ID   GLNA2_DICDI             Reviewed;         521 AA.
AC   P0C7B6; C7G063;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Type-1 glutamine synthetase 2;
DE            Short=Type-1 GS 2;
DE            EC=6.3.1.2;
DE   AltName: Full=Type-1 glutamate--ammonia ligase 2;
GN   Name=glnA2; ORFNames=DDB_G0295755;
OS   Dictyostelium discoideum (Slime mold).
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   PROTEIN SEQUENCE OF 88-98; 280-289 AND 468-478, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Veltman D.M., Insall R.H.;
RL   Submitted (JAN-2010) to UniProtKB.
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   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AAFI02000135; EEU04062.1; -; Genomic_DNA.
DR   RefSeq; XP_002649114.1; XM_002649068.1.
DR   AlphaFoldDB; P0C7B6; -.
DR   SMR; P0C7B6; -.
DR   STRING; 44689.DDB0252590; -.
DR   PaxDb; P0C7B6; -.
DR   EnsemblProtists; EEU04062; EEU04062; DDB_G0295755.
DR   GeneID; 8627058; -.
DR   KEGG; ddi:DDB_G0295755; -.
DR   dictyBase; DDB_G0295755; glnA2.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_017290_0_1_1; -.
DR   InParanoid; P0C7B6; -.
DR   OMA; NPGQHEI; -.
DR   PhylomeDB; P0C7B6; -.
DR   PRO; PR:P0C7B6; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR036651; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..521
FT                   /note="Type-1 glutamine synthetase 2"
FT                   /id="PRO_0000330937"
FT   DOMAIN          76..176
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          183..521
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   521 AA;  59201 MW;  E4E77C3AEB67391A CRC64;
     MNKLVNKNIF INKNNSLKNF VNNYSTKTNN NNNNIFNKNK NDLKSFSSSS KLNNNNNNNN
     KYEESKLMNA EDLILNQIKI SKSPFVKIAG SDIDGILRGK YLDKSKFESS IKKGLGFCSV
     IFGWDSSDSA YDNVKFTGNH TGYPDMGARP DLSTFRTIPW EYDVPLFLMD FIGTNGEPLP
     ICPRSTLKKV IKKCHEHQFD PVQGMEFEWY NYSENNKSLL NKNFSNLEPL SNGMFGYSLL
     RTSQNSEFMN SLAELQGFGV PLEGLHTETG PGVYEAAIRF STALESADRA ILFKHCTKEI
     ASLQGIMASF MAKPFKDLPG CSGHMHQNFN CLKTGKNLFL DESDPNHMSD IFKSFVAGQL
     LLLPEFLPFF APTINSYKRL VDGYWAPTTP TWGMDNRTVA LRIIKGGKAT RSEFRVTGSD
     VNPYISIAAS FAAGLYGVIN KLELKQKPII GNSYDLYKKG LVERLPRSLA ESTELLSKSK
     IAKEYLGEEF VDHFVETRRW EYRQFNHQVH KWELERYLEI I