ID U3U5D3_9GAMM Unreviewed; 470 AA.
AC U3U5D3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:BAO00045.1};
GN ORFNames=BMSBPS_0541 {ECO:0000313|EMBL:AKC32327.1}, HHS_00750
GN {ECO:0000313|EMBL:BAO00045.1};
OS Candidatus Pantoea carbekii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1235990 {ECO:0000313|EMBL:BAO00045.1, ECO:0000313|Proteomes:UP000016900};
RN [1] {ECO:0000313|EMBL:BAO00045.1, ECO:0000313|Proteomes:UP000016900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kobayashi H., Fujii-Muramatsu R., Takeishi K., Noda H.;
RT "Genome sequence of the symbiont of the pentatomidae stink bug Halyomorpha
RT halys.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKC32327.1, ECO:0000313|Proteomes:UP000060036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US {ECO:0000313|EMBL:AKC32327.1,
RC ECO:0000313|Proteomes:UP000060036};
RX PubMed=25587021; DOI=10.1093/gbe/evv006;
RA Kenyon L.J., Meulia T., Sabree Z.L.;
RT "Habitat visualization and genomic analysis of "Candidatus Pantoea
RT carbekii," the primary symbiont of the brown marmorated stink bug.";
RL Genome Biol. Evol. 7:620-635(2015).
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; CP010907; AKC32327.1; -; Genomic_DNA.
DR EMBL; AP012554; BAO00045.1; -; Genomic_DNA.
DR RefSeq; WP_022564064.1; NZ_CP010907.1.
DR AlphaFoldDB; U3U5D3; -.
DR STRING; 1235990.BMSBPS_0541; -.
DR KEGG; hhs:HHS_00750; -.
DR KEGG; pck:BMSBPS_0541; -.
DR PATRIC; fig|1235990.3.peg.75; -.
DR eggNOG; COG0174; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000016900; Chromosome.
DR Proteomes; UP000060036; 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: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}; 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:UP000016900}.
FT DOMAIN 13..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 105..470
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 265..266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 272..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 322
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 328
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 361
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 399
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 470 AA; 52557 MW; 36C8A8A0D715679D CRC64;
MSSEHVLSII NERQVKFVDL RFTDTKGKEQ HVTIPAHQVN SNFFKEGKMF DGSSINGWKD
INESDMLLMP DTSTAIIDPF FKESTLLIRC DILEPITLQG YDRDPRSISK RAENFLCSSG
IADVALFGPE PEFFLFDDIR FGSASSGSHV IIDDIEAYWN TLKIYEGGNK GHRPALKGGY
FPVPPVDSSQ EIRSLMCITM EKMGLIVEAH HHEVASAGQN EVATRFNSMT KKADEIQIYK
YVVHNIAQAH GKTATFMPKP IFGDNGSGMH CHISLFKNGI NLFSGEEYGG LSEIALFCIG
GIINHAKAIN AFTNPTTNSY KRLVAGYEAP VMLAYSERNR SAAIRIPIAT SSTKTRRIEV
RFPDPAANPY LAFATLLMAS LDGVINRIDP GDAIDNNLYK PLQKTNSRIQ KVATSLEEAL
NALDKDREFL TRGNVFTHDT INAYIELRKL DVDRLRMTPH PIEFELYYSV
//
