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Database: UniProt
Entry: A0A137SUD8_9FIRM
LinkDB: A0A137SUD8_9FIRM
Original site: A0A137SUD8_9FIRM 
ID   A0A137SUD8_9FIRM        Unreviewed;       686 AA.
AC   A0A137SUD8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN   ORFNames=HMPREF3189_01015 {ECO:0000313|EMBL:KXO16045.1};
OS   Clostridiales bacterium KA00134.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO16045.1, ECO:0000313|Proteomes:UP000070500};
RN   [1] {ECO:0000313|EMBL:KXO16045.1, ECO:0000313|Proteomes:UP000070500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00134 {ECO:0000313|EMBL:KXO16045.1,
RC   ECO:0000313|Proteomes:UP000070500};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXO16045.1}.
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DR   EMBL; LTAF01000026; KXO16045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137SUD8; -.
DR   STRING; 1588750.HMPREF3189_01015; -.
DR   PATRIC; fig|1588750.3.peg.994; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000070500; Unassembled WGS sequence.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic 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; 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; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070500}.
FT   DOMAIN          155..586
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
FT   COILED          602..636
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   686 AA;  77916 MW;  489C849B803501DD CRC64;
     MREEIDFAKM CFNKKKMKEY LPQPIYQSWK KALRLQEDLD RNTADAIAHA MKEWAISMGA
     SHYSHLFYPL NGLSARKLES FLDRSKDNEP IYHFSGAELI KSEPDASSFP SGGMRSTFEA
     RGYAYWDLSA NSFIENGVLY IPSIFVSYTG ESLDKRAPLL RATEALSKAG TRLLNILDRK
     NKTYRMKSKL GLEQEFFLID KDIYKKRIDL QSCGRTLVGS SAVKGQTLED HYFGRTPKRV
     EDFYKDVNKK LWELGIYAKT EHNEVAPCQF ELAVLYENTN VAIDDNQLVM SILTSTALEH
     NLVCLLHEKP FAGVNGSGKH NNYSITNNYG LNCFNPGKKP EENLVFLLFT AAMIELVDRA
     GAILRVVSSG PSNDYRLGGN EAPPSIMSIF LGQDIQEIFE AISLGKRDFK SYDSSIRVSS
     LGDIPKDRSD RNRTSPMAFT GNKFEFRMLG SSRNASDVNV VLNTFMADIL DRIANLLKDV
     SSKNLKDKSY EIIEDILKAH GKVMYTGDNY SKSWKALAEK RGLRSFDNLF QALAFLKNDE
     NLKVFEDYKI FSRKELKAIY DVYLEEIVNY HTIEARACIN LIDKDILPSA LREISDLKNS
     GLRFLEDRKA HLEGLLEALM NLRNELSANL SKYKDIACLE EKAKACQIGL ADKLLDVRKV
     ADEMEDLISK NNYSLVGYDE IFNSLI
//
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