[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2004708 [NCBI, ExPASy, EBI, Israel, Japan] Menotti-Raymond M., Starmer W.T., Sullivan D.T.; "Characterization of the structure and evolution of the Adh region of Drosophila hydei."; Genetics 127:355-366(1991).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) 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

EMBL

X58694; CAA41540.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15712; S15712.

3D structure databases

HSSP

P10807; 1B16. [HSSP ENTRY / PDB]

SMR

P23236; 1-254.

ModBase

P23236.

Organism-specific databases

FlyBase

FBgn0012358; Dhyd\Adh1.

Ontologies

GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0006066;	Biological process: cellular alcohol metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002425; Insect_AlcDHase.
IPR002424; Insect_AlcDHase_fam.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR01168; ALCDHDRGNASE.
PR01167; INSADHFAMILY.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

ProtoNet

P23236.

Other

UniRef

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

Keywords

NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 254`	`253`	`Alcohol dehydrogenase 1.`	`PRO_0000054466`
`NP_BIND`	`10 33`	`24`	`NAD (By similarity).`
`ACT_SITE`	`151 151`		`Proton acceptor (By similarity).`
`BINDING`	`138 138`		`Substrate (By similarity).`

Sequence information

Length: 254 AA [This is the length of the unprocessed precursor]

Molecular weight: 27401 Da [This is the MW of the unprocessed precursor]

CRC64: 6D71E5872C0D75F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAIANKNIIF VAGLGGIGLD TSREIVKSGP KNLVILDRID NPAAIAELKA INPKVTVTFY 

        70         80         90        100        110        120 
PYDVTVSVAE STKLLKVIFD KLKTVDLLIN GAGILDDYQI ERTIAVNFAG TVNTTTAIMA 

       130        140        150        160        170        180 
FWDKRKGGPG GVIANICSVT GFNAIYQVPV YSASKAAALS FTNSLAKLAP ITGVTAYSIN 

       190        200        210        220        230        240 
PGITKTTLVH KFNSWLDVEP RVAELLLEHP TQTSLQCAQN FVKAIEANQN GAIWKLDLGR 

       250 
LEAIEWTKHW DSGI

P23236 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