PROTEIN SEQUENCE.
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1993.tb18115.x; PubMed=8365416 [NCBI, ExPASy, EBI, Israel, Japan]
Persson B., Bergman T., Keung W.M., Waldenstroem U., Holmquist B., Vallee B.L., Joernvall H.;
"Basic features of class-I alcohol dehydrogenase: variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme.";
Eur. J. Biochem. 216:49-56(1993).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
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

S35669; S35669.

3D structure databases

HSSP

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

SMR

P80222; 1-374.

ModBase

P80222.

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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Phylogenomic databases

HOVERGEN

P80222; -.

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_0000160675`
`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`	`186 186`	`1`	`D -> T.`
`VARIANT`	`317 317`	`1`	`S -> T.`

Sequence information

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

Molecular weight: 39670 Da [This is the MW of the unprocessed precursor]

CRC64: 384BCB2D36E2FA32 [This is a checksum on the sequence]

        10         20         30         40         50         60 
STAGKVIKCK AAITWEIKKP FSIEEIEVAP PKAHEVRIKI LATGICRSDD HVTAGLLTMP 

        70         80         90        100        110        120 
LPMILGHEAA GVVESTGEGV TSLKPGDKVI PLFVPQCGEC MPCLKSNGNL CIRNDLGSPS 

       130        140        150        160        170        180 
GLMADGTSRF TCKGKDIHHF IGTSTFTEYT VVHETAVARI DAAAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAVKDAKVE PGSTCAVFGL GGVGLSTIMG CKAAGASRII GIDINKDKFA KAKELGATEC 

       250        260        270        280        290        300 
INPLDCKKPI QEVLSEMTGG GVDYSFEVIG RIDTMTAALA CCQDNYGTSV IVGVPPASEK 

       310        320        330        340        350        360 
ITFNPMMLFT GRTWKGSVFG GWKSKESVPK LVADYMEKKI NLDGLITHTL PFDKINEGFE 

       370 
LLRTGKSIRS VLTF

P80222 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