ID A0A6I2GFR5_9LACT Unreviewed; 447 AA.
AC A0A6I2GFR5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:MRI86046.1};
GN ORFNames=GF867_10210 {ECO:0000313|EMBL:MRJ47936.1}, GIY09_09240
GN {ECO:0000313|EMBL:MRI86046.1}, GIY11_06950
GN {ECO:0000313|EMBL:MRI81752.1};
OS Fundicoccus ignavus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Fundicoccus.
OX NCBI_TaxID=2664442 {ECO:0000313|EMBL:MRI86046.1, ECO:0000313|Proteomes:UP000430975};
RN [1] {ECO:0000313|EMBL:MRJ47936.1, ECO:0000313|Proteomes:UP000440066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 109652 {ECO:0000313|EMBL:MRJ47936.1,
RC ECO:0000313|Proteomes:UP000440066};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae from bulk tank milk.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000430975, ECO:0000313|Proteomes:UP000469870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 109653 {ECO:0000313|EMBL:MRI81752.1,
RC ECO:0000313|Proteomes:UP000469870}, and WS4759
RC {ECO:0000313|EMBL:MRI86046.1, ECO:0000313|Proteomes:UP000430975};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae isolated from bulk tank milk.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:MRI86046.1}.
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DR EMBL; WJQR01000005; MRI81752.1; -; Genomic_DNA.
DR EMBL; WJQS01000008; MRI86046.1; -; Genomic_DNA.
DR EMBL; WJQT01000016; MRJ47936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I2GFR5; -.
DR Proteomes; UP000430975; Unassembled WGS sequence.
DR Proteomes; UP000440066; Unassembled WGS sequence.
DR Proteomes; UP000469870; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
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 InterPro; IPR027302; Gln_synth_N_conserv_site.
DR NCBIfam; TIGR00653; GlnA; 1.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 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; PS00180; GLNA_1; 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 ECO:0000256|RuleBase:RU004356}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:MRI86046.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR604809-2,
KW ECO:0000256|RuleBase:RU004356};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000430975}.
FT DOMAIN 17..104
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 111..447
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 243..244
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 301
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 307
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 319
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 338
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 376
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 447 AA; 50735 MW; DE2975C8E8924D5E CRC64;
MSTKWTKEAI IKDAKEKNVR FIRLMFTDIA GTIKNVEVPF SQLEKALDGN MMFDGSSIEG
FVRIEESDMY LVPDFDTWLI FNWHAEEGAG RIARLICDVE NTNREPFAGD PRSNLKRMLK
QMHAMGFTDF NLGPEPEFFL FKLNDNGEPT MSLNDNGGYF DLAPTDLAEN CRRDIVLELE
ELGFEIEASH HEVAPGQHEI DWKYSDAITA CDNIQTFKLI VKSVARRHNL HATFMPKPIF
GINGSGMHFN MSLFTEAGNA FFDPETDDQL SQTALYFIGG MLKYARSFTA VCNPTVNSYK
RLVPGYEAPV YVAWSEQNRS PLIRIPASRG NSTRVEIRSV DPSANPYLAL AVLLQAGLEG
IKQELTPPSS VDRNIYAMTR EERLAEGVND LPGSLREALK ELKKEPIILD ALGPHISENF
IAEKTMEYFA YQRHVTQWEV DKYLKLY
//
