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Protein

Aldehyde dehydrogenase 5, mitochondrial

Gene

ALD5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Induced by potassium ions.

Kineticsi

  1. KM=0.64 mM for NADP (with acetaldehyde as cosubstrate)1 Publication
  2. KM=3.47 mM for NADP (with propionaldehyde as cosubstrate)1 Publication
  3. KM=6.43 mM for NAD (with propionaldehyde as cosubstrate)1 Publication
  4. KM=0.058 mM for acetaldehyde (with NADP as cosubstrate)1 Publication
  5. KM=0.39 mM for propionaldehyde (with NADP as cosubstrate)1 Publication
  6. KM=0.83 mM for propionaldehyde (with NAD as cosubstrate)1 Publication
  1. Vmax=1.1 µmol/min/mg enzyme with acetaldehyde and NADP as substrates1 Publication
  2. Vmax=0.45 µmol/min/mg enzyme with propionaldehyde and NADP as substrates1 Publication
  3. Vmax=0.011 µmol/min/mg enzyme with propionaldehyde and NAD as substrates1 Publication

Pathway:iethanol degradation

This protein is involved in step 2 of the subpathway that synthesizes acetate from ethanol.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Aldehyde dehydrogenase 5, mitochondrial (ALD5), Magnesium-activated aldehyde dehydrogenase, cytosolic (ALD6)
This subpathway is part of the pathway ethanol degradation, which is itself part of Alcohol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetate from ethanol, the pathway ethanol degradation and in Alcohol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei190 – 1901Transition state stabilizerBy similarity
Active sitei288 – 2881Proton acceptorPROSITE-ProRule annotation
Active sitei322 – 3221NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2716NADBy similarity

GO - Molecular functioni

  • aldehyde dehydrogenase (NAD) activity Source: SGD
  • aldehyde dehydrogenase [NAD(P)+] activity Source: SGD

GO - Biological processi

  • acetate biosynthetic process Source: SGD
  • ethanol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13665.
YEAST:MONOMER-13665.
YEAST:YER073W-MONOMER.
UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase 5, mitochondrial (EC:1.2.1.5)
Gene namesi
Name:ALD5
Synonyms:ALD3, ALDH5
Ordered Locus Names:YER073W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER073W.
SGDiS000000875. ALD5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionSequence AnalysisAdd
BLAST
Chaini24 – 520497Aldehyde dehydrogenase 5, mitochondrialPRO_0000007166Add
BLAST

Proteomic databases

MaxQBiP40047.
PaxDbiP40047.
PeptideAtlasiP40047.
PRIDEiP40047.

Interactioni

Protein-protein interaction databases

BioGridi36816. 51 interactions.
DIPiDIP-3872N.
IntActiP40047. 9 interactions.
MINTiMINT-488437.

Structurei

3D structure databases

ProteinModelPortaliP40047.
SMRiP40047. Positions 9-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP40047.
KOiK00128.
OMAiHRDSIES.
OrthoDBiEOG7S226Z.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P40047-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRTRAAAP NSRIFTRSLL RLYSQAPLRV PITLPNGFTY EQPTGLFING
60 70 80 90 100
EFVASKQKKT FDVINPSNEE KITTVYKAME DDVDEAVAAA KKAFETKWSI
110 120 130 140 150
VEPEVRAKAL FNLADLVEKH QETLAAIESM DNGKSLFCAR GDVALVSKYL
160 170 180 190 200
RSCGGWADKI YGNVIDTGKN HFTYSIKEPL GVCGQIIPWN FPLLMWSWKI
210 220 230 240 250
GPALATGNTV VLKPAETTPL SALFASQLCQ EAGIPAGVVN ILPGSGRVVG
260 270 280 290 300
ERLSAHPDVK KIAFTGSTAT GRHIMKVAAD TVKKVTLELG GKSPNIVFAD
310 320 330 340 350
ADLDKAVKNI AFGIFYNSGE VCCAGSRIYI QDTVYEEVLQ KLKDYTESLK
360 370 380 390 400
VGDPFDEEVF QGAQTSDKQL HKILDYVDVA KSEGARLVTG GARHGSKGYF
410 420 430 440 450
VKPTVFADVK EDMRIVKEEV FGPIVTVSKF STVDEVIAMA NDSQYGLAAG
460 470 480 490 500
IHTNDINKAV DVSKRVKAGT VWINTYNNFH QNVPFGGFGQ SGIGREMGEA
510 520
ALSNYTQTKS VRIAIDKPIR
Length:520
Mass (Da):56,693
Last modified:July 27, 2011 - v4
Checksum:iDCD382A1157F800A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481I → T in AAB01220 (PubMed:9059631).Curated
Sequence conflicti90 – 901A → L in AAB01220 (PubMed:9059631).Curated
Sequence conflicti93 – 10412AFETK…IVEPE → LLKRSVYCRAG in AAB01220 (PubMed:9059631).CuratedAdd
BLAST
Sequence conflicti411 – 4111E → G in AAB64612 (PubMed:9169868).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56605 Genomic DNA. Translation: AAB01220.1.
U18814 Genomic DNA. Translation: AAB64612.1.
BK006939 Genomic DNA. Translation: DAA07732.2.
PIRiS50576.
RefSeqiNP_010996.2. NM_001178964.2.

Genome annotation databases

EnsemblFungiiYER073W; YER073W; YER073W.
GeneIDi856804.
KEGGisce:YER073W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56605 Genomic DNA. Translation: AAB01220.1.
U18814 Genomic DNA. Translation: AAB64612.1.
BK006939 Genomic DNA. Translation: DAA07732.2.
PIRiS50576.
RefSeqiNP_010996.2. NM_001178964.2.

3D structure databases

ProteinModelPortaliP40047.
SMRiP40047. Positions 9-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36816. 51 interactions.
DIPiDIP-3872N.
IntActiP40047. 9 interactions.
MINTiMINT-488437.

Proteomic databases

MaxQBiP40047.
PaxDbiP40047.
PeptideAtlasiP40047.
PRIDEiP40047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER073W; YER073W; YER073W.
GeneIDi856804.
KEGGisce:YER073W.

Organism-specific databases

EuPathDBiFungiDB:YER073W.
SGDiS000000875. ALD5.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP40047.
KOiK00128.
OMAiHRDSIES.
OrthoDBiEOG7S226Z.

Enzyme and pathway databases

UniPathwayiUPA00780; UER00768.
BioCyciMetaCyc:MONOMER-13665.
YEAST:MONOMER-13665.
YEAST:YER073W-MONOMER.

Miscellaneous databases

NextBioi983056.
PROiP40047.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR015657. Aminobutyraldehyde_DH.
[Graphical view]
PANTHERiPTHR11699:SF46. PTHR11699:SF46. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. 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.

Entry informationi

Entry nameiALDH5_YEAST
AccessioniPrimary (citable) accession number: P40047
Secondary accession number(s): D3DLX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 23300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.