DHDH_PIG
ID DHDH_PIG Reviewed; 335 AA.
AC Q9TV69;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Sus2DD;
GN Name=DHDH; Synonyms=2DD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-77; 157-184; 245-259;
RP 303-318 AND 325-334, 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.
RC TISSUE=Lens;
RX PubMed=2018468; DOI=10.1042/bj2750121;
RA Hara A., Shinoda M., Kanazu T., Nakayama T., Deyashiki Y., Sawada H.;
RT "Inhibition of dimeric dihydrodiol dehydrogenases of rabbit and pig lens by
RT ascorbic acid.";
RL Biochem. J. 275:121-126(1991).
RN [3]
RP IDENTIFICATION OF D-XYLOSE DEHYDROGENASE ACTIVITY, ACTIVITY REGULATION, AND
RP 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 chloromercuriphenylsulphonate. Stimulated by
CC various salts. {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:2018468}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for benzene dihydrodiol (at pH 7.5)
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:2018468};
CC KM=0.8 mM for D-xylose (at pH 7.5) {ECO:0000269|PubMed:11306093,
CC ECO:0000269|PubMed:2018468};
CC Vmax=0.56 umol/min/mg enzyme with benzene dihydrodiol as substrate
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:2018468};
CC Vmax=3.3 umol/min/mg enzyme with D-xylose as substrate
CC {ECO:0000269|PubMed:11306093, ECO:0000269|PubMed:2018468};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10477285}.
CC -!- TISSUE SPECIFICITY: Liver, lens, spleen, kidney 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; AB021929; BAA83486.1; -; mRNA.
DR RefSeq; NP_999331.1; NM_214166.1.
DR AlphaFoldDB; Q9TV69; -.
DR SMR; Q9TV69; -.
DR STRING; 9823.ENSSSCP00000003404; -.
DR PaxDb; Q9TV69; -.
DR PeptideAtlas; Q9TV69; -.
DR PRIDE; Q9TV69; -.
DR Ensembl; ENSSSCT00025026338; ENSSSCP00025011146; ENSSSCG00025019423.
DR Ensembl; ENSSSCT00030092231; ENSSSCP00030042439; ENSSSCG00030065918.
DR Ensembl; ENSSSCT00045019357; ENSSSCP00045013278; ENSSSCG00045011300.
DR Ensembl; ENSSSCT00050105630; ENSSSCP00050046507; ENSSSCG00050076835.
DR Ensembl; ENSSSCT00070055699; ENSSSCP00070047308; ENSSSCG00070027762.
DR GeneID; 397337; -.
DR KEGG; ssc:397337; -.
DR CTD; 27294; -.
DR eggNOG; KOG2741; Eukaryota.
DR HOGENOM; CLU_023194_7_2_1; -.
DR InParanoid; Q9TV69; -.
DR OMA; FINYCQY; -.
DR OrthoDB; 943656at2759; -.
DR TreeFam; TF324504; -.
DR SABIO-RK; Q9TV69; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
DR Genevisible; Q9TV69; SS.
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_0000315365"
FT SITE 71
FT /note="May play an important role in coenzyme binding"
FT SITE 79
FT /note="May play an important role in coenzyme binding"
FT SITE 97
FT /note="May play an important role in coenzyme binding"
FT SITE 176
FT /note="May play an important role for the adaptation of the
FT alcohol substrate into the binding site"
FT SITE 180
FT /note="May play an important role in catalytic activity"
SQ SEQUENCE 335 AA; 36527 MW; 658641205A359133 CRC64;
MALRWGIVSA GLISSDFTTV LRLLPRSEHQ VVAVAARDLS RAKEFARKHD IPKAYGSYEE
LAKDPNVEVA YIGTQHPQHK ATVLLCLAAG KAVLCEKPMG VNAAEVREMV AEARSRGLFL
MEAIWTRFFP AVEALRSVLA QETLGDLRVV QANFGKSIAN VPRSVDWAQA GGSLLDLGIY
CLQFISMVYG GQKPEKISAV GRRYETGVDD TVSVLLQYPG GVQGSFTCSI TSQLSNTVSV
SGTKGMAQIL DPCWCPTELV VKGEHKEFPL PSAPGEEFNY TNGMGMCYEA KHVRECLKKG
LKESPMITLA ESELLADILE EVRKAIGVTF PQDKC
