P53871 (DUG3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable glutamine amidotransferase DUG3

Alternative name(s):
Deficient in utilization of glutathione protein 3
GSH degradosomal complex subunit DUG3

Gene names

Name:	DUG3
Ordered Locus Names:	YNL191W
ORF Names:	N1410

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Ref.6
Subunit structure	Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3. Ref.6
Subcellular location	Cytoplasm Ref.4 Ref.6.
Miscellaneous	Present with 7300 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DUG3 family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glutathione catabolic process Inferred from mutant phenotype Ref.6PubMed 22277648. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.4Ref.6. Source: SGD
Molecular_function	omega peptidase activity Inferred from genetic interaction Ref.6. Source: SGD transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 357	357	Probable glutamine amidotransferase DUG3		PRO_0000203401
Regions
	Domain	2 – 260	259	Glutamine amidotransferase type-2
Sites
	Active site	2	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53871 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: AFAAEFE7152CFE1A	FASTA	357	40,181
	10 20 30 40 50 60 MCRFLIFKGK QPIRLSHLLT RPAHSIINQS FDSRLRLDRR RPMNGDGFGV AYYPLDTELS 70 80 90 100 110 120 EDGPCLFKAI TPAWNNQNLS TLAEKTKSDL VFAHVRASTY GVLSETNCHP FTYHSLCFMH 130 140 150 160 170 180 NGGISNFKGI KRKLLNHIKD EYLNFIQGST DSECAFALFL DTLDKLGYDP KKQDGDFGNV 190 200 210 220 230 240 ALRKAMLRTI DYIRDWTKEA NKDEAHVEPS LLNFAVTDGS TVVVSRYITS KTDEAASLHF 250 260 270 280 290 300 SCGSSFVETS PGEYRVERLD RNQDVIMVAS EPLTFERGDW TAVPTNSILT IKKQTILLHP 310 320 330 340 350 IIDEYYQEDP LYLRSSTLAE SKGLMGSIPL AKAVEKNVPP LEREGRTRPP TAVAHIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71467 Genomic DNA. Translation: CAA96085.1. AY692717 Genomic DNA. Translation: AAT92736.1. BK006947 Genomic DNA. Translation: DAA10362.1.
PIR	S63146.
RefSeq	NP_014208.1. NM_001183029.1.
3D structure databases
ProteinModelPortal	P53871.
SMR	P53871. Positions 46-291.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3956N.
IntAct	P53871. 4 interactions.
MINT	MINT-501795.
STRING	4932.YNL191W.
Proteomic databases
PaxDb	P53871.
PeptideAtlas	P53871.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL191W; YNL191W; YNL191W.
GeneID	855530.
KEGG	sce:YNL191W.
Organism-specific databases
CYGD	YNL191w.
SGD	S000005135. DUG3.
Phylogenomic databases
eggNOG	COG0121.
HOGENOM	HOG000256686.
KO	K07008.
OMA	STDSECC.
OrthoDB	EOG4H1F4D.
Gene expression databases
Genevestigator	P53871.
GermOnline	YNL191W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017932. GATase_2_dom. IPR026869. Put_GATase_2. [Graphical view]
Pfam	PF13230. GATase_4. 1 hit. [Graphical view]
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979577.

Entry information

Entry name

DUG3_YEAST

Accession

Primary (citable) accession number: P53871
Secondary accession number(s): D6W0Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program