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DHDH_DANRE
ID   DHDH_DANRE              Reviewed;         334 AA.
AC   Q642M9; A8E7G1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 101.
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; ORFNames=ch211-203b17.3, zgc:101723;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-299.
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAP09380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC081393; AAH81393.1; -; mRNA.
DR   EMBL; BX119923; CAP09380.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_001005600.1; NM_001005600.1.
DR   AlphaFoldDB; Q642M9; -.
DR   SMR; Q642M9; -.
DR   STRING; 7955.ENSDARP00000115782; -.
DR   PaxDb; Q642M9; -.
DR   Ensembl; ENSDART00000158547; ENSDARP00000141650; ENSDARG00000019081.
DR   GeneID; 449558; -.
DR   KEGG; dre:449558; -.
DR   CTD; 449558; -.
DR   ZFIN; ZDB-GENE-040927-25; dhdh.2.
DR   eggNOG; KOG2741; Eukaryota.
DR   GeneTree; ENSGT00390000007946; -.
DR   InParanoid; Q642M9; -.
DR   OMA; FINYCQY; -.
DR   OrthoDB; 943656at2759; -.
DR   PhylomeDB; Q642M9; -.
DR   PRO; PR:Q642M9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 18.
DR   Bgee; ENSDARG00000019081; Expressed in muscle tissue and 27 other tissues.
DR   ExpressionAtlas; Q642M9; baseline and differential.
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; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase"
FT                   /id="PRO_0000315368"
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        25
FT                   /note="P -> Q (in Ref. 1; AAH81393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="G -> A (in Ref. 1; AAH81393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="S -> T (in Ref. 1; AAH81393)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36566 MW;  C246A390F506702C CRC64;
     MALRWGICSA GKISHDFTVA LRTLPAEQHQ VVAVAARELA HAQEFAQKHS IPRAYGSYEE
     LAEDPEIDVV YVGTIHPHHL RVGLLFMNAK KNVLCEKPLA MNLKEVQQMI SAARRSDVFL
     MEAVWTRFFP ASLEISRLLS QNAVGQVKLV RADFGAALLG VPRAVQKHLG GGALLDIGIY
     CIQFVLMVFN GEKPEQIQAS GVCLDTGVDE AMVVTLKFSG HRLAVCTCTV AAELPNEALI
     VGTEGTIKVP AHMWCPTSLL VNGVETQFPV PDPHLPLNFI NSTGMRYEAE EVRRCVLAGL
     KESSRMSHAD SALLADIMDE ARRQVGVVYS QDSQ
 
 
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