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Reviewed, UniProtKB/Swiss-Prot P38113 (ADH5_YEAST)

Last modified January 19, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 5
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase V
Gene names
Name: ADH5
Ordered Locus Names: YBR145W
ORF Names: YBR1122
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Miscellaneous

Present with 1310 molecules/cell in log phase SD medium. Ref.2

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Alcohol dehydrogenase 5
PRO_0000160733

Regions

Nucleotide binding181 – 1877NAD By similarity
Nucleotide binding272 – 2743NAD By similarity

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding701Zinc 1; catalytic By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1831Zinc 1; catalytic By similarity
Binding site2051NAD By similarity
Binding site2101NAD By similarity
Binding site3441NAD By similarity

Amino acid modifications

Modified residue2521Phosphoserine Ref.4
Modified residue3051Phosphothreonine Ref.4 Ref.3

Sequences

Sequence LengthMass (Da)Tools
P38113-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F4084DAD1E3C19DE

FASTA35137,648
        10         20         30         40         50         60 
MPSQVIPEKQ KAIVFYETDG KLEYKDVTVP EPKPNEILVH VKYSGVCHSD LHAWHGDWPF 

        70         80         90        100        110        120 
QLKFPLIGGH EGAGVVVKLG SNVKGWKVGD FAGIKWLNGT CMSCEYCEVG NESQCPYLDG 

       130        140        150        160        170        180 
TGFTHDGTFQ EYATADAVQA AHIPPNVNLA EVAPILCAGI TVYKALKRAN VIPGQWVTIS 

       190        200        210        220        230        240 
GACGGLGSLA IQYALAMGYR VIGIDGGNAK RKLFEQLGGE IFIDFTEEKD IVGAIIKATN 

       250        260        270        280        290        300 
GGSHGVINVS VSEAAIEAST RYCRPNGTVV LVGMPAHAYC NSDVFNQVVK SISIVGSCVG 

       310        320        330        340        350 
NRADTREALD FFARGLIKSP IHLAGLSDVP EIFAKMEKGE IVGRYVVETS K 

« Hide

References

[1]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"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].
[3]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305, MASS SPECTROMETRY.
[4]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND THR-305, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36014 Genomic DNA. Translation: CAA85103.1.
PIRS46016.
RefSeqNP_009703.1.

3D structure databases

SMRP38113. Positions 6-351.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4500N.
IntActP38113. 7 interactions.
STRINGP38113.

Proteomic databases

PeptideAtlasP38113.
PRIDEP38113.

Genome annotation databases

EnsemblYBR145W; YBR145W; YBR145W; Saccharomyces cerevisiae. [Genome view]
GeneID852442.
KEGGsce:YBR145W.
NMPDRfig|4932.3.peg.409.

Organism-specific databases

CYGDYBR145w.
SGDS000000349. ADH5.

Phylogenomic databases

eggNOGfuNOG04605.
HOGENOMHBG753318.
OMANARNEDS.
OrthoDBEOG95HTDV.
PhylomeDBP38113.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11839.
BRENDA1.1.1.1. 250.

Gene expression databases

ArrayExpressP38113.
GenevestigatorP38113.
GermOnlineYBR145W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio971342.

Entry information

Entry nameADH5_YEAST
AccessionPrimary (citable) accession number: P38113
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 19, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents