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UniProtKB/Swiss-Prot entry P40047


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

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Entry information
Entry name ALDH5_YEAST
Primary accession number P40047
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on April 29, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 76)
Name and origin of the protein
Protein name Aldehyde dehydrogenase 5, mitochondrial [Precursor]
Synonyms EC 1.2.1.3
EC 1.2.1.4
Gene name
Name: ALD5
Synonyms: ALD3, ALDH5
OrderedLocusNames: YER073W
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 [GENOMIC DNA].
PubMed=9059631 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Bai Y., Ni L., Weiner H.;
"Saccharomyces cerevisiae aldehyde dehydrogenases. Identification and expression.";
Adv. Exp. Med. Biol. 414:277-280(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[3]
CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=9473035 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Mann C.J., Bai Y., Ni L., Weiner H.;
"Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae.";
J. Bacteriol. 180:822-830(1998).
[4]
FUNCTION.
DOI=10.1111/j.1574-6968.1999.tb08856.x; PubMed=10585550 [NCBI, ExPASy, EBI, Israel, Japan]
Kurita O., Nishida Y.;
"Involvement of mitochondrial aldehyde dehydrogenase ALD5 in maintenance of the mitochondrial electron transport chain in Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 181:281-287(1999).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[8]
FUNCTION.
DOI=10.1099/mic.0.26999-0; PubMed=15256563 [NCBI, ExPASy, EBI, Israel, Japan]
Saint-Prix F., Boenquist L., Dequin S.;
"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.";
Microbiology 150:2209-2220(2004).
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
U56605; AAB01220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18814; AAB64612.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S50576; S50576.
RefSeq NP_010996.1; -.
3D structure databases
HSSP Q63639; 1BI9. [HSSP ENTRY / PDB]
ModBase P40047.
Protein-protein interaction databases
DIP DIP:3872N; -.
IntAct P40047; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13665; -.
Organism-specific databases
CYGD YER073w; -.
SGD S000000875; ALD5.
Yeast-GFP YER073W.
Gene expression databases
ArrayExpress P40047; -.
GermOnline YER073W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
GO:0033721; Molecular function: aldehyde dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0004030; Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0019413; Biological process: acetate biosynthetic process (inferred from mutant phenotype from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
ProtoNet P40047.
Proteomic databases
PeptideAtlas P40047; -.
Genome annotation databases
Ensembl YER073W; Saccharomyces cerevisiae. [Contig view]
GeneID 856804; -.
GenomeReviews U00092_GR; YER073W.
KEGG sce:YER073W; -.
Phylogenomic databases
HOGENOM P40047; -.
Other
LinkHub P40047; -.
NextBio 983056; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Mitochondrion; NAD; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    23  23     Mitochondrion (Potential). 
CHAIN   24   520  497     Aldehyde dehydrogenase 5, mitochondrial. PRO_0000007166
NP_BIND   266   271  6     NAD (By similarity). 
ACT_SITE   288   288        Proton acceptor (By similarity). 
ACT_SITE   322   322        Nucleophile (By similarity). 
SITE   190   190  1     Transition state stabilizer (By similarity). 
CONFLICT   48    48        I -> T (in Ref. 1; AAB01220). 
CONFLICT   90    90        A -> L (in Ref. 1; AAB01220). 
CONFLICT   93   104        AFETKWSIVEPE -> LLKRSVYCRAG (in Ref. 1; AAB01220). 
CONFLICT   411   411        G -> E (in Ref. 1; AAB01220). 
Sequence information
Length: 520 AA [This is the length of the unprocessed precursor] Molecular weight: 56621 Da [This is the MW of the unprocessed precursor] CRC64: 316559CF2D9D2022 [This is a checksum on the sequence]
        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 GDMRIVKEEV 

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

       490        500        510        520 
QNVPFGGFGQ SGIGREMGEA ALSNYTQTKS VRIAIDKPIR 

P40047 in FASTA format

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