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Reviewed, UniProtKB/Swiss-Prot Q9TQS6 (DHDH_MACFA)

Last modified February 9, 2010. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
    EC=1.3.1.20
Alternative name(s):
    Dimeric dihydrodiol dehydrogenase
    D-xylose-NADP dehydrogenase
    EC=1.1.1.179
    D-xylose 1-dehydrogenase
    Cmo2DD
Gene names
Name: DHDH
Synonyms: 2DD
OrganismMacaca fascicularis (Crab eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

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Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.

D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH.

Subunit structure

Homodimer. Ref.1

Tissue specificity

Kidney. Ref.1

Sequence similarities

Belongs to the gfo/idh/mocA family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
PRO_0000315362

Sites

Site711May play an important role in coenzyme binding By similarity
Site791May play an important role in coenzyme binding By similarity
Site971May play an important role in coenzyme binding By similarity
Site1761May play an important role for the adaptation of the alcohol substrate into the binding site By similarity
Site1801May play an important role in catalytic activity By similarity

Experimental info

Mutagenesis1481R → A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-202. Ref.2
Mutagenesis2021R → A: No effect on activity. Reduced activity and exhibits significant temperature sensitivity; when associated with A-148. Ref.2

Secondary structure

1 .............................................................. 334
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9TQS6-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D319AF45660667C9

FASTA33436,435
        10         20         30         40         50         60 
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE 

        70         80         90        100        110        120 
LAKDPNVEVA YVGTQHPQHK AAVMLCLAAG KAVLCEKPMG VNAAEVREMV TEARSRGLFL 

       130        140        150        160        170        180 
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLTH VPRAVDWAQA GGALLDLGIY 

       190        200        210        220        230        240 
CVQFISMVFG GQKPEKISVM GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV 

       250        260        270        280        290        300 
SGTKGMAQLL NPCWCPTELV VKGEHKEFLL PPVPKNCNFD NGAGMSYEAK HVRECLRKGL 

       310        320        330 
KESPVIPLVE SELLADILEE VRRAIGVTFP QDKH

« Hide

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References

[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: 10477285] [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(2007) [PubMed: 17654552] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF ARG-148 AND ARG-202.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB021932 mRNA. Translation: BAA83489.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O48X-ray2.59X1-334[»]
2O4UX-ray2.00X1-334[»]
2POQX-ray2.59X1-334[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENQ9TQS6.

Enzyme and pathway databases

BRENDA1.1.1.179. 3438.
1.3.1.20. 3438.

Family and domain databases

InterProIPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
IPR004104. OxRdtase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01408. GFO_IDH_MocA. 1 hit.
PF02894. GFO_IDH_MocA_C. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDHDH_MACFA
AccessionPrimary (citable) accession number: Q9TQS6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2000
Last modified: February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents