NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-40.
STRAIN=DSM 2334 / Var. Non-diastaticus;
DOI=10.1016/0167-4781(94)90199-6; PubMed=8049268 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson G.A., Bailey C.J., Dowds B.C.A.;
"Gene structure and amino acid sequences of alcohol dehydrogenases of Bacillus stearothermophilus.";
Biochim. Biophys. Acta 1218:432-434(1994).

Comments

FUNCTION: Active with primary alcohols, including methanol.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
ENZYME REGULATION: The rate-limiting step is NADH release. Catabolite repression.
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

Z25544; CAA80989.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S47643; S47643.

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

SMR

P42327; 1-338.

ModBase

P42327.

Ontologies

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.

Other

P42327; -.

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

Keywords

Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 339`	`339`	`Alcohol dehydrogenase.`	`PRO_0000160737`
`METAL`	`38 38`		`Zinc 1; catalytic (By similarity).`
`METAL`	`61 61`		`Zinc 1; catalytic (By similarity).`
`METAL`	`92 92`		`Zinc 2 (By similarity).`
`METAL`	`95 95`		`Zinc 2 (By similarity).`
`METAL`	`98 98`		`Zinc 2 (By similarity).`
`METAL`	`106 106`		`Zinc 2 (By similarity).`
`METAL`	`148 148`		`Zinc 1; catalytic (By similarity).`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 36205 Da [This is the MW of the unprocessed precursor]

CRC64: 0EC33CE7287D7476 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAAVVNEFK KALEIKEVER PKLEEGEVLV KIEACGVCHT DLHAAHGDWP IKPKLPLIPG 

        70         80         90        100        110        120 
HEGVGIVVEV AKGVKSIKVG DRVGIPWLYS ACGECEYCLT GQETLCPHQL NGGYSVDGGY 

       130        140        150        160        170        180 
AEYCKAPADY VAKIPDNLDP VEVAPILCAG VTTYKALKVS GARPGEWVAI YGIGGLGHIA 

       190        200        210        220        230        240 
LQYAKAMGLN VVAVDISDEK SKLAKDLGAD IAINGLKEDP VKAIHDQVGG VHAAISVAVN 

       250        260        270        280        290        300 
KKAFEQAYQS VKRGGTLVVV GLPNADLPIP IFDTVLNGVS VKGSIVGTRK DMQEALDFAA 

       310        320        330 
RGKVRPIVET AELEEINEVF ERMEKGKING RIVLKLKED

P42327 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