ID A0A0J1FGV2_9FIRM Unreviewed; 695 AA.
AC A0A0J1FGV2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364};
GN Name=glnA_2 {ECO:0000313|EMBL:KLU62213.1};
GN ORFNames=CEB3_c14330 {ECO:0000313|EMBL:KLU62213.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU62213.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU62213.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU62213.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, 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:KLU62213.1}.
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DR EMBL; LDXJ01000047; KLU62213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FGV2; -.
DR STRING; 999898.CEB3_c14330; -.
DR PATRIC; fig|999898.3.peg.1630; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000035957; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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}; Ligase {ECO:0000313|EMBL:KLU62213.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035957}.
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"
FT COILED 619..653
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 695 AA; 76867 MW; E9BCA8AA8767E81B CRC64;
MDLFGVNVFN DSAMKERLPK NTYKALRRTI DEGLALDPSV AEVVANAMKD WAIEKGATHF
THWFQPMTGL TAEKHDSFIS PTSDGRVIME FSGKELIKGE PDASSFPSGG IRATFEARGY
TAWDATSPAF LKEDEGGVVL CIPTAFCAYT GEALDKKTPL LRSMEALSKQ ALRILRIFGN
TASKQVKSTV GPEQEYFLID KKFYEQRLDL LLTGRTLFGA SAPKGQEMED HYFGSIKERI
SRFMKDLNTE LWKLGIPAKT QHKEVAPAQY EIAPVFETTN IATDHNQLVM DTLQKVALRH
DLVCLLHEKP FAGVNGSGKH NNWSMSTDDG LNLLDPGRTP HDNAQFLTFL CAVIKAVDEY
ADVLRVAAAN PGNDHRLGAN EAPPAIISIF LGEQLSDVFA QLGNGGPKSS KQGGHLTIGV
TTLPTLAKDS TDRNRTSPFA FTGNKFEFRM VPSSLSISGP NIVLNTIVAE ALAQIADRLE
KASDFRVELA LILKEIVNEH GRVVFDGNNY SDDWIAEAER RGLPNIRSTV EAIPVLISDK
TVALYEKHGV FSRVELHSRY EILLEQYAKH LNIEAQTMIH MAKRQMLPAG MKYAAELAQG
IGAIKAVSNV PVSVQEDKLR EVSAVLALIQ KRLSELEQAC EEAKSVADAY EQGVFYRDVV
FKAMGSLRED VDRLEMQVDA GLWPLPTYAE MLFLL
//
