GLNA_YEAST
ID GLNA_YEAST Reviewed; 370 AA.
AC P32288; D6W445; Q03959;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Glutamine synthetase;
DE Short=GS;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GLN1; OrderedLocusNames=YPR035W; ORFNames=YP3085.01, YP9367.15;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1347768; DOI=10.1128/jb.174.6.1828-1836.1992;
RA Minehart P.L., Magasanik B.;
RT "Sequence of the GLN1 gene of Saccharomyces cerevisiae: role of the
RT upstream region in regulation of glutamine synthetase expression.";
RL J. Bacteriol. 174:1828-1836(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 251 AND 264.
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 [4]
RP PROTEIN SEQUENCE OF 2-8; 149-166; 171-178; 220-224 AND 286-293.
RX PubMed=2891705; DOI=10.1016/s0021-9258(19)35430-4;
RA Kim K.H., Rhee S.G.;
RT "Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase.
RT N-terminal peptide and ATP-binding domain.";
RL J. Biol. Chem. 263:833-838(1988).
RN [5]
RP ACETYLATION AT ALA-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [6]
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 [7]
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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-283; LYS-324 AND LYS-363, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 346000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34644.1; Type=Miscellaneous discrepancy; Note=The submitted sequence does not correspond to the sequence published in the paper.; Evidence={ECO:0000305};
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DR EMBL; M65157; AAA34644.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z68111; CAA92141.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94985.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89289.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11461.2; -; Genomic_DNA.
DR PIR; S61058; S61058.
DR RefSeq; NP_015360.2; NM_001184132.2.
DR PDB; 3FKY; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-370.
DR PDBsum; 3FKY; -.
DR AlphaFoldDB; P32288; -.
DR SMR; P32288; -.
DR BioGRID; 36213; 143.
DR DIP; DIP-6699N; -.
DR IntAct; P32288; 8.
DR MINT; P32288; -.
DR STRING; 4932.YPR035W; -.
DR iPTMnet; P32288; -.
DR SWISS-2DPAGE; P32288; -.
DR MaxQB; P32288; -.
DR PaxDb; P32288; -.
DR PRIDE; P32288; -.
DR EnsemblFungi; YPR035W_mRNA; YPR035W; YPR035W.
DR GeneID; 856147; -.
DR KEGG; sce:YPR035W; -.
DR SGD; S000006239; GLN1.
DR VEuPathDB; FungiDB:YPR035W; -.
DR eggNOG; KOG0683; Eukaryota.
DR GeneTree; ENSGT00940000171472; -.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; P32288; -.
DR OMA; DRRPNAN; -.
DR BioCyc; MetaCyc:YPR035W-MON; -.
DR BioCyc; YEAST:YPR035W-MON; -.
DR Reactome; R-SCE-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-SCE-8964539; Glutamate and glutamine metabolism.
DR EvolutionaryTrace; P32288; -.
DR PRO; PR:P32288; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32288; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:SGD.
DR GO; GO:0006542; P:glutamine biosynthetic process; IDA:SGD.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Ligase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2891705,
FT ECO:0000269|PubMed:9298649, ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..370
FT /note="Glutamine synthetase"
FT /id="PRO_0000153166"
FT DOMAIN 24..103
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 110..370
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9298649,
FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 165
FT /note="G -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="M -> V (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="T -> A (in Ref. 2; CAA92141/CAA94985)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="M -> T (in Ref. 2; CAA92141/CAA94985)"
FT /evidence="ECO:0000305"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3FKY"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:3FKY"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3FKY"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 209..227
FT /evidence="ECO:0007829|PDB:3FKY"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:3FKY"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3FKY"
FT HELIX 341..353
FT /evidence="ECO:0007829|PDB:3FKY"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:3FKY"
SQ SEQUENCE 370 AA; 41766 MW; 43139C40E97DB34D CRC64;
MAEASIEKTQ ILQKYLELDQ RGRIIAEYVW IDGTGNLRSK GRTLKKRITS IDQLPEWNFD
GSSTNQAPGH DSDIYLKPVA YYPDPFRRGD NIVVLAACYN NDGTPNKFNH RHEAAKLFAA
HKDEEIWFGL EQEYTLFDMY DDVYGWPKGG YPAPQGPYYC GVGAGKVYAR DMIEAHYRAC
LYAGLEISGI NAEVMPSQWE FQVGPCTGID MGDQLWMARY FLHRVAEEFG IKISFHPKPL
KGDWNGAGCH TNVSTKEMRQ PGGMKYIEQA IEKLSKRHAE HIKLYGSDND MRLTGRHETA
SMTAFSSGVA NRGSSIRIPR SVAKEGYGYF EDRRPASNID PYLVTGIMCE TVCGAIDNAD
MTKEFERESS
