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Protein

D-xylulose reductase

Gene

XYL2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Xylitol + NAD+ = D-xylulose + NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=1.1 mM for D-xylose1 Publication
  2. KM=240 µM for NADH1 Publication
  3. KM=25 mM for xylitol1 Publication
  4. KM=100 µM for NAD1 Publication

    Pathwayi: L-arabinose degradation via L-arabinitol

    This protein is involved in step 4 of the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route).
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. D-xylulose reductase (XYL2)
    5. no protein annotated in this organism
    This subpathway is part of the pathway L-arabinose degradation via L-arabinitol, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-arabinose (fungal route), the pathway L-arabinose degradation via L-arabinitol and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi44 – 441Zinc; catalyticBy similarity
    Metal bindingi69 – 691Zinc; catalyticBy similarity
    Metal bindingi155 – 1551Zinc; catalyticBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi179 – 1846NADSequence analysis

    GO - Molecular functioni

    • D-xylulose reductase activity Source: SGD
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Xylose metabolism

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YLR070C-MONOMER.
    ReactomeiR-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
    UniPathwayiUPA00146; UER00577.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-xylulose reductase (EC:1.1.1.9)
    Alternative name(s):
    Xylitol dehydrogenase
    Short name:
    XDH
    Gene namesi
    Name:XYL2
    Ordered Locus Names:YLR070C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XII

    Organism-specific databases

    EuPathDBiFungiDB:YLR070C.
    SGDiS000004060. XYL2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356D-xylulose reductasePRO_0000270925Add
    BLAST

    Expressioni

    Inductioni

    By xylose.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi31344. 26 interactions.
    DIPiDIP-4533N.
    IntActiQ07993. 2 interactions.
    MINTiMINT-499230.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07993.
    SMRiQ07993. Positions 7-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00840000130391.
    HOGENOMiHOG000294670.
    InParanoidiQ07993.
    KOiK05351.
    OMAiTHGRIAN.
    OrthoDBiEOG79CZ8G.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07993-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDLTTQEAI VLERPGKITL TNVSIPKISD PNEVIIQIKA TGICGSDIHY
    60 70 80 90 100
    YTHGRIANYV VESPMVLGHE SSGIVALIGE NVKTLKVGDR VALEPGIPDR
    110 120 130 140 150
    FSPEMKEGRY NLDPNLKFAA TPPFDGTLTK YYKTMKDFVY KLPDDVSFEE
    160 170 180 190 200
    GALIEPLSVA IHANKLAKIK FGARCVVFGA GPIGLLAGKV ASVFGAADVV
    210 220 230 240 250
    FVDLLENKLE TARQFGATHI VNSGDLPHGV TVDSVIKKAI GKKGADVVFE
    260 270 280 290 300
    CSGAEPCVRA GIEVCKAGGT IVQVGMGQEE IQFPISIIPT KELTFQGCFR
    310 320 330 340 350
    YCQGDYSDSI ELVSSRKLSL KPFITHRYSF KDAVEAFEET SHHPLNNIKT

    IIEGPE
    Length:356
    Mass (Da):38,600
    Last modified:November 1, 1996 - v1
    Checksum:i5DFD19BDB2E0AE00
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z73242 Genomic DNA. Translation: CAA97627.1.
    BK006945 Genomic DNA. Translation: DAA09387.1.
    PIRiS64902.
    RefSeqiNP_013171.1. NM_001181957.1.

    Genome annotation databases

    EnsemblFungiiYLR070C; YLR070C; YLR070C.
    GeneIDi850759.
    KEGGisce:YLR070C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z73242 Genomic DNA. Translation: CAA97627.1.
    BK006945 Genomic DNA. Translation: DAA09387.1.
    PIRiS64902.
    RefSeqiNP_013171.1. NM_001181957.1.

    3D structure databases

    ProteinModelPortaliQ07993.
    SMRiQ07993. Positions 7-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31344. 26 interactions.
    DIPiDIP-4533N.
    IntActiQ07993. 2 interactions.
    MINTiMINT-499230.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYLR070C; YLR070C; YLR070C.
    GeneIDi850759.
    KEGGisce:YLR070C.

    Organism-specific databases

    EuPathDBiFungiDB:YLR070C.
    SGDiS000004060. XYL2.

    Phylogenomic databases

    GeneTreeiENSGT00840000130391.
    HOGENOMiHOG000294670.
    InParanoidiQ07993.
    KOiK05351.
    OMAiTHGRIAN.
    OrthoDBiEOG79CZ8G.

    Enzyme and pathway databases

    UniPathwayiUPA00146; UER00577.
    BioCyciYEAST:YLR070C-MONOMER.
    ReactomeiR-SCE-5652227. Fructose biosynthesis.
    R-SCE-5661270. Catabolism of glucuronate to xylulose-5-phosphate.

    Miscellaneous databases

    NextBioi966906.
    PROiQ07993.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Evidence that the gene YLR070c of Saccharomyces cerevisiae encodes a xylitol dehydrogenase."
      Richard P., Toivari M.H., Penttilae M.
      FEBS Lett. 457:135-138(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiXYL2_YEAST
    AccessioniPrimary (citable) accession number: Q07993
    Secondary accession number(s): D6VY71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2007
    Last sequence update: November 1, 1996
    Last modified: May 11, 2016
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.