[1]	PROTEIN SEQUENCE. TISSUE=Liver; DOI=10.1021/bi00130a004; PubMed=1567829 [NCBI, ExPASy, EBI, Israel, Japan] Danielsson O., Eklund H., Joernvall H.; "The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenases of classes I and III."; Biochemistry 31:3751-3759(1992).
[2]	X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). TISSUE=Liver; PubMed=8845755 [NCBI, ExPASy, EBI, Israel, Japan] Ramaswamy S., el Ahmad M., Danielsson O., Joernvall H., Eklund H.; "Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments."; Protein Sci. 5:663-671(1996).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Functionally related to class-I mammalian enzymes, but structurally related to class-III.
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

PIR

A42343; A42343.

3D structure databases

PDB

1CDO; X-ray; 2.05 A; A/B=1-374.

[ExPASy / RCSB / EBI]

PDBsum

1CDO; -.

ModBase

P26325.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

P26325.

Phylogenomic databases

HOVERGEN

P26325; -.

Other

LinkHub

P26325; -.

UniRef

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

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 375`	`375`	`Alcohol dehydrogenase 1.`	`PRO_0000160679`
`METAL`	`46 46`		`Zinc 1; catalytic.`
`METAL`	`68 68`		`Zinc 1; catalytic.`
`METAL`	`98 98`		`Zinc 2.`
`METAL`	`101 101`		`Zinc 2.`
`METAL`	`104 104`		`Zinc 2.`
`METAL`	`112 112`		`Zinc 2.`
`METAL`	`175 175`		`Zinc 1; catalytic.`
`MOD_RES`	`1 1`		`N-acetylalanine.`
`STRAND`	`7 14`	`8`
`STRAND`	`22 28`	`7`
`STRAND`	`35 44`	`10`
`HELIX`	`47 54`	`8`
`STRAND`	`63 65`	`3`
`STRAND`	`70 77`	`8`
`STRAND`	`89 92`	`4`
`STRAND`	`99 101`	`3`
`HELIX`	`102 105`	`4`
`HELIX`	`116 118`	`3`
`TURN`	`121 124`	`4`
`STRAND`	`131 133`	`3`
`STRAND`	`136 140`	`5`
`HELIX`	`141 143`	`3`
`STRAND`	`147 154`	`8`
`HELIX`	`155 157`	`3`
`STRAND`	`158 160`	`3`
`HELIX`	`167 170`	`4`
`HELIX`	`171 174`	`4`
`HELIX`	`176 185`	`10`
`TURN`	`186 188`	`3`
`STRAND`	`195 199`	`5`
`HELIX`	`203 214`	`12`
`STRAND`	`218 223`	`6`
`HELIX`	`227 229`	`3`
`HELIX`	`230 235`	`6`
`STRAND`	`240 242`	`3`
`HELIX`	`244 246`	`3`
`HELIX`	`251 259`	`9`
`STRAND`	`263 268`	`6`
`HELIX`	`273 281`	`9`
`TURN`	`285 287`	`3`
`STRAND`	`289 292`	`4`
`STRAND`	`297 299`	`3`
`STRAND`	`301 303`	`3`
`HELIX`	`305 309`	`5`
`STRAND`	`313 316`	`4`
`HELIX`	`319 321`	`3`
`HELIX`	`324 336`	`13`
`HELIX`	`343 345`	`3`
`STRAND`	`346 351`	`6`
`HELIX`	`352 354`	`3`
`HELIX`	`355 363`	`9`
`STRAND`	`368 373`	`6`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 40128 Da [This is the MW of the unprocessed precursor]

CRC64: 0A8BDEAA0C9BCEAD [This is a checksum on the sequence]

        10         20         30         40         50         60 
ATVGKVIKCK AAVAWEANKP LVIEEIEVDV PHANEIRIKI IATGVCHTDL YHLFEGKHKD 

        70         80         90        100        110        120 
GFPVVLGHEG AGIVESVGPG VTEFQPGEKV IPLFISQCGE CRFCQSPKTN QCVKGWANES 

       130        140        150        160        170        180 
PDVMSPKETR FTCKGRKVLQ FLGTSTFSQY TVVNQIAVAK IDPSAPLDTV CLLGCGVSTG 

       190        200        210        220        230        240 
FGAAVNTAKV EPGSTCAVFG LGAVGLAAVM GCHSAGAKRI IAVDLNPDKF EKAKVFGATD 

       250        260        270        280        290        300 
FVNPNDHSEP ISQVLSKMTN GGVDFSLECV GNVGVMRNAL ESCLKGWGVS VLVGWTDLHD 

       310        320        330        340        350        360 
VATRPIQLIA GRTWKGSMFG GFKGKDGVPK MVKAYLDKKV KLDEFITHRM PLESVNDAID 

       370 
LMKHGKCIRT VLSLE

P26325 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