQ EANMQCPKAK 

       310        320        330        340        350        360 
KRLGEIALHF GASQEDPEET IKALHVLNRT MNIPRNLKEL GVKTEDFEIL AEHAMHDACH 

       370        380 
LTNPVQFTKE QVVAIIKKAY EY 

« Hide

References

[1]"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789."
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. expand/collapse author list , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M.
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YJM789.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFW02000099 Genomic DNA. Translation: EDN61873.1. Different initiation.

3D structure databases

ProteinModelPortalA6ZTT5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[Graphical view]
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH4_YEAS7
AccessionPrimary (citable) accession number: A6ZTT5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: September 21, 2011
This is version 23 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families