[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/12.9.3983; PubMed=6328449 [NCBI, ExPASy, EBI, Israel, Japan] Dennis E.S., Gerlach W.L., Pryor A.J., Bennetzen J.L., Inglis A., Llewellyn D.J., Sachs M.M., Ferl R.J., Peacock W.J.; "Molecular analysis of the alcohol dehydrogenase (Adh1) gene of maize."; Nucleic Acids Res. 12:3983-4000(1984).
[2]	NUCLEOTIDE SEQUENCE. 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).
[3]	NUCLEOTIDE SEQUENCE. PubMed=6378620 [NCBI, ExPASy, EBI, Israel, Japan] Braenden C.-I., Eklund H., Cambillau C., Pryor A.J.; "Correlation of exons with structural domains in alcohol dehydrogenase."; EMBO J. 3:1307-1310(1984).
[4]	NUCLEOTIDE SEQUENCE (ALLELE ADH1-F). STRAIN=cv. Berkeley Fast; PubMed=17246333 [NCBI, ExPASy, EBI, Israel, Japan] Sachs M.M., Dennis E.S., Gerlach W.L., Peacock W.J.; "Two alleles of maize alcohol dehydrogenase 1 have 3'-structural and poly(A) addition polymorphisms."; Genetics 113:449-467(1986).
[5]	NUCLEOTIDE SEQUENCE (ALLELE ADH1-CM). DOI=10.1007/BF00016138; PubMed=2577507 [NCBI, ExPASy, EBI, Israel, Japan] Osterman J.C., Dennis E.S.; "Molecular analysis of the ADH1-Cm allele of maize."; Plant Mol. Biol. 13:203-212(1989).
[6]	NUCLEOTIDE SEQUENCE OF 212-379. PubMed=16593188 [NCBI, ExPASy, EBI, Israel, Japan] Gerlach W.L., Pryor A.J., Dennis E.S., Ferl R.J., Sachs M.M., Peacock W.J.; "cDNA cloning and induction of the alcohol dehydrogenase gene (Adh1) of maize."; Proc. Natl. Acad. Sci. U.S.A. 79:2981-2985(1982).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
POLYMORPHISM: The sequence shown is that of allele ADH1-F.
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

X04049; CAA27681.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00580; CAA25239.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04050; CAA27682.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32984; AAA33434.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S04571; S04571.

NP_001105409.1; -.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P00333.

Organism-specific databases

Gramene

P00333; -.

MaizeGDB

13844; -.

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

P00333.

Genome annotation databases

GeneID

542363; -.

Other

ProtoNet

P00333.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 379`	`379`	`Alcohol dehydrogenase 1.`	`PRO_0000160703`
`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).`
`VARIANT`	`52 52`	`1`	`Y -> D (in allele ADH1-Cm).`
`VARIANT`	`127 127`	`1`	`A -> G (in allele ADH1-S).`
`VARIANT`	`179 179`	`1`	`Y -> I (in allele ADH1-Cm and allele ADH1-S).`
`VARIANT`	`363 363`	`1`	`D -> N (in allele ADH1-S).`

Sequence information

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

Molecular weight: 40981 Da [This is the MW of the unprocessed precursor]

CRC64: 5E0618F7E1A4B973 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAGKVIKC KAAVAWEAGK PLSIEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQT 

        70         80         90        100        110        120 
PVFPRIFGHE AGGIIESVGE GVTDVAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT 

       130        140        150        160        170        180 
DRGVMIADGK SRFSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPQAPLD KVCVLSCGYS 

       190        200        210        220        230        240 
TGLGASINVA KPPKGSTVAV FGLGAVGLAA AEGARIAGAS RIIGVDLNPS RFEEARKFGC 

       250        260        270        280        290        300 
TEFVNPKDHN KPVQEVLAEM TNGGVDRSVE CTGNINAMIQ AFECVHDGWG VAVLVGVPHK 

       310        320        330        340        350        360 
DAEFKTHPMN FLNERTLKGT FFGNYKPRTD LPNVVELYMK KELEVEKFIT HSVPFAEINK 

       370 
AFDLMAKGEG IRCIIRMEN

P00333 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