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P25377 (ADH7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADP-dependent alcohol dehydrogenase 7
EC=1.1.1.2
Alternative name(s):
NADP-dependent alcohol dehydrogenase VII
Short name=ADHVII
Gene names
Name:ADH7
Ordered Locus Names:YCR105W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NADP-dependent alcohol dehydrogenase with a broad substrate specificity.

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer. Ref.3

Miscellaneous

Present with 2870 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361NADP-dependent alcohol dehydrogenase 7
PRO_0000160735

Regions

Nucleotide binding188 – 1936NAD By similarity
Nucleotide binding276 – 2783NAD By similarity

Sites

Metal binding461Zinc 1; catalytic By similarity
Metal binding681Zinc 1; catalytic By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1641Zinc 1; catalytic By similarity
Binding site2161NAD By similarity
Binding site3491NAD By similarity

Amino acid modifications

Modified residue3161Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P25377 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: BFB0E6C5F93D3F07

FASTA36139,348
        10         20         30         40         50         60 
MLYPEKFQGI GISNAKDWKH PKLVSFDPKP FGDHDVDVEI EACGICGSDF HIAVGNWGPV 

        70         80         90        100        110        120 
PENQILGHEI IGRVVKVGSK CHTGVKIGDR VGVGAQALAC FECERCKSDN EQYCTNDHVL 

       130        140        150        160        170        180 
TMWTPYKDGY ISQGGFASHV RLHEHFAIQI PENIPSPLAA PLLCGGITVF SPLLRNGCGP 

       190        200        210        220        230        240 
GKRVGIVGIG GIGHMGILLA KAMGAEVYAF SRGHSKREDS MKLGADHYIA MLEDKGWTEQ 

       250        260        270        280        290        300 
YSNALDLLVV CSSSLSKVNF DSIVKIMKIG GSIVSIAAPE VNEKLVLKPL GLMGVSISSS 

       310        320        330        340        350        360 
AIGSRKEIEQ LLKLVSEKNV KIWVEKLPIS EEGVSHAFTR MESGDVKYRF TLVDYDKKFH 


K

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family."
Larroy C., Pares X., Biosca J.A.
Eur. J. Biochem. 269:5738-5745(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBUNIT.
[4]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59720 Genomic DNA. Translation: CAA42237.1.
BK006937 Genomic DNA. Translation: DAA07574.1.
PIRS19417.
RefSeqNP_010030.1. NM_001178812.1.

3D structure databases

ProteinModelPortalP25377.
SMRP25377. Positions 1-359.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-7661N.
MINTMINT-2789097.
STRING4932.YCR105W.

Proteomic databases

PaxDbP25377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR105W; YCR105W; YCR105W.
GeneID850469.
KEGGsce:YCR105W.

Organism-specific databases

CYGDYCR105w.
SGDS000000702. ADH7.

Phylogenomic databases

eggNOGCOG1064.
GeneTreeENSGT00550000075527.
HOGENOMHOG000294667.
KOK00002.
OMADYILDTV.
OrthoDBEOG40ZV6H.

Gene expression databases

GenevestigatorP25377.
GermOnlineYCR105W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966116.

Entry information

Entry nameADH7_YEAST
AccessionPrimary (citable) accession number: P25377
Secondary accession number(s): D6VRA5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 3, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome III

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents