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DHDH_XENLA
ID   DHDH_XENLA              Reviewed;         330 AA.
AC   Q6DKE0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC074201; AAH74201.1; -; mRNA.
DR   RefSeq; NP_001086110.1; NM_001092641.1.
DR   AlphaFoldDB; Q6DKE0; -.
DR   SMR; Q6DKE0; -.
DR   GeneID; 444539; -.
DR   KEGG; xla:444539; -.
DR   CTD; 444539; -.
DR   Xenbase; XB-GENE-968491; dhdh-like.1.L.
DR   OMA; NVRWGIM; -.
DR   OrthoDB; 943656at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 444539; Expressed in kidney and 19 other tissues.
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   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..330
FT                   /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT                   /id="PRO_0000315369"
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   330 AA;  36346 MW;  7D82C9FC1FA0D6D4 CRC64;
     MATKWGICST GRISNDFVVA LSTLPAVDHQ VVAVAARDLE KAKNFAQIHN IPKAYGSYEE
     LAKDPDIDVI YVGAIHPVHR DVVLMCLQNG KNVLCEKPLA MNSAQVRELI AAARKFNVFL
     MEAFWSRFFP VYEEIRTLLS QKAIGDVKFI RAEFGTPIYT VPRAVEKELG GGALLDIGCY
     CVQFVTMVFN GEKPESVTAR GFLHETGVDE TISIILEYSG KRQAILSSTI MAALPNQTAI
     CGTKGIIQIP SFMWSPTSVI VNGKETKFDV PHTTEPMNFS NGTGMSYEAE HVRQCLLKGL
     KESPIMSLAD SEMIATIMDE ALEQLGVMYP
 
 
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