[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/13.3.727; PubMed=2987807 [NCBI, ExPASy, EBI, Israel, Japan] Dennis E.S., Sachs M.M., Gerlach W.L., Finnegan E.J., Peacock W.J.; "Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize."; Nucleic Acids Res. 13:727-743(1985).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: In maize there are two isozymes.
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

X01965; CAA26001.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A23084; A23084.

NP_001105410.1; -.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P04707.

Organism-specific databases

Gramene

P04707; -.

MaizeGDB

13844; -.

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.

Genome annotation databases

GeneID

542364; -.

Other

UniRef

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`	`1 379`	`379`	`Alcohol dehydrogenase 2.`	`PRO_0000160705`
`METAL`	`47 47`		`Zinc 1; catalytic (By similarity).`
`METAL`	`69 69`		`Zinc 1; catalytic (By similarity).`
`METAL`	`99 99`		`Zinc 2 (By similarity).`
`METAL`	`102 102`		`Zinc 2 (By similarity).`
`METAL`	`105 105`		`Zinc 2 (By similarity).`
`METAL`	`113 113`		`Zinc 2 (By similarity).`
`METAL`	`177 177`		`Zinc 1; catalytic (By similarity).`

Sequence information

Length: 379 AA [This is the length of the unprocessed precursor]

Molecular weight: 41054 Da [This is the MW of the unprocessed precursor]

CRC64: BC09E47DD5EA894F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAGKVIKC RAAVTWEAGK PLSIEEVEVA PPQAMEVRIK ILYTALCHTD VYFWEAKGQT 

        70         80         90        100        110        120 
PVFPRILGHE AGGIVESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSEES NMCDLLRINV 

       130        140        150        160        170        180 
DRGVMIGDGK SRFTISGQPI FHFVGTSTFS EYTVIHVGCL AKINPEAPLD KVCILSCGIS 

       190        200        210        220        230        240 
TGLGATLNVA KPAKGSTVAI FGLGAVGLAA MEGARLAGAS RIIGVDINPA KYEQAKKFGC 

       250        260        270        280        290        300 
TEFVNPKDHD KPVQEVLIEL TNGGVDRSVE CTGNVNAMIS AFECVHDGWG VAVLVGVPHK 

       310        320        330        340        350        360 
DDQFKTHPMN FLSEKTLKGT FFGNYKPRTD LPNVVEMYMK KELELEKFIT HSVPFSEINT 

       370 
AFDLMLKGES LRCIMRMED

P04707 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