[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1105/tpc.12.3.381; PubMed=10715324 [NCBI, ExPASy, EBI, Israel, Japan] Tarchini R., Biddle P., Wineland R., Tingey S., Rafalski A.; "The complete sequence of 340 kb of DNA around the rice Adh1-Adh2 region reveals interrupted colinearity with maize chromosome 4."; Plant Cell 12:381-391(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1186/1741-7007-3-20; PubMed=16188032 [NCBI, ExPASy, EBI, Israel, Japan] The rice chromosomes 11 and 12 sequencing consortia; "The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications."; BMC Biol. 3:20-20(2005).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1038/nature03895; PubMed=16100779 [NCBI, ExPASy, EBI, Israel, Japan] International rice genome sequencing project (IRGSP); "The map-based sequence of the rice genome."; Nature 436:793-800(2005).
[4]	GENOME REANNOTATION. STRAIN=cv. Nipponbare; DOI=10.1101/gr.5509507; PubMed=17210932 [NCBI, ExPASy, EBI, Israel, Japan] The rice annotation project (RAP); "Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana."; Genome Res. 17:175-183(2007).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Nipponbare; DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan] The rice full-length cDNA consortium; "Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."; Science 301:376-379(2003).

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.
SEQUENCE CAUTION:
- Sequence=AK102799; Type=Frameshift; Positions=369;
- Sequence=BAF27848.1; Type=Erroneous gene model prediction;

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

AF172282; AAF34412.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DP000010; ABA92034.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008217; BAF27848.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK102799; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

RefSeq

NP_001067485.1; -.

UniGene

Os.8815

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

Q0ITW7.

Organism-specific databases

Gramene

Q2R8Z2; -.

Ontologies

GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

BLOCKS

Q0ITW7.

Genome annotation databases

GeneID

4350054; -.

KEGG

osa:4350054; -.

Other

ProtoNet

Q0ITW7.

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_0000160708`
`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).`
`CONFLICT`	`42 42`		`L -> I (in Ref. 5; AK102799).`

Sequence information

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

Molecular weight: 41207 Da [This is the MW of the unprocessed precursor]

CRC64: 2DF98CF6B6BEE8EA [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
PVFPRILGHE AGGIVESVGE GVTELAPGDH VLPVFTGECK ECDHCKSEES NMCDLLRINV 

       130        140        150        160        170        180 
DRGVMIGDGK SRFTIKGKPI FHFVGTSTFS EYTVIHVGCL AKINPEAPLD KVCILSCGFS 

       190        200        210        220        230        240 
TGFGATVNVA KPKKGQTVAI FGLGAVGLAA MEGARLSGAS RIIGVDLNPA KFEQAKKFGC 

       250        260        270        280        290        300 
TDFVNPKDHS KPVHEVLIEM TNGGLDRAVE CTGNINAMIS CFECVHDGWG VAVLVGVPTK 

       310        320        330        340        350        360 
DDVFKTHPMN FLNEKTLKGT FFGNYKPRTD LPNVVELYMK KELELEKFIT HSVPFSEINT 

       370 
AFDLMLKGES LRCVMRMDE

Q0ITW7 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