ID DHDH_XENTR Reviewed; 330 AA. AC Q6DF30; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 02-SEP-2026, entry version 114. DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; DE EC=1.3.1.20 {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=D-arabinose 1-dehydrogenase; DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=D-galactose 1-dehydrogenase; DE EC=1.1.1.120 {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=D-glucose 1-dehydrogenase; DE EC=1.1.1.119 {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=D-ribose 1-dehydrogenase; DE EC=1.1.1.115 {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=D-xylose 1-dehydrogenase; DE AltName: Full=D-xylose-NADP dehydrogenase; DE EC=1.1.1.179 {ECO:0000250|UniProtKB:Q7JK39}; DE AltName: Full=Dimeric dihydrodiol dehydrogenase; GN Name=dhdh; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADP(+)-linked oxidation of trans-dihydrodiols CC of aromatic hydrocarbons to the corresponding catechols. It also CC catalyzes the oxidation of several pentoses and hexoses. In the reverse CC reaction in the presence of NADPH, it acts as NADPH-linked reductase on CC a broad range of substrates including aldehydes, chetones, and alpha- CC dicarbonyl compounds such as 3-deoxyglucosone, camphorquinone and CC methylglyoxal. {ECO:0000250|UniProtKB:Q7JK39}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + CC NADPH + H(+); Xref=Rhea:RHEA:16729, ChEBI:CHEBI:10702, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.20; CC Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + NADPH + H(+); CC Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867, CC ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.179; Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + NADPH + H(+); CC Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.119; Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-galactose + NADP(+) = D-galactono-1,5-lactone + NADPH + CC H(+); Xref=Rhea:RHEA:18625, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15945, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.120; Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-ribose + NADP(+) + H2O = D-ribonate + NADPH + 2 H(+); CC Xref=Rhea:RHEA:11676, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17773, ChEBI:CHEBI:47013, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.1.1.115; CC Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-arabinose + NADP(+) = D-arabinono-1,5-lactone + NADPH + CC H(+); Xref=Rhea:RHEA:75267, ChEBI:CHEBI:15378, ChEBI:CHEBI:46994, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:194242; CC Evidence={ECO:0000250|UniProtKB:Q7JK39}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9TQS6}. CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC076913; AAH76913.1; -; mRNA. DR RefSeq; NP_001005045.1; NM_001005045.2. DR AlphaFoldDB; Q6DF30; -. DR SMR; Q6DF30; -. DR FunCoup; Q6DF30; 164. DR STRING; 8364.ENSXETP00000026524; -. DR PaxDb; 8364-ENSXETP00000026524; -. DR DNASU; 448579; -. DR Ensembl; ENSXETT00000057315; ENSXETP00000057315; ENSXETG00000027480. DR GeneID; 448579; -. DR KEGG; xtr:448579; -. DR CTD; 448579; -. DR Xenbase; XB-GENE-968486; dhdhl. DR eggNOG; KOG2741; Eukaryota. DR GeneTree; ENSGT00390000007946; -. DR HOGENOM; CLU_023194_7_2_1; -. DR InParanoid; Q6DF30; -. DR OMA; KMIQAPF; -. DR OrthoDB; 2129491at2759; -. DR PhylomeDB; Q6DF30; -. DR Proteomes; UP000008143; Chromosome 7. DR Bgee; ENSXETG00000027480; Expressed in mesonephros and 12 other cell types or tissues. DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0047910; F:galactose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0047935; F:glucose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0050259; F:ribose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0042843; P:D-xylose catabolic process; IBA:GO_Central. DR FunFam; 3.30.360.10:FF:000031; Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000269; Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N. DR InterPro; IPR050984; Gfo/Idh/MocA_domain. DR InterPro; IPR055170; GFO_IDH_MocA-like_dom. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR22604; OXIDOREDUCTASES; 1. DR PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 1. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF22725; GFO_IDH_MocA_C3; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 2: Evidence at transcript level; KW NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..330 FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase" FT /id="PRO_0000315370" SQ SEQUENCE 330 AA; 36310 MW; 6363E88F2B298EAA CRC64; MATKWGICSA GKISNDFVVA LSTLPAVDHQ VVAIAARDLE KAKNFAQNHN IPKAYGSYEE LAKDPDIDVI YVGAIHPVHR DVVLMCLQNG KNILCEKPLA MNAAQVQELI ATARKFNVFL MEAFWSRFFP VYEEIRALLS QKAIGDVKFI RAEFGVEIYK VPRAVEKELG GGALLDIGCY CVQFVTMVFN GERPESVTAK GFLHETGVDE SMSLILQYSG KRQAVLSSTI MATLPNQAAI CGTKGIIQIP SDMWSPTSII VNGKERKFDI PHTTKPMNFS NGTGMSYEAE HVRQCLLKGL KESPIMSLAD SEMVASIMDE ALQQLGVTYP //