DHDH_CANLF
ID DHDH_CANLF Reviewed; 335 AA.
AC Q9TV68;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
DE EC=1.3.1.20;
DE AltName: Full=Can2DD;
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; Synonyms=2DD;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-80; 92-114; 157-191;
RP 245-262; 277-291; 303-323 AND 325-333, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
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.
RX PubMed=7852295; DOI=10.1093/oxfordjournals.jbchem.a124585;
RA Sato K., Nakanishi M., Deyashiki Y., Hara A., Matsuura K., Ohya I.;
RT "Purification and characterization of dimeric dihydrodiol dehydrogenase
RT from dog liver.";
RL J. Biochem. 116:711-717(1994).
RN [3]
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
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: Strongly inhibited by isoascorbic acid, 4-
CC hydroxyacetophenone and 4-chloromercuriphenylsulphonate. Stimulated by
CC various salts. {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:7852295}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for naphthalene dihydrodiol (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC KM=0.27 mM for benzene dihydrodiol (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC KM=1.6 mM for D-xylose {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:7852295};
CC KM=0.68 mM for 3-deoxyglucosone (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC KM=0.07 mM for camphorquinone (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC KM=0.59 mM for methylglyoxal (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC Vmax=3.27 umol/min/mg enzyme with naphthalene dihydrodiol as
CC substrate (at pH 7.5) {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:7852295};
CC Vmax=2.76 umol/min/mg enzyme with benzene dihydrodiol as substrate
CC (at pH 7.5) {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:7852295};
CC Vmax=4.4 umol/min/mg enzyme with D-xylose as substrate
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC Vmax=3.55 umol/min/mg enzyme with reduced 3-deoxyglucosone as
CC substrate (at pH 7.5) {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:7852295};
CC Vmax=5.54 umol/min/mg enzyme with camphorquinone as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC Vmax=3.11 umol/min/mg enzyme with methylglyoxal as substrate (at pH
CC 7.5) {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:7852295};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10477285}.
CC -!- TISSUE SPECIFICITY: Liver and kidney. {ECO:0000269|PubMed:10477285}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AB021930; BAA83487.1; -; mRNA.
DR RefSeq; NP_001003160.1; NM_001003160.1.
DR AlphaFoldDB; Q9TV68; -.
DR SMR; Q9TV68; -.
DR STRING; 9612.ENSCAFP00000005770; -.
DR PaxDb; Q9TV68; -.
DR PRIDE; Q9TV68; -.
DR Ensembl; ENSCAFT00030026186; ENSCAFP00030022867; ENSCAFG00030014104.
DR Ensembl; ENSCAFT00040001177; ENSCAFP00040000998; ENSCAFG00040000654.
DR Ensembl; ENSCAFT00845000856; ENSCAFP00845000645; ENSCAFG00845000526.
DR GeneID; 403786; -.
DR KEGG; cfa:403786; -.
DR CTD; 27294; -.
DR VEuPathDB; HostDB:ENSCAFG00845000526; -.
DR eggNOG; KOG2741; Eukaryota.
DR GeneTree; ENSGT00390000007946; -.
DR HOGENOM; CLU_023194_7_2_1; -.
DR InParanoid; Q9TV68; -.
DR OMA; FINYCQY; -.
DR OrthoDB; 943656at2759; -.
DR TreeFam; TF324504; -.
DR SABIO-RK; Q9TV68; -.
DR Proteomes; UP000002254; Chromosome 1.
DR Bgee; ENSCAFG00000003869; Expressed in liver and 49 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 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..335
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315360"
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 335 AA; 36425 MW; CA36887E8097081E CRC64;
MALRWGIVSA GLISSDFTTV LGTLPRSEHQ VVAVAARDLS RAKEFARKHD IPKAYGSYEE
LAKDPNVEVA YIGTQHPQHK AAVLLCLAAG KAVLCEKPMG VNAAEVREMV AEARSRGLFL
MEAIWTRFFP AIEALRAALS QGTLGELRVA RAEFGKNFTH IPRSVDWAQA GGGLLDLGIY
CIQFISMVFG GQKPEKISAV GRRYETGVDD TVTVLLQYPG GIHGSFTCSI SAQLSNMAFV
SGTKGIGQIL DPCWCPTELV LKGEHKEFPL PPAPSKEFNF TNGAGMAYEA KHVRECLRKG
LKESPVIPLA ESELLADILE EIRKAIGVTF PQDTR
