Full text data of DHDH
DHDH
(2DD)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; 1.3.1.20 (D-xylose 1-dehydrogenase; D-xylose-NADP dehydrogenase; 1.1.1.179; Dimeric dihydrodiol dehydrogenase; Hum2DD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; 1.3.1.20 (D-xylose 1-dehydrogenase; D-xylose-NADP dehydrogenase; 1.1.1.179; Dimeric dihydrodiol dehydrogenase; Hum2DD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00004470
IPI00004470 Dimeric dihydrodiol dehydrogenase Dimeric dihydrodiol dehydrogenase membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00004470 Dimeric dihydrodiol dehydrogenase Dimeric dihydrodiol dehydrogenase membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q9UQ10
ID DHDH_HUMAN Reviewed; 334 AA.
AC Q9UQ10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 97.
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=Hum2DD;
GN Name=DHDH; Synonyms=2DD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=10477285; DOI=10.1042/0264-6021:3420721;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) =
CC catechol + NADPH.
CC -!- CATALYTIC ACTIVITY: D-xylose + NADP(+) = D-xylono-1,5-lactone +
CC NADPH.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Small intestine.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BC032730; AAH32730.1; -; mRNA.
DR EMBL; AB021933; BAA83490.1; -; mRNA.
DR EMBL; CH471177; EAW52414.1; -; Genomic_DNA.
DR RefSeq; NP_055290.1; NM_014475.3.
DR UniGene; Hs.631555; -.
DR ProteinModelPortal; Q9UQ10; -.
DR SMR; Q9UQ10; 2-332.
DR STRING; 9606.ENSP00000221403; -.
DR DMDM; 74735193; -.
DR PaxDb; Q9UQ10; -.
DR PRIDE; Q9UQ10; -.
DR DNASU; 27294; -.
DR Ensembl; ENST00000221403; ENSP00000221403; ENSG00000104808.
DR GeneID; 27294; -.
DR KEGG; hsa:27294; -.
DR UCSC; uc002ple.1; human.
DR CTD; 27294; -.
DR GeneCards; GC19P049436; -.
DR HGNC; HGNC:17887; DHDH.
DR HPA; HPA044131; -.
DR MIM; 606377; gene.
DR neXtProt; NX_Q9UQ10; -.
DR PharmGKB; PA27322; -.
DR eggNOG; COG0673; -.
DR HOGENOM; HOG000227440; -.
DR HOVERGEN; HBG105348; -.
DR InParanoid; Q9UQ10; -.
DR KO; K00078; -.
DR OMA; KGMYWEA; -.
DR OrthoDB; EOG78D7KF; -.
DR PhylomeDB; Q9UQ10; -.
DR GenomeRNAi; 27294; -.
DR NextBio; 50258; -.
DR PRO; PR:Q9UQ10; -.
DR ArrayExpress; Q9UQ10; -.
DR Bgee; Q9UQ10; -.
DR CleanEx; HS_DHDH; -.
DR Genevestigator; Q9UQ10; -.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; TAS:ProtInc.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000683; Oxidoreductase_N.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
PE 1: Evidence at protein level;
KW Complete proteome; NADP; Oxidoreductase; Polymorphism;
KW Reference proteome.
FT CHAIN 1 334 Trans-1,2-dihydrobenzene-1,2-diol
FT dehydrogenase.
FT /FTId=PRO_0000315361.
FT SITE 71 71 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 79 79 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 97 97 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 176 176 May play an important role for the
FT adaptation of the alcohol substrate into
FT the binding site (By similarity).
FT SITE 180 180 May play an important role in catalytic
FT activity (By similarity).
FT VARIANT 2 2 A -> P (in dbSNP:rs10401800).
FT /FTId=VAR_038174.
FT VARIANT 66 66 S -> N (in dbSNP:rs2270941).
FT /FTId=VAR_038175.
FT VARIANT 200 200 V -> M (in dbSNP:rs35453148).
FT /FTId=VAR_038176.
FT VARIANT 247 247 V -> A (in dbSNP:rs11666105).
FT /FTId=VAR_038177.
FT VARIANT 282 282 G -> R (in dbSNP:rs3765148).
FT /FTId=VAR_038178.
SQ SEQUENCE 334 AA; 36382 MW; 1E2E11DF0B55214B CRC64;
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE
LAKDPSVEVA YIGTQHPQHK AAVMLCLAAG KAVLCEKPTG VNAAEVREMV AEARSRALFL
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLIH VPRAVDRAQA GGALLDIGIY
CVQFTSMVFG GQKPEKISVV GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TVQLSNTASV
SGTKGMVQLL NPCWCPTELV VKGEHKEFPL PPVPKDCNFD NGAGMSYEAK HVWECLRKGM
KESPVIPLSE SELLADILEE VRKAIGVTFP QDKR
//
ID DHDH_HUMAN Reviewed; 334 AA.
AC Q9UQ10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 97.
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=Hum2DD;
GN Name=DHDH; Synonyms=2DD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Small intestine;
RX PubMed=10477285; DOI=10.1042/0264-6021:3420721;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY: Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) =
CC catechol + NADPH.
CC -!- CATALYTIC ACTIVITY: D-xylose + NADP(+) = D-xylono-1,5-lactone +
CC NADPH.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Small intestine.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BC032730; AAH32730.1; -; mRNA.
DR EMBL; AB021933; BAA83490.1; -; mRNA.
DR EMBL; CH471177; EAW52414.1; -; Genomic_DNA.
DR RefSeq; NP_055290.1; NM_014475.3.
DR UniGene; Hs.631555; -.
DR ProteinModelPortal; Q9UQ10; -.
DR SMR; Q9UQ10; 2-332.
DR STRING; 9606.ENSP00000221403; -.
DR DMDM; 74735193; -.
DR PaxDb; Q9UQ10; -.
DR PRIDE; Q9UQ10; -.
DR DNASU; 27294; -.
DR Ensembl; ENST00000221403; ENSP00000221403; ENSG00000104808.
DR GeneID; 27294; -.
DR KEGG; hsa:27294; -.
DR UCSC; uc002ple.1; human.
DR CTD; 27294; -.
DR GeneCards; GC19P049436; -.
DR HGNC; HGNC:17887; DHDH.
DR HPA; HPA044131; -.
DR MIM; 606377; gene.
DR neXtProt; NX_Q9UQ10; -.
DR PharmGKB; PA27322; -.
DR eggNOG; COG0673; -.
DR HOGENOM; HOG000227440; -.
DR HOVERGEN; HBG105348; -.
DR InParanoid; Q9UQ10; -.
DR KO; K00078; -.
DR OMA; KGMYWEA; -.
DR OrthoDB; EOG78D7KF; -.
DR PhylomeDB; Q9UQ10; -.
DR GenomeRNAi; 27294; -.
DR NextBio; 50258; -.
DR PRO; PR:Q9UQ10; -.
DR ArrayExpress; Q9UQ10; -.
DR Bgee; Q9UQ10; -.
DR CleanEx; HS_DHDH; -.
DR Genevestigator; Q9UQ10; -.
DR GO; GO:0047837; F:D-xylose 1-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; TAS:ProtInc.
DR GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000683; Oxidoreductase_N.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
PE 1: Evidence at protein level;
KW Complete proteome; NADP; Oxidoreductase; Polymorphism;
KW Reference proteome.
FT CHAIN 1 334 Trans-1,2-dihydrobenzene-1,2-diol
FT dehydrogenase.
FT /FTId=PRO_0000315361.
FT SITE 71 71 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 79 79 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 97 97 May play an important role in coenzyme
FT binding (By similarity).
FT SITE 176 176 May play an important role for the
FT adaptation of the alcohol substrate into
FT the binding site (By similarity).
FT SITE 180 180 May play an important role in catalytic
FT activity (By similarity).
FT VARIANT 2 2 A -> P (in dbSNP:rs10401800).
FT /FTId=VAR_038174.
FT VARIANT 66 66 S -> N (in dbSNP:rs2270941).
FT /FTId=VAR_038175.
FT VARIANT 200 200 V -> M (in dbSNP:rs35453148).
FT /FTId=VAR_038176.
FT VARIANT 247 247 V -> A (in dbSNP:rs11666105).
FT /FTId=VAR_038177.
FT VARIANT 282 282 G -> R (in dbSNP:rs3765148).
FT /FTId=VAR_038178.
SQ SEQUENCE 334 AA; 36382 MW; 1E2E11DF0B55214B CRC64;
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE
LAKDPSVEVA YIGTQHPQHK AAVMLCLAAG KAVLCEKPTG VNAAEVREMV AEARSRALFL
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLIH VPRAVDRAQA GGALLDIGIY
CVQFTSMVFG GQKPEKISVV GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TVQLSNTASV
SGTKGMVQLL NPCWCPTELV VKGEHKEFPL PPVPKDCNFD NGAGMSYEAK HVWECLRKGM
KESPVIPLSE SELLADILEE VRKAIGVTFP QDKR
//
MIM
606377
*RECORD*
*FIELD* NO
606377
*FIELD* TI
*606377 DIMERIC DIHYDRODIOL DEHYDROGENASE; DHDH
;;HUM2DD
*FIELD* TX
DESCRIPTION
Trans-dihydrodiol dehydrogenase (DD; EC 1.3.1.20) catalyzes the
read moreNADP(+)-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons
to the corresponding catechols. DD exists in mammalian tissues in
monomeric and dimeric forms with similar but distinct enzymatic
properties. See 600449 and 600450 for additional background information
on dihydrodiol dehydrogenase.
CLONING
Arimitsu et al. (1999) purified dimeric DD proteins from monkey, dog,
and pig for peptide sequencing and determined the full-length cDNA
sequence for these species. They cloned the full-length human DD cDNA,
HUM2DD, from human intestine using PCR techniques. HUM2DD encodes a
deduced 334-amino acid protein that shares sequence identity with DDs
from Cynomolgus monkey (94%), dog (86%), pig (84%), and rabbit (82%).
Arimitsu et al. (1999) confirmed the identity of HUM2DD by expressing a
recombinant enzyme with DD activity. They observed a subunit molecular
mass of 39 kD and a nondenatured molecular mass of 76 kD. Using
site-directed mutagenesis studies, Arimitsu et al. (1999) found that the
his79 residue of HUM2DD may be important in catalysis or substrate
binding.
By RT-PCR analysis, Arimitsu et al. (1999) detected HUM2DD expression
specifically in small intestine and noted that the tissue distribution
differed between mammalian species. Based on expression data, Arimitsu
et al. (1999) hypothesized that HUM2DD may act as a detoxification
enzyme against food-derived reactive dicarbonyl compounds.
GENE FAMILY
Arimitsu et al. (1999) presented a phylogenetic tree of dimeric DDs and
related proteins. HUM2DD has a distinct primary structure and is the
first complete sequence for a DD that does not belong to the previously
named aldo-keto reductase and short-chain dehydrogenase/reductase
families. The authors suggested that HUM2DD is part of a novel protein
family that may function as pyridine nucleotide-dependent dehydrogenases
or reductases and tentatively named the novel protein family the
medium-chain dehydrogenase/reductase family.
*FIELD* RF
1. Arimitsu, E.; Aoki, S.; Ishkura, S.; Nakanishi, K.; Matsuura, K.;
Hara, A.: Cloning and sequencing of the cDNA species for mammalian
dimeric dihydrodiol dehydrogenases. Biochem. J. 342: 721-728, 1999.
*FIELD* CD
Dawn Watkins-Chow: 10/11/2001
*FIELD* ED
joanna: 01/31/2002
carol: 10/11/2001
*RECORD*
*FIELD* NO
606377
*FIELD* TI
*606377 DIMERIC DIHYDRODIOL DEHYDROGENASE; DHDH
;;HUM2DD
*FIELD* TX
DESCRIPTION
Trans-dihydrodiol dehydrogenase (DD; EC 1.3.1.20) catalyzes the
read moreNADP(+)-linked oxidation of trans-dihydrodiols of aromatic hydrocarbons
to the corresponding catechols. DD exists in mammalian tissues in
monomeric and dimeric forms with similar but distinct enzymatic
properties. See 600449 and 600450 for additional background information
on dihydrodiol dehydrogenase.
CLONING
Arimitsu et al. (1999) purified dimeric DD proteins from monkey, dog,
and pig for peptide sequencing and determined the full-length cDNA
sequence for these species. They cloned the full-length human DD cDNA,
HUM2DD, from human intestine using PCR techniques. HUM2DD encodes a
deduced 334-amino acid protein that shares sequence identity with DDs
from Cynomolgus monkey (94%), dog (86%), pig (84%), and rabbit (82%).
Arimitsu et al. (1999) confirmed the identity of HUM2DD by expressing a
recombinant enzyme with DD activity. They observed a subunit molecular
mass of 39 kD and a nondenatured molecular mass of 76 kD. Using
site-directed mutagenesis studies, Arimitsu et al. (1999) found that the
his79 residue of HUM2DD may be important in catalysis or substrate
binding.
By RT-PCR analysis, Arimitsu et al. (1999) detected HUM2DD expression
specifically in small intestine and noted that the tissue distribution
differed between mammalian species. Based on expression data, Arimitsu
et al. (1999) hypothesized that HUM2DD may act as a detoxification
enzyme against food-derived reactive dicarbonyl compounds.
GENE FAMILY
Arimitsu et al. (1999) presented a phylogenetic tree of dimeric DDs and
related proteins. HUM2DD has a distinct primary structure and is the
first complete sequence for a DD that does not belong to the previously
named aldo-keto reductase and short-chain dehydrogenase/reductase
families. The authors suggested that HUM2DD is part of a novel protein
family that may function as pyridine nucleotide-dependent dehydrogenases
or reductases and tentatively named the novel protein family the
medium-chain dehydrogenase/reductase family.
*FIELD* RF
1. Arimitsu, E.; Aoki, S.; Ishkura, S.; Nakanishi, K.; Matsuura, K.;
Hara, A.: Cloning and sequencing of the cDNA species for mammalian
dimeric dihydrodiol dehydrogenases. Biochem. J. 342: 721-728, 1999.
*FIELD* CD
Dawn Watkins-Chow: 10/11/2001
*FIELD* ED
joanna: 01/31/2002
carol: 10/11/2001