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Protein

Potassium-activated aldehyde dehydrogenase, mitochondrial

Gene

ALD4

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

Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose.1 Publication

Catalytic activityi

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei192 – 1921Transition state stabilizerBy similarity
Active sitei290 – 2901Proton acceptorPROSITE-ProRule annotation
Active sitei324 – 3241NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi268 – 2736NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: SGD
  2. aldehyde dehydrogenase [NAD(P)+] activity Source: SGD

GO - Biological processi

  1. acetate biosynthetic process Source: SGD
  2. ethanol metabolic process Source: SGD
  3. NADPH regeneration Source: SGD
  4. pyruvate metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciYEAST:YOR374W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-activated aldehyde dehydrogenase, mitochondrial (EC:1.2.1.5)
Alternative name(s):
K(+)-activated acetaldehyde dehydrogenase
Short name:
K(+)-ACDH
Gene namesi
Name:ALD4
Synonyms:ALD7, ALDH2
Ordered Locus Names:YOR374W
ORF Names:O6730
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR374w.
SGDiS000005901. ALD4.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. mitochondrial nucleoid Source: SGD
  2. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424Mitochondrion2 PublicationsAdd
BLAST
Chaini25 – 519495Potassium-activated aldehyde dehydrogenase, mitochondrialPRO_0000007165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Phosphoserine1 Publication
Modified residuei216 – 2161Phosphothreonine1 Publication
Modified residuei500 – 5001Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP46367.
PaxDbiP46367.
PeptideAtlasiP46367.
PRIDEiP46367.

Expressioni

Gene expression databases

GenevestigatoriP46367.

Interactioni

Protein-protein interaction databases

BioGridi34757. 27 interactions.
DIPiDIP-4053N.
IntActiP46367. 5 interactions.
MINTiMINT-539582.
STRINGi4932.YOR374W.

Structurei

3D structure databases

ProteinModelPortaliP46367.
SMRiP46367. Positions 31-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP46367.
KOiK00128.
OMAiICEIQEA.
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.
[Graphical view]
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.

P46367-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSRSTLCLK TSASSIGRLQ LRYFSHLPMT VPIKLPNGLE YEQPTGLFIN
60 70 80 90 100
NKFVPSKQNK TFEVINPSTE EEICHIYEGR EDDVEEAVQA ADRAFSNGSW
110 120 130 140 150
NGIDPIDRGK ALYRLAELIE QDKDVIASIE TLDNGKAISS SRGDVDLVIN
160 170 180 190 200
YLKSSAGFAD KIDGRMIDTG RTHFSYTKRQ PLGVCGQIIP WNFPLLMWAW
210 220 230 240 250
KIAPALVTGN TVVLKTAEST PLSALYVSKY IPQAGIPPGV INIVSGFGKI
260 270 280 290 300
VGEAITNHPK IKKVAFTGST ATGRHIYQSA AAGLKKVTLE LGGKSPNIVF
310 320 330 340 350
ADAELKKAVQ NIILGIYYNS GEVCCAGSRV YVEESIYDKF IEEFKAASES
360 370 380 390 400
IKVGDPFDES TFQGAQTSQM QLNKILKYVD IGKNEGATLI TGGERLGSKG
410 420 430 440 450
YFIKPTVFGD VKEDMRIVKE EIFGPVVTVT KFKSADEVIN MANDSEYGLA
460 470 480 490 500
AGIHTSNINT ALKVADRVNA GTVWINTYND FHHAVPFGGF NASGLGREMS
510
VDALQNYLQV KAVRAKLDE
Length:519
Mass (Da):56,724
Last modified:November 1, 1997 - v2
Checksum:iE7D9944EA25F948E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511N → NN AA sequence (PubMed:1989592)Curated
Sequence conflicti63 – 631E → V AA sequence (PubMed:1989592)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75282 Genomic DNA. Translation: CAA99705.1.
BK006948 Genomic DNA. Translation: DAA11133.1.
PIRiS67286.
RefSeqiNP_015019.1. NM_001183794.1.

Genome annotation databases

EnsemblFungiiYOR374W; YOR374W; YOR374W.
GeneIDi854556.
KEGGisce:YOR374W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75282 Genomic DNA. Translation: CAA99705.1.
BK006948 Genomic DNA. Translation: DAA11133.1.
PIRiS67286.
RefSeqiNP_015019.1. NM_001183794.1.

3D structure databases

ProteinModelPortaliP46367.
SMRiP46367. Positions 31-519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34757. 27 interactions.
DIPiDIP-4053N.
IntActiP46367. 5 interactions.
MINTiMINT-539582.
STRINGi4932.YOR374W.

Proteomic databases

MaxQBiP46367.
PaxDbiP46367.
PeptideAtlasiP46367.
PRIDEiP46367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR374W; YOR374W; YOR374W.
GeneIDi854556.
KEGGisce:YOR374W.

Organism-specific databases

CYGDiYOR374w.
SGDiS000005901. ALD4.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP46367.
KOiK00128.
OMAiICEIQEA.
OrthoDBiEOG7S226Z.

Enzyme and pathway databases

BioCyciYEAST:YOR374W-MONOMER.

Miscellaneous databases

NextBioi976985.

Gene expression databases

GenevestigatoriP46367.

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.
[Graphical view]
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. "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.
    , 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. 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. 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].

Entry informationi

Entry nameiALDH4_YEAST
AccessioniPrimary (citable) accession number: P46367
Secondary accession number(s): D6W367, Q08898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 22200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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