Reviewed, UniProtKB/Swiss-Prot Q9TV68 (DHDH_CANFA)

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
    Can2DD

Gene names

Name:	DHDH
Synonyms:	2DD

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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 4-chloromercuriphenylsulphonate. Stimulated by various salts. Ref.2 Ref.3
Subunit structure	Homodimer. Ref.1
Tissue specificity	Liver and kidney. Ref.1
Sequence similarities	Belongs to the gfo/idh/mocA family.
Biophysicochemical properties	Kinetic parameters: KM=1.6 mM for naphthalene dihydrodiol (at pH 7.5) KM=0.27 mM for benzene dihydrodiol (at pH 7.5) KM=1.6 mM for D-xylose KM=0.68 mM for 3-deoxyglucosone (at pH 7.5) KM=0.07 mM for camphorquinone (at pH 7.5) KM=0.59 mM for methylglyoxal (at pH 7.5) Vmax=3.27 µmol/min/mg enzyme with naphthalene dihydrodiol as substrate (at pH 7.5) Vmax=2.76 µmol/min/mg enzyme with benzene dihydrodiol as substrate (at pH 7.5) Vmax=4.4 µmol/min/mg enzyme with D-xylose as substrate Vmax=3.55 µmol/min/mg enzyme with reduced 3-deoxyglucosone as substrate (at pH 7.5) Vmax=5.54 µmol/min/mg enzyme with camphorquinone as substrate (at pH 7.5) Vmax=3.11 µmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.5)

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 trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 335	335	Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase		PRO_0000315360
Sites
	Site	71	1	May play an important role in coenzyme binding By similarity
	Site	79	1	May play an important role in coenzyme binding By similarity
	Site	97	1	May play an important role in coenzyme binding By similarity
	Site	176	1	May play an important role for the adaptation of the alcohol substrate into the binding site By similarity
	Site	180	1	May play an important role in catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9TV68-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: CA36887E8097081E	FASTA	335	36,425
	10 20 30 40 50 60 MALRWGIVSA GLISSDFTTV LGTLPRSEHQ VVAVAARDLS RAKEFARKHD IPKAYGSYEE 70 80 90 100 110 120 LAKDPNVEVA YIGTQHPQHK AAVLLCLAAG KAVLCEKPMG VNAAEVREMV AEARSRGLFL 130 140 150 160 170 180 MEAIWTRFFP AIEALRAALS QGTLGELRVA RAEFGKNFTH IPRSVDWAQA GGGLLDLGIY 190 200 210 220 230 240 CIQFISMVFG GQKPEKISAV GRRYETGVDD TVTVLLQYPG GIHGSFTCSI SAQLSNMAFV 250 260 270 280 290 300 SGTKGIGQIL DPCWCPTELV LKGEHKEFPL PPAPSKEFNF TNGAGMAYEA KHVRECLRKG 310 320 330 LKESPVIPLA ESELLADILE EIRKAIGVTF PQDTR

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 54-80; 92-114; 157-191; 245-262; 277-291; 303-323 AND 325-333, SUBUNIT, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Purification and characterization of dimeric dihydrodiol dehydrogenase from dog liver." Sato K., Nakanishi M., Deyashiki Y., Hara A., Matsuura K., Ohya I. J. Biochem. 116:711-717(1994) [PubMed: 7852295] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[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: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021930 mRNA. Translation: BAA83487.1.
RefSeq	NP_001003160.1.
UniGene	Cfa.3648
3D structure databases
SMR	Q9TV68. Positions 2-333.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9TV68.
Genome annotation databases
Ensembl	ENSCAFT00000006229; ENSCAFP00000005770; ENSCAFG00000003869; Canis familiaris. [Genome view]
GeneID	403786.
KEGG	cfa:403786.
Organism-specific databases
CTD	403786.
Phylogenomic databases
eggNOG	maNOG16421.
HOVERGEN	Q9TV68.
InParanoid	Q9TV68.
OMA	DSHAQYA.
OrthoDB	EOG9NZXD5.
PhylomeDB	Q9TV68.
Enzyme and pathway databases
BRENDA	1.1.1.179. 463. 1.3.1.20. 463.
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...

Entry information

Entry name

DHDH_CANFA

Accession

Primary (citable) accession number: Q9TV68

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)