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Database: UniProt
Entry: L0F6C5_DESDL
LinkDB: L0F6C5_DESDL
Original site: L0F6C5_DESDL 
ID   L0F6C5_DESDL            Unreviewed;       697 AA.
AC   L0F6C5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN   OrderedLocusNames=Desdi_1048 {ECO:0000313|EMBL:AGA68565.1};
OS   Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA68565.1, ECO:0000313|Proteomes:UP000010797};
RN   [1] {ECO:0000313|Proteomes:UP000010797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA   de Vos W.M., Boon N., Smidt H., Woyke T.;
RT   "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL   Submitted (FEB-2012) 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; CP003344; AGA68565.1; -; Genomic_DNA.
DR   RefSeq; WP_015261561.1; NC_019903.1.
DR   AlphaFoldDB; L0F6C5; -.
DR   STRING; 871963.Desdi_1048; -.
DR   KEGG; ddl:Desdi_1048; -.
DR   eggNOG; COG3968; Bacteria.
DR   HOGENOM; CLU_024307_0_0_9; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000010797; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000010797}.
FT   DOMAIN          58..151
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          156..586
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   697 AA;  77705 MW;  0A90A378ED46D87F CRC64;
     MDFFGKNVFN DTVMREKLPK NTYKALHKTL DEGLPLQLEV AEVVANAMKD WAIENGATHY
     THWFQPMTGY TAEKHDSFIS PTADGRVIME FSGKELIKGE PDASSFPNGG IRSTFEARGY
     TAWDCTSPAF LREDAGKVIL CIPTAFCSYT GEALDKKTPL LRSMETLSKQ ALRILRLFGN
     STAKRVTPTV GAEQEFFLIE KKYHQKRLDL MLTGRTLFGV LPPKGQEMED HYFGSINERV
     TAFMQEVNIE LWKLGVPAKT QHKEAAPGQY EIAPIFATTN IATDHNQLIM DTLHKVANRH
     ALACLLHEKP FAGVNGSGKH NNWSLSTDEG ANLLEPGTTP HENAQFLTFI CAVIKAVDDN
     AELLRASAAN PGNDHRLGAN EAPPAIISIF LGDELSDIIE QLKIGKPNTS KQGGQMTIGV
     STLPSLPKDS TDRNRTSPFA FTGNKFEFRM VPSSLSIAGP NVIINTIVAE VLSQMADRLE
     QADDFHSELQ AILREVAINH SRVIFDGNGY SEEWVKEAER RGLPNLTSTV EAISALISNK
     TIDLFKKHGV FSHTELHSRY EIYLELYSKT INIEALTMID VAKRQVLPAV VRYSTELANS
     INTIRTADPK ADVSAQKDLL NEIAPLLKDL GLIIKDLQDA TTAAKQLHGD AYRQGILYRD
     LVFKTMNELR QIVDHLEVLV DYEMWPLPSY TKMLFRL
//
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