[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; PubMed=9546172 [NCBI, ExPASy, EBI, Israel, Japan] Cho J.Y., Jeffries T.W.; "Pichia stipitis genes for alcohol dehydrogenase with fermentative and respiratory functions."; Appl. Environ. Microbiol. 64:1350-1358(1998).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542; DOI=10.1002/(SICI)1097-0061(1998100)14:14<1311::AID-YEA315>3.3.CO;2-K; PubMed=9802210 [NCBI, ExPASy, EBI, Israel, Japan] Passoth V., Schaefer B., Liebel B., Weierstall T., Klinner U.; "Molecular cloning of alcohol dehydrogenase genes of the yeast Pichia stipitis and identification of the fermentative ADH."; Yeast 14:1311-1325(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545; DOI=10.1038/nbt1290; PubMed=17334359 [NCBI, ExPASy, EBI, Israel, Japan] Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.; "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."; Nat. Biotechnol. 25:319-326(2007).

Comments

FUNCTION: Converts ethanol to acetaldehyde and plays a major role in xylose fermentation.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
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

AF008245; AAC49991.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13397; CAA73827.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000496; ABN64893.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001382922.1; -.

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

SMR

O00097; 2-348.

ModBase

O00097.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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.

Genome annotation databases

GeneID

4836752; -.

KEGG

pic:PICST_68558; -.

Other

ProtoNet

O00097.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Alcohol dehydrogenase 1.`	`PRO_0000160727`
`NP_BIND`	`178 184`	`7`	`NAD (By similarity).`
`NP_BIND`	`269 271`	`3`	`NAD (By similarity).`
`METAL`	`44 44`		`Zinc 1; catalytic (By similarity).`
`METAL`	`67 67`		`Zinc 1; catalytic (By similarity).`
`METAL`	`98 98`		`Zinc 2 (By similarity).`
`METAL`	`101 101`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 2 (By similarity).`
`METAL`	`112 112`		`Zinc 2 (By similarity).`
`METAL`	`154 154`		`Zinc 1; catalytic (By similarity).`
`BINDING`	`202 202`		`NAD (By similarity).`
`BINDING`	`207 207`		`NAD (By similarity).`
`BINDING`	`341 341`		`NAD (By similarity).`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 36520 Da [This is the MW of the unprocessed precursor]

CRC64: 49C06B545D5350F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVPTTQKAV VFESNGGPLL YKDIPVPTPK PNEILINVKY SGVCHTDLHA WKGDWPLDTK 

        70         80         90        100        110        120 
LPLVGGHEGA GVVVGIGSNV TGWELGDYAG IKWLNGSCLN CEFCQHSDEP NCAKADLSGY 

       130        140        150        160        170        180 
THDGSFQQYA TADAVQAARL PKGTDLAQAA PILCAGITVY KALKTAQIQP GNWVCISGAG 

       190        200        210        220        230        240 
GGLGSLAIQY AKAMGFRVIA IDGGEEKGEF VKSLGAEAYV DFTVSKDIVK DIQTATDGGP 

       250        260        270        280        290        300 
HAAINVSVSE KAIAQSCQYV RSTGTVVLVG LPAGAKVVAP VFDAVVKSIS IRGSYVGNRA 

       310        320        330        340 
DSAEAIDFFT RGLIKCPIKV VGLSELPKVY ELMEAGKVIG RYVVDTSK

O00097 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