ID   LXRA_ASPNA              Reviewed;         298 AA.
AC   G3YG17;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=L-xylulose reductase {ECO:0000303|PubMed:20654618};
DE            EC=1.1.1.10 {ECO:0000269|PubMed:20654618};
GN   Name=lxrA {ECO:0000303|PubMed:20654618}; ORFNames=ASPNIDRAFT_177736;
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC   328 / USDA 3528.7;
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
RN   [2]
RP   INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=20654618; DOI=10.1016/j.febslet.2010.06.037;
RA   Mojzita D., Vuoristo K., Koivistoinen O.M., Penttilae M., Richard P.;
RT   "The 'true' L-xylulose reductase of filamentous fungi identified in
RT   Aspergillus niger.";
RL   FEBS Lett. 584:3540-3544(2010).
CC   -!- FUNCTION: L-xylulose reductase involved in the catabolism of L-
CC       arabinose through an oxidoreductive pathway. Catalyzes the NADPH-
CC       dependent reduction of L-xylulose. {ECO:0000269|PubMed:20654618}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + xylitol = H(+) + L-xylulose + NADPH;
CC         Xref=Rhea:RHEA:17025, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151,
CC         ChEBI:CHEBI:17399, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.10;
CC         Evidence={ECO:0000269|PubMed:20654618};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 mM for L-xylulose {ECO:0000269|PubMed:20654618};
CC         Vmax=650 umol/min/mg enzyme towards L-xylulose
CC         {ECO:0000269|PubMed:20654618};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route):
CC       step 3/5. {ECO:0000305}.
CC   -!- INDUCTION: Transcription is repressed by D-glucose and induced by D-
CC       xylose and L-arabinose. {ECO:0000269|PubMed:20654618}.
CC   -!- DISRUPTION PHENOTYPE: Reduces slightly growth rate on L-arabinose and
CC       abolishes L-xylulose reductase activity. {ECO:0000269|PubMed:20654618}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; ACJE01000021; EHA17862.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3YG17; -.
DR   SMR; G3YG17; -.
DR   STRING; 380704.G3YG17; -.
DR   EnsemblFungi; EHA17862; EHA17862; ASPNIDRAFT_177736.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_177736; -.
DR   HOGENOM; CLU_010194_1_3_1; -.
DR   SABIO-RK; G3YG17; -.
DR   UniPathway; UPA00146; UER00576.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
DR   GO; GO:0050038; F:L-xylulose reductase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Arabinose catabolism; Carbohydrate metabolism; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..298
FT                   /note="L-xylulose reductase"
FT                   /id="PRO_0000433645"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT   BINDING         11..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT   BINDING         179
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
SQ   SEQUENCE   298 AA;  31924 MW;  7845F86EC2462BF2 CRC64;
     MSRSLEGKFA IITGGSRGIG EAIAHNLASK GCSLLLNYTS DSSRTRTESL CNTLSTTHKI
     TCIPVQADLS DPAPAVNTII SAAKTHFTSP TTNTLTIDIL INNAGVSKDR FLNDPSSGPI
     DPAYFNWHYT INVLAPLLLT QACAEYLPRK PAHSGRIINI SSISSSLGFT GQSVYGGTKA
     ALEAMTRTWA RELADVATVN AVNPGPVVGD MYFATGEEFW KQMQGFQDNT PLSKLVDGEE
     AVEELLSEEQ KRLIREKMGG RRPAFTREIA GVVGMLCTED GAWCTGSVVC ANGGLKFT