[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8506356 [NCBI, ExPASy, EBI, Israel, Japan] Gaut B.S., Clegg M.T.; "Molecular evolution of the Adh1 locus in the genus Zea."; Proc. Natl. Acad. Sci. U.S.A. 90:5095-5099(1993).

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.

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

L08588; AAA74639.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L08590; AAA74641.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Zm.1540

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

Q07264.

Organism-specific databases

Gramene

Q07264; -.

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.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

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; PARTIAL.

Other

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

Keywords

Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >293`	`>293`	`Alcohol dehydrogenase 1.`	`PRO_0000160704`
`METAL`	`26 26`		`Zinc 2 (By similarity).`
`METAL`	`29 29`		`Zinc 2 (By similarity).`
`METAL`	`32 32`		`Zinc 2 (By similarity).`
`METAL`	`40 40`		`Zinc 2 (By similarity).`
`METAL`	`104 104`		`Zinc 1; catalytic (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`293 293`

Sequence information

Length: 293 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 31490 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E1B343AE6EF9CBD4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
IIESVGEGVT DVAPGDHVLP VFTGECKECA HCKSAESNMC DLLRINTDRG VMIGDGKSRF 

        70         80         90        100        110        120 
SINGKPIYHF VGTSTFSEYT VMHVGCVAKI NPQAPLDKVC VLSCGISTGL GASINVAKPP 

       130        140        150        160        170        180 
KGSTVAVFGL GAVGLAAAEG ARIAGASRII GVDLNPSRFE EARKFGCTEF VNPKDHNKPV 

       190        200        210        220        230        240 
QEVLAEMTNG GVDRSVECTG NINAMIQAFE CVHDGWGVAV LVGVPHKDAE FKTHPMNFLN 

       250        260        270        280        290 
ERTLKGTFFG NYKPRTDLPN VVELYMKKEL EVEKFITHSV PFAEINKAFD LMA

Q07264 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