(data stored in ACNUC7421 zone)

SWISSPROT: XYL1_ASPNC

ID   XYL1_ASPNC              Reviewed;         319 AA.
AC   A2Q8B5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 74.
DE   RecName: Full=Probable NAD(P)H-dependent D-xylose reductase xyl1;
DE            Short=XR;
DE            EC=1.1.1.307;
GN   Name=xyl1; Synonyms=xyrA; ORFNames=An01g03740;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
DR   EMBL; AM269959; CAK36912.1; -; Genomic_DNA.
DR   SMR; A2Q8B5; -.
DR   PaxDb; A2Q8B5; -.
DR   PRIDE; A2Q8B5; -.
DR   EnsemblFungi; CAK36912; CAK36912; An01g03740.
DR   HOGENOM; HOG000250272; -.
DR   BioCyc; MetaCyc:MONOMER-13190; -.
DR   UniPathway; UPA00810; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0032866; F:D-xylose:NADP reductase activity; IMP:AspGD.
DR   GO; GO:0019568; P:arabinose catabolic process; IMP:AspGD.
DR   GO; GO:0042843; P:D-xylose catabolic process; IMP:AspGD.
DR   CDD; cd06660; Aldo_ket_red; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR020471; Aldo/keto_reductase.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR11732; PTHR11732; 1.
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.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q8B5.
DR   SWISS-2DPAGE; A2Q8B5.
KW   Carbohydrate metabolism; Glycoprotein; NAD; NADP; Oxidoreductase;
KW   Xylose metabolism.
FT   CHAIN           1..319
FT                   /note="Probable NAD(P)H-dependent D-xylose reductase xyl1"
FT                   /id="PRO_0000393500"
FT   NP_BIND         166..167
FT                   /note="NAD or NADP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         215..224
FT                   /note="NAD or NADP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         271..281
FT                   /note="NAD or NADP"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        50
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  36095 MW;  C7D6DB56D37E973F CRC64;
     MASPTVKLNS GYDMPLVGFG LWKVNNDTCA DQIYHAIKEG YRLFDGACDY GNEVEAGQGI
     ARAIKDGLVK REELFIVSKL WNSFHDGDRV EPICRKQLAD WGIDYFDLYI VHFPISLKYV
     DPAVRYPPGW KSEKDELEFG NATIQETWTA MESLVDKKLA RSIGISNFSA QLVMDLLRYA
     RIRPATLQIE HHPYLTQTRL VEYAQKEGLT VTAYSSFGPL SFLELSVQNA VDSPPLFEHQ
     LVKSIAEKHG RTPAQVLLRW ATQRGIAVIP KSNNPQRLKQ NLDVTGWNLE EEEIKAISGL
     DRGLRFNDPL GYGLYAPIF
//

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