[1]	PROTEIN SEQUENCE. TISSUE=Liver; DOI=10.1111/j.1432-1033.1994.00373.x; PubMed=7925350 [NCBI, ExPASy, EBI, Israel, Japan] Estonius M., Hjelmqvist L., Joernvall H.; "Diversity of vertebrate class I alcohol dehydrogenase. Mammalian and non-mammalian enzyme functions correlated through the structure of a ratite enzyme."; Eur. J. Biochem. 224:373-378(1994).
[2]	PROTEIN SEQUENCE OF 1-13, AND ACETYLATION AT SER-1. DOI=10.1016/0014-5793(96)00657-6; PubMed=8706859 [NCBI, ExPASy, EBI, Israel, Japan] Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.; "Alcoholytic deblocking of N-terminally acetylated peptides and proteins for sequence analysis."; FEBS Lett. 390:199-202(1996).
[3]	PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT SER-1. DOI=10.1016/0014-5793(95)00572-Q; PubMed=7607314 [NCBI, ExPASy, EBI, Israel, Japan] Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J., Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Jornvall H.; "Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme."; FEBS Lett. 367:237-240(1995).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

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

S48157; S48157.

3D structure databases

HSSP

P00327; 1HEU. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

SMR

P80338; 1-374.

ModBase

P80338.

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

P80338.

Phylogenomic databases

HOVERGEN

P80338; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 374`	`374`	`Alcohol dehydrogenase 1.`	`PRO_0000160674`
`METAL`	`46 46`		`Zinc 1; catalytic (By similarity).`
`METAL`	`67 67`		`Zinc 1; catalytic (By similarity).`
`METAL`	`97 97`		`Zinc 2 (By similarity).`
`METAL`	`100 100`		`Zinc 2 (By similarity).`
`METAL`	`103 103`		`Zinc 2 (By similarity).`
`METAL`	`111 111`		`Zinc 2 (By similarity).`
`METAL`	`174 174`		`Zinc 1; catalytic (By similarity).`
`MOD_RES`	`1 1`		`N-acetylserine.`
`VARIANT`	`112 112`	`1`	`R -> C.`

Sequence information

Length: 374 AA [This is the length of the unprocessed precursor]

Molecular weight: 39583 Da [This is the MW of the unprocessed precursor]

CRC64: 3ACC5386332EEC3C [This is a checksum on the sequence]

        10         20         30         40         50         60 
STAGKVIKCK AAVLWEPKKP FSIEEVEVAP PKAHEVRVKI IATGICRSDD HVISGVLVMP 

        70         80         90        100        110        120 
FPIILGHEAA GVVESVGEGV TSVKPGDKVI PLFVPQCGEC SVCLSTKGNL CRKNDIGPAS 

       130        140        150        160        170        180 
ALMPDGTSRF TCKGKAIHHF AGTSTFTEYT VLHETAVAKI DAAAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAALQTAKVE PGSTCAVFGL GGVGLSVVMG CKAAGASRII GVDINKDKFA KAKELGATDC 

       250        260        270        280        290        300 
VNPKDFTKPI HEVLMEMTGL GVDYSFEVIG HTETMAAALA SCHFNYGVSV IVGVPPAAEK 

       310        320        330        340        350        360 
LSFDPMLLFS GRTWKGSVFG GWKSKDSVPK LVADYMEKKF VLDPLITHTL PFHKINEGFD 

       370 
LLRTGKSIRS VLLF

P80338 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