Aldehyde dehydrogenase 5, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40047 (ALDH5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aldehyde dehydrogenase 5, mitochondrial
EC=1.2.1.3
EC=1.2.1.4

Gene names

Name:	ALD5
Synonyms:	ALD3, ALDH5
Ordered Locus Names:	YER073W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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⁺ + H₂O = a carboxylate + NADH. An aldehyde + NADP⁺ + H₂O = a carboxylate + NADPH.
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: K_M=0.64 mM for NADP (with acetaldehyde as cosubstrate) Ref.4 K_M=3.47 mM for NADP (with propionaldehyde as cosubstrate) K_M=6.43 mM for NAD (with propionaldehyde as cosubstrate) K_M=0.058 mM for acetaldehyde (with NADP as cosubstrate) K_M=0.39 mM for propionaldehyde (with NADP as cosubstrate) K_M=0.83 mM for propionaldehyde (with NAD as cosubstrate) V_max=1.1 µmol/min/mg enzyme with acetaldehyde and NADP as substrates V_max=0.45 µmol/min/mg enzyme with propionaldehyde and NADP as substrates V_max=0.011 µmol/min/mg enzyme with propionaldehyde and NAD as substrates

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetate biosynthetic process Inferred from mutant phenotype Ref.9. Source: SGD ethanol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.8 PubMed 16823961. Source: SGD
Molecular_function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase [NAD(P)+] activity Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 23

Mitochondrion Potential

Chain

24 – 520

497

Aldehyde dehydrogenase 5, mitochondrial

PRO_0000007166

Regions

Nucleotide binding

266 – 271

NAD By similarity

Sites

Active site

288

Proton acceptor By similarity

Active site

322

Nucleophile By similarity

Site

190

Transition state stabilizer By similarity

Experimental info

Sequence conflict

I → T in AAB01220. Ref.1

Sequence conflict

A → L in AAB01220. Ref.1

Sequence conflict

93 – 104

AFETK…IVEPE → LLKRSVYCRAG in AAB01220. Ref.1

Sequence conflict

411

E → G in AAB64612. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P40047 [UniParc].

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

FASTA

520

56,693

        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' referencesShow '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. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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], MASS SPECTROMETRY. 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.
PIR	S50576.
RefSeq	NP_010996.2. NM_001178964.2.
3D structure databases
ProteinModelPortal	P40047.
SMR	P40047. Positions 9-517.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3872N.
IntAct	P40047. 10 interactions.
MINT	MINT-488437.
STRING	4932.YER073W.
Proteomic databases
PaxDb	P40047.
PeptideAtlas	P40047.
PRIDE	P40047.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER073W; YER073W; YER073W.
GeneID	856804.
KEGG	sce:YER073W.
Organism-specific databases
SGD	S000000875. ALD5.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	ENSGT00550000074289.
HOGENOM	HOG000271505.
KO	K00128.
OMA	NIGEWIS.
OrthoDB	EOG4Q885T.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13665.
UniPathway	UPA00780; UER00768.
Gene expression databases
Genevestigator	P40047.
GermOnline	YER073W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.309.10. 1 hit. 3.40.605.10. 1 hit.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view]
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983056.

Entry information

Entry name

ALDH5_YEAST

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome V

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents