[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[2]	CHARACTERIZATION. DOI=10.1002/(SICI)1097-0061(199907)15:10A<829::AID-YEA423>3.0.CO;2-9; PubMed=10407263 [NCBI, ExPASy, EBI, Israel, Japan] Navarro-Avino J.P., Prasad R., Miralles V.J., Benito R.M., Serrano R.; "A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces cerevisiae and characterization of the stress-inducible ALD2 and ALD3 genes."; Yeast 15:829-842(1999).
[3]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

CATALYTIC ACTIVITY: An aldehyde + NAD(P)⁺ + H₂O = an acid + NAD(P)H.
MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z49705; CAA89805.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S54527; S54527.

RefSeq

NP_013892.1; -.

3D structure databases

HSSP

Q28399; 1O9J. [HSSP ENTRY / PDB]

ModBase

P54114.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13668; -.

Organism-specific databases

YMR169c; -.

S000004779; ALD3.

Gene expression databases

ArrayExpress

P54114; -.

GermOnline

YMR169C; Saccharomyces cerevisiae.

Ontologies

GO:0004029;	Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from direct assay from SGD).
GO:0019483;	Biological process: beta-alanine biosynthetic process (inferred from mutant phenotype from SGD).
GO:0006598;	Biological process: polyamine catabolic process (inferred from genetic interaction from SGD).
GO:0006950;	Biological process: response to stress (inferred from expression pattern from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

P54114.

Proteomic databases

PeptideAtlas

P54114; -.

Genome annotation databases

Ensembl

YMR169C; Saccharomyces cerevisiae. [Contig view]

855205; -.

Z71257_GR; YMR169C.

sce:YMR169C; -.

fig|4932.3.peg.4942; -.

Phylogenomic databases

HOGENOM

P54114; -.

Other

P54114; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 506`	`506`	`Aldehyde dehydrogenase [NAD(P)+] 2.`	`PRO_0000056440`
`ACT_SITE`	`268 268`		`Proton acceptor (By similarity).`
`ACT_SITE`	`302 302`		`Nucleophile (By similarity).`
`SITE`	`169 169`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 506 AA [This is the length of the unprocessed precursor]

Molecular weight: 55385 Da [This is the MW of the unprocessed precursor]

CRC64: 11687E520B7E97DD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTLYTDIEI PQLKISLKQP LGLFINNEFC PSSDGKTIET VNPATGEPIT SFQAANEKDV 

        70         80         90        100        110        120 
DKAVKAARAA FDNVWSKTSS EQRGIYLSNL LKLIEEEQDT LAALETLDAG KPFHSNAKQD 

       130        140        150        160        170        180 
LAQIIELTRY YAGAVDKFNM GETIPLTFNK FAYTLKVPFG VVAQIVPWNY PLAMACRKMQ 

       190        200        210        220        230        240 
GALAAGNTVI IKPAENTSLS LLYFATLIKK AGFPPGVVNV IPGYGSVVGK ALGTHMDIDK 

       250        260        270        280        290        300 
ISFTGSTKVG GSVLEASGQS NLKDITLECG GKSPALVFED ADLDKAIEWV ANGIFFNSGQ 

       310        320        330        340        350        360 
ICTANSRVYV QSSIYDKFVE KFKETAKKEW DVAGKFDPFD EKCIVGPVIS STQYDRIKSY 

       370        380        390        400        410        420 
IERGKKEEKL DMFQTSEFPI GGAKGYFIPP TIFTDVPETS KLLRDEIFGP VVVVSKFTNY 

       430        440        450        460        470        480 
DDALKLANDT CYGLASAVFT KDVKKAHMFA RDIKAGTVWI NQTNQEEAKV PFGGFKMSGI 

       490        500 
GRESGDTGVD NYLQIKSVHV DLSLDK

P54114 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools