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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)DescriptionActionsGraphical viewLength
    Active sitei52Proton donor1
    Sitei81Lowers pKa of active site TyrBy similarity1
    Binding sitei114SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi169 – 170NAD or NADP3 Publications2
    Nucleotide bindingi218 – 227NAD or NADP3 Publications10
    Nucleotide bindingi274 – 284NAD or NADP3 PublicationsAdd BLAST11

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi24W → F or Y: Strongly reduced affinity for xylose. Reduces NADH-dependent enzyme activity by over 96%. 1 Publication1
    Mutagenesisi51D → A: Slightly reduced enzyme activity. 1 Publication1
    Mutagenesisi274K → E: Reduces enzyme activity about 1000-fold. 1 Publication1
    Mutagenesisi274K → G or M: Reduces affinity for NAD and NADP. 1 Publication1
    Mutagenesisi274K → R: Increases affinity for NAD. Strongly reduced enzyme activity with NADP; when associated with D-276. 1 Publication1
    Mutagenesisi275S → A: Decreases affinity for NAD and NADP. 1 Publication1
    Mutagenesisi276N → D: Increases affinity for NAD. Decreases affinity for NADP. Strongly reduced enzyme activity with NADP; when associated with R-274. 1 Publication1
    Mutagenesisi280R → H: Increases affinity for NAD. 1 Publication1
    Mutagenesisi310N → A or D: Strongly decreased affinity for xylose. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001246611 – 322NAD(P)H-dependent D-xylose reductaseAdd BLAST322

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Structurei

    Secondary structure

    1322
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 9Combined sources3
    Beta strandi15 – 19Combined sources5
    Helixi28 – 40Combined sources13
    Beta strandi45 – 47Combined sources3
    Helixi50 – 52Combined sources3
    Helixi55 – 67Combined sources13
    Helixi73 – 75Combined sources3
    Beta strandi77 – 82Combined sources6
    Helixi84 – 86Combined sources3
    Helixi89 – 103Combined sources15
    Beta strandi108 – 113Combined sources6
    Turni124 – 126Combined sources3
    Helixi147 – 159Combined sources13
    Beta strandi162 – 170Combined sources9
    Helixi173 – 182Combined sources10
    Beta strandi189 – 193Combined sources5
    Helixi201 – 209Combined sources9
    Beta strandi213 – 217Combined sources5
    Turni219 – 222Combined sources4
    Helixi223 – 226Combined sources4
    Turni227 – 229Combined sources3
    Helixi231 – 234Combined sources4
    Helixi239 – 241Combined sources3
    Helixi243 – 252Combined sources10
    Helixi256 – 265Combined sources10
    Turni266 – 268Combined sources3
    Helixi278 – 283Combined sources6
    Helixi294 – 301Combined sources8
    Helixi313 – 316Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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
    PDB 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.
    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: November 2, 2016
    This is version 74 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.