[1]	NUCLEOTIDE SEQUENCE. DOI=10.1016/S0965-1748(98)00114-3; PubMed=10196734 [NCBI, ExPASy, EBI, Israel, Japan] Wolfe G.R., Smith C.A., Hendrix D.L., Salvucci M.E.; "Molecular basis for thermoprotection in Bemisia: structural differences between whitefly ketose reductase and other medium-chain dehydrogenases/reductases."; Insect Biochem. Mol. Biol. 29:113-120(1999).
[2]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1006/jmbi.2000.4381; PubMed=11237597 [NCBI, ExPASy, EBI, Israel, Japan] Banfield M.J., Salvucci M.E., Baker E.N., Smith C.A.; "Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 A resolution."; J. Mol. Biol. 306:239-250(2001).

Comments

COFACTOR: Zinc (By similarity).

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

AF067126; AAD02817.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1E3J; X-ray; 2.30 A; A=1-352.

[ExPASy / RCSB / EBI]

PDBsum

1E3J; -.

ModBase

O96496.

Ontologies

GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
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.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
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.

PRINTS

PR00368; FADPNR.

PROSITE

PS00059; ADH_ZINC; 1.

Other

UniRef

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

Keywords

Metal-binding; Oxidoreductase; Zinc.

Features

None

Sequence information

Length: 352 AA

Molecular weight: 38164 Da

CRC64: 56360D3D2EDA6D26 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASDNLSAVL YKQNDLRLEQ RPIPEPKEDE VLLQMAYVGI CGSDVHYYEH GRIADFIVKD 

        70         80         90        100        110        120 
PMVIGHEASG TVVKVGKNVK HLKKGDRVAV EPGVPCRRCQ FCKEGKYNLC PDLTFCATPP 

       130        140        150        160        170        180 
DDGNLARYYV HAADFCHKLP DNVSLEEGAL LEPLSVGVHA CRRAGVQLGT TVLVIGAGPI 

       190        200        210        220        230        240 
GLVSVLAAKA YGAFVVCTAR SPRRLEVAKN CGADVTLVVD PAKEEESSII ERIRSAIGDL 

       250        260        270        280        290        300 
PNVTIDCSGN EKCITIGINI TRTGGTLMLV GMGSQMVTVP LVNACAREID IKSVFRYCND 

       310        320        330        340        350 
YPIALEMVAS GRCNVKQLVT HSFKLEQTVD AFEAARKKAD NTIKVMISCR QG

O96496 in FASTA format

View entry in original UniProtKB/TrEMBL format
View entry in raw text format (no links)
Request for annotation of this UniProtKB/TrEMBL 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