Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase - Macaca fuscata fuscata (Japanese macaque)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7JK39 (DHDH_MACFU)

Last modified June 16, 2009. Version 24. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

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

Hide | Top

Names and origin

Protein names

Recommended 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
    JMO2DD

Gene names

Name:	DHDH
Synonyms:	2DD

Organism

Macaca fuscata fuscata (Japanese macaque)

Taxonomic identifier

9543 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Hide | Top

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	Trans-1,2-dihydrobenzene-1,2-diol + NADP⁺ = catechol + NADPH. D-xylose + NADP⁺ = D-xylono-1,5-lactone + NADPH.
Enzyme regulation	Strongly inhibited by isoascorbic acid, 4-hydroxyacetophenone and chloromercuriphenylsulphonate. Stimulated by various salts. Ref.1 Ref.2 Ref.3
Subunit structure	Homodimer. Ref.1 Ref.2
Tissue specificity	Kidney. Ref.1
Sequence similarities	Belongs to the gfo/idh/mocA family.
Biophysicochemical properties	Kinetic parameters: K_M=2.6 mM for naphthalene dihydrodiol (at pH 10.0) K_M=0.9 mM for benzene dihydrodiol (at pH 10.0) K_M=1.2 mM for 3-deoxyglucosone (at pH 7.5) K_M=0.12 mM for camphorquinone (at pH 7.5) K_M=1.3 mM for methylglyoxal (at pH 7.5) K_M=6.4 mM for D-xylose (at pH 7.5) K_M=29 mM for D-glucose (at pH 7.5) V_max=36 µmol/min/mg enzyme with naphthalene dihydrodiol as substrate (at pH 10.0) V_max=16 µmol/min/mg enzyme with benzene dihydrodiol as substrate (at pH 10.0) V_max=17 µmol/min/mg enzyme with reduced 3-deoxyglucosone as substrate (at pH 7.5) V_max=34 µmol/min/mg enzyme with camphorquinone as substrate (at pH 7.5) V_max=10 µmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.5) V_max=9.0 µmol/min/mg enzyme with D-xylose as substrate (at pH 7.5) V_max=1.1 µmol/min/mg enzyme with D-glucose as substrate (at pH 7.5)

Hide | Top

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	D-xylose 1-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 334

334

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

PRO_0000315363

Sites

Site

May play an important role in coenzyme binding By similarity

Site

May play an important role in coenzyme binding

Site

May play an important role in coenzyme binding By similarity

Site

176

May play an important role for the adaptation of the alcohol substrate into the binding site By similarity

Site

180

May play an important role in catalytic activity

Experimental info

Mutagenesis

H → E: Decrease in K(d) and K(m) value for NADPH. Elimination of the fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation. Potent inhibition of the dehydrogenase activity by high ionic strength. Ref.2

Mutagenesis

180

Y → F: Significant loss of activity. No effect on the high affinity for NADPH, fluorescence-energy transfer and enhancement of NADPH fluorescence by the binary complex formation. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q7JK39-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D319AF45660667C9
Show »

FASTA

334

36,435

        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

Hide | Top

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 44-80; 92-97; 99-105; 137-148; 174-180; 245-262; 267-290 AND 302-333, SUBUNIT, TISSUE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Kidney.
[2]	"Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function." Asada Y., Aoki S., Ishikura S., Usami N., Hara A. Biochem. Biophys. Res. Commun. 278:333-337(2000) [PubMed: 11097839] [Abstract] Cited for: SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF HIS-79 AND TYR-180.
[3]	"Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-xylose dehydrogenase in pig liver." Aoki S., Ishikura S., Asada Y., Usami N., Hara A. Chem. Biol. Interact. 130:775-784(2001) [PubMed: 11306093] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Kidney.

Hide | Top

Cross-references

Sequence databases
	AB021931 mRNA. Translation: BAA83488.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q7JK39.
Enzyme and pathway databases
BRENDA	1.1.1.179. 276174. 1.3.1.20. 276174.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. IPR000683. Oxidoreductase_N. IPR004104. OxRdtase_C. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01408. GFO_IDH_MocA. 1 hit. PF02894. GFO_IDH_MocA_C. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

DHDH_MACFU

Accession

Primary (citable) accession number: Q7JK39

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents