ID A0A0P0LJ59_9BURK Unreviewed; 471 AA.
AC A0A0P0LJ59;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN ORFNames=L63ED372_01843 {ECO:0000313|EMBL:ALK89047.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK89047.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK89047.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK89047.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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|RuleBase:RU004356};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP011774; ALK89047.1; -; Genomic_DNA.
DR RefSeq; WP_062405497.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0P0LJ59; -.
DR STRING; 1678128.L63ED372_01843; -.
DR KEGG; lih:L63ED372_01843; -.
DR PATRIC; fig|1678128.3.peg.1831; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000059510; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; 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; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF2; 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; 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}; Isomerase {ECO:0000313|EMBL:ALK89047.1};
KW Ligase {ECO:0000256|RuleBase:RU004356};
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:UP000059510}.
FT DOMAIN 15..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..471
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 267..268
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 274..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 324
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 330
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 342
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 362
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 400
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 471 AA; 52256 MW; 0E3B99AAB8AAE29B CRC64;
MAKTVADVMN MVKENEVKFV DFRFTDTRGK WQHITAPVSQ FDESKFEDGQ AFDGSSIAGW
KGIEASDMLL IPDPNSAIID PFFEEVTLVL ICDVIEPTDG KAYERDPRSI AKRAETYLKQ
SGLGDTAYFG PEPEFFLFDE VRWSTEPNNT FYAIDEAEAP WNSGTKMDGG NKGHRNRVKG
GYFPVPPVDS THDMRSEMSL ILESVGIPVE VHHHEVAGAG QCEIGTRFST LVERADWTLL
QKYVIHNVAN AYGKTATFMP KPYAGDNGSG MHVHQSIWKD GKNLFAGNGY AGLSEFALFY
IGGIIKHARA LNAITNPGTN SYKRLVPHYE APVKLAYSAK NRSASIRIPN VASDKGRRVE
ARFPDPLCNP YLGFAALLMA GLDGVENKIH PGEAATKDLY HLPPEEDKLV PTVCSSLDQA
LDALNADRAF LTKGGVFTDS WIDAYIDLKM QEVNRSRVEV SPVEYDMYYS L
//
