NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 12424 / NRRL Y-610;
DOI=10.1016/S0378-1119(00)00310-3; PubMed=10974568 [NCBI, ExPASy, EBI, Israel, Japan]
Ladriere J.-M., Georis I., Guerineau M., Vandenhaute J.;
"Kluyveromyces marxianus exhibits an ancestral Saccharomyces cerevisiae genome organization downstream of ADH2.";
Gene 255:83-91(2000).

Comments

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

AF225206; AAF91235.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

SMR

Q9P4C2; 2-348.

ModBase

Q9P4C2.

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.

Other

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

Keywords

Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 348`	`347`	`Alcohol dehydrogenase 2.`	`PRO_0000160725`
`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).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`

Sequence information

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

Molecular weight: 36968 Da [This is the MW of the unprocessed precursor]

CRC64: 5083E01524DAFEC1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIPTTQKGV IFYENGGQLY YKDIPVPKPK SNELLINVKY SGVCHTDLHA WKGDWPLDTK 

        70         80         90        100        110        120 
LPLVGGHEGA GVVVAMGDNV KGWKIGDLAG IKWLNGSCMN CEECELSNES NCPDADLSGY 

       130        140        150        160        170        180 
THDGSFQQYA TADAVQAAHI PAGTDLAQVA PILCAGVTVY KALKTAEMKA GDWVAISGAA 

       190        200        210        220        230        240 
GGLGSLAVQY AKAMGFRVLG IDGGEGKEEL FKSLGGEVFI DFTKSKDIVG EVIKATNGGA 

       250        260        270        280        290        300 
HGVINVSVSE KAIESSIEYC RSNGTVVLVG LPKDAKCKSD VFNQVVKSIH IVGSYVGNRA 

       310        320        330        340 
DTREALDFFC RGLVNAPIKV VGLSTLPEIY EKMEQGKVLG RYVVDTSK

Q9P4C2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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