NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=NRRL 3357 / SRRC 167 / IAM 13836 / JCM 12722;
PubMed=8135521 [NCBI, ExPASy, EBI, Israel, Japan]
Woloshuk C.P., Payne G.A.;
"The alcohol dehydrogenase gene adh1 is induced in Aspergillus flavus grown on medium conducive to aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 60:670-676(1994).

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

L27434; AAA32684.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L27433; AAA32683.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

ModBase

P41747.

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

P41747.

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`	`1 349`	`349`	`Alcohol dehydrogenase 1.`	`PRO_0000160716`
`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).`

Sequence information

Length: 349 AA [This is the length of the unprocessed precursor]

Molecular weight: 36901 Da [This is the MW of the unprocessed precursor]

CRC64: F917FA2A03914E2F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIPEMQWAQ VAEQKGGPLI YKQIPVPKPG PDEILVKVRY SGVCHTDLHA LKGDWPLPVK 

        70         80         90        100        110        120 
MPLVGGHEGA GVVVARGDLV TEFEIGDHAG LKWLNGSCLA CEFCKQADEP LCPNASLSGY 

       130        140        150        160        170        180 
TVDGTFQQYA IGKATHASKL PKNVPLDAVA PVLCAGITVY KGLKESGVRP GQTVAIVGAG 

       190        200        210        220        230        240 
GGLGSLALQY AKAMGIRVVA IDGGEEKQAM CEQLGAEAYV DFTKTQDLVA DVKAATPEGL 

       250        260        270        280        290        300 
GAHAVILLAV AEKPFQQAAE YVSRGTVVAI GLPAGAFLRA PVFNTVVRMI NIKGSYVGNR 

       310        320        330        340 
QDGVEAVDFF ARGLIKAPFK TAPLQDLPKI FELMEQGKIA GRYVLEIPE

P41747 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