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Protein

Glyoxalase 3

Gene

GLX3

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. Selective for MG, does not use glyoxal as substrate. Plays a role in detoxifying endogenously produced MG, particularly when glycerol is the principal carbon source (PubMed:24302734). Important for viability in stationary phase (By similarity).By similarity1 Publication

Catalytic activityi

(R)-lactate = methylglyoxal + H2O.1 Publication

Kineticsi

kcat is 7.8 sec(-1) with methylglyoxal as substrate.1 Publication

  1. KM=5.5 mM for methylglyoxal1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei136 – 13611 Publication
    Active sitei137 – 13711 Publication
    Active sitei168 – 16811 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Stress response

    Protein family/group databases

    MEROPSiC56.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyoxalase 31 Publication (EC:4.2.1.1301 Publication)
    Alternative name(s):
    Glutathione-independent glyoxalase1 Publication
    Gene namesi
    Name:GLX31 Publication
    ORF Names:CaO19.251, CaO19.7882, orf19.251, orf19.7882
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    Proteomesi
    • UP000000559 Componenti: Unassembled WGS sequence

    Pathology & Biotechi

    Disruption phenotypei

    Has a 3- to 5-fold increase in levels of intracellular methylglyoxal compared with wild-type cells grown in the same media.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi136 – 1361C → S: Abolishes catalytic activity. 1 Publication
    Mutagenesisi137 – 1371H → F: Reduces catalytic activity by 75%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Glyoxalase 3PRO_0000432110Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361Cysteine sulfinic acid (-SO2H)By similarity

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76Combined sources
    Helixi26 – 3914Combined sources
    Beta strandi42 – 509Combined sources
    Helixi56 – 583Combined sources
    Turni61 – 633Combined sources
    Helixi66 – 738Combined sources
    Helixi78 – 847Combined sources
    Helixi89 – 913Combined sources
    Helixi94 – 963Combined sources
    Beta strandi98 – 1025Combined sources
    Helixi108 – 1114Combined sources
    Helixi112 – 1143Combined sources
    Helixi116 – 12712Combined sources
    Beta strandi131 – 1355Combined sources
    Helixi138 – 1425Combined sources
    Turni148 – 1503Combined sources
    Beta strandi151 – 1533Combined sources
    Turni154 – 1574Combined sources
    Helixi165 – 1706Combined sources
    Helixi174 – 1796Combined sources
    Helixi185 – 1928Combined sources
    Beta strandi207 – 2104Combined sources
    Beta strandi213 – 2164Combined sources
    Helixi219 – 2213Combined sources
    Helixi222 – 23312Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LRUX-ray1.60A1-236[»]
    ProteinModelPortaliQ5AF03.
    SMRiQ5AF03. Positions 3-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    InParanoidiQ5AF03.
    OrthoDBiEOG73547H.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR002818. DJ-1/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5AF03-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVKVLLALTS YNETFYSDGK KTGVFVVEAL HPFEVFRKKG YEIQLASETG
    60 70 80 90 100
    TFGWDDHSVV PDFLNGEDKE IFDNVNSEFN VALKNLKKAS DLDPNDYDIF
    110 120 130 140 150
    FGSAGHGTLF DYPNAKDLQK IATTVYDKGG VVSAVCHGPA IFENLNDPKT
    160 170 180 190 200
    GEPLIKGKKI TGFTDIGEDI LGVTDIMKKG NLLTIKQVAE KEGATYIEPE
    210 220 230
    GPWDNFTVTD GRIVTGVNPQ SAVKTAEDVI AAFECN
    Length:236
    Mass (Da):25,812
    Last modified:April 26, 2005 - v1
    Checksum:i4C77E841710C4542
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti85 – 851N → I in allele CaO19.251. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AACQ01000026 Genomic DNA. Translation: EAL01225.1.
    AACQ01000027 Genomic DNA. Translation: EAL01090.1.
    RefSeqiXP_719950.1. XM_714857.1.
    XP_720081.1. XM_714988.1.

    Genome annotation databases

    EnsemblFungiiEAL01090; EAL01090; CaO19.251.
    EAL01225; EAL01225; CaO19.7882.
    GeneIDi3638251.
    3638325.
    KEGGical:CaO19.251.
    cal:CaO19.7882.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AACQ01000026 Genomic DNA. Translation: EAL01225.1.
    AACQ01000027 Genomic DNA. Translation: EAL01090.1.
    RefSeqiXP_719950.1. XM_714857.1.
    XP_720081.1. XM_714988.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LRUX-ray1.60A1-236[»]
    ProteinModelPortaliQ5AF03.
    SMRiQ5AF03. Positions 3-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiC56.004.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiEAL01090; EAL01090; CaO19.251.
    EAL01225; EAL01225; CaO19.7882.
    GeneIDi3638251.
    3638325.
    KEGGical:CaO19.251.
    cal:CaO19.7882.

    Phylogenomic databases

    InParanoidiQ5AF03.
    OrthoDBiEOG73547H.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR002818. DJ-1/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SC5314 / ATCC MYA-2876.
    2. "A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans."
      Hasim S., Hussin N.A., Alomar F., Bidasee K.R., Nickerson K.W., Wilson M.A.
      J. Biol. Chem. 289:1662-1674(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF CYS-136 AND HIS-137, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiHSP31_CANAL
    AccessioniPrimary (citable) accession number: Q5AF03
    Secondary accession number(s): Q5AEL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 4, 2015
    Last sequence update: April 26, 2005
    Last modified: July 6, 2016
    This is version 59 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, Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. 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.