Q9TV69 (DHDH_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
Sus2DD

Gene names

Name:	DHDH
Synonyms:	2DD

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 chloromercuriphenylsulphonate. Stimulated by various salts. Ref.2 Ref.3
Subunit structure	Homodimer. Ref.1
Tissue specificity	Liver, lens, spleen, kidney and small intestine. Ref.1
Sequence similarities	Belongs to the gfo/idh/mocA family.
Biophysicochemical properties	Kinetic parameters: KM=0.24 mM for benzene dihydrodiol (at pH 7.5) Ref.2 Ref.3 KM=0.8 mM for D-xylose (at pH 7.5) Vmax=0.56 µmol/min/mg enzyme with benzene dihydrodiol as substrate Vmax=3.3 µmol/min/mg enzyme with D-xylose as substrate

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Molecular function	D-xylose 1-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC nucleotide 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_0000315365
Sites
	Site	71	1	May play an important role in coenzyme binding
	Site	79	1	May play an important role in coenzyme binding
	Site	97	1	May play an important role in coenzyme binding
	Site	176	1	May play an important role for the adaptation of the alcohol substrate into the binding site
	Site	180	1	May play an important role in catalytic activity

Sequences

	Sequence		Length	Mass (Da)
	Q9TV69 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 658641205A359133	FASTA	335	36,527
	10 20 30 40 50 60 MALRWGIVSA GLISSDFTTV LRLLPRSEHQ VVAVAARDLS RAKEFARKHD IPKAYGSYEE 70 80 90 100 110 120 LAKDPNVEVA YIGTQHPQHK ATVLLCLAAG KAVLCEKPMG VNAAEVREMV AEARSRGLFL 130 140 150 160 170 180 MEAIWTRFFP AVEALRSVLA QETLGDLRVV QANFGKSIAN VPRSVDWAQA GGSLLDLGIY 190 200 210 220 230 240 CLQFISMVYG GQKPEKISAV GRRYETGVDD TVSVLLQYPG GVQGSFTCSI TSQLSNTVSV 250 260 270 280 290 300 SGTKGMAQIL DPCWCPTELV VKGEHKEFPL PSAPGEEFNY TNGMGMCYEA KHVRECLKKG 310 320 330 LKESPMITLA ESELLADILE EVRKAIGVTF PQDKC

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 54-77; 157-184; 245-259; 303-318 AND 325-334, SUBUNIT, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Inhibition of dimeric dihydrodiol dehydrogenases of rabbit and pig lens by ascorbic acid." Hara A., Shinoda M., Kanazu T., Nakayama T., Deyashiki Y., Sawada H. Biochem. J. 275:121-126(1991) [PubMed: 2018468] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Lens.
[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: IDENTIFICATION OF D-XYLOSE DEHYDROGENASE ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021929 mRNA. Translation: BAA83486.1.
RefSeq	NP_999331.1. NM_214166.1.
UniGene	Ssc.59800.
3D structure databases
ProteinModelPortal	Q9TV69.
SMR	Q9TV69. Positions 2-333.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9TV69.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397337.
KEGG	ssc:397337.
Organism-specific databases
CTD	397337.
Phylogenomic databases
GeneTree	ENSGT00390000007946.
HOVERGEN	HBG105348.
OrthoDB	EOG46144D.
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.
KO	K00078.
Pfam	PF01408. GFO_IDH_MocA. 1 hit. PF02894. GFO_IDH_MocA_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHDH_PIG

Accession

Primary (citable) accession number: Q9TV69

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program