Reviewed, UniProtKB/Swiss-Prot P25984 (ADH_CLOBE)

Names and origin

Protein names

Recommended name:
    NADP-dependent alcohol dehydrogenase
    EC=1.1.1.2
Alternative name(s):
    CbADH

Gene names

Name:

adh

Organism

Clostridium beijerinckii (Clostridium MP)

Taxonomic identifier

1520 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An alcohol + NADP+ = an aldehyde + NADPH.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Ligand	Metal-binding NADP Zinc
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase (NADP+) 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 – 351

351

NADP-dependent alcohol dehydrogenase

PRO_0000160739

Sites

Metal binding

37

1

Zinc; catalytic

Metal binding

59

1

Zinc; catalytic

Metal binding

60

1

Zinc; catalytic

Metal binding

150

1

Zinc; catalytic

Secondary structure

1

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351

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

11 – 16

6

Beta strand

27 – 34

8

Helix

38 – 46

9

Beta strand

53 – 56

4

Beta strand

61 – 68

8

Beta strand

80 – 83

4

Beta strand

90 – 92

3

Helix

93 – 96

4

Helix

100 – 102

3

Turn

106 – 109

4

Turn

113 – 115

3

Beta strand

119 – 128

10

Helix

129 – 132

4

Helix

142 – 146

5

Turn

147 – 150

4

Helix

151 – 161

11

Beta strand

170 – 173

4

Helix

177 – 187

11

Turn

188 – 190

3

Beta strand

194 – 197

4

Helix

201 – 210

10

Beta strand

213 – 216

4

Helix

218 – 220

3

Helix

223 – 230

8

Turn

231 – 233

3

Beta strand

236 – 241

6

Helix

248 – 255

8

Beta strand

256 – 264

9

Beta strand

270 – 277

8

Turn

278 – 281

4

Helix

282 – 284

3

Beta strand

289 – 293

5

Helix

298 – 310

13

Helix

316 – 319

4

Beta strand

320 – 326

7

Helix

327 – 329

3

Helix

330 – 339

10

Beta strand

345 – 350

6

Sequences

	Sequence		Length	Mass (Da)
	P25984-1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: E1E925D37D7513B7	FASTA	351	37,716
	10 20 30 40 50 60 MKGFAMLGIN KLGWIEKERP VAGSYDAIVR PLAVSPCTSD IHTVFEGALG DRKNMILGHE 70 80 90 100 110 120 AVGEVVEVGS EVKDFKPGDR VIVPCTTPDW RSLEVQAGFQ QHSNGMLAGW KFSNFKDGVF 130 140 150 160 170 180 GEYFHVNDAD MNLAILPKDM PLENAVMITD MMTTGFHGAE LADIQMGSSV VVIGIGAVGL 190 200 210 220 230 240 MGIAGAKLRG AGRIIGVGSR PICVEAAKFY GATDILNYKN GHIVDQVMKL TNGKGVDRVI 250 260 270 280 290 300 MAGGGSETLS QAVSMVKPGG IISNINYHGS GDALLIPRVE WGCGMAHKTI KGGLCPGGRL 310 320 330 340 350 RAEMLRDMVV YNRVDLSKLV THVYHGFDHI EEALLLMKDK PKDLIKAVVI L

References

[1]	"Cloning and sequence analysis of a gene encoding a medium-chain zinc-containing alcohol dehydrogenase from the Gram-positive anaerobe Clostridium beijerinckii NRRL B593." Rifaat M.M., Chen J.S. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NRRL B-593.
[2]	"Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii." Ismaiel A.A., Zhu C.X., Colby G.D., Chen J.S. J. Bacteriol. 175:5097-5105(1993) [PubMed: 8349550] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. Strain: NESTE 255 and NRRL B-593.
[3]	"NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii." Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. J. Mol. Biol. 278:967-981(1998) [PubMed: 9836873] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[4]	"Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging." Bogin O., Levin I., Hacham Y., Tel-Or S., Peretz M., Frolow F., Burstein Y. Protein Sci. 11:2561-2574(2002) [PubMed: 12381840] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF157307 Genomic DNA. Translation: AAA23199.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JQB	X-ray	1.97	A/B/C/D	1-351	[»]
1KEV	X-ray	2.05	A/B/C/D	1-351	[»]
1PED	X-ray	2.15	A/B/C/D	1-351	[»]
2B83	X-ray	2.25	A/B/C/D	1-351	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.2. 2864.

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

ADH_CLOBE

Accession

Primary (citable) accession number: P25984
Secondary accession number(s): Q9R559

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 4, 2007
Last modified:	June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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