DUG3_YEAST
ID DUG3_YEAST Reviewed; 357 AA.
AC P53871; D6W0Z6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable glutamine amidotransferase DUG3;
DE AltName: Full=Deficient in utilization of glutathione protein 3;
DE AltName: Full=GSH degradosomal complex subunit DUG3;
GN Name=DUG3; OrderedLocusNames=YNL191W; ORFNames=N1410;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17179087; DOI=10.1534/genetics.106.066944;
RA Ganguli D., Kumar C., Bachhawat A.K.;
RT "The alternative pathway of glutathione degradation is mediated by a novel
RT protein complex involving three new genes in Saccharomyces cerevisiae.";
RL Genetics 175:1137-1151(2007).
CC -!- FUNCTION: Component of the GSH degradosomal complex involved in the
CC degradation of glutathione (GSH) and other peptides containing a gamma-
CC glu-X bond. {ECO:0000269|PubMed:17179087}.
CC -!- SUBUNIT: Component of the GSH degradosomal complex composed of at least
CC DUG1, DUG2 and DUG3. {ECO:0000269|PubMed:17179087}.
CC -!- INTERACTION:
CC P53871; P38149: DUG2; NbExp=4; IntAct=EBI-29079, EBI-21176;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17179087}.
CC -!- MISCELLANEOUS: Present with 7300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DUG3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71467; CAA96085.1; -; Genomic_DNA.
DR EMBL; AY692717; AAT92736.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10362.1; -; Genomic_DNA.
DR PIR; S63146; S63146.
DR RefSeq; NP_014208.1; NM_001183029.1.
DR AlphaFoldDB; P53871; -.
DR SMR; P53871; -.
DR BioGRID; 35642; 22.
DR ComplexPortal; CPX-325; Glutathione hydrolase complex.
DR DIP; DIP-3956N; -.
DR IntAct; P53871; 4.
DR STRING; 4932.YNL191W; -.
DR MaxQB; P53871; -.
DR PaxDb; P53871; -.
DR PRIDE; P53871; -.
DR EnsemblFungi; YNL191W_mRNA; YNL191W; YNL191W.
DR GeneID; 855530; -.
DR KEGG; sce:YNL191W; -.
DR SGD; S000005135; DUG3.
DR VEuPathDB; FungiDB:YNL191W; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_042555_4_0_1; -.
DR InParanoid; P53871; -.
DR OMA; PFRHGRW; -.
DR BioCyc; MetaCyc:G3O-33202-MON; -.
DR BioCyc; YEAST:G3O-33202-MON; -.
DR PRO; PR:P53871; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53871; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0061672; C:glutathione hydrolase complex; IDA:SGD.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; ISS:SGD.
DR GO; GO:0008242; F:omega peptidase activity; IGI:SGD.
DR GO; GO:0008233; F:peptidase activity; IGI:SGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:SGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR026869; EgtC-like.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR Pfam; PF13230; GATase_4; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glutamine amidotransferase; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..357
FT /note="Probable glutamine amidotransferase DUG3"
FT /id="PRO_0000203401"
FT DOMAIN 2..260
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 40181 MW; AFAAEFE7152CFE1A CRC64;
MCRFLIFKGK QPIRLSHLLT RPAHSIINQS FDSRLRLDRR RPMNGDGFGV AYYPLDTELS
EDGPCLFKAI TPAWNNQNLS TLAEKTKSDL VFAHVRASTY GVLSETNCHP FTYHSLCFMH
NGGISNFKGI KRKLLNHIKD EYLNFIQGST DSECAFALFL DTLDKLGYDP KKQDGDFGNV
ALRKAMLRTI DYIRDWTKEA NKDEAHVEPS LLNFAVTDGS TVVVSRYITS KTDEAASLHF
SCGSSFVETS PGEYRVERLD RNQDVIMVAS EPLTFERGDW TAVPTNSILT IKKQTILLHP
IIDEYYQEDP LYLRSSTLAE SKGLMGSIPL AKAVEKNVPP LEREGRTRPP TAVAHIA
