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P43616

- DUG1_YEAST

UniProt

P43616 - DUG1_YEAST

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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: 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

  1. metal ion binding Source: UniProtKB-KW
  2. metallodipeptidase activity Source: SGD
  3. omega peptidase activity Source: SGD
  4. tripeptidase activity Source: InterPro

GO - Biological processi

  1. 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_188464. Sulfur amino acid metabolism.
REACT_256904. 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
ProteomesiUP000002311: Chromosome VI

Organism-specific databases

CYGDiYFR044c.
SGDiS000001940. DUG1.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. 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.

Expressioni

Gene expression databases

GenevestigatoriP43616.

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.
STRINGi4932.YFR044C.

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.
OMAiTDGAHSI.
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 .
PIRi S56299.
RefSeqi NP_116702.1. NM_001180009.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4G1P X-ray 2.55 A 1-481 [» ]
ProteinModelPortali P43616.
SMRi P43616. Positions 1-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31202. 24 interactions.
DIPi DIP-6492N.
IntActi P43616. 2 interactions.
MINTi MINT-640305.
STRINGi 4932.YFR044C.

Protein family/group databases

MEROPSi M20.017.

Proteomic databases

MaxQBi P43616.
PaxDbi P43616.
PeptideAtlasi P43616.
PRIDEi P43616.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YFR044C ; YFR044C ; YFR044C .
GeneIDi 850605.
KEGGi sce:YFR044C.

Organism-specific databases

CYGDi YFR044c.
SGDi S000001940. DUG1.

Phylogenomic databases

eggNOGi COG0624.
GeneTreei ENSGT00390000009682.
HOGENOMi HOG000216709.
InParanoidi P43616.
KOi K15428.
OMAi TDGAHSI.
OrthoDBi EOG7ZD249.

Enzyme and pathway databases

BioCyci YEAST:G3O-30491-MONOMER.
YEAST:MONOMER3O-4.
Reactomei REACT_188464. Sulfur amino acid metabolism.
REACT_256904. Glutathione synthesis and recycling.
SABIO-RK P43616.

Miscellaneous databases

NextBioi 966481.
PROi P43616.

Gene expression databases

Genevestigatori P43616.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR017153. GSH_degradosome_DUG1.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF037242. CNDP_dipeptidase. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 133 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