ID DCXR_TRIRE Reviewed; 266 AA. AC Q8NK50; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 25-NOV-2008, entry version 30. DE RecName: Full=L-xylulose reductase; DE Short=XR; DE EC=1.1.1.10; GN Name=lxr1; OS Trichoderma reesei (Hypocrea jecorina). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae; OC Hypocrea. OX NCBI_TaxID=51453; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ENZYME ACTIVITY. RX MEDLINE=22005794; PubMed=12009906; DOI=10.1021/bi025529i; RA Richard P., Putkonen M., Vaeaenaenen R., Londesborough J., RA Penttilae M.; RT "The missing link in the fungal L-arabinose catabolic pathway, RT identification of the L-xylulose reductase gene."; RL Biochemistry 41:6432-6437(2002). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of L-xylulose, CC D-xylulose, D-fructose, and L-sorbose, with the highest affinity CC for L-xylulose. CC -!- CATALYTIC ACTIVITY: Xylitol + NADP(+) = L-xylulose + NADPH. CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungi route): CC step 3/5. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF375616; AAM20896.1; -; mRNA. DR HSSP; Q9ZFY9; 1FK8. DR BioCyc; MetaCyc:MON-13194; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0050038; F:L-xylulose reductase activity; IEA:EC. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002198; DHase_sc/Rdtase_SDR. DR InterPro; IPR002347; Glc/ribitol_DHase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR19410; ADH_short_C2; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; FALSE_NEG. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; NADP; Oxidoreductase; Xylose metabolism. FT CHAIN 1 266 L-xylulose reductase. FT /FTId=PRO_0000054558. FT NP_BIND 23 53 NADP (By similarity). FT ACT_SITE 174 174 Proton acceptor (By similarity). FT ACT_SITE 178 178 By similarity. FT BINDING 159 159 Substrate (By similarity). SQ SEQUENCE 266 AA; 28478 MW; 1CF56334DA86F109 CRC64; MPQPVPTANR LLDLFSLKGK VVVVTGASGP RGMGIEAARG CAEMGADLAI TYSSRKEGAE KNAEELTKEY GVKVKVYKVN QSDYNDVERF VNQVVSDFGK IDAFIANAGA TANSGVVDGS ASDWDHVIQV DLSGTAYCAK AVGAHFKKQG HGSLVITASM SGHVANYPQE QTSYNVAKAG CIHLARSLAN EWRDFARVNS ISPGYIDTGL SDFIDEKTQE LWRSMIPMGR NGDAKELKGA YVYLVSDASS YTTGADIVID GGYTTR //