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P54115 (ALDH6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Names and origin

Protein namesRecommended name:
Magnesium-activated aldehyde dehydrogenase, cytosolic

EC=1.2.1.4
Alternative name(s):
Mg(2+)-activated acetaldehyde dehydrogenase
Short name=Mg(2+)-ACDH
Gene names
Name:ALD6
Synonyms:ALDH1
Ordered Locus Names:YPL061W
ORF Names:LPE9
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytosolic aldehyde dehydrogenase which utilizes NADP+ as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate. Ref.1

Catalytic activity

An aldehyde + NADP+ + H2O = a carboxylate + NADPH. Ref.1

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 135000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=40 µM for NADP (with acetaldehyde as cosubstrate) Ref.1

KM=99 µM for NADP (with propionaldehyde as cosubstrate)

KM=17.4 mM for NAD (with propionaldehyde as cosubstrate)

KM=24 µM for acetaldehyde (with NADP as cosubstrate)

KM=30 µM for propionaldehyde (with NADP as cosubstrate)

KM=0.7 mM for propionaldehyde (with NAD as cosubstrate)

Vmax=24 µmol/min/mg enzyme with acetaldehyde and NADP as substrates

Vmax=14 µmol/min/mg enzyme with propionaldehyde and NADP as substrates

Vmax=8.3 µmol/min/mg enzyme with propionaldehyde and NAD as substrates

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 500499Magnesium-activated aldehyde dehydrogenase, cytosolic
PRO_0000056441

Regions

Nucleotide binding249 – 2546NAD By similarity

Sites

Active site2721Proton acceptor By similarity
Active site3061Nucleophile By similarity
Site1731Transition state stabilizer By similarity

Amino acid modifications

Cross-link3Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Experimental info

Sequence conflict1211L → FK in AAB01219. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54115 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 542AA956EFA0E676

FASTA50054,414
        10         20         30         40         50         60 
MTKLHFDTAE PVKITLPNGL TYEQPTGLFI NNKFMKAQDG KTYPVEDPST ENTVCEVSSA 

        70         80         90        100        110        120 
TTEDVEYAIE CADRAFHDTE WATQDPRERG RLLSKLADEL ESQIDLVSSI EALDNGKTLA 

       130        140        150        160        170        180 
LARGDVTIAI NCLRDAAAYA DKVNGRTINT GDGYMNFTTL EPIGVCGQII PWNFPIMMLA 

       190        200        210        220        230        240 
WKIAPALAMG NVCILKPAAV TPLNALYFAS LCKKVGIPAG VVNIVPGPGR TVGAALTNDP 

       250        260        270        280        290        300 
RIRKLAFTGS TEVGKSVAVD SSESNLKKIT LELGGKSAHL VFDDANIKKT LPNLVNGIFK 

       310        320        330        340        350        360 
NAGQICSSGS RIYVQEGIYD ELLAAFKAYL ETEIKVGNPF DKANFQGAIT NRQQFDTIMN 

       370        380        390        400        410        420 
YIDIGKKEGA KILTGGEKVG DKGYFIRPTV FYDVNEDMRI VKEEIFGPVV TVAKFKTLEE 

       430        440        450        460        470        480 
GVEMANSSEF GLGSGIETES LSTGLKVAKM LKAGTVWINT YNDFDSRVPF GGVKQSGYGR 

       490        500 
EMGEEVYHAY TEVKAVRIKL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae."
Wang X., Mann C.J., Bai Y., Ni L., Weiner H.
J. Bacteriol. 180:822-830(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DBY939.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
Norbeck J., Blomberg A.
J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 76-79 AND 482-488.
Strain: ATCC 44827 / SKQ2N.
[5]"The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase."
Meaden P.G., Dickinson F.M., Mifsud A., Tessier W., Westwater J., Bussey H., Midgley M.
Yeast 13:1319-1327(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.
[6]"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].
[7]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3.
Strain: SUB592.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56604 Genomic DNA. Translation: AAB01219.1.
U39205 Genomic DNA. Translation: AAB68304.1.
BK006949 Genomic DNA. Translation: DAA11369.1.
PIRS60929.
RefSeqNP_015264.1. NM_001183875.1.

3D structure databases

ProteinModelPortalP54115.
SMRP54115. Positions 20-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36117. 75 interactions.
DIPDIP-8324N.
IntActP54115. 25 interactions.
MINTMINT-500664.
STRING4932.YPL061W.

Proteomic databases

PaxDbP54115.
PeptideAtlasP54115.
PRIDEP54115.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL061W; YPL061W; YPL061W.
GeneID856044.
KEGGsce:YPL061W.

Organism-specific databases

SGDS000005982. ALD6.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00740000115528.
HOGENOMHOG000271505.
KOK00128.
OMANSMKIMQ.
OrthoDBEOG7S226Z.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13664.
YEAST:MONOMER-13664.
YEAST:YPL061W-MONOMER.
UniPathwayUPA00780; UER00768.

Gene expression databases

GenevestigatorP54115.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980989.

Entry information

Entry nameALDH6_YEAST
AccessionPrimary (citable) accession number: P54115
Secondary accession number(s): D6W3V3, Q02782
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways