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Protein

Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase

Gene

Dhdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei71 – 711May play an important role in coenzyme bindingBy similarity
Sitei79 – 791May play an important role in coenzyme bindingBy similarity
Sitei97 – 971May play an important role in coenzyme bindingBy similarity
Sitei176 – 1761May play an important role for the adaptation of the alcohol substrate into the binding siteBy similarity
Sitei180 – 1801May play an important role in catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

  • D-xylose catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.20. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
Alternative name(s):
D-xylose 1-dehydrogenase
D-xylose-NADP dehydrogenase (EC:1.1.1.179)
Dimeric dihydrodiol dehydrogenase
Gene namesi
Name:Dhdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919005. Dhdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Trans-1,2-dihydrobenzene-1,2-diol dehydrogenasePRO_0000315364Add
BLAST

Proteomic databases

EPDiQ9DBB8.
MaxQBiQ9DBB8.
PaxDbiQ9DBB8.
PRIDEiQ9DBB8.

PTM databases

iPTMnetiQ9DBB8.

Expressioni

Gene expression databases

BgeeiQ9DBB8.
CleanExiMM_DHDH.
GenevisibleiQ9DBB8. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9DBB8. 2 interactions.
MINTiMINT-1869308.
STRINGi10090.ENSMUSP00000011526.

Structurei

3D structure databases

ProteinModelPortaliQ9DBB8.
SMRiQ9DBB8. Positions 2-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Phylogenomic databases

eggNOGiKOG2741. Eukaryota.
COG0673. LUCA.
GeneTreeiENSGT00390000007946.
HOVERGENiHBG105348.
InParanoidiQ9DBB8.
KOiK00078.
OMAiVKGEHKE.
OrthoDBiEOG78D7KF.
PhylomeDBiQ9DBB8.
TreeFamiTF324504.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DBB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRWGIVSA GLIANDFTTV LSSLPSSEHQ VVAVAARDLN RAEEFAQKFN
60 70 80 90 100
IPKAYGSYEE LAKDPNVEVA YIATQHPQHK PAVLLCLAAG KAVLCEKPMG
110 120 130 140 150
VNAAEVREMV AKARSQGVFL MEAIWSRFFP AMEALREVLV QGTIGDLRVA
160 170 180 190 200
RAEFGFDLSH IPRATDWNQA GGGLLDLGIY CVQFLSMIFG AQKPEKISAV
210 220 230 240 250
GRIHETGVDD TVSVLLQYPG GVHGSFTCSI SSNLPNTAYV SGTKGMAQIQ
260 270 280 290 300
KLWAPTELVV NGERKEFPPP VLGKDYNFVN GSCMLYEANH VRECLRKGLK
310 320 330
ESPVVPLAES ELLAEILEEA RKAIGVTFPQ DKR
Length:333
Mass (Da):36,301
Last modified:June 1, 2001 - v1
Checksum:i24CCCB8DB0423074
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151S → F in AAI16415 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005050 mRNA. Translation: BAB23776.1.
AK154452 mRNA. Translation: BAE32596.1.
BC116414 mRNA. Translation: AAI16415.1.
CCDSiCCDS21247.1.
RefSeqiNP_082179.1. NM_027903.3.
UniGeneiMm.34208.

Genome annotation databases

EnsembliENSMUST00000011526; ENSMUSP00000011526; ENSMUSG00000011382.
GeneIDi71755.
KEGGimmu:71755.
UCSCiuc009gvj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005050 mRNA. Translation: BAB23776.1.
AK154452 mRNA. Translation: BAE32596.1.
BC116414 mRNA. Translation: AAI16415.1.
CCDSiCCDS21247.1.
RefSeqiNP_082179.1. NM_027903.3.
UniGeneiMm.34208.

3D structure databases

ProteinModelPortaliQ9DBB8.
SMRiQ9DBB8. Positions 2-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBB8. 2 interactions.
MINTiMINT-1869308.
STRINGi10090.ENSMUSP00000011526.

PTM databases

iPTMnetiQ9DBB8.

Proteomic databases

EPDiQ9DBB8.
MaxQBiQ9DBB8.
PaxDbiQ9DBB8.
PRIDEiQ9DBB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000011526; ENSMUSP00000011526; ENSMUSG00000011382.
GeneIDi71755.
KEGGimmu:71755.
UCSCiuc009gvj.1. mouse.

Organism-specific databases

CTDi27294.
MGIiMGI:1919005. Dhdh.

Phylogenomic databases

eggNOGiKOG2741. Eukaryota.
COG0673. LUCA.
GeneTreeiENSGT00390000007946.
HOVERGENiHBG105348.
InParanoidiQ9DBB8.
KOiK00078.
OMAiVKGEHKE.
OrthoDBiEOG78D7KF.
PhylomeDBiQ9DBB8.
TreeFamiTF324504.

Enzyme and pathway databases

BRENDAi1.3.1.20. 3474.

Miscellaneous databases

PROiQ9DBB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBB8.
CleanExiMM_DHDH.
GenevisibleiQ9DBB8. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Liver and Lung.

Entry informationi

Entry nameiDHDH_MOUSE
AccessioniPrimary (citable) accession number: Q9DBB8
Secondary accession number(s): Q14B09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.