ID A0A2M9BBH7_9MICO Unreviewed; 445 AA.
AC A0A2M9BBH7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=L-glutamine synthetase {ECO:0000313|EMBL:PJJ55300.1};
GN ORFNames=CLV54_3190 {ECO:0000313|EMBL:PJJ55300.1};
OS Compostimonas suwonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Compostimonas.
OX NCBI_TaxID=1048394 {ECO:0000313|EMBL:PJJ55300.1, ECO:0000313|Proteomes:UP000230161};
RN [1] {ECO:0000313|EMBL:PJJ55300.1, ECO:0000313|Proteomes:UP000230161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25625 {ECO:0000313|EMBL:PJJ55300.1,
RC ECO:0000313|Proteomes:UP000230161};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC 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:PJJ55300.1}.
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DR EMBL; PGFB01000006; PJJ55300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9BBH7; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000230161; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR004809; Gln_synth_I.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF11; GLUTAMINE SYNTHETASE; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000230161}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..445
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 245..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 296
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 302
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 314
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 336
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
SQ SEQUENCE 445 AA; 49761 MW; EB784E40181E4A24 CRC64;
MDKQRDFVLR TIEERGIKFV RLWFTDVIGT LKSVAIAPAE VEGAFAEGLG FDGSAIEGLT
RSFESDLLAH PDPTTFQILP WRGEVDPTAR MFCDITTPDG QPAVADPRNV LKRTLEKAAD
LGFTFYTHPE IEFYLLKSSQ FGANGPEPVD SAGYFDNVPG GTAHDFRRRS VRMLEDLGIS
VEFSHHEAGP GQNEIDLRYA DALTTADNIM TFRTVIKEVA IEQGVYATFM PKPMSGHPGS
GMHTHMSLFE GDTNAFYEAG AQYQLSKIGR NFIAGLLHHA PEITAVTNQF VNSYKRLWGG
DEAPSFVCWG HNNRSALVRV PLYKPNKGQS SRVEYRAIDS AANPYLAFSL MLAAGLKGIE
EGYELPPEAE DNVWSLTDTE RRALGYNQLP ASLDHAVQYM EESELVAETL GEQVFNHVLS
NKRREWHQYR DQVTPFELRS NLEML
//
