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Protein

Cys-Gly metallodipeptidase DUG1

Gene

DUG1

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

Functioni

Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides.2 Publications

Cofactori

Zn2+1 Publication, Mn2+1 Publication

Kineticsi

  1. KM=0.4 mM for Cys-Gly (at pH 8.0 and in the presence of 20 µM manganese ions)
  2. KM=0.8 mM for Cys-Gly (at pH 8.0 and in the presence of 200 µM zinc ions)

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi102Zinc 2By similarity1
    Active sitei104By similarity1
    Metal bindingi137Zinc 1By similarity1
    Metal bindingi137Zinc 2By similarity1
    Active sitei171Proton acceptorBy similarity1
    Metal bindingi172Zinc 1By similarity1
    Metal bindingi200Zinc 2By similarity1
    Metal bindingi450Zinc 1By similarity1

    GO - Molecular functioni

    • metallodipeptidase activity Source: SGD
    • omega peptidase activity Source: SGD
    • zinc ion binding Source: GO_Central

    GO - Biological processi

    • glutathione catabolic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Dipeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-4.
    YEAST:MONOMER3O-4.
    ReactomeiR-SCE-1614635. Sulfur amino acid metabolism.
    R-SCE-174403. Glutathione synthesis and recycling.
    SABIO-RKP43616.

    Protein family/group databases

    MEROPSiM20.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cys-Gly metallodipeptidase DUG1 (EC:3.4.13.-)
    Alternative name(s):
    Deficient in utilization of glutathione protein 1
    GSH degradosomal complex subunit DUG1
    Gene namesi
    Name:DUG1
    Ordered Locus Names:YFR044C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VI

    Organism-specific databases

    EuPathDBiFungiDB:YFR044C.
    SGDiS000001940. DUG1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Accumulation of Cys-Gly dipeptide and enhanced GSH toxicity.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001852751 – 481Cys-Gly metallodipeptidase DUG1Add BLAST481

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei451PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP43616.
    PRIDEiP43616.

    PTM databases

    iPTMnetiP43616.

    Interactioni

    Subunit structurei

    Homodimer. Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3.2 Publications

    Protein-protein interaction databases

    BioGridi31202. 25 interactors.
    DIPiDIP-6492N.
    IntActiP43616. 3 interactors.
    MINTiMINT-640305.

    Structurei

    Secondary structure

    1481
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi5 – 14Combined sources10
    Helixi16 – 28Combined sources13
    Helixi36 – 38Combined sources3
    Helixi39 – 55Combined sources17
    Beta strandi59 – 64Combined sources6
    Beta strandi83 – 88Combined sources6
    Beta strandi96 – 102Combined sources7
    Helixi110 – 112Combined sources3
    Beta strandi122 – 124Combined sources3
    Turni125 – 128Combined sources4
    Beta strandi129 – 131Combined sources3
    Turni133 – 138Combined sources6
    Helixi139 – 154Combined sources16
    Beta strandi161 – 169Combined sources9
    Helixi171 – 173Combined sources3
    Turni174 – 177Combined sources4
    Helixi178 – 185Combined sources8
    Turni186 – 192Combined sources7
    Beta strandi195 – 198Combined sources4
    Beta strandi204 – 208Combined sources5
    Beta strandi210 – 215Combined sources6
    Beta strandi217 – 226Combined sources10
    Beta strandi228 – 230Combined sources3
    Turni234 – 236Combined sources3
    Turni238 – 240Combined sources3
    Helixi244 – 252Combined sources9
    Helixi267 – 270Combined sources4
    Helixi276 – 281Combined sources6
    Turni282 – 284Combined sources3
    Helixi289 – 296Combined sources8
    Helixi306 – 314Combined sources9
    Beta strandi318 – 327Combined sources10
    Beta strandi330 – 332Combined sources3
    Beta strandi339 – 349Combined sources11
    Helixi355 – 371Combined sources17
    Beta strandi376 – 387Combined sources12
    Helixi397 – 410Combined sources14
    Beta strandi415 – 421Combined sources7
    Helixi426 – 433Combined sources8
    Beta strandi437 – 439Combined sources3
    Beta strandi451 – 453Combined sources3
    Beta strandi455 – 457Combined sources3
    Helixi458 – 477Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4G1PX-ray2.55A1-481[»]
    ProteinModelPortaliP43616.
    SMRiP43616.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000009682.
    HOGENOMiHOG000216709.
    InParanoidiP43616.
    KOiK15428.
    OMAiCNVKFMI.
    OrthoDBiEOG092C1SDA.

    Family and domain databases

    CDDicd05676. M20_dipept_like_CNDP. 1 hit.
    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017153. CNDP/DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P43616-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSHSLTSVFQ KIDSLKPQFF SRLTKAIQIP AVSSDESLRS KVFDKAKFIS
    60 70 80 90 100
    EQLSQSGFHD IKMVDLGIQP PPISTPNLSL PPVILSRFGS DPSKKTVLVY
    110 120 130 140 150
    GHYDVQPAQL EDGWDTEPFK LVIDEAKGIM KGRGVTDDTG PLLSWINVVD
    160 170 180 190 200
    AFKASGQEFP VNLVTCFEGM EESGSLKLDE LIKKEANGYF KGVDAVCISD
    210 220 230 240 250
    NYWLGTKKPV LTYGLRGCNY YQTIIEGPSA DLHSGIFGGV VAEPMIDLMQ
    260 270 280 290 300
    VLGSLVDSKG KILIDGIDEM VAPLTEKEKA LYKDIEFSVE ELNAATGSKT
    310 320 330 340 350
    SLYDKKEDIL MHRWRYPSLS IHGVEGAFSA QGAKTVIPAK VFGKFSIRTV
    360 370 380 390 400
    PDMDSEKLTS LVQKHCDAKF KSLNSPNKCR TELIHDGAYW VSDPFNAQFT
    410 420 430 440 450
    AAKKATKLVY GVDPDFTREG GSIPITLTFQ DALNTSVLLL PMGRGDDGAH
    460 470 480
    SINEKLDISN FVGGMKTMAA YLQYYSESPE N
    Length:481
    Mass (Da):52,871
    Last modified:November 1, 1995 - v1
    Checksum:i3E53773A945F5EBC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50617 Genomic DNA. Translation: BAA09283.1.
    AY692702 Genomic DNA. Translation: AAT92721.1.
    BK006940 Genomic DNA. Translation: DAA12487.1.
    PIRiS56299.
    RefSeqiNP_116702.1. NM_001180009.1.

    Genome annotation databases

    EnsemblFungiiBAA09283; BAA09283; BAA09283.
    YFR044C; YFR044C; YFR044C.
    GeneIDi850605.
    KEGGisce:YFR044C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D50617 Genomic DNA. Translation: BAA09283.1.
    AY692702 Genomic DNA. Translation: AAT92721.1.
    BK006940 Genomic DNA. Translation: DAA12487.1.
    PIRiS56299.
    RefSeqiNP_116702.1. NM_001180009.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4G1PX-ray2.55A1-481[»]
    ProteinModelPortaliP43616.
    SMRiP43616.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31202. 25 interactors.
    DIPiDIP-6492N.
    IntActiP43616. 3 interactors.
    MINTiMINT-640305.

    Protein family/group databases

    MEROPSiM20.017.

    PTM databases

    iPTMnetiP43616.

    Proteomic databases

    MaxQBiP43616.
    PRIDEiP43616.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiBAA09283; BAA09283; BAA09283.
    YFR044C; YFR044C; YFR044C.
    GeneIDi850605.
    KEGGisce:YFR044C.

    Organism-specific databases

    EuPathDBiFungiDB:YFR044C.
    SGDiS000001940. DUG1.

    Phylogenomic databases

    GeneTreeiENSGT00390000009682.
    HOGENOMiHOG000216709.
    InParanoidiP43616.
    KOiK15428.
    OMAiCNVKFMI.
    OrthoDBiEOG092C1SDA.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-4.
    YEAST:MONOMER3O-4.
    ReactomeiR-SCE-1614635. Sulfur amino acid metabolism.
    R-SCE-174403. Glutathione synthesis and recycling.
    SABIO-RKP43616.

    Miscellaneous databases

    PROiP43616.

    Family and domain databases

    CDDicd05676. M20_dipept_like_CNDP. 1 hit.
    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017153. CNDP/DUG1.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037242. CNDP_dipeptidase. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDUG1_YEAST
    AccessioniPrimary (citable) accession number: P43616
    Secondary accession number(s): D6VTS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: November 2, 2016
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 22300 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome VI
      Yeast (Saccharomyces cerevisiae) chromosome VI: 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.