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P40047 (ALDH5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 128. 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:
Aldehyde dehydrogenase 5, mitochondrial

EC=1.2.1.5
Gene names
Name:ALD5
Synonyms:ALD3, ALDH5
Ordered Locus Names:YER073W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose. Ref.5 Ref.9

Catalytic activity

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.

Enzyme regulation

Induced by potassium ions.

Pathway

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

Subcellular location

Mitochondrion matrix Ref.4 Ref.6 Ref.8.

Miscellaneous

Present with 23300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.64 mM for NADP (with acetaldehyde as cosubstrate) Ref.4

KM=3.47 mM for NADP (with propionaldehyde as cosubstrate)

KM=6.43 mM for NAD (with propionaldehyde as cosubstrate)

KM=0.058 mM for acetaldehyde (with NADP as cosubstrate)

KM=0.39 mM for propionaldehyde (with NADP as cosubstrate)

KM=0.83 mM for propionaldehyde (with NAD as cosubstrate)

Vmax=1.1 µmol/min/mg enzyme with acetaldehyde and NADP as substrates

Vmax=0.45 µmol/min/mg enzyme with propionaldehyde and NADP as substrates

Vmax=0.011 µmol/min/mg enzyme with propionaldehyde and NAD as substrates

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetate biosynthetic process

Inferred from mutant phenotype Ref.9. Source: SGD

ethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from direct assay Ref.4. Source: SGD

aldehyde dehydrogenase [NAD(P)+] activity

Inferred from direct assay Ref.4. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion Potential
Chain24 – 520497Aldehyde dehydrogenase 5, mitochondrial
PRO_0000007166

Regions

Nucleotide binding266 – 2716NAD By similarity

Sites

Active site2881Proton acceptor By similarity
Active site3221Nucleophile By similarity
Site1901Transition state stabilizer By similarity

Experimental info

Sequence conflict481I → T in AAB01220. Ref.1
Sequence conflict901A → L in AAB01220. Ref.1
Sequence conflict93 – 10412AFETK…IVEPE → LLKRSVYCRAG in AAB01220. Ref.1
Sequence conflict4111E → G in AAB64612. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40047 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: DCD382A1157F800A

FASTA52056,693
        10         20         30         40         50         60 
MLSRTRAAAP NSRIFTRSLL RLYSQAPLRV PITLPNGFTY EQPTGLFING EFVASKQKKT 

        70         80         90        100        110        120 
FDVINPSNEE KITTVYKAME DDVDEAVAAA KKAFETKWSI VEPEVRAKAL FNLADLVEKH 

       130        140        150        160        170        180 
QETLAAIESM DNGKSLFCAR GDVALVSKYL RSCGGWADKI YGNVIDTGKN HFTYSIKEPL 

       190        200        210        220        230        240 
GVCGQIIPWN FPLLMWSWKI GPALATGNTV VLKPAETTPL SALFASQLCQ EAGIPAGVVN 

       250        260        270        280        290        300 
ILPGSGRVVG ERLSAHPDVK KIAFTGSTAT GRHIMKVAAD TVKKVTLELG GKSPNIVFAD 

       310        320        330        340        350        360 
ADLDKAVKNI AFGIFYNSGE VCCAGSRIYI QDTVYEEVLQ KLKDYTESLK VGDPFDEEVF 

       370        380        390        400        410        420 
QGAQTSDKQL HKILDYVDVA KSEGARLVTG GARHGSKGYF VKPTVFADVK EDMRIVKEEV 

       430        440        450        460        470        480 
FGPIVTVSKF STVDEVIAMA NDSQYGLAAG IHTNDINKAV DVSKRVKAGT VWINTYNNFH 

       490        500        510        520 
QNVPFGGFGQ SGIGREMGEA ALSNYTQTKS VRIAIDKPIR 

« Hide

References

« Hide 'large scale' references
[1]"Saccharomyces cerevisiae aldehyde dehydrogenases. Identification and expression."
Wang X., Bai Y., Ni L., Weiner H.
Adv. Exp. Med. Biol. 414:277-280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 411.
Strain: ATCC 204508 / S288c.
[4]"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: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[5]"Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae."
Kurita O., Nishida Y.
FEMS Microbiol. Lett. 181:281-287(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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].
[8]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[9]"Functional analysis of the ALD gene family of Saccharomyces cerevisiae during anaerobic growth on glucose: the NADP+-dependent Ald6p and Ald5p isoforms play a major role in acetate formation."
Saint-Prix F., Boenquist L., Dequin S.
Microbiology 150:2209-2220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56605 Genomic DNA. Translation: AAB01220.1.
U18814 Genomic DNA. Translation: AAB64612.1.
BK006939 Genomic DNA. Translation: DAA07732.2.
PIRS50576.
RefSeqNP_010996.2. NM_001178964.2.

3D structure databases

ProteinModelPortalP40047.
SMRP40047. Positions 9-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36816. 51 interactions.
DIPDIP-3872N.
IntActP40047. 9 interactions.
MINTMINT-488437.
STRING4932.YER073W.

Proteomic databases

PaxDbP40047.
PeptideAtlasP40047.
PRIDEP40047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER073W; YER073W; YER073W.
GeneID856804.
KEGGsce:YER073W.

Organism-specific databases

SGDS000000875. ALD5.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00740000115528.
HOGENOMHOG000271505.
KOK00128.
OMADNGRDKG.
OrthoDBEOG7S226Z.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13665.
YEAST:MONOMER-13665.
YEAST:YER073W-MONOMER.
UniPathwayUPA00780; UER00768.

Gene expression databases

GenevestigatorP40047.

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.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983056.

Entry information

Entry nameALDH5_YEAST
AccessionPrimary (citable) accession number: P40047
Secondary accession number(s): D3DLX8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 128 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 V

Yeast (Saccharomyces cerevisiae) chromosome V: 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