ID   A0A1I0HVJ3_9FIRM        Unreviewed;       692 AA.
AC   A0A1I0HVJ3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN   ORFNames=SAMN04489758_1643 {ECO:0000313|EMBL:SET88276.1};
OS   Thomasclavelia cocleata.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=69824 {ECO:0000313|EMBL:SET88276.1, ECO:0000313|Proteomes:UP000198558};
RN   [1] {ECO:0000313|Proteomes:UP000198558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1551 {ECO:0000313|Proteomes:UP000198558};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; FOIN01000064; SET88276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0HVJ3; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000198558; 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; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198558}.
FT   DOMAIN          64..152
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          168..583
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   COILED          608..635
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   692 AA;  77081 MW;  E55CF45402F2B57D CRC64;
     MEMNKLLEDY GCLTFSDDVM KERIPKSIYK AFHASLDKGE ELSKECATVI ANAMKIWAVE
     NGATHFTHWF MPMTGSTAEK HDAFLEPDGS KAVLEFSGKT LRKGEPDASS FPSGGLRATF
     EARGYTAWDC TSPAFVKDGS LYIPTLFCSY TGEALDKKTP LLRSCDALSK AACRLLPKLG
     IEGVTKVTAS VGAEQEYFLV LDEYYQKRMD LKLTGRTLFG AMAPKGQELD DHYFGSLKRK
     VAAFMKDLDH ELWRYGIPSK TKHNEVAPAQ HEVAIVYSKV NITTDNNHLL MQLMQDIAKK
     HGLRCLLHEK PFAGVNGSGK HDNWSVITNT GINLFDPGSN PAKNKSFIAA LACTIKAVDE
     YSDLLRMSIA SAGNDHRLGA NEAPPAIISM FLGEELEALI EEICEGKKTN KTDATRFATG
     VSVVPTFSKD NTDRNRTSPF AFTGNKFEFR AVGSSQSVAG PNTILNAILA NAMEEMATEL
     ETGKSFDDVV KSFISNHKRI IFNGDGYSAE WEEEAFKRGL LNNKNTVDAL KCLKDEKNIE
     MLKRLGVYSE LELASRYEIL LEGYIKTIQV EALTALKMTK TQIYPAVCEY LAKFSAEVIT
     NKEAGLDIDF LADDLKILAE LVKKMREQMV TLDNNISAAQ ILNTDIFDQA VVWRDEVFEM
     MQELRQTVDT IEESVDAEYW PIPTYIDLLF GI
//