ID   E9EAG0_METAQ            Unreviewed;       482 AA.
AC   E9EAG0;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN   ORFNames=MAC_06858 {ECO:0000313|EMBL:EFY87069.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY87069.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87069.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; GL698533; EFY87069.1; -; Genomic_DNA.
DR   RefSeq; XP_007813198.1; XM_007815007.1.
DR   AlphaFoldDB; E9EAG0; -.
DR   STRING; 655827.E9EAG0; -.
DR   GeneID; 19251169; -.
DR   KEGG; maw:MAC_06858; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_017290_0_1_1; -.
DR   InParanoid; E9EAG0; -.
DR   OMA; MFCDILM; -.
DR   OrthoDB; 2783297at2759; -.
DR   Proteomes; UP000002499; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000002499}.
FT   DOMAIN          119..482
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   482 AA;  53312 MW;  DEE9CDBD9BEEC3E7 CRC64;
     MGSQITASSL PQLLEHDTCV KLAGIDVDGI LRGKLVSKKK FLSIAEAGFG FCSVIFGWDM
     HDQTYLKELK VSNAENGYRD ILAIPDLSTF RRVPWENNVP FFLVNFFDPD TKKPIAPCSR
     GLLKTQLDKV HAKGYGAMAG ESLTKAEYEF YTFRNPNNDS ASPAAFLQQN PPHQLPSLTE
     GMFGYSLNRP VHNKDWYYNV YSTCARFSCD IEGWHTESGP GVYEAALEFG EVADMADRAS
     LFKYVVKSVG IKHGITPCFM AKPKQGLPGN SGHMHISIVD GDGKNLLARD TMDPDAKWND
     IAALSDLGRH FLAGLLEGLP DIMPMLAPTV NSYKRLVENF WAPVTVSWGL EHRAASIRLI
     SPPTSKPGAT RFEVRTPGAD SNPHFVLAAI LGCGWCGVEK KLEIPCPPLA MGQDTGGAGD
     MGERLAKSLK EATARFMRKD SIAREIFGDD FVEHFGGTRE NEVRLFDEAV TDWEMKRYIE
     TV
//