ID   GLNA3_DICDI             Reviewed;         735 AA.
AC   Q54WR9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Type-3 glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Type-3 glutamate--ammonia ligase;
DE            Short=Type-3 GS;
GN   Name=glnA3; Synonyms=glnB; ORFNames=DDB_G0279591;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. Type 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000031; EAL67734.1; -; Genomic_DNA.
DR   RefSeq; XP_641648.1; XM_636556.1.
DR   AlphaFoldDB; Q54WR9; -.
DR   SMR; Q54WR9; -.
DR   STRING; 44689.Q54WR9; -.
DR   PaxDb; 44689-DDB0231551; -.
DR   EnsemblProtists; EAL67734; EAL67734; DDB_G0279591.
DR   GeneID; 8622055; -.
DR   KEGG; ddi:DDB_G0279591; -.
DR   dictyBase; DDB_G0279591; glnA3.
DR   eggNOG; ENOG502QQE3; Eukaryota.
DR   HOGENOM; CLU_024307_0_0_1; -.
DR   InParanoid; Q54WR9; -.
DR   OMA; QFLVFCA; -.
DR   PhylomeDB; Q54WR9; -.
DR   PRO; PR:Q54WR9; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR   Gene3D; 1.20.120.1560; -; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR040577; Gln-synt_C.
DR   InterPro; IPR008147; 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; IPR022147; GSIII_N.
DR   PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF18318; Gln-synt_C-ter; 1.
DR   Pfam; PF12437; GSIII_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 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   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..735
FT                   /note="Type-3 glutamine synthetase"
FT                   /id="PRO_0000330468"
FT   DOMAIN          89..183
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          188..621
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   735 AA;  82616 MW;  9B2B44F894566A08 CRC64;
     MSNRRREFIE YIDSREPVEA DIDISDKADR LTDIYDSDTY GLNAMRETLP SHCYKKIREV
     MQTGSALDPE IADMVANGMK EWAIKQGATH YCHWFLPLNG LAAEKHDSFI SIFPGDDKVL
     LEFSGMQLIK GEPDASSFPS GGIRSTWEAR GYTVWDATSP AFIRREKNGA ILCIPTAFCS
     WTGEALDQKT PLLRSMEYVS NESIITLSSL FNEKHKRISP TLGIEQEFFL IDRKFYLARP
     DLVNCGRTLI GAKPPKGQEM EDHYFGTMNS RIISCIQEVE WKMWRLGMPL KTRHNEVAPG
     QYEVAPIFER ANIAADHNMM LMDILKNVST KHGLVCLFHE KPFAGVNGSG KHNNWSLSTD
     GGSNLLEPGH TPSQNARFIL FLTAIIRAVD IHADLLRASV AVPGNEHRLG ANEAPPAIIS
     IYLGKELDTV INNIINNTDI QAPGSDDMDL GVVGFPPLPK DSTDRNRTSP FAFTGNKFEF
     RAVGSSQVVN FPCIVLNTIV AESLRFIREE ILREMKVSSR QTAFNKIIKD TLIQHVRVVF
     NGDGYSGDWK ELAKSRGLAN LPSTPEALTN INSEKNIKLF SESNILSPVE LESRQEILFE
     IYNKSIKIEA NSLYDLVSTL VLPACFAHQK NIAESVNSIM PFIQSQKSFS QPNHQYSHLS
     EVVESVNLLI EANQKLLALI KQTKDFNSEH SLATFLNQSV IPQMNEVRKF SDHLEGIVED
     KSWPVPKYSE ILFLR
//