[1]	PROTEIN SEQUENCE. DOI=10.1111/j.1432-1033.1996.00563.x; PubMed=8612630 [NCBI, ExPASy, EBI, Israel, Japan] Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H.; "Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions. Characterization of isozymes in Uromastix hardwickii."; Eur. J. Biochem. 236:563-570(1996).
[2]	PROTEIN SEQUENCE OF 1-18. TISSUE=Liver; DOI=10.1016/0014-5793(92)80080-Z; PubMed=1544464 [NCBI, ExPASy, EBI, Israel, Japan] Hjelmqvist L., Ericsson M., Shafqat J., Carlquist M., Siddiqi A.R., Hoeoeg J.-O., Joernvall H.; "Reptilian alcohol dehydrogenase. Heterogeneity relevant to class multiplicity of the mammalian enzyme."; FEBS Lett. 298:297-300(1992).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Multimeric (with different ratios of monomers).
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: In U.hardwickii there are two isozymes of alcohol dehydrogenase I.
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

S62639; S62639.

3D structure databases

HSSP

P00326; 1HT0. [HSSP ENTRY / PDB]

SMR

P25406; 1-375.

ModBase

P25406.

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

P25406.

Phylogenomic databases

HOVERGEN

P25406; -.

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`	`1 375`	`375`	`Alcohol dehydrogenase 1B.`	`PRO_0000160678`
`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.`

Sequence information

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

Molecular weight: 40060 Da [This is the MW of the unprocessed precursor]

CRC64: 392071E594C32E0D [This is a checksum on the sequence]

        10         20         30         40         50         60 
STAGKVIKCK AAVVWEPKKP FSIVEIEVAP PKAHEVRIKI LASGICRSDD HVLSGALKVN 

        70         80         90        100        110        120 
FPIILGHEAA GVVESVGEGV TSMKPGDKVI PIFLPQCGEC NSCRHPRGNV CKKSELGPFT 

       130        140        150        160        170        180 
GLLYDGTSRF TYQGKPVYHF VRTGTFTEYT VAPEDSVVKI DASAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAAINSAKVQ PGSTCAVFGL GGVGLSAVMG CKAAGASRII GIDINKEKFP KAKELGATEC 

       250        260        270        280        290        300 
VNPLDYKKPI NEVLFDMTDG EGVEYSFEVI GRTDTMTAAL ASCHNNYGTS VIVGVPPSAS 

       310        320        330        340        350        360 
QIAFDPLLLF TGRTWKGSVF GGWKSKDAVP RLVSDFMGKK FILDPLITHT MPFEKINEGF 

       370 
ELLRSGKSIR TVLTF

P25406 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