ID A0A1E7WDV8_9BURK Unreviewed; 471 AA.
AC A0A1E7WDV8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN ORFNames=DUPY_40660 {ECO:0000313|EMBL:OEZ96103.1};
OS Duganella phyllosphaerae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=762836 {ECO:0000313|EMBL:OEZ96103.1, ECO:0000313|Proteomes:UP000175989};
RN [1] {ECO:0000313|Proteomes:UP000175989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T54 {ECO:0000313|Proteomes:UP000175989};
RX PubMed=27833590;
RA Haack F.S., Poehlein A., Kroger C., Voigt C.A., Piepenbring M., Bode H.B.,
RA Daniel R., Schafer W., Streit W.R.;
RT "Molecular Keys to the Janthinobacterium and Duganella spp. Interaction
RT with the Plant Pathogen Fusarium graminearum.";
RL Front. Microbiol. 7:1668-1668(2016).
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}.
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:OEZ96103.1}.
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DR EMBL; LROM01000113; OEZ96103.1; -; Genomic_DNA.
DR RefSeq; WP_070250565.1; NZ_LROM01000113.1.
DR AlphaFoldDB; A0A1E7WDV8; -.
DR PATRIC; fig|762836.4.peg.4192; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000175989; Unassembled WGS sequence.
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:OEZ96103.1};
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:UP000175989}.
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 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; 52056 MW; 1A477E6C3F6F394D CRC64;
MAMTAAEVLK MVQENEVKFV DFRFADTRGK EQHVTVPVSH FDIDKFESGH AFDGSSIAGW
KGIEASDMIL MPDPNTANID PFMEETTLFM QCDVIEPADG KGYDRDPRSI AKRAEAYLKS
SGLGDTAYFG PEPEFFIFDS VRWKIDMSGC FVKIDSDEAS WSTGEKIEGG NSGHRPTVKG
GYFPVPPVDS FQDMRSEMCL ILESLGIPVE VHHHEVAGAG QNEIGTKFST LVERADWTQN
LKYVVWNVAH SYGKTATFMP KPIVGDNGSG MHVHQSIWKD GVNLFAGDGY AGLSDTALFY
IGGIIKHAKA LNAITNPGTN SYKRLVPGFE APVKLAYSAK NRSASIRIPH VANPKGRRIE
TRFPDPLANV YLCFAALLMA GLDGIANKIH PGEAASKDLY HLPPEEDALI PTVCASLEEA
LENLDKDREF LTRGGVFSDS MIDAYIELKM QDVQRMRMTT HPAEFDMYYS L
//
