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   03-AUG-2022, entry version 98.
DE   RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
DE            EC=1.3.1.20;
DE   AltName: Full=D-xylose 1-dehydrogenase;
DE   AltName: Full=D-xylose-NADP dehydrogenase;
DE            EC=1.1.1.179;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,2R)-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol +
CC         H(+) + NADPH; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
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;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR   EMBL; BC076913; AAH76913.1; -; mRNA.
DR   RefSeq; NP_001005045.1; NM_001005045.2.
DR   AlphaFoldDB; Q6DF30; -.
DR   SMR; Q6DF30; -.
DR   STRING; 8364.ENSXETP00000057315; -.
DR   PaxDb; Q6DF30; -.
DR   DNASU; 448579; -.
DR   Ensembl; ENSXETT00000057315; ENSXETP00000057315; ENSXETG00000027480.
DR   GeneID; 448579; -.
DR   KEGG; xtr:448579; -.
DR   CTD; 448579; -.
DR   Xenbase; XB-GENE-968486; dhdh-like.1.
DR   eggNOG; KOG2741; Eukaryota.
DR   HOGENOM; CLU_023194_7_2_1; -.
DR   InParanoid; Q6DF30; -.
DR   OrthoDB; 943656at2759; -.
DR   PhylomeDB; Q6DF30; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000027480; Expressed in mesonephros and 12 other tissues.
DR   GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 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"
FT   SITE            71
FT                   /note="May play an important role in coenzyme binding"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="May play an important role in coenzyme binding"
FT                   /evidence="ECO:0000250"
FT   SITE            97
FT                   /note="May play an important role in coenzyme binding"
FT                   /evidence="ECO:0000250"
FT   SITE            176
FT                   /note="May play an important role for the adaptation of the
FT                   alcohol substrate into the binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            180
FT                   /note="May play an important role in catalytic activity"
FT                   /evidence="ECO:0000250"
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