ID   GLNA_YEAST              Reviewed;         370 AA.
AC   P32288; Q03959;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-NOV-2008, entry version 84.
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 (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92193267; PubMed=1347768;
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 204511 / S288c / AB972;
RX   MEDLINE=97313271; 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.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   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.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-8; 149-166; 171-178; 220-224 AND 286-293.
RX   MEDLINE=88087208; PubMed=2891705;
RA   Kim K.H., Rhee S.G.;
RT   "Sequence of peptides from Saccharomyces cerevisiae glutamine
RT   synthetase. N-terminal peptide and ATP-binding domain.";
RL   J. Biol. Chem. 263:833-838(1988).
RN   [4]
RP   ACETYLATION AT ALA-2.
RX   MEDLINE=97443978; 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.,
RA   Mesquita-Fuentes R., Payne W.E.;
RT   "Proteome studies of Saccharomyces cerevisiae: identification and
RT   characterization of abundant proteins.";
RL   Electrophoresis 18:1347-1360(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND MASS
RP   SPECTROMETRY.
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
RA   Marsischky G., Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [7]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-324, AND MASS
RP   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
RT   to mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- INTERACTION:
CC       P40318:SSM4; NbExp=1; IntAct=EBI-7665, EBI-18208;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 346000 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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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   PIR; S61058; S61058.
DR   HSSP; P06201; 1LGR.
DR   DIP; DIP:6699N; -.
DR   IntAct; P32288; -.
DR   SWISS-2DPAGE; P32288; -.
DR   PeptideAtlas; P32288; -.
DR   Ensembl; YPR035W; Saccharomyces cerevisiae.
DR   GenomeReviews; U00094_GR; YPR035W.
DR   CYGD; YPR035w; -.
DR   SGD; S000006239; GLN1.
DR   HOGENOM; P32288; -.
DR   BioCyc; MetaCyc:MON-12439; -.
DR   LinkHub; P32288; -.
DR   ArrayExpress; P32288; -.
DR   GermOnline; YPR035W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   InterPro; IPR008146; Gln_synth_cat.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   ProDom; PD001057; Gln_synt_C; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Ligase; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    370       Glutamine synthetase.
FT                                /FTId=PRO_0000153166.
FT   MOD_RES       2      2       N-acetylalanine.
FT   CROSSLNK    324    324       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    165    165       G -> D (in Ref. 3; AA sequence).
FT   CONFLICT    172    172       M -> V (in Ref. 3; AA sequence).
FT   CONFLICT    251    251       T -> A (in Ref. 2; CAA92141/CAA94985).
FT   CONFLICT    264    264       M -> T (in Ref. 2; CAA92141/CAA94985).
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
//