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UniProtKB - O74237 (XYL1_CANTE)

Entry version 85 (02 Jun 2021)
Sequence version 1 (01 Nov 1998)
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Protein

NAD(P)H-dependent D-xylose reductase

Gene

XYL1

Organism
Candida tenuis (Yeast) (Yamadazyma tenuis)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei52Proton donor1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei81Lowers pKa of active site TyrBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei114SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi169 – 170NAD or NADP3 Publications2
    Nucleotide bindingi218 – 227NAD or NADP3 Publications10
    Nucleotide bindingi274 – 284NAD or NADP3 PublicationsAdd BLAST11

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processCarbohydrate metabolism, Xylose metabolism
    LigandNAD, NADP

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.1.1.307, 1144

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		O74237

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00810

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    NAD(P)H-dependent D-xylose reductase (EC:1.1.1.307)
    Short name:
    XR
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:XYL1
    Synonyms:XYLR
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCandida tenuis (Yeast) (Yamadazyma tenuis)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri2315449 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Yamadazyma

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001246611 – 322NAD(P)H-dependent D-xylose reductaseAdd BLAST322

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    4 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1322
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		O74237

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		O74237

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd19113, AKR_AKR2B1-10, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.20.20.100, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR020471, AKR
    IPR044486, AKR2B1
    IPR018170, Aldo/ket_reductase_CS
    IPR023210, NADP_OxRdtase_dom
    IPR036812, NADP_OxRdtase_dom_sf

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00248, Aldo_ket_red, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000097, AKR, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00069, ALDKETRDTASE

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51430, SSF51430, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00798, ALDOKETO_REDUCTASE_1, 1 hit
    PS00062, ALDOKETO_REDUCTASE_2, 1 hit
    PS00063, ALDOKETO_REDUCTASE_3, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C74A8FBC9357690
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		AF074484 Genomic DNA Translation: AAC25601.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    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[»]
    SMRiO74237
    ModBaseiSearch...
    PDBe-KBiSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00810
    BRENDAi1.1.1.307, 1144
    SABIO-RKiO74237

    Miscellaneous databases

    EvolutionaryTraceiO74237

    Family and domain databases

    CDDicd19113, AKR_AKR2B1-10, 1 hit
    Gene3Di3.20.20.100, 1 hit
    InterProiView protein in InterPro
    IPR020471, AKR
    IPR044486, AKR2B1
    IPR018170, Aldo/ket_reductase_CS
    IPR023210, NADP_OxRdtase_dom
    IPR036812, NADP_OxRdtase_dom_sf
    PfamiView protein in Pfam
    PF00248, Aldo_ket_red, 1 hit
    PIRSFiPIRSF000097, AKR, 1 hit
    PRINTSiPR00069, ALDKETRDTASE
    SUPFAMiSSF51430, SSF51430, 1 hit
    PROSITEiView protein in PROSITE
    PS00798, ALDOKETO_REDUCTASE_1, 1 hit
    PS00062, ALDOKETO_REDUCTASE_2, 1 hit
    PS00063, ALDOKETO_REDUCTASE_3, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXYL1_CANTE
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O74237
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: November 1, 1998
    Last modified: June 2, 2021
    This is version 85 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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