[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]	CRYSTALLIZATION. DOI=10.1107/S090744490201661X; PubMed=12554944 [NCBI, ExPASy, EBI, Israel, Japan] Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I., Pares X., Ochoa W.F.; "Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi."; Acta Crystallogr. D 59:334-337(2003).
[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).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan] Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.; "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."; Mol. Cell. Proteomics 4:310-327(2005).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-131; SER-210 AND SER-359, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

Comments

FUNCTION: NADP-dependent alcohol dehydrogenase with a broad substrate specificity.
CATALYTIC ACTIVITY: An alcohol + NADP⁺ = an aldehyde + NADPH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
MISCELLANEOUS: Present with 21700 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the zinc-containing alcohol 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

Z54141; CAA90836.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S59311; S59311.

RefSeq

NP_014051.1; -.

3D structure databases

PDB

1PIW; X-ray; 3.00 A; A/B=1-360.	[ExPASy / RCSB / EBI]
1PS0; X-ray; 3.01 A; A=1-360.	[ExPASy / RCSB / EBI]
1Q1N; X-ray; 3.15 A; A=1-360.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1PIW; -.
1PS0; -.
1Q1N; -.

ModBase

Q04894.

Protein-protein interaction databases

DIP

DIP:6308N; -.

IntAct

Q04894; -.

Organism-specific databases

YMR318c; -.

S000004937; ADH6.

Gene expression databases

ArrayExpress

Q04894; -.

GermOnline

YMR318C; Saccharomyces cerevisiae.

Ontologies

GO:0005625;	Cellular component: soluble fraction (inferred from direct assay from SGD).
GO:0008106;	Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0033833;	Molecular function: hydroxymethylfurfural reductase (NADH) activity (inferred from mutant phenotype from SGD).
GO:0033845;	Molecular function: hydroxymethylfurfural reductase (NADPH) activity (inferred from mutant phenotype from SGD).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006066;	Biological process: cellular alcohol metabolic process (inferred from direct assay from SGD).
GO:0033859;	Biological process: furaldehyde metabolic process (inferred from mutant phenotype from SGD).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

Q04894.

Proteomic databases

PeptideAtlas

Q04894; -.

Genome annotation databases

Ensembl

YMR318C; Saccharomyces cerevisiae. [Contig view]

855368; -.

Z71257_GR; YMR318C.

sce:YMR318C; -.

fig|4932.3.peg.5111; -.

Phylogenomic databases

HOGENOM

Q04894; -.

Other

LinkHub

Q04894; -.

NextBio

979148; -.

UniRef

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

Keywords

3D-structure; Complete proteome; Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 360`	`360`	`NADP-dependent alcohol dehydrogenase 6.`	`PRO_0000160734`
`METAL`	`46 46`		`Zinc 1; catalytic (By similarity).`
`METAL`	`68 68`		`Zinc 1; catalytic (By similarity).`
`METAL`	`100 100`		`Zinc 2 (By similarity).`
`METAL`	`103 103`		`Zinc 2 (By similarity).`
`METAL`	`106 106`		`Zinc 2 (By similarity).`
`METAL`	`114 114`		`Zinc 2 (By similarity).`
`METAL`	`163 163`		`Zinc 1; catalytic (By similarity).`
`MOD_RES`	`122 122`		`Phosphoserine.`
`MOD_RES`	`131 131`		`Phosphoserine.`
`MOD_RES`	`210 210`		`Phosphoserine.`
`MOD_RES`	`359 359`		`Phosphoserine.`
`TURN`	`3 5`	`3`
`STRAND`	`7 12`	`6`
`STRAND`	`15 17`	`3`
`STRAND`	`22 26`	`5`
`STRAND`	`35 45`	`11`
`HELIX`	`47 53`	`7`
`TURN`	`54 57`	`4`
`STRAND`	`62 64`	`3`
`STRAND`	`70 77`	`8`
`STRAND`	`90 93`	`4`
`STRAND`	`95 98`	`4`
`HELIX`	`104 107`	`4`
`HELIX`	`111 113`	`3`
`STRAND`	`118 122`	`5`
`STRAND`	`134 142`	`9`
`HELIX`	`143 145`	`3`
`STRAND`	`146 148`	`3`
`HELIX`	`155 158`	`4`
`HELIX`	`159 162`	`4`
`HELIX`	`164 174`	`11`
`STRAND`	`182 186`	`5`
`HELIX`	`190 202`	`13`
`STRAND`	`205 213`	`9`
`HELIX`	`216 221`	`6`
`STRAND`	`225 229`	`5`
`HELIX`	`230 232`	`3`
`HELIX`	`236 239`	`4`
`STRAND`	`244 249`	`6`
`TURN`	`259 261`	`3`
`HELIX`	`262 265`	`4`
`STRAND`	`266 274`	`9`
`STRAND`	`284 286`	`3`
`HELIX`	`288 290`	`3`
`STRAND`	`295 298`	`4`
`HELIX`	`304 316`	`13`
`STRAND`	`323 329`	`7`
`HELIX`	`330 342`	`13`
`STRAND`	`346 352`	`7`
`HELIX`	`355 358`	`4`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 39618 Da [This is the MW of the unprocessed precursor]

CRC64: 3F785BE0C5ED8CF1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYPEKFEGI AIQSHEDWKN PKKTKYDPKP FYDHDIDIKI EACGVCGSDI HCAAGHWGNM 

        70         80         90        100        110        120 
KMPLVVGHEI VGKVVKLGPK SNSGLKVGQR VGVGAQVFSC LECDRCKNDN EPYCTKFVTT 

       130        140        150        160        170        180 
YSQPYEDGYV SQGGYANYVR VHEHFVVPIP ENIPSHLAAP LLCGGLTVYS PLVRNGCGPG 

       190        200        210        220        230        240 
KKVGIVGLGG IGSMGTLISK AMGAETYVIS RSSRKREDAM KMGADHYIAT LEEGDWGEKY 

       250        260        270        280        290        300 
FDTFDLIVVC ASSLTDIDFN IMPKAMKVGG RIVSISIPEQ HEMLSLKPYG LKAVSISYSA 

       310        320        330        340        350        360 
LGSIKELNQL LKLVSEKDIK IWVETLPVGE AGVHEAFERM EKGDVRYRFT LVGYDKEFSD

Q04894 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