Reviewed, UniProtKB/Swiss-Prot P00327 (ADH1E_HORSE)

Names and origin

Protein names	Recommended name:     Alcohol dehydrogenase E chain     EC=1.1.1.1
Organism	Equus caballus (Horse)
Taxonomic identifier	9796 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit.
Subunit structure	Dimer of identical or non-identical chains of two types (E and S) coded by 2 separate genes at different loci.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
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 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

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 375

374

Alcohol dehydrogenase E chain

PRO_0000160656

Regions

Nucleotide binding

200 – 205

6

NAD

Nucleotide binding

293 – 295

3

NAD

Sites

Metal binding

47

1

Zinc 1; catalytic Ref.3

Metal binding

68

1

Zinc 1; catalytic Ref.3

Metal binding

98

1

Zinc 2 Ref.3

Metal binding

101

1

Zinc 2 Ref.3

Metal binding

104

1

Zinc 2 Ref.3

Metal binding

112

1

Zinc 2 Ref.3

Metal binding

175

1

Zinc 1; catalytic

Binding site

224

1

NAD

Binding site

229

1

NAD

Binding site

370

1

NAD

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.2

Secondary structure

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375

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Beta strand

23 – 29

7

Beta strand

36 – 45

10

Helix

48 – 54

7

Beta strand

62 – 65

4

Beta strand

69 – 77

9

Beta strand

89 – 92

4

Beta strand

99 – 101

3

Helix

102 – 105

4

Beta strand

106 – 108

3

Beta strand

116 – 119

4

Beta strand

130 – 133

4

Beta strand

136 – 139

4

Turn

142 – 144

3

Beta strand

147 – 154

8

Helix

155 – 157

3

Beta strand

158 – 160

3

Helix

167 – 170

4

Helix

171 – 174

4

Helix

176 – 185

10

Turn

186 – 188

3

Beta strand

195 – 199

5

Helix

203 – 214

12

Beta strand

218 – 223

6

Helix

227 – 229

3

Helix

230 – 236

7

Beta strand

239 – 242

4

Helix

244 – 246

3

Helix

251 – 258

8

Beta strand

263 – 268

6

Helix

273 – 282

10

Turn

285 – 287

3

Beta strand

289 – 292

4

Beta strand

302 – 304

3

Helix

307 – 310

4

Beta strand

314 – 317

4

Helix

320 – 322

3

Helix

325 – 337

13

Helix

344 – 346

3

Beta strand

347 – 352

6

Helix

353 – 355

3

Helix

356 – 364

9

Beta strand

369 – 374

6

Sequences

	Sequence		Length	Mass (Da)
	P00327-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: DA701D2F6AB69C9D	FASTA	375	39,936
	10 20 30 40 50 60 MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHVVSGTLVT 70 80 90 100 110 120 PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK CRVCKHPEGN FCLKNDLSMP 130 140 150 160 170 180 RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY TVVDEISVAK IDAASPLEKV CLIGCGFSTG 190 200 210 220 230 240 YGSAVKVAKV TQGSTCAVFG LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE 250 260 270 280 290 300 CVNPQDYKKP IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ 310 320 330 340 350 360 NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV LPFEKINEGF 370 DLLRSGESIR TILTF

References

[1]	"Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites." Park D.H., Plapp B.V. J. Biol. Chem. 266:13296-13302(1991) [PubMed: 1712777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes." Joernvall H. Eur. J. Biochem. 16:41-49(1970) [PubMed: 5466062] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-375. Tissue: Liver.
[3]	"Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A resolution." Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I., Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A. J. Mol. Biol. 102:27-59(1976) [PubMed: 178875] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]	"Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase." Eklund H., Samama J.-P., Jones T.A. Biochemistry 23:5982-5996(1984) [PubMed: 6098306] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[5]	"Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8-A resolution." Al-Karadaghi S., Cedergren-Zeppezauer E.S., Hovmoeller S., Petratos K., Terry H., Wilson K.S. Acta Crystallogr. D 50:793-807(1994) [PubMed: 15299346] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M64864 mRNA. Translation: AAA30931.1.

PIR

DEHOAL. A39872.

RefSeq

NP_001075997.1.

UniGene

Eca.13382

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A71	X-ray	2.00	A/B	2-374	[»]
1A72	X-ray	2.60	A	2-374	[»]
1ADB	X-ray	2.40	A/B	2-374	[»]
1ADC	X-ray	2.70	A/B	2-374	[»]
1ADF	X-ray	2.90	A	2-374	[»]
1ADG	X-ray	2.70	A	2-374	[»]
1AXE	X-ray	2.00	A/B	2-374	[»]
1AXG	X-ray	2.50	A/B/C/D	2-374	[»]
1BTO	X-ray	2.00	A/B/C/D	2-374	[»]
1HET	X-ray	1.15	A/B	2-375	[»]
1HEU	X-ray	1.15	A/B	2-375	[»]
1HF3	X-ray	1.95	A/B	2-375	[»]
1HLD	X-ray	2.10	A/B	2-374	[»]
1JU9	X-ray	2.00	A/B	2-374	[»]
1LDE	X-ray	2.50	A/B/C/D	2-374	[»]
1LDY	X-ray	2.50	A/B/C/D	2-374	[»]
1MG0	X-ray	1.80	A/B/C/D	2-374	[»]
1MGO	X-ray	1.20	A/B	2-374	[»]
1N8K	X-ray	1.13	A/B	2-374	[»]
1N92	X-ray	1.47	A/B	2-374	[»]
1P1R	X-ray	1.57	A/B/C/D	2-374	[»]
1QLH	X-ray	2.07	A	2-375	[»]
1QLJ	X-ray	2.80	A	2-375	[»]
1QV6	X-ray	1.80	A/B	2-374	[»]
1QV7	X-ray	1.80	A/B	2-374	[»]
1YE3	X-ray	1.59	A	2-374	[»]
2JHF	X-ray	1.00	A/B	2-374	[»]
2JHG	X-ray	1.20	A/B	2-374	[»]
2OHX	X-ray	1.80	A/B	2-375	[»]
2OXI	X-ray	2.10	A/B	2-374	[»]
3BTO	X-ray	1.66	A/B/C/D	2-374	[»]
5ADH	X-ray	2.90	A	2-374	[»]
6ADH	X-ray	2.90	A/B	2-374	[»]
7ADH	X-ray	3.20	A	2-374	[»]
8ADH	X-ray	2.40	A	2-374	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSECAG00000019267. Equus caballus. [Contig view]

GeneID

100034242.

KEGG

ecb:100034242.

Phylogenomic databases

HOVERGEN

P00327.

Enzyme and pathway databases

BRENDA

1.1.1.1. 1464.

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...

Other Resources

DrugBank

DB01093. Dimethyl sulfoxide.

Entry information

Entry name

ADH1E_HORSE

Accession

Primary (citable) accession number: P00327

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)