Reviewed, UniProtKB/Swiss-Prot P42328 (ADH3_BACST)

Names and origin

Protein names	Recommended name:     Alcohol dehydrogenase     EC=1.1.1.1 Alternative name(s):     ADH-HT
Organism	Bacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier	1422 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Thermophilic NAD+-dependent alcohol dehydrogenase. Bears mainly an ethanol-dehydrogenase activity.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
biophysicochemical properties	Temperature dependence: Thermostable.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 339

339

Alcohol dehydrogenase

PRO_0000160738

Regions

Nucleotide binding

172 – 177

6

NAD By similarity

Nucleotide binding

260 – 262

3

NAD By similarity

Sites

Metal binding

38

1

Zinc 1; catalytic By similarity

Metal binding

61

1

Zinc 1; catalytic By similarity

Metal binding

92

1

Zinc 2 By similarity

Metal binding

95

1

Zinc 2 By similarity

Metal binding

98

1

Zinc 2 By similarity

Metal binding

106

1

Zinc 2 By similarity

Metal binding

148

1

Zinc 1; catalytic By similarity

Binding site

195

1

NAD By similarity

Binding site

200

1

NAD By similarity

Binding site

331

1

NAD By similarity

Secondary structure

1

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339

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

14 – 17

4

Beta strand

27 – 37

11

Helix

39 – 46

8

Beta strand

49 – 51

3

Beta strand

55 – 57

3

Beta strand

63 – 70

8

Beta strand

82 – 85

4

Beta strand

87 – 90

4

Helix

96 – 99

4

Helix

103 – 105

3

Turn

112 – 114

3

Beta strand

119 – 127

9

Helix

128 – 130

3

Helix

140 – 143

4

Helix

144 – 146

3

Helix

149 – 160

12

Beta strand

167 – 171

5

Helix

177 – 186

10

Beta strand

190 – 194

5

Helix

198 – 206

9

Beta strand

210 – 213

4

Turn

215 – 217

3

Helix

220 – 228

9

Beta strand

229 – 238

10

Helix

241 – 250

10

Beta strand

251 – 259

9

Beta strand

264 – 270

7

Helix

271 – 276

6

Beta strand

280 – 283

4

Helix

289 – 300

12

Beta strand

308 – 312

5

Helix

313 – 315

3

Helix

316 – 324

9

Beta strand

329 – 335

7

Sequences

	Sequence		Length	Mass (Da)
	P42328-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: AED17E4A34163430	FASTA	339	36,338
	10 20 30 40 50 60 MKAAVVEQFK EPLKIKEVEK PTISYGEVLV RIKACGVCHT DLHAAHGDWP VKPKLPLIPG 70 80 90 100 110 120 HEGVGIVEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS GQETLCEHQK NAGYSVDGGY 130 140 150 160 170 180 AEYCRAAADY VVKIPDNLSF EEAAPIFCAG VTTYKALKVT GAKPGEWVAI YGIGGLGHVA 190 200 210 220 230 240 VQYAKAMGLN VVAVDIGDEK LELAKELGAD LVVNPLKEDA AKFMKEKVGG VHAAVVTAVS 250 260 270 280 290 300 KPAFQSAYNS IRRGGACVLV GLPPEEMPIP IFDTVLNGIK IIGSIVGTRK DLQEALQFAA 310 320 330 EGKVKTIIEV QPLEKINEVF DRMLKGQING RVVLTLEDK

References

[1]	"A few amino acid substitutions are responsible for the higher thermostability of a novel NAD(+)-dependent bacillar alcohol dehydrogenase." Cannio R., Rossi M., Bartolucci S. Eur. J. Biochem. 222:345-352(1994) [PubMed: 8020473] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIMB 12403 / LLD-R.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z27089 Genomic DNA. Translation: CAA81612.1.

PIR

S45605.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RJW	X-ray	2.35	A/B/C/D	1-339	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.1. 266715.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

PROSITE

PS00059. ADH_ZINC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ADH3_BACST

Accession

Primary (citable) accession number: P42328

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)