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UniProtKB/Swiss-Prot entry P46367


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDH4_YEAST
Primary accession number P46367
Secondary accession number Q08898
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 76)
Name and origin of the protein
Protein name Potassium-activated aldehyde dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
K(+)-activated acetaldehyde dehydrogenase
K(+)-ACDH
Gene name
Name: ALD4
Synonyms: ALD7, ALDH2
OrderedLocusNames: YOR374W
ORFNames: O6730
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
PROTEIN SEQUENCE OF 25-65.
PubMed=1989592 [NCBI, ExPASy, EBI, Israel, Japan]
Chalmers R.M., Keen J.N., Fewson C.A.;
"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.";
Biochem. J. 273:99-107(1991).
[3]
PROTEIN SEQUENCE OF 25-34 AND 378-386.
PubMed=9150920 [NCBI, ExPASy, EBI, Israel, Japan]
Larsson T., Norbeck J., Karlsson H., Karlsson K.-A., Blomberg A.;
"Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry.";
Electrophoresis 18:418-423(1997).
[4]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
DOI=10.1111/j.1574-6968.1998.tb13063.x; PubMed=9675847 [NCBI, ExPASy, EBI, Israel, Japan]
Tessier W.D., Meaden P.G., Dickinson F.M., Midgley M.;
"Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 164:29-34(1998).
[5]
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216 AND SER-500, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700098-MCP200; PubMed=17761666 [NCBI, ExPASy, EBI, Israel, Japan]
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z75282; CAA99705.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67286; S67286.
RefSeq NP_015019.1; -.
3D structure databases
HSSP Q63639; 1BI9. [HSSP ENTRY / PDB]
ModBase P46367.
Protein-protein interaction databases
DIP DIP:4053N; -.
IntAct P46367; -.
Organism-specific databases
CYGD YOR374w; -.
SGD S000005901; ALD4.
Yeast-GFP YOR374W.
Gene expression databases
GermOnline YOR374W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0042645; Cellular component: mitochondrial nucleoid (inferred from direct assay from SGD).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from direct assay from SGD).
GO:0004030; Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (inferred from direct assay from SGD).
GO:0006067; Biological process: ethanol metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS P46367.
Proteomic databases
PeptideAtlas P46367; -.
Genome annotation databases
Ensembl YOR374W; Saccharomyces cerevisiae. [Contig view]
GeneID 854556; -.
GenomeReviews Y13140_GR; YOR374W.
KEGG sce:YOR374W; -.
NMPDR fig|4932.3.peg.6138; -.
Phylogenomic databases
HOGENOM P46367; -.
Other
LinkHub P46367; -.
ProtoNet P46367.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    24  24     Mitochondrion. 
CHAIN   25   519  495     Potassium-activated aldehyde dehydrogenase, mitochondrial. PRO_0000007165
NP_BIND   268   273  6     NAD (By similarity). 
ACT_SITE   290   290        Proton acceptor (By similarity). 
ACT_SITE   324   324        Nucleophile (By similarity). 
SITE   192   192  1     Transition state stabilizer (By similarity). 
MOD_RES   216   216        Phosphothreonine. 
MOD_RES   500   500        Phosphoserine. 
CONFLICT   51    51        N -> NN (in Ref. 2; AA sequence). 
CONFLICT   63    63        E -> V (in Ref. 2; AA sequence). 
Sequence information
Length: 519 AA [This is the length of the unprocessed precursor] Molecular weight: 56724 Da [This is the MW of the unprocessed precursor] CRC64: E7D9944EA25F948E [This is a checksum on the sequence]
        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 

P46367 in FASTA format

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