[1]	NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY. TISSUE=Lens; DOI=10.1042/0264-6021:3420721; PubMed=10477285 [NCBI, ExPASy, EBI, Israel, Japan] Arimitsu E., Aoki S., Ishikura S., Nakanishi K., Matsuura K., Hara A.; "Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases."; Biochem. J. 342:721-728(1999).
[2]	ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. TISSUE=Lens; DOI=10.1016/S0009-2797(00)00307-0; PubMed=11306093 [NCBI, ExPASy, EBI, Israel, Japan] Aoki S., Ishikura S., Asada Y., Usami N., Hara A.; "Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-xylose dehydrogenase in pig liver."; Chem. Biol. Interact. 130:775-784(2001).

Comments

CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP⁺ = catechol + NADPH.
CATALYTIC ACTIVITY: D-xylose + NADP⁺ = D-xylono-1,5-lactone + NADPH.
ENZYME REGULATION: Stimulated by various salts.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=4.4 mM for D-xylose;
V_max=3.6 µmol/min/mg enzyme with D-xylose as substrate;
SUBUNIT: Homodimer.
TISSUE SPECIFICITY: Lens, liver and small intestine.
SIMILARITY: Belongs to the gfo/idh/mocA 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

AB021928; BAA83485.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Ocu.6266

3D structure databases

ModBase

Q9TV70.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0047837;	Molecular function: D-xylose 1-dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0047115;	Molecular function: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000683; GFO/IDH/MocA_N.
IPR016040; NAD(P)-bd.
IPR004104; OxRdtase_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01408; GFO_IDH_MocA; 1.
PF02894; GFO_IDH_MocA_C; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSOCUG00000006419; Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGEN

Q9TV70; -.

Other

UniRef

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

Keywords

NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 329`	`>329`	`Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase.`	`PRO_0000315367`
`SITE`	`65 65`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`73 73`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`91 91`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`170 170`	`1`	`May play an important role for the adaptation of the alcohol substrate into the binding site (By similarity).`
`SITE`	`174 174`	`1`	`May play an important role in catalytic activity (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 329 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 35795 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: DD61E87AC0BAD4E2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
VVSAGLIAGD FVTVLQALPR SEHQVVAVAA RDLRRAEEFA RTHGIPKAYG SYEELAKDPD 

        70         80         90        100        110        120 
VEVAYIGTQH PQHKAAVLLF LAAGKAVLCE KPLGVNAAEV REMVAEARSR GLFLMEAIWT 

       130        140        150        160        170        180 
RCFPAVDALK SLLAQGALGD LRVARAEFGE NLTQVLRSVD WAQAGGGLLD LGIYCVQFIS 

       190        200        210        220        230        240 
MVFGGQKPEK ISAVGRRYET GVDDTVTVLL QYPGGVHGSF TCSISSKLSN TCSVSGTKGI 

       250        260        270        280        290        300 
AQLLEPCWCP TELVVNKERK EFPLAPEENK KFNYRNGMGM SYEAQHVRDC LRKGLKESPV 

       310        320 
IPLAESQLLA DILEEVRKAI GVTFPQDKH

Q9TV70 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