DHDH_MACFA
ID DHDH_MACFA Reviewed; 334 AA.
AC Q9TQS6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase;
DE EC=1.3.1.20;
DE AltName: Full=Cmo2DD;
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-73; 92-97; 245-253;
RP 276-280 AND 291-298, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS OF ARG-148 AND
RP ARG-202.
RX PubMed=17654552; DOI=10.1002/prot.21566;
RA Carbone V., Endo S., Sumii R., Chung R.P.-T., Matsunaga T., Hara A.,
RA El-Kabbani O.;
RT "Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor
RT complex: probing the subunit interface with site-directed mutagenesis.";
RL Proteins 70:176-187(2008).
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:0000269|PubMed:10477285}.
CC -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:10477285}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AB021932; BAA83489.1; -; mRNA.
DR RefSeq; NP_001271017.1; NM_001284088.1.
DR PDB; 2O48; X-ray; 2.59 A; X=1-334.
DR PDB; 2O4U; X-ray; 2.00 A; X=1-334.
DR PDB; 2POQ; X-ray; 2.59 A; X=1-334.
DR PDB; 3OHS; X-ray; 1.90 A; X=1-334.
DR PDBsum; 2O48; -.
DR PDBsum; 2O4U; -.
DR PDBsum; 2POQ; -.
DR PDBsum; 3OHS; -.
DR AlphaFoldDB; Q9TQS6; -.
DR SMR; Q9TQS6; -.
DR STRING; 9541.XP_005589892.1; -.
DR GeneID; 102133381; -.
DR CTD; 27294; -.
DR VEuPathDB; HostDB:ENSMFAG00000036688; -.
DR eggNOG; KOG2741; Eukaryota.
DR OMA; FINYCQY; -.
DR OrthoDB; 943656at2759; -.
DR BRENDA; 1.1.1.179; 1793.
DR BRENDA; 1.3.1.20; 1793.
DR EvolutionaryTrace; Q9TQS6; -.
DR PRO; PR:Q9TQS6; -.
DR Proteomes; UP000233100; Chromosome 19.
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 3D-structure; Direct protein sequencing; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT /id="PRO_0000315362"
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 MUTAGEN 148
FT /note="R->A: No effect on activity. Reduced activity and
FT exhibits significant temperature sensitivity; when
FT associated with A-202."
FT /evidence="ECO:0000269|PubMed:17654552"
FT MUTAGEN 202
FT /note="R->A: No effect on activity. Reduced activity and
FT exhibits significant temperature sensitivity; when
FT associated with A-148."
FT /evidence="ECO:0000269|PubMed:17654552"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3OHS"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 92..102
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 130..141
FT /evidence="ECO:0007829|PDB:3OHS"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:3OHS"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:3OHS"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:3OHS"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:3OHS"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3OHS"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:3OHS"
SQ SEQUENCE 334 AA; 36435 MW; D319AF45660667C9 CRC64;
MALRWGIVSV GLISSDFTAV LQTLPRSEHQ VVAVAARDLS RAKEFAQKHD IPKAYGSYEE
LAKDPNVEVA YVGTQHPQHK AAVMLCLAAG KAVLCEKPMG VNAAEVREMV TEARSRGLFL
MEAIWTRFFP ASEALRSVLA QGTLGDLRVA RAEFGKNLTH VPRAVDWAQA GGALLDLGIY
CVQFISMVFG GQKPEKISVM GRRHETGVDD TVTVLLQYPG EVHGSFTCSI TAQLSNTASV
SGTKGMAQLL NPCWCPTELV VKGEHKEFLL PPVPKNCNFD NGAGMSYEAK HVRECLRKGL
KESPVIPLVE SELLADILEE VRRAIGVTFP QDKH
