[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00016510; PubMed=2102855 [NCBI, ExPASy, EBI, Israel, Japan] Matton D.P., Constabel P., Brisson N.; "Alcohol dehydrogenase gene expression in potato following elicitor and stress treatment."; Plant Mol. Biol. 14:775-783(1990).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: By fungal elicitor.
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

M25154; AAA33806.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53242; CAA37333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11853; DEPOA1.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P14673.

Ontologies

GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
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.

Other

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`	`1 380`	`380`	`Alcohol dehydrogenase 1.`	`PRO_0000160712`
`METAL`	`48 48`		`Zinc 1 (catalytic) (By similarity).`
`METAL`	`70 70`		`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`	`178 178`		`Zinc 1 (catalytic) (By similarity).`
`CONFLICT`	`87 87`		`G -> A (in Ref. 1; CAA37333).`

Sequence information

Length: 380 AA [This is the length of the unprocessed precursor]

Molecular weight: 41094 Da [This is the MW of the unprocessed precursor]

CRC64: 624E75A168BCA9B3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTTVGQVIR CKAAVAWEAG KPLVMEEVDV APPQKMEVRL KILYTSLCHT DVYFWEAKGQ 

        70         80         90        100        110        120 
NPVFPRILGH EAAGIVESVG EGVTELGPGD HVLPVFTGEC KDCAHCKSEE SNMCSLLRIN 

       130        140        150        160        170        180 
TDRGVMINDG QSRFSINGKP IYHFVGTSTF SEYTVVHVGC VAKINPLAPL DKVCVLSCGI 

       190        200        210        220        230        240 
STGLGATLNV AKPTKGSSVA IFGLGAVGLA AAEGARIAGA SRIIGVDLNA SRFEQAKKFG 

       250        260        270        280        290        300 
VTEFVNPKDY SKPVQEVIAE MTDGGVDRSV ECTGHIDAMI SAFECVHDGW GVAVLVGVPH 

       310        320        330        340        350        360 
KEAVFKTHPM NLLNERTLKG TFFGNYKPRS DIPSVVEKYM NKELELEKFI THTLPFAEIN 

       370        380 
KAFDLMLKGE GLRCIITMED

P14673 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