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P46367 (ALDH4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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

Names and origin

Protein namesRecommended name:
Potassium-activated aldehyde dehydrogenase, mitochondrial

EC=1.2.1.5
Alternative name(s):
K(+)-activated acetaldehyde dehydrogenase
Short name=K(+)-ACDH
Gene names
Name:ALD4
Synonyms:ALD7, ALDH2
Ordered Locus Names:YOR374W
ORF Names:O6730
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose. Ref.9

Catalytic activity

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H. Ref.6

Subcellular location

Mitochondrion matrix Ref.7.

Miscellaneous

Present with 22200 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Ref.3 Ref.4
Chain25 – 519495Potassium-activated aldehyde dehydrogenase, mitochondrial
PRO_0000007165

Regions

Nucleotide binding268 – 2736NAD By similarity

Sites

Active site2901Proton acceptor By similarity
Active site3241Nucleophile By similarity
Site1921Transition state stabilizer By similarity

Amino acid modifications

Modified residue961Phosphoserine Ref.11
Modified residue2161Phosphothreonine Ref.10
Modified residue5001Phosphoserine Ref.10 Ref.11

Experimental info

Sequence conflict511N → NN AA sequence Ref.3
Sequence conflict631E → V AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P46367 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E7D9944EA25F948E

FASTA51956,724
        10         20         30         40         50         60 
MFSRSTLCLK TSASSIGRLQ LRYFSHLPMT VPIKLPNGLE YEQPTGLFIN NKFVPSKQNK 

        70         80         90        100        110        120 
TFEVINPSTE EEICHIYEGR EDDVEEAVQA ADRAFSNGSW NGIDPIDRGK ALYRLAELIE 

       130        140        150        160        170        180 
QDKDVIASIE TLDNGKAISS SRGDVDLVIN YLKSSAGFAD KIDGRMIDTG RTHFSYTKRQ 

       190        200        210        220        230        240 
PLGVCGQIIP WNFPLLMWAW KIAPALVTGN TVVLKTAEST PLSALYVSKY IPQAGIPPGV 

       250        260        270        280        290        300 
INIVSGFGKI VGEAITNHPK IKKVAFTGST ATGRHIYQSA AAGLKKVTLE LGGKSPNIVF 

       310        320        330        340        350        360 
ADAELKKAVQ NIILGIYYNS GEVCCAGSRV YVEESIYDKF IEEFKAASES IKVGDPFDES 

       370        380        390        400        410        420 
TFQGAQTSQM QLNKILKYVD IGKNEGATLI TGGERLGSKG YFIKPTVFGD VKEDMRIVKE 

       430        440        450        460        470        480 
EIFGPVVTVT KFKSADEVIN MANDSEYGLA AGIHTSNINT ALKVADRVNA GTVWINTYND 

       490        500        510 
FHHAVPFGGF NASGLGREMS VDALQNYLQV KAVRAKLDE 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [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]"Comparison of benzyl alcohol dehydrogenases and benzaldehyde dehydrogenases from the benzyl alcohol and mandelate pathways in Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid compositions and immunological cross-reactions."
Chalmers R.M., Keen J.N., Fewson C.A.
Biochem. J. 273:99-107(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-65.
[4]"Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry."
Larsson T., Norbeck J., Karlsson H., Karlsson K.-A., Blomberg A.
Electrophoresis 18:418-423(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-34 AND 378-386.
[5]"Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae."
Tessier W.D., Meaden P.G., Dickinson F.M., Midgley M.
FEMS Microbiol. Lett. 164:29-34(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[6]"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: CATALYTIC ACTIVITY.
[7]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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.
[10]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75282 Genomic DNA. Translation: CAA99705.1.
BK006948 Genomic DNA. Translation: DAA11133.1.
PIRS67286.
RefSeqNP_015019.1. NM_001183794.1.

3D structure databases

ProteinModelPortalP46367.
SMRP46367. Positions 31-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34757. 24 interactions.
DIPDIP-4053N.
IntActP46367. 5 interactions.
MINTMINT-539582.
STRING4932.YOR374W.

Proteomic databases

PaxDbP46367.
PeptideAtlasP46367.
PRIDEP46367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR374W; YOR374W; YOR374W.
GeneID854556.
KEGGsce:YOR374W.

Organism-specific databases

CYGDYOR374w.
SGDS000005901. ALD4.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00740000115528.
HOGENOMHOG000271505.
KOK00128.
OMAMCGGERF.
OrthoDBEOG7S226Z.

Enzyme and pathway databases

BioCycYEAST:YOR374W-MONOMER.

Gene expression databases

GenevestigatorP46367.

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

NextBio976985.

Entry information

Entry nameALDH4_YEAST
AccessionPrimary (citable) accession number: P46367
Secondary accession number(s): D6W367, Q08898
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families