ID A0A124BXX0_ASPNG Unreviewed; 282 AA. AC A0A124BXX0; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 02-JUN-2021, entry version 19. DE RecName: Full=D-xylose reductase {ECO:0000256|ARBA:ARBA00012845}; DE EC=1.1.1.307 {ECO:0000256|ARBA:ARBA00012845}; GN ORFNames=ABL_06379 {ECO:0000313|EMBL:GAQ43718.1}; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ43718.1, ECO:0000313|Proteomes:UP000068243}; RN [1] {ECO:0000313|Proteomes:UP000068243} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243}; RX PubMed=26893421; DOI=10.1128/genomeA.01700-15; RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.; RT "Draft genome sequence of Aspergillus niger strain An76."; RL Genome Announc. 4:E0170015-E0170015(2016). 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. {ECO:0000256|ARBA:ARBA00003261}. 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; Evidence={ECO:0000256|ARBA:ARBA00000578}; 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; Evidence={ECO:0000256|ARBA:ARBA00001334}; CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAQ43718.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BCMY01000010; GAQ43718.1; -; Genomic_DNA. DR EnsemblFungi; GAQ43718; GAQ43718; ABL_06379. DR Proteomes; UP000068243; Unassembled WGS sequence. DR GO; GO:0047834; F:D-threo-aldose 1-dehydrogenase activity; IEA:InterPro. DR GO; GO:0032866; F:D-xylose:NADP reductase activity; IEA:RHEA. DR Gene3D; 3.20.20.100; -; 1. DR InterPro; IPR020471; AKR. 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; 2. DR PIRSF; PIRSF000097; AKR; 2. 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 4: Predicted; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000068243}. FT DOMAIN 29..206 FT /note="Aldo_ket_red" FT /evidence="ECO:0000259|Pfam:PF00248" FT DOMAIN 209..265 FT /note="Aldo_ket_red" FT /evidence="ECO:0000259|Pfam:PF00248" FT ACT_SITE 55 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1" FT BINDING 113 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2" FT SITE 80 FT /note="Lowers pKa of active site Tyr" FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3" SQ SEQUENCE 282 AA; 31661 MW; C4017EDAE5C2C42C CRC64; MSALQSLRST YRLNSGHEIP ILGYGVYLIP ASQTEKAVLE ALKVGYRHVD SAIMYRNEKA CGRAIANSGL PRSEIFFTTK IPPGSMGYDR TKRAIDSSLR EAQQEYFDLI LLHAPYGGKE ARLGSWKALV EAQKAGKTRS IGVSNYGIHH LDELEEYIKS GGGGQIDVGQ YELHPWLDRS EIAEWLQKRD IVVQAYSPLA HGTRMGERVL KELGKKYGKS PAQIMIRWGL QKGFVPLPKS VTPSRIQENA EVFDFALTEE EMKLLHTGEY SPTDWDPTVD YD //