DHDH_MOUSE
ID DHDH_MOUSE Reviewed; 333 AA.
AC Q9DBB8; Q14B09;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK005050; BAB23776.1; -; mRNA.
DR EMBL; AK154452; BAE32596.1; -; mRNA.
DR EMBL; BC116414; AAI16415.1; -; mRNA.
DR CCDS; CCDS21247.1; -.
DR RefSeq; NP_082179.1; NM_027903.3.
DR AlphaFoldDB; Q9DBB8; -.
DR SMR; Q9DBB8; -.
DR STRING; 10090.ENSMUSP00000011526; -.
DR iPTMnet; Q9DBB8; -.
DR PhosphoSitePlus; Q9DBB8; -.
DR EPD; Q9DBB8; -.
DR jPOST; Q9DBB8; -.
DR MaxQB; Q9DBB8; -.
DR PaxDb; Q9DBB8; -.
DR PRIDE; Q9DBB8; -.
DR ProteomicsDB; 279646; -.
DR DNASU; 71755; -.
DR Ensembl; ENSMUST00000011526; ENSMUSP00000011526; ENSMUSG00000011382.
DR GeneID; 71755; -.
DR KEGG; mmu:71755; -.
DR UCSC; uc009gvj.1; mouse.
DR CTD; 27294; -.
DR MGI; MGI:1919005; Dhdh.
DR VEuPathDB; HostDB:ENSMUSG00000011382; -.
DR eggNOG; KOG2741; Eukaryota.
DR GeneTree; ENSGT00390000007946; -.
DR HOGENOM; CLU_023194_7_2_1; -.
DR InParanoid; Q9DBB8; -.
DR OMA; FINYCQY; -.
DR OrthoDB; 943656at2759; -.
DR PhylomeDB; Q9DBB8; -.
DR TreeFam; TF324504; -.
DR BRENDA; 1.3.1.20; 3474.
DR BioGRID-ORCS; 71755; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Dhdh; mouse.
DR PRO; PR:Q9DBB8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DBB8; protein.
DR Bgee; ENSMUSG00000011382; Expressed in hindlimb stylopod muscle and 195 other tissues.
DR Genevisible; Q9DBB8; MM.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IDA:MGI.
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; IDA:MGI.
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..333
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315364"
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"
FT CONFLICT 115
FT /note="S -> F (in Ref. 2; AAI16415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36301 MW; 24CCCB8DB0423074 CRC64;
MALRWGIVSA GLIANDFTTV LSSLPSSEHQ VVAVAARDLN RAEEFAQKFN IPKAYGSYEE
LAKDPNVEVA YIATQHPQHK PAVLLCLAAG KAVLCEKPMG VNAAEVREMV AKARSQGVFL
MEAIWSRFFP AMEALREVLV QGTIGDLRVA RAEFGFDLSH IPRATDWNQA GGGLLDLGIY
CVQFLSMIFG AQKPEKISAV GRIHETGVDD TVSVLLQYPG GVHGSFTCSI SSNLPNTAYV
SGTKGMAQIQ KLWAPTELVV NGERKEFPPP VLGKDYNFVN GSCMLYEANH VRECLRKGLK
ESPVVPLAES ELLAEILEEA RKAIGVTFPQ DKR
