ID A0A086XRD4_9RHOB Unreviewed; 469 AA.
AC A0A086XRD4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:KFI24584.1};
GN ORFNames=CG50_09655 {ECO:0000313|EMBL:KFI24584.1};
OS Paenirhodobacter enshiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paenirhodobacter.
OX NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI24584.1, ECO:0000313|Proteomes:UP000028824};
RN [1] {ECO:0000313|EMBL:KFI24584.1, ECO:0000313|Proteomes:UP000028824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW2-9 {ECO:0000313|EMBL:KFI24584.1,
RC ECO:0000313|Proteomes:UP000028824};
RA Wang D., Wang G.;
RT "Genome of Paenirhodobacter enshiensis DW2-9.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000256|ARBA:ARBA00011258}.
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:KFI24584.1}.
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DR EMBL; JFZB01000042; KFI24584.1; -; Genomic_DNA.
DR RefSeq; WP_036639680.1; NZ_JFZB01000042.1.
DR AlphaFoldDB; A0A086XRD4; -.
DR STRING; 1105367.CG50_09655; -.
DR eggNOG; COG0174; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000028824; 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:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:KFI24584.1};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
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:UP000028824}.
FT DOMAIN 14..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 106..469
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT BINDING 209
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 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 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 360
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 398
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 469 AA; 52322 MW; 41CD87D475FC340D CRC64;
MSAVKKALEL MKAEDVEYVD VRFTDPRGKL QHVTLVVDLI DEDFFEEGFM FDGSSIAGWK
SIDQSDMKLI PDATSVYIDP FYAEKTMCVH CNVVEPDTNE PYTRDPRSTA EKAEAYLKSS
GIGDSFFCGP EAEFFIFDDV RYSVTPHKVS YQVDAEAAAW NTDAEIEGGN LAHRANFKGG
YFPVNPVDEA ADLRGEMLST MKRIGMKVDK HHHEVATCQH ELGMIFGTLT EQADNIQKYK
YVIHNVAAAY GKTVTFMPKP IKGDNGSGMH VNMSIWKDGK PLFAGDKYAD LSQEALYFIG
GILKHAKALN ALTNPTTNSY KRLIPGFEAP VLRAYSARNR SGCVRIPWTE SPKAKRVEAR
FPDPAANPYL AFSALLMAGL DGIKNKIDPG APSDKDLYDL PPEELAEIPT VCGSLREALT
ELEADMDFLL AGDVFTKDQI EGYIALKWEE VYAFEHTPHP VEYQMYYSC
//