ID   F7Y7Y0_MESOW            Unreviewed;       456 AA.
AC   F7Y7Y0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Glutamate--ammonia ligase {ECO:0000313|EMBL:AEH86362.1};
DE            EC=6.3.1.2 {ECO:0000313|EMBL:AEH86362.1};
GN   OrderedLocusNames=Mesop_1881 {ECO:0000313|EMBL:AEH86362.1};
OS   Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH86362.1, ECO:0000313|Proteomes:UP000001623};
RN   [1] {ECO:0000313|EMBL:AEH86362.1, ECO:0000313|Proteomes:UP000001623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC   {ECO:0000313|Proteomes:UP000001623};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA   Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; CP002279; AEH86362.1; -; Genomic_DNA.
DR   RefSeq; WP_013893088.1; NC_015675.1.
DR   AlphaFoldDB; F7Y7Y0; -.
DR   STRING; 536019.Mesop_1881; -.
DR   KEGG; mop:Mesop_1881; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_0_3_5; -.
DR   Proteomes; UP000001623; Chromosome.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:AEH86362.1}.
FT   DOMAIN          120..456
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   456 AA;  51574 MW;  009913E9DF5F8914 CRC64;
     MAGNFSFDQL KKAVSSGEID TVLACIVDLQ GRLAGKRFLA QYFVDSAHDE THGCNYLLAA
     DIDMEPVPGY KAASWSKGYG DFVMKPDLAT LRRIPWLEKT ALVICDVLDH HTHDDLPHSP
     RAILKKQIKR LTERGYIGYF ASELEFYLFN ETYDSARKKH WQGLDTASPY IGDYQIGITT
     KEEGVMRRLR NEMEAAGIPI ENSKGEWGPG QEEINVRYAE ALDMADRHVI LKNGAKEIAE
     SEGKAISFMS KYNYGLAGNS SHIHNSLWSA DGKTPLFFDK KADWTLSTLG QQWAAGQLKY
     AKEFTWFLAP YINSYKRFQA GTFAPTKIMW SEDNRTAGFR LCGEGTKGIR MECRIGGADL
     NPYLAFAALI AAGLAGIDEK LELQKPFVGD AYQASRLPEI PKTLRDATET LAKSKMLKQA
     LGEDVLEHYV HTAKWEQFEY DRRITDWELH RGFERY
//