ID XYL2_YEAST Reviewed; 356 AA. AC Q07993; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 56. DE RecName: Full=D-xylulose reductase; DE EC=1.1.1.9; DE AltName: Full=Xylitol dehydrogenase; DE Short=XDH; GN Name=XYL2; OrderedLocusNames=YLR070C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313267; PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(1997). RN [2] RP INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10486580; DOI=10.1016/S0014-5793(99)01016-9; RA Richard P., Toivari M.H., Penttilae M.; RT "Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a RT xylitol dehydrogenase."; RL FEBS Lett. 457:135-138(1999). CC -!- CATALYTIC ACTIVITY: Xylitol + NAD(+) = D-xylulose + NADH. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.1 mM for D-xylose; CC KM=240 uM for NADH; CC KM=25 mM for xylitol; CC KM=100 uM for NAD; CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC arabinitol; D-xylulose 5-phosphate from L-arabinose (fungi route): CC step 4/5. CC -!- INDUCTION: By xylose. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC 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; Z73242; CAA97627.1; -; Genomic_DNA. DR PIR; S64902; S64902. DR RefSeq; NP_013171.1; -. DR HSSP; Q00796; 1PL7. DR DIP; DIP:4533N; -. DR IntAct; Q07993; 4. DR Ensembl; YLR070C; Saccharomyces cerevisiae. DR GeneID; 850759; -. DR GenomeReviews; Y13138_GR; YLR070C. DR KEGG; sce:YLR070C; -. DR NMPDR; fig|4932.3.peg.4162; -. DR CYGD; YLR070c; -. DR SGD; S000004060; XYL2. DR HOGENOM; Q07993; -. DR OMA; Q07993; THGRIAN. DR BRENDA; 1.1.1.9; 250. DR NextBio; 966906; -. DR GO; GO:0046526; F:D-xylulose reductase activity; IDA:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0005999; P:xylulose biosynthetic process; IDA:SGD. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR002328; ADH_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR ProDom; PD040557; GroES_related; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Metal-binding; NAD; KW Oxidoreductase; Xylose metabolism; Zinc. FT CHAIN 1 356 D-xylulose reductase. FT /FTId=PRO_0000270925. FT NP_BIND 179 184 NAD (Potential). FT METAL 44 44 Zinc; catalytic (By similarity). FT METAL 69 69 Zinc; catalytic (By similarity). FT METAL 155 155 Zinc; catalytic (By similarity). SQ SEQUENCE 356 AA; 38600 MW; 5DFD19BDB2E0AE00 CRC64; MTDLTTQEAI VLERPGKITL TNVSIPKISD PNEVIIQIKA TGICGSDIHY YTHGRIANYV VESPMVLGHE SSGIVALIGE NVKTLKVGDR VALEPGIPDR FSPEMKEGRY NLDPNLKFAA TPPFDGTLTK YYKTMKDFVY KLPDDVSFEE GALIEPLSVA IHANKLAKIK FGARCVVFGA GPIGLLAGKV ASVFGAADVV FVDLLENKLE TARQFGATHI VNSGDLPHGV TVDSVIKKAI GKKGADVVFE CSGAEPCVRA GIEVCKAGGT IVQVGMGQEE IQFPISIIPT KELTFQGCFR YCQGDYSDSI ELVSSRKLSL KPFITHRYSF KDAVEAFEET SHHPLNNIKT IIEGPE //