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Protein

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

Gene

DHDH

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.179. 1793.
1.3.1.20. 1793.

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
Alternative name(s):
Cmo2DD
D-xylose 1-dehydrogenase
D-xylose-NADP dehydrogenase (EC:1.1.1.179)
Dimeric dihydrodiol dehydrogenase
Gene namesi
Name:DHDH
Synonyms:2DD
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi148 – 1481R → A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-202. 1 Publication
Mutagenesisi202 – 2021R → A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-148. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Trans-1,2-dihydrobenzene-1,2-diol dehydrogenasePRO_0000315362Add
BLAST

Expressioni

Tissue specificityi

Kidney.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi12 – 2110Combined sources
Turni26 – 283Combined sources
Beta strandi29 – 357Combined sources
Helixi39 – 4911Combined sources
Beta strandi54 – 574Combined sources
Helixi58 – 636Combined sources
Beta strandi69 – 724Combined sources
Helixi76 – 783Combined sources
Helixi79 – 8810Combined sources
Beta strandi92 – 10211Combined sources
Helixi103 – 11513Combined sources
Beta strandi120 – 1234Combined sources
Helixi125 – 1284Combined sources
Helixi130 – 14112Combined sources
Turni142 – 1443Combined sources
Beta strandi146 – 15510Combined sources
Helixi162 – 1654Combined sources
Turni167 – 1704Combined sources
Helixi173 – 1764Combined sources
Helixi178 – 18811Combined sources
Turni189 – 1913Combined sources
Beta strandi195 – 2039Combined sources
Beta strandi207 – 21812Combined sources
Turni219 – 2213Combined sources
Beta strandi222 – 23211Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi245 – 2495Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2674Combined sources
Helixi282 – 2854Combined sources
Helixi286 – 29712Combined sources
Beta strandi304 – 3063Combined sources
Helixi308 – 32417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O48X-ray2.59X1-334[»]
2O4UX-ray2.00X1-334[»]
2POQX-ray2.59X1-334[»]
3OHSX-ray1.90X1-334[»]
ProteinModelPortaliQ9TQS6.
SMRiQ9TQS6. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9TQS6.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfo/Idh/MocA family.Curated

Phylogenomic databases

HOVERGENiHBG105348.
KOiK00078.

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.

Q9TQS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD
60 70 80 90 100
IPKAYGSYEE LAKDPNVEVA YVGTQHPQHK AAVMLCLAAG KAVLCEKPMG
110 120 130 140 150
VNAAEVREMV TEARSRGLFL MEAIWTRFFP ASEALRSVLA QGTLGDLRVA
160 170 180 190 200
RAEFGKNLTH VPRAVDWAQA GGALLDLGIY CVQFISMVFG GQKPEKISVM
210 220 230 240 250
GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV SGTKGMAQLL
260 270 280 290 300
NPCWCPTELV VKGEHKEFLL PPVPKNCNFD NGAGMSYEAK HVRECLRKGL
310 320 330
KESPVIPLVE SELLADILEE VRRAIGVTFP QDKH
Length:334
Mass (Da):36,435
Last modified:May 1, 2000 - v1
Checksum:iD319AF45660667C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021932 mRNA. Translation: BAA83489.1.
RefSeqiNP_001271017.1. NM_001284088.1.
UniGeneiMfa.5414.

Genome annotation databases

GeneIDi102133381.
KEGGimcf:102133381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021932 mRNA. Translation: BAA83489.1.
RefSeqiNP_001271017.1. NM_001284088.1.
UniGeneiMfa.5414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O48X-ray2.59X1-334[»]
2O4UX-ray2.00X1-334[»]
2POQX-ray2.59X1-334[»]
3OHSX-ray1.90X1-334[»]
ProteinModelPortaliQ9TQS6.
SMRiQ9TQS6. Positions 2-332.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102133381.
KEGGimcf:102133381.

Organism-specific databases

CTDi27294.

Phylogenomic databases

HOVERGENiHBG105348.
KOiK00078.

Enzyme and pathway databases

BRENDAi1.1.1.179. 1793.
1.3.1.20. 1793.

Miscellaneous databases

EvolutionaryTraceiQ9TQS6.

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. "Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases."
    Arimitsu E., Aoki S., Ishikura S., Nakanishi K., Matsuura K., Hara A.
    Biochem. J. 342:721-728(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-73; 92-97; 245-253; 276-280 AND 291-298, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis."
    Carbone V., Endo S., Sumii R., Chung R.P.-T., Matsunaga T., Hara A., El-Kabbani O.
    Proteins 70:176-187(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF ARG-148 AND ARG-202.

Entry informationi

Entry nameiDHDH_MACFA
AccessioniPrimary (citable) accession number: Q9TQS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2000
Last modified: December 9, 2015
This is version 71 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.