Reviewed, UniProtKB/Swiss-Prot P10127 (ADH4_YEAST)

Names 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

Name:	ADH4
Synonyms:	ZRG5
Ordered Locus Names:	YGL256W
ORF Names:	NRC465

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	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Cofactor	Zinc. May bind iron when zinc levels are limiting.
Enzyme regulation	Inhibited by EDTA.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion.
Induction	Induced by transcription factor ZAP1 in response to zinc deficiency.
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.
Sequence similarities	Belongs to the iron-containing alcohol dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=59 mM for NAD KM=122 µM for NADH KM=2.83 mM for acetaldehyde KM=16.7 mM for ethanol pH dependence: Optimum pH is 8.3.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	amino acid catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction. Source: SGD fermentation Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Ref.7 Inferred from direct assay. Source: SGD
Molecular function	alcohol dehydrogenase activity Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 382	382	Alcohol dehydrogenase 4
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

	Sequence		Length	Mass (Da)
	P10127-1 [UniParc]. Last modified July 22, 2008. Version 3. Checksum: 7DFFD43830FB269B	FASTA	382	41,142
	10 20 30 40 50 60 MSSVTGFYIP PISFFGEGAL EETADYIKNK DYKKALIVTD PGIAAIGLSG RVQKMLEERD 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

References

	« Hide 'large scale' referencesShow '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. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"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.
[5]	"Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon tagging." Yuan D.S. Genetics 156:45-58(2000) [PubMed: 10978274] [Abstract] Cited for: INDUCTION.
[6]	"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.
[7]	"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].
[8]	"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].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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
EMBLGenBankDDBJ	X05992 Genomic DNA. Translation: CAA29410.1. X94357 Genomic DNA. Translation: CAA64131.1. Different initiation. Z72778 Genomic DNA. Translation: CAA96976.1. Different initiation.
PIR	DEBY4. S61605.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4812N.
IntAct	P10127.
Proteomic databases
PeptideAtlas	P10127.
Genome annotation databases
Ensembl	YGL256W. Saccharomyces cerevisiae. [Contig view]
GenomeReviews	Gene locus YGL256W in contig Y13135_GR.
KEGG	sce:YGL256W.
NMPDR	fig|4932.3.peg.2361.
Organism-specific databases
CYGD	YGL256w.
SGD	S000003225. ADH4.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P10127.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-11725.
Gene expression databases
ArrayExpress	P10127.
GermOnline	YGL256W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001670. Fe_AlcDHase. [Graphical view]
Pfam	PF00465. Fe-ADH. 1 hit. [Graphical view]
PROSITE	PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view]
ProDom	P10127. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P10127.
ProtoNet	Search...

Entry information

Entry name

ADH4_YEAST

Accession

Primary (citable) accession number: P10127

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 22, 2008
Last modified:	September 2, 2008
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)