[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. IR26; TISSUE=Seedling; DOI=10.1007/BF00027335; PubMed=2562760 [NCBI, ExPASy, EBI, Israel, Japan] Xie Y., Wu R.; "Rice alcohol dehydrogenase genes: anaerobic induction, organ specific expression and characterization of cDNA clones."; Plant Mol. Biol. 13:53-68(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s00122-004-1752-3; PubMed=15480535 [NCBI, ExPASy, EBI, Israel, Japan] Yoshida K., Miyashita N.T., Ishii T.; "Nucleotide polymorphism in the Adh1 locus region of the wild rice Oryza rufipogon."; Theor. Appl. Genet. 109:1406-1416(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. 93-11; DOI=10.1371/journal.pbio.0030038; PubMed=15685292 [NCBI, ExPASy, EBI, Israel, Japan] Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; "The genomes of Oryza sativa: a history of duplications."; PLoS Biol. 3:266-281(2005).

Comments

CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
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

X16296; CAA34363.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB118962; BAC87776.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CM000136; EAY80331.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JQ0474; JQ0474.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

Q75ZX4.

Organism-specific databases

Gramene

Q75ZX4; -.

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

Q75ZX4.

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 1.`	`PRO_0000291461`
`METAL`	`47 47`		`Zinc 1; catalytic (By similarity).`
`METAL`	`69 69`		`Zinc 1; catalytic (By similarity).`
`METAL`	`100 100`		`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).`
`CONFLICT`	`19 19`		`A -> G (in Ref. 1; CAA34363).`
`CONFLICT`	`23 23`		`V -> S (in Ref. 1; CAA34363).`
`CONFLICT`	`31 34`		`PPQA -> KE (in Ref. 1; CAA34363).`
`CONFLICT`	`144 144`		`V -> I (in Ref. 1; CAA34363).`
`CONFLICT`	`192 192`		`Missing (in Ref. 1; CAA34363).`
`CONFLICT`	`217 217`		`A -> R (in Ref. 1; CAA34363).`
`CONFLICT`	`291 291`		`V -> I (in Ref. 1; CAA34363).`
`CONFLICT`	`370 370`		`G -> A (in Ref. 1; CAA34363).`

Sequence information

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

Molecular weight: 40984 Da [This is the MW of the unprocessed precursor]

CRC64: 1281E87F3DB30545 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAGKVIKC KAAVAWEAAK PLVIEEVEVA PPQAMEVRVK ILFTSLCHTD VYFWEAKGQT 

        70         80         90        100        110        120 
PVFPRIFGHE AGGIVESVGE GVTDLAPGDH VLPVFTGECK ECAHCKSAES NMCDLLRINT 

       130        140        150        160        170        180 
DRGVMIGDGK SRFSINGKPI YHFVGTSTFS EYTVMHVGCV AKINPAAPLD KVCVLSCGIS 

       190        200        210        220        230        240 
TGLGATINVA KPPKGSTVAI FGLGAVGLAA AEGARIAGAS RIIGIDLNAN RFEEARKFGC 

       250        260        270        280        290        300 
TEFVNPKDHD KPVQQVLAEM TNGGVDRSVE CTGNINAMIQ AFECVHDGWG VAVLVGVPHK 

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

       370 
AFDLMHKGEG IRCIIRMEN

Q75ZX4 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