PROTEIN SEQUENCE.
TISSUE=Liver;
DOI=10.1021/bi00225a011; PubMed=2007119 [NCBI, ExPASy, EBI, Israel, Japan]
Cederlund E., Peralba J.M., Pares X., Joernvall H.;
"Amphibian alcohol dehydrogenase, the major frog liver enzyme. Relationships to other forms and assessment of an early gene duplication separating vertebrate class I and class III alcohol dehydrogenases.";
Biochemistry 30:2811-2816(1991).

[2]

PROTEIN SEQUENCE OF 1-5.
DOI=10.1016/0014-5793(90)81152-E; PubMed=2387402 [NCBI, ExPASy, EBI, Israel, Japan]
Egestad B., Estonius M., Danielsson O., Persson B., Cederlund E., Kaiser R., Holmquist B., Vallee B., Pares X., Jefferey J., Joernvall H.;
"Fast atom bombardment mass spectrometry and chemical analysis in determinations of acyl-blocked protein structures.";
FEBS Lett. 269:194-196(1990).

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	A38405; A38405. S11075; S11075.
3D structure databases
HSSP	P00326; 1HT0. [HSSP ENTRY / PDB]
SMR	P22797; 1-375.
ModBase	P22797.
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.
BLOCKS	P22797.
Phylogenomic databases
HOVERGEN	P22797; -.
Other
ProtoNet	P22797.
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`	`1 375`	`375`	`Alcohol dehydrogenase 1.`	`PRO_0000160680`
`METAL`	`46 46`		`Zinc 1; catalytic (By similarity).`
`METAL`	`68 68`		`Zinc 1; catalytic (By similarity).`
`METAL`	`98 98`		`Zinc 2 (By similarity).`
`METAL`	`101 101`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 2 (By similarity).`
`METAL`	`112 112`		`Zinc 2 (By similarity).`
`METAL`	`175 175`		`Zinc 1; catalytic (By similarity).`
`MOD_RES`	`1 1`		`N-acetylalanine.`

Sequence information

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

Molecular weight: 40185 Da [This is the MW of the unprocessed precursor]

CRC64: 283E0A60E3339195 [This is a checksum on the sequence]

        10         20         30         40         50         60 
ATAGKVIKCK AAVCWGPKQP LSIEEIEVAP PKRHEVRVKI VATGICRSDD HVISGALSDM 

        70         80         90        100        110        120 
KFPVILGHEA AGVVESVGEG VTKFKPGDKV IPLFVPQCGE CRCCKNPESN LCYKNDIGKY 

       130        140        150        160        170        180 
DGVLLDKTSR FTCKGKSIHN FISTSTFTEY TVLDEIAVAK IHEDAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVNTGKV KPGSTCAVFG LGGVGLSVII GCKVAGASRI IGVDLNSDKF TTAKECGATE 

       250        260        270        280        290        300 
CINPKDYNIP IHEVLAKMTD DGVDYAFEVI GNTTVMTSAL SSSHFGCGKT VIVGLAPSSA 

       310        320        330        340        350        360 
VMSFDPLLIL TGRILTGAVF GGWKSKDDVP KLVRDYLNKK FDFDPLITHY MPFEKINEGF 

       370 
ELLRNGKSIR TILTF

P22797 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