NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Violet 30;
DOI=10.1007/BF00036804; PubMed=1678286 [NCBI, ExPASy, EBI, Israel, Japan]
Gregerson R., McLean M., Beld M., Gerats A.G.M., Strommer J.;
"Structure, expression, chromosomal location and product of the gene encoding ADH1 in Petunia.";
Plant Mol. Biol. 17:37-48(1991).

Comments

FUNCTION: This protein is responsible for the conversion of alcohols to aldehydes in plants and is important for NAD metabolism during anaerobic respiration.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homodimer.
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

X54106; CAA38039.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S16596; DEPJA1.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P25141.

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.

ProtoNet

P25141.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`Alcohol dehydrogenase 1.`	`PRO_0000160711`
`METAL`	`49 49`		`Zinc 1; catalytic (By similarity).`
`METAL`	`71 71`		`Zinc 1; catalytic (By similarity).`
`METAL`	`101 101`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 2 (By similarity).`
`METAL`	`107 107`		`Zinc 2 (By similarity).`
`METAL`	`115 115`		`Zinc 2 (By similarity).`
`METAL`	`179 179`		`Zinc 1; catalytic (By similarity).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41574 Da [This is the MW of the unprocessed precursor]

CRC64: 43DFFE215650EDE0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSNTAGQVI RCKAAVAWEA GKPLVIEEVE VAPPQKMEVR LKILFTSLCH TDVYFWEAKG 

        70         80         90        100        110        120 
QTPLFPRIFG HEAGGIVESV GEGVTDLKPG DHVLPVFTGE CQQCRHCKSE ESNMCDLLRI 

       130        140        150        160        170        180 
NTDRGVMIHD GQTRFSKDGK PIYHFVGTST FSEYTVCHSG CVTKIDPQAP LDKVCVLSCG 

       190        200        210        220        230        240 
ISTGLGATLN VAKPTKGSTV AIFGLGAVGL AAAEGARIAG ASRIIGVDLN PSRFNDAKKF 

       250        260        270        280        290        300 
GVTEFVNPKD HGDKPVQQVI AEMTDGGVDR SVECTGNVNA MISAFECVHD GWGVAVLVGV 

       310        320        330        340        350        360 
PNKDDAFKTH PMNLLNERTL KGTFFGNYKP KSDIPSVVDK YMKKELELEK FITHQVPFSE 

       370        380 
INKAFDYMLK GESIRCMITM EH

P25141 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