[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Thalamus; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP⁺ = catechol + NADPH.
CATALYTIC ACTIVITY: D-xylose + NADP⁺ = D-xylono-1,5-lactone + NADPH.
SUBUNIT: Homodimer (By similarity).
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

BC118168; AAI18169.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001069937.1; -.

UniGene

Bt.22630

3D structure databases

ModBase

Q148L6.

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

ENSBTAG00000013337; Bos taurus. [Contig view]

GeneID

617564; -.

KEGG

bta:617564; -.

Phylogenomic databases

HOVERGEN

Q148L6; -.

Other

ProtoNet

Q148L6.

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`	`1 335`	`335`	`Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase.`	`PRO_0000315359`
`SITE`	`71 71`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`79 79`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`97 97`	`1`	`May play an important role in coenzyme binding (By similarity).`
`SITE`	`176 176`	`1`	`May play an important role for the adaptation of the alcohol substrate into the binding site (By similarity).`
`SITE`	`180 180`	`1`	`May play an important role in catalytic activity (By similarity).`

Sequence information

Length: 335 AA [This is the length of the unprocessed precursor]

Molecular weight: 36583 Da [This is the MW of the unprocessed precursor]

CRC64: 3D6B91F2F9220BAA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRWGIVSA GLISSDFTTM LRMLPRSEHQ VVAVAARDLS RAKEFAKKHD IPKAYGSYEE 

        70         80         90        100        110        120 
LAKDPDVEVA YIGTQHPQHK AAVLLCLTAG KAVLCEKPMG VNAAEVREMV AEARSRGLFF 

       130        140        150        160        170        180 
MEAIWTRFFP AVEALRSVLA QGTLGDLRVV RAEFGKNLTH VHRATDWAQA GGGLLDLGIY 

       190        200        210        220        230        240 
CLQFISMVFG GQKPEKISAV GRRHETGVDD TVTVILQYPG GVHGSFTCSI SAQLSNTVSV 

       250        260        270        280        290        300 
SGTKGMAQLL DPCWSPTELV VKGEHKEFPL PPAPGKEFNF TNGMGMSYEA KHVRECLQKG 

       310        320        330 
LKESPVIPLV ESELLADILE EVRKAIGITF PQDKH

Q148L6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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