[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 25829 / DSM 6675 / NCTC 417; Gallo M.A., Mortlock R.P.; "Molecular characterization of xylitol catabolic pathways in the Enterobacteriaceae."; Thesis (1991), University of Wisconsin-Madison, United States.
[2]	CHARACTERIZATION. STRAIN=ATCC 25829 / DSM 6675 / NCTC 417; PubMed=3886639 [NCBI, ExPASy, EBI, Israel, Japan] Doten R.C., Mortlock R.P.; "Inducible xylitol dehydrogenases in enteric bacteria."; J. Bacteriol. 162:845-848(1985).

Comments

CATALYTIC ACTIVITY: Xylitol + NAD⁺ = D-xylulose + NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Homotetramer (Potential).
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

L34345; AAA25324.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

O96496; 1E3J. [HSSP ENTRY / PDB]

ModBase

Q59545.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12199; -.

Ontologies

GO:0046526;	Molecular function: D-xylulose reductase activity (inferred from electronic annotation from EC).
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.

ProDom

PD040557; GroES_related; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00059; ADH_ZINC; 1.

Other

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

Keywords

Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 338`	`338`	`D-xylulose reductase.`	`PRO_0000160885`
`METAL`	`40 40`		`Zinc (catalytic) (By similarity).`
`METAL`	`65 65`		`Zinc (catalytic) (By similarity).`
`METAL`	`151 151`		`Zinc (catalytic) (By similarity).`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 35952 Da [This is the MW of the unprocessed precursor]

CRC64: 4C6119553DC51873 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIMKALVLEK AGKIAIQDWQ SNEVLGDDDV EIKIHTVGIC GSDVHYYQHG RIGPFVVDEP 

        70         80         90        100        110        120 
MVLGHEASGV ITAAGKNVKH LKVGDRVCME PGIPDLQSPQ SRAGIYNLDP AVRFWATPPI 

       130        140        150        160        170        180 
DGCLRESVIH PAAFTFKLPD NVSFAQGAMV EPLAIGMQSA TKAGIKPGDI GLVIGAGTIG 

       190        200        210        220        230        240 
IITQSALAGG CSDVIICDVF DEKLKVAEKY QGLHAVNSKD QQALADKVRE LTGGEGVNVL 

       250        260        270        280        290        300 
FECSGAKPVI ASISDHIAPG GTAVLVGMPI DPAPLDIVAA QAKEVTFKTI LRYANMYPRT 

       310        320        330 
IRLLSSGKLN VAPLLSATYK FKDSVEAYER AAEPVRLM

Q59545 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