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XYL1_MAGO7
ID   XYL1_MAGO7              Reviewed;         324 AA.
AC   G4N708; Q3MSM7;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=NAD(P)H-dependent D-xylose reductase XYR1;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=XYR1; ORFNames=MGG_03648;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=P1.2;
RX   PubMed=23499935; DOI=10.1016/j.febslet.2013.03.003;
RA   Klaubauf S., Ribot C., Melayah D., Lagorce A., Lebrun M.H., de Vries R.P.;
RT   "The pentose catabolic pathway of the rice-blast fungus Magnaporthe oryzae
RT   involves a novel pentose reductase restricted to few fungal species.";
RL   FEBS Lett. 587:1346-1352(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Catalyzes the initial reaction in the xylose utilization
CC       pathway by reducing D-xylose into xylitol. Xylose is a major component
CC       of hemicelluloses such as xylan. Most fungi utilize D-xylose via three
CC       enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase
CC       (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters
CC       pentose phosphate pathway (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH;
CC         Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.307;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH;
CC         Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.307;
CC   -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC   -!- INDUCTION: Overexpressed during growth on both D-xylose or L-arabinose
CC       compared to D-glucose. Significantly expressed during late stages of
CC       infection of barley leaves. {ECO:0000269|PubMed:23499935}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; AJ890447; CAI67591.1; -; mRNA.
DR   EMBL; CM001234; EHA49921.1; -; Genomic_DNA.
DR   RefSeq; XP_003716240.1; XM_003716192.1.
DR   AlphaFoldDB; G4N708; -.
DR   SMR; G4N708; -.
DR   STRING; 318829.MGG_03648T0; -.
DR   EnsemblFungi; MGG_03648T0; MGG_03648T0; MGG_03648.
DR   GeneID; 2676633; -.
DR   KEGG; mgr:MGG_03648; -.
DR   VEuPathDB; FungiDB:MGG_03648; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; G4N708; -.
DR   OMA; ECGEGVA; -.
DR   OrthoDB; 1016440at2759; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000009058; Chromosome 4.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:InterPro.
DR   GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd19115; AKR_AKR2D1; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044487; AKR2D.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome;
KW   Xylose metabolism.
FT   CHAIN           1..324
FT                   /note="NAD(P)H-dependent D-xylose reductase XYR1"
FT                   /id="PRO_0000425415"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         273..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36631 MW;  EA7067EE14977862 CRC64;
     MASPTMKLNN GLDMPQVGFG LWKVENSVCA DVVYNAIKAG YRLFDGACDY GNEVECGQGV
     KRAIDEGLVK REELFIVSKL WNTFHDGERV EPIVKKQLAD WGIEYFDLYL IHFPVALEYV
     DPSVRYPPGW HYDDAGTEIR PSKASIQETW TAMEKLVDAG LSKAIGVSNF QAQLLYDMLR
     YARIRPATLQ IEHHPYLVQQ RLIEACKTEG IVVTAYSSFG PASFKEFNME HAEALTPLLE
     EPTIVKLAEK YGKDPGQVLL RWATQRGLAV IPKSSREKTM KSNFEAVGWD MEDSDIKTIS
     ALDKGIRFNQ PANYFSTDKL WIFG
 
 
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