P54115 (ALDH6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Magnesium-activated aldehyde dehydrogenase, cytosolic
EC=1.2.1.3

Alternative name(s):
Mg(2+)-activated acetaldehyde dehydrogenase
Short name=Mg(2+)-ACDH

Gene names

Name:	ALD6
Synonyms:	ALDH1
Ordered Locus Names:	YPL061W
ORF Names:	LPE9

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	500 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)

Catalytic activity	An aldehyde + NAD+ + H2O = a carboxylate + NADH.
Pathway	Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 135000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium NAD
Molecular function	Oxidoreductase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADPH regeneration Inferred from genetic interaction PubMed 12584194. Source: SGD acetate biosynthetic process Inferred from mutant phenotype PubMed 11870853. Source: SGD ethanol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to salt stress Inferred from mutant phenotype PubMed 15146068. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 16806052. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16806052PubMed 16823961. Source: SGD
Molecular_function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase [NAD(P)+] activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 500	499	Magnesium-activated aldehyde dehydrogenase, cytosolic		PRO_0000056441
Regions
	Nucleotide binding	249 – 254	6	NAD By similarity
Sites
	Active site	272	1	Proton acceptor By similarity
	Active site	306	1	Nucleophile By similarity
	Site	173	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	250	1	Phosphoserine Ref.9
	Modified residue	251	1	Phosphothreonine Ref.9
	Modified residue	262	1	Phosphoserine Ref.9
	Modified residue	491	1	Phosphothreonine Ref.8
	Cross-link	3		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Experimental info
	Sequence conflict	121	1	L → FK in AAB01219. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P54115 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 542AA956EFA0E676	FASTA	500	54,414
	10 20 30 40 50 60 MTKLHFDTAE PVKITLPNGL TYEQPTGLFI NNKFMKAQDG KTYPVEDPST ENTVCEVSSA 70 80 90 100 110 120 TTEDVEYAIE CADRAFHDTE WATQDPRERG RLLSKLADEL ESQIDLVSSI EALDNGKTLA 130 140 150 160 170 180 LARGDVTIAI NCLRDAAAYA DKVNGRTINT GDGYMNFTTL EPIGVCGQII PWNFPIMMLA 190 200 210 220 230 240 WKIAPALAMG NVCILKPAAV TPLNALYFAS LCKKVGIPAG VVNIVPGPGR TVGAALTNDP 250 260 270 280 290 300 RIRKLAFTGS TEVGKSVAVD SSESNLKKIT LELGGKSAHL VFDDANIKKT LPNLVNGIFK 310 320 330 340 350 360 NAGQICSSGS RIYVQEGIYD ELLAAFKAYL ETEIKVGNPF DKANFQGAIT NRQQFDTIMN 370 380 390 400 410 420 YIDIGKKEGA KILTGGEKVG DKGYFIRPTV FYDVNEDMRI VKEEIFGPVV TVAKFKTLEE 430 440 450 460 470 480 GVEMANSSEF GLGSGIETES LSTGLKVAKM LKAGTVWINT YNDFDSRVPF GGVKQSGYGR 490 500 EMGEEVYHAY TEVKAVRIKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], CHARACTERIZATION. 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 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"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].
[7]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3, MASS SPECTROMETRY. Strain: SUB592.
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-491, MASS SPECTROMETRY.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250; THR-251 AND SER-262, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U56604 Genomic DNA. Translation: AAB01219.1. U39205 Genomic DNA. Translation: AAB68304.1. BK006949 Genomic DNA. Translation: DAA11369.1.
PIR	S60929.
RefSeq	NP_015264.1. NM_001183875.1.
3D structure databases
ProteinModelPortal	P54115.
SMR	P54115. Positions 28-500.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-8324N.
IntAct	P54115. 21 interactions.
MINT	MINT-500664.
STRING	4932.YPL061W.
Proteomic databases
PaxDb	P54115.
PeptideAtlas	P54115.
PRIDE	P54115.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YPL061W; YPL061W; YPL061W.
GeneID	856044.
KEGG	sce:YPL061W.
Organism-specific databases
SGD	S000005982. ALD6.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	ENSGT00550000074289.
HOGENOM	HOG000271505.
KO	K00128.
OMA	TCLTIGR.
OrthoDB	EOG4FN7S7.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13664.
UniPathway	UPA00780; UER00768.
Gene expression databases
ArrayExpress	P54115.
Genevestigator	P54115.
GermOnline	YPL061W. 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. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980989.

Entry information

Entry name

ALDH6_YEAST

Accession

Primary (citable) accession number: P54115
Secondary accession number(s): D6W3V3, Q02782

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program