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Protein

NAD(P)H-dependent D-xylose reductase

Gene

XYL1

Organism
Candida tenuis (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.

Catalytic activityi

Xylitol + NAD(P)+ = D-xylose + NAD(P)H.

Kineticsi

  1. KM=142 mM for xylose2 Publications
  2. KM=38 µM for NADH2 Publications
  3. KM=3 µM for NADPH2 Publications

    Pathwayi: D-xylose degradation

    This protein is involved in the pathway D-xylose degradation, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway D-xylose degradation and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei52 – 521Proton donor
    Sitei81 – 811Lowers pKa of active site TyrBy similarity
    Binding sitei114 – 1141SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi169 – 1702NAD or NADP3 Publications
    Nucleotide bindingi218 – 22710NAD or NADP3 Publications
    Nucleotide bindingi274 – 28411NAD or NADP3 PublicationsAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Xylose metabolism

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.307. 1144.
    SABIO-RKO74237.
    UniPathwayiUPA00810.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD(P)H-dependent D-xylose reductase (EC:1.1.1.307)
    Short name:
    XR
    Gene namesi
    Name:XYL1
    Synonyms:XYLR
    OrganismiCandida tenuis (Yeast)
    Taxonomic identifieri45596 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeYamadazymaYamadazyma/Candida clade

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241W → F or Y: Strongly reduced affinity for xylose. Reduces NADH-dependent enzyme activity by over 96%. 1 Publication
    Mutagenesisi51 – 511D → A: Slightly reduced enzyme activity. 1 Publication
    Mutagenesisi274 – 2741K → E: Reduces enzyme activity about 1000-fold. 1 Publication
    Mutagenesisi274 – 2741K → G or M: Reduces affinity for NAD and NADP. 1 Publication
    Mutagenesisi274 – 2741K → R: Increases affinity for NAD. Strongly reduced enzyme activity with NADP; when associated with D-276. 1 Publication
    Mutagenesisi275 – 2751S → A: Decreases affinity for NAD and NADP. 1 Publication
    Mutagenesisi276 – 2761N → D: Increases affinity for NAD. Decreases affinity for NADP. Strongly reduced enzyme activity with NADP; when associated with R-274. 1 Publication
    Mutagenesisi280 – 2801R → H: Increases affinity for NAD. 1 Publication
    Mutagenesisi310 – 3101N → A or D: Strongly decreased affinity for xylose. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322NAD(P)H-dependent D-xylose reductasePRO_0000124661Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Structurei

    Secondary structure

    1
    322
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Beta strandi15 – 195Combined sources
    Helixi28 – 4013Combined sources
    Beta strandi45 – 473Combined sources
    Helixi50 – 523Combined sources
    Helixi55 – 6713Combined sources
    Helixi73 – 753Combined sources
    Beta strandi77 – 826Combined sources
    Helixi84 – 863Combined sources
    Helixi89 – 10315Combined sources
    Beta strandi108 – 1136Combined sources
    Turni124 – 1263Combined sources
    Helixi147 – 15913Combined sources
    Beta strandi162 – 1709Combined sources
    Helixi173 – 18210Combined sources
    Beta strandi189 – 1935Combined sources
    Helixi201 – 2099Combined sources
    Beta strandi213 – 2175Combined sources
    Turni219 – 2224Combined sources
    Helixi223 – 2264Combined sources
    Turni227 – 2293Combined sources
    Helixi231 – 2344Combined sources
    Helixi239 – 2413Combined sources
    Helixi243 – 25210Combined sources
    Helixi256 – 26510Combined sources
    Turni266 – 2683Combined sources
    Helixi278 – 2836Combined sources
    Helixi294 – 3018Combined sources
    Helixi313 – 3164Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEZX-ray2.20A/B1-322[»]
    1K8CX-ray2.10A/B/C/D1-322[»]
    1MI3X-ray1.80A/B/C/D1-322[»]
    1R38X-ray2.20A/B/C/D1-322[»]
    1SM9X-ray2.20A/B/C/D1-322[»]
    1YE4X-ray2.40A/B/C/D1-322[»]
    1YE6X-ray2.30A/B/C/D1-322[»]
    1Z9AX-ray2.40A/B/C/D2-322[»]
    ProteinModelPortaliO74237.
    SMRiO74237. Positions 4-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO74237.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O74237-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSASIPDIKL SSGHLMPSIG FGCWKLANAT AGEQVYQAIK AGYRLFDGAE
    60 70 80 90 100
    DYGNEKEVGD GVKRAIDEGL VKREEIFLTS KLWNNYHDPK NVETALNKTL
    110 120 130 140 150
    ADLKVDYVDL FLIHFPIAFK FVPIEEKYPP GFYCGDGNNF VYEDVPILET
    160 170 180 190 200
    WKALEKLVAA GKIKSIGVSN FPGALLLDLL RGATIKPAVL QVEHHPYLQQ
    210 220 230 240 250
    PKLIEFAQKA GVTITAYSSF GPQSFVEMNQ GRALNTPTLF AHDTIKAIAA
    260 270 280 290 300
    KYNKTPAEVL LRWAAQRGIA VIPKSNLPER LVQNRSFNTF DLTKEDFEEI
    310 320
    AKLDIGLRFN DPWDWDNIPI FV
    Length:322
    Mass (Da):36,021
    Last modified:November 1, 1998 - v1
    Checksum:i4C74A8FBC9357690
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF074484 Genomic DNA. Translation: AAC25601.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF074484 Genomic DNA. Translation: AAC25601.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEZX-ray2.20A/B1-322[»]
    1K8CX-ray2.10A/B/C/D1-322[»]
    1MI3X-ray1.80A/B/C/D1-322[»]
    1R38X-ray2.20A/B/C/D1-322[»]
    1SM9X-ray2.20A/B/C/D1-322[»]
    1YE4X-ray2.40A/B/C/D1-322[»]
    1YE6X-ray2.30A/B/C/D1-322[»]
    1Z9AX-ray2.40A/B/C/D2-322[»]
    ProteinModelPortaliO74237.
    SMRiO74237. Positions 4-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00810.
    BRENDAi1.1.1.307. 1144.
    SABIO-RKO74237.

    Miscellaneous databases

    EvolutionaryTraceiO74237.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 2 hits.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiXYL1_CANTE
    AccessioniPrimary (citable) accession number: O74237
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: November 1, 1998
    Last modified: September 7, 2016
    This is version 72 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

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.