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Protein

Magnesium-activated aldehyde dehydrogenase, cytosolic

Gene

ALD6

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

Cytosolic aldehyde dehydrogenase which utilizes NADP+ as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate.1 Publication

Catalytic activityi

An aldehyde + NADP+ + H2O = a carboxylate + NADPH.1 Publication

Kineticsi

  1. KM=40 µM for NADP (with acetaldehyde as cosubstrate)1 Publication
  2. KM=99 µM for NADP (with propionaldehyde as cosubstrate)1 Publication
  3. KM=17.4 mM for NAD (with propionaldehyde as cosubstrate)1 Publication
  4. KM=24 µM for acetaldehyde (with NADP as cosubstrate)1 Publication
  5. KM=30 µM for propionaldehyde (with NADP as cosubstrate)1 Publication
  6. KM=0.7 mM for propionaldehyde (with NAD as cosubstrate)1 Publication
  1. Vmax=24 µmol/min/mg enzyme with acetaldehyde and NADP as substrates1 Publication
  2. Vmax=14 µmol/min/mg enzyme with propionaldehyde and NADP as substrates1 Publication
  3. Vmax=8.3 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
Sitei173 – 1731Transition state stabilizerBy similarity
Active sitei272 – 2721Proton acceptorPROSITE-ProRule annotation
Active sitei306 – 3061NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi249 – 2546NADBy similarity

GO - Molecular functioni

GO - Biological processi

  • acetate biosynthetic process Source: SGD
  • ethanol catabolic process Source: UniProtKB-UniPathway
  • NADPH regeneration Source: SGD
  • response to salt stress Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Magnesium, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13664.
YEAST:MONOMER-13664.
YEAST:YPL061W-MONOMER.
UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium-activated aldehyde dehydrogenase, cytosolic (EC:1.2.1.4)
Alternative name(s):
Mg(2+)-activated acetaldehyde dehydrogenase
Short name:
Mg(2+)-ACDH
Gene namesi
Name:ALD6
Synonyms:ALDH1
Ordered Locus Names:YPL061W
ORF Names:LPE9
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL061W.
SGDiS000005982. ALD6.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 500499Magnesium-activated aldehyde dehydrogenase, cytosolicPRO_0000056441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki3 – 3Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP54115.
PaxDbiP54115.
PeptideAtlasiP54115.
PRIDEiP54115.

Interactioni

Protein-protein interaction databases

BioGridi36117. 78 interactions.
DIPiDIP-8324N.
IntActiP54115. 26 interactions.
MINTiMINT-500664.

Structurei

3D structure databases

ProteinModelPortaliP54115.
SMRiP54115. Positions 28-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP54115.
KOiK00128.
OMAiKAWKPGN.
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.
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.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P54115-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKLHFDTAE PVKITLPNGL TYEQPTGLFI NNKFMKAQDG KTYPVEDPST
60 70 80 90 100
ENTVCEVSSA TTEDVEYAIE CADRAFHDTE WATQDPRERG RLLSKLADEL
110 120 130 140 150
ESQIDLVSSI EALDNGKTLA LARGDVTIAI NCLRDAAAYA DKVNGRTINT
160 170 180 190 200
GDGYMNFTTL EPIGVCGQII PWNFPIMMLA WKIAPALAMG NVCILKPAAV
210 220 230 240 250
TPLNALYFAS LCKKVGIPAG VVNIVPGPGR TVGAALTNDP RIRKLAFTGS
260 270 280 290 300
TEVGKSVAVD SSESNLKKIT LELGGKSAHL VFDDANIKKT LPNLVNGIFK
310 320 330 340 350
NAGQICSSGS RIYVQEGIYD ELLAAFKAYL ETEIKVGNPF DKANFQGAIT
360 370 380 390 400
NRQQFDTIMN YIDIGKKEGA KILTGGEKVG DKGYFIRPTV FYDVNEDMRI
410 420 430 440 450
VKEEIFGPVV TVAKFKTLEE GVEMANSSEF GLGSGIETES LSTGLKVAKM
460 470 480 490 500
LKAGTVWINT YNDFDSRVPF GGVKQSGYGR EMGEEVYHAY TEVKAVRIKL
Length:500
Mass (Da):54,414
Last modified:January 23, 2007 - v4
Checksum:i542AA956EFA0E676
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211L → FK in AAB01219 (PubMed:9473035).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56604 Genomic DNA. Translation: AAB01219.1.
U39205 Genomic DNA. Translation: AAB68304.1.
BK006949 Genomic DNA. Translation: DAA11369.1.
PIRiS60929.
RefSeqiNP_015264.1. NM_001183875.1.

Genome annotation databases

EnsemblFungiiYPL061W; YPL061W; YPL061W.
GeneIDi856044.
KEGGisce:YPL061W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56604 Genomic DNA. Translation: AAB01219.1.
U39205 Genomic DNA. Translation: AAB68304.1.
BK006949 Genomic DNA. Translation: DAA11369.1.
PIRiS60929.
RefSeqiNP_015264.1. NM_001183875.1.

3D structure databases

ProteinModelPortaliP54115.
SMRiP54115. Positions 28-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36117. 78 interactions.
DIPiDIP-8324N.
IntActiP54115. 26 interactions.
MINTiMINT-500664.

Proteomic databases

MaxQBiP54115.
PaxDbiP54115.
PeptideAtlasiP54115.
PRIDEiP54115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL061W; YPL061W; YPL061W.
GeneIDi856044.
KEGGisce:YPL061W.

Organism-specific databases

EuPathDBiFungiDB:YPL061W.
SGDiS000005982. ALD6.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
InParanoidiP54115.
KOiK00128.
OMAiKAWKPGN.
OrthoDBiEOG7S226Z.

Enzyme and pathway databases

UniPathwayiUPA00780; UER00768.
BioCyciMetaCyc:MONOMER-13664.
YEAST:MONOMER-13664.
YEAST:YPL061W-MONOMER.

Miscellaneous databases

NextBioi980989.
PROiP54115.

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.
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.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: DBY939.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway."
    Norbeck J., Blomberg A.
    J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-79 AND 482-488.
    Strain: ATCC 44827 / SKQ2N.
  5. "The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase."
    Meaden P.G., Dickinson F.M., Mifsud A., Tessier W., Westwater J., Bussey H., Midgley M.
    Yeast 13:1319-1327(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3.
    Strain: SUB592.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiALDH6_YEAST
AccessioniPrimary (citable) accession number: P54115
Secondary accession number(s): D6W3V3, Q02782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 144 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 135000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.