DHDH_PONAB
ID DHDH_PONAB Reviewed; 334 AA.
AC Q5R5J5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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}.
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; CR860863; CAH92971.1; -; mRNA.
DR RefSeq; NP_001127612.1; NM_001134140.1.
DR AlphaFoldDB; Q5R5J5; -.
DR SMR; Q5R5J5; -.
DR STRING; 9601.ENSPPYP00000011432; -.
DR GeneID; 100174691; -.
DR KEGG; pon:100174691; -.
DR CTD; 27294; -.
DR eggNOG; KOG2741; Eukaryota.
DR InParanoid; Q5R5J5; -.
DR OrthoDB; 943656at2759; -.
DR BRENDA; 1.3.1.20; 9017.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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 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..334
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315366"
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 334 AA; 36437 MW; 13FCCA0EAE897B4B CRC64;
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEVAEKHD IPKAYGSYEE
LAKDPNVEVA YIGTQHPQHK AAVMLCLAAG EAVLCEKPMG VNVAEVREMV AEARSRDLFL
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLTH IPRAIDWAQA GGALLDIGIY
CVQFISMVFG GQKPEKISVV GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV
SGTKGMAQLL NPCWCPTELV VKGEHKEFPL PPVPKDCNFD NGAGMSYEAK HVRECLRKGM
KESPVIPLSE SELLADILEE VRKAIGVTFP QDKR