[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS. STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924; PubMed=1735726 [NCBI, ExPASy, EBI, Israel, Japan] Sakoda H., Imanaka T.; "Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and rational shift of the optimum pH."; J. Bacteriol. 174:1397-1402(1992).
[2]	PROTEIN SEQUENCE OF 1-45. DOI=10.1016/0014-5793(73)80144-9; PubMed=4578954 [NCBI, ExPASy, EBI, Israel, Japan] Bridgen J., Kolb E., Harris J.I.; "Amino acid sequence homology in alcohol dehydrogenase."; FEBS Lett. 33:1-3(1973).
[3]	PROTEIN SEQUENCE OF 34-54. PubMed=436831 [NCBI, ExPASy, EBI, Israel, Japan] Jeck R., Woenckhaus C., Harris J.I., Runswick M.J.; "Identification of the amino acid residue modified in Bacillus stearothermophilus alcohol dehydrogenase by the NAD+ analogue 4-(3-bromoacetylpyridinio)butyldiphosphoadenosine."; Eur. J. Biochem. 93:57-64(1979).
[4]	PROTEIN SEQUENCE OF 1-37; 188-197; 247-263 AND 324-336. STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924; 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: NAD(+)-dependent alcohol dehydrogenase.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
ENZYME REGULATION: Substrate inhibition is not observed with any alcohols, and the enzyme-NADH dissociation is not considered to be a rate-limiting step.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Thermostable;
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

D90421; BAA14411.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42654; A42654.

3D structure databases

HSSP

P39462; 1JVB. [HSSP ENTRY / PDB]

SMR

P12311; 1-337.

ModBase

P12311.

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

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 337`	`337`	`Alcohol dehydrogenase.`	`PRO_0000160736`
`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).`
`MUTAGEN`	`38 38`		`C->S: No activity.`
`MUTAGEN`	`40 40`		`T->A: No activity.`
`MUTAGEN`	`40 40`		`T->S: Little decrease in activity.`
`MUTAGEN`	`43 43`		`H->A: No activity.`
`MUTAGEN`	`43 43`		`H->R: Higher level of activity at pH 9.`
`CONFLICT`	`22 22`		`Missing (in Ref. 2; AA sequence).`
`CONFLICT`	`33 33`		`Missing (in Ref. 2; AA sequence).`
`CONFLICT`	`52 53`		`KP -> PK (in Ref. 3; AA sequence).`

Sequence information

Length: 337 AA [This is the length of the unprocessed precursor]

Molecular weight: 36100 Da [This is the MW of the unprocessed precursor]

CRC64: B9B35A80EE9B7A86 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKAAVVEQFK KPLQVKEVEK PKISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG 

        70         80         90        100        110        120 
HEGVGVIEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCERQQ NAGYSVDGGY 

       130        140        150        160        170        180 
AEYCRAAADY VVKIPDNLSF EEAAPIFCAG VTTYKALKVT GAKPGEWVAI YGIGGLGHVA 

       190        200        210        220        230        240 
VQYAKAMGLN VVAVDLGDEK LELAKQLGAD LVVNPKHDDA AQWIKEKVGG VHATVVTAVS 

       250        260        270        280        290        300 
KAAFESAYKS IRRGGACVLV GLPPEEIPIP IFDTVLNGVK IIGSIVGTRK DLQEALQFAA 

       310        320        330 
EGKVKTIVEV QPLENINDVF DRMLKGQING RVVLKVD

P12311 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