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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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi102 – 1021Zinc 2By similarity
    Active sitei104 – 1041By similarity
    Metal bindingi137 – 1371Zinc 1By similarity
    Metal bindingi137 – 1371Zinc 2By similarity
    Active sitei171 – 1711Proton acceptorBy similarity
    Metal bindingi172 – 1721Zinc 1By similarity
    Metal bindingi200 – 2001Zinc 2By similarity
    Metal bindingi450 – 4501Zinc 1By similarity

    GO - Molecular functioni

    • metal ion binding Source: UniProtKB-KW
    • metallodipeptidase activity Source: SGD
    • omega peptidase activity Source: SGD
    • tripeptidase activity Source: InterPro

    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

    BioCyciYEAST:G3O-30491-MONOMER.
    YEAST:MONOMER3O-4.
    ReactomeiREACT_303899. Glutathione synthesis and recycling.
    REACT_347986. Sulfur amino acid metabolism.
    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
    ProteomesiUP000002311 Componenti: Chromosome VI

    Organism-specific databases

    CYGDiYFR044c.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Cys-Gly metallodipeptidase DUG1PRO_0000185275Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei451 – 4511Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP43616.
    PaxDbiP43616.
    PeptideAtlasiP43616.
    PRIDEiP43616.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself1EBI-5137,EBI-5137

    Protein-protein interaction databases

    BioGridi31202. 24 interactions.
    DIPiDIP-6492N.
    IntActiP43616. 2 interactions.
    MINTiMINT-640305.

    Structurei

    Secondary structure

    1
    481
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 1410Combined sources
    Helixi16 – 2813Combined sources
    Helixi36 – 383Combined sources
    Helixi39 – 5517Combined sources
    Beta strandi59 – 646Combined sources
    Beta strandi83 – 886Combined sources
    Beta strandi96 – 1027Combined sources
    Helixi110 – 1123Combined sources
    Beta strandi122 – 1243Combined sources
    Turni125 – 1284Combined sources
    Beta strandi129 – 1313Combined sources
    Turni133 – 1386Combined sources
    Helixi139 – 15416Combined sources
    Beta strandi161 – 1699Combined sources
    Helixi171 – 1733Combined sources
    Turni174 – 1774Combined sources
    Helixi178 – 1858Combined sources
    Turni186 – 1927Combined sources
    Beta strandi195 – 1984Combined sources
    Beta strandi204 – 2085Combined sources
    Beta strandi210 – 2156Combined sources
    Beta strandi217 – 22610Combined sources
    Beta strandi228 – 2303Combined sources
    Turni234 – 2363Combined sources
    Turni238 – 2403Combined sources
    Helixi244 – 2529Combined sources
    Helixi267 – 2704Combined sources
    Helixi276 – 2816Combined sources
    Turni282 – 2843Combined sources
    Helixi289 – 2968Combined sources
    Helixi306 – 3149Combined sources
    Beta strandi318 – 32710Combined sources
    Beta strandi330 – 3323Combined sources
    Beta strandi339 – 34911Combined sources
    Helixi355 – 37117Combined sources
    Beta strandi376 – 38712Combined sources
    Helixi397 – 41014Combined sources
    Beta strandi415 – 4217Combined sources
    Helixi426 – 4338Combined sources
    Beta strandi437 – 4393Combined sources
    Beta strandi451 – 4533Combined sources
    Beta strandi455 – 4573Combined sources
    Helixi458 – 47720Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G1PX-ray2.55A1-481[»]
    ProteinModelPortaliP43616.
    SMRiP43616. Positions 1-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    eggNOGiCOG0624.
    GeneTreeiENSGT00390000009682.
    HOGENOMiHOG000216709.
    InParanoidiP43616.
    KOiK15428.
    OMAiHSPNEHY.
    OrthoDBiEOG7ZD249.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017153. GSH_degradosome_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

    EnsemblFungiiYFR044C; 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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G1PX-ray2.55A1-481[»]
    ProteinModelPortaliP43616.
    SMRiP43616. Positions 1-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi31202. 24 interactions.
    DIPiDIP-6492N.
    IntActiP43616. 2 interactions.
    MINTiMINT-640305.

    Protein family/group databases

    MEROPSiM20.017.

    Proteomic databases

    MaxQBiP43616.
    PaxDbiP43616.
    PeptideAtlasiP43616.
    PRIDEiP43616.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYFR044C; YFR044C; YFR044C.
    GeneIDi850605.
    KEGGisce:YFR044C.

    Organism-specific databases

    CYGDiYFR044c.
    EuPathDBiFungiDB:YFR044C.
    SGDiS000001940. DUG1.

    Phylogenomic databases

    eggNOGiCOG0624.
    GeneTreeiENSGT00390000009682.
    HOGENOMiHOG000216709.
    InParanoidiP43616.
    KOiK15428.
    OMAiHSPNEHY.
    OrthoDBiEOG7ZD249.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30491-MONOMER.
    YEAST:MONOMER3O-4.
    ReactomeiREACT_303899. Glutathione synthesis and recycling.
    REACT_347986. Sulfur amino acid metabolism.
    SABIO-RKP43616.

    Miscellaneous databases

    NextBioi966481.
    PROiP43616.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR017153. GSH_degradosome_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...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Analysis of a 36.2 kb DNA sequence including the right telomere of chromosome VI from Saccharomyces cerevisiae."
      Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.
      Yeast 12:149-167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
      Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
      Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae."
      Ganguli D., Kumar C., Bachhawat A.K.
      Genetics 175:1137-1151(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, SUBCELLULAR LOCATION.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases."
      Kaur H., Kumar C., Junot C., Toledano M.B., Bachhawat A.K.
      J. Biol. Chem. 284:14493-14502(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, FUNCTION, COFACTOR, DISRUPTION PHENOTYPE.

    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: July 22, 2015
    This is version 139 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

    External Data

    Dasty 3

    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 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.