DHDH_RABIT
ID DHDH_RABIT Reviewed; 329 AA.
AC Q9TV70;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 88.
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;
DE AltName: Full=Ory2DD;
DE Flags: Fragment;
GN Name=DHDH; Synonyms=2DD;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Lens;
RX PubMed=10477285; DOI=10.1042/bj3420721;
RA Arimitsu E., Aoki S., Ishikura S., Nakanishi K., Matsuura K., Hara A.;
RT "Cloning and sequencing of the cDNA species for mammalian dimeric
RT dihydrodiol dehydrogenases.";
RL Biochem. J. 342:721-728(1999).
RN [2]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Lens;
RX PubMed=11306093; DOI=10.1016/s0009-2797(00)00307-0;
RA Aoki S., Ishikura S., Asada Y., Usami N., Hara A.;
RT "Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-
RT xylose dehydrogenase in pig liver.";
RL Chem. Biol. Interact. 130:775-784(2001).
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 -!- ACTIVITY REGULATION: Stimulated by various salts.
CC {ECO:0000269|PubMed:11306093}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 mM for D-xylose {ECO:0000269|PubMed:11306093};
CC Vmax=3.6 umol/min/mg enzyme with D-xylose as substrate
CC {ECO:0000269|PubMed:11306093};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10477285}.
CC -!- TISSUE SPECIFICITY: Lens, liver and small intestine.
CC {ECO:0000269|PubMed:10477285}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AB021928; BAA83485.1; -; mRNA.
DR AlphaFoldDB; Q9TV70; -.
DR SMR; Q9TV70; -.
DR STRING; 9986.ENSOCUP00000005550; -.
DR eggNOG; KOG2741; Eukaryota.
DR InParanoid; Q9TV70; -.
DR SABIO-RK; Q9TV70; -.
DR Proteomes; UP000001811; 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 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN <1..329
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315367"
FT SITE 65
FT /note="May play an important role in coenzyme binding"
FT /evidence="ECO:0000250"
FT SITE 73
FT /note="May play an important role in coenzyme binding"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="May play an important role in coenzyme binding"
FT /evidence="ECO:0000250"
FT SITE 170
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 174
FT /note="May play an important role in catalytic activity"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 329 AA; 35795 MW; DD61E87AC0BAD4E2 CRC64;
VVSAGLIAGD FVTVLQALPR SEHQVVAVAA RDLRRAEEFA RTHGIPKAYG SYEELAKDPD
VEVAYIGTQH PQHKAAVLLF LAAGKAVLCE KPLGVNAAEV REMVAEARSR GLFLMEAIWT
RCFPAVDALK SLLAQGALGD LRVARAEFGE NLTQVLRSVD WAQAGGGLLD LGIYCVQFIS
MVFGGQKPEK ISAVGRRYET GVDDTVTVLL QYPGGVHGSF TCSISSKLSN TCSVSGTKGI
AQLLEPCWCP TELVVNKERK EFPLAPEENK KFNYRNGMGM SYEAQHVRDC LRKGLKESPV
IPLAESQLLA DILEEVRKAI GVTFPQDKH
