ID A0A0L1JUF7_9RHOB Unreviewed; 468 AA.
AC A0A0L1JUF7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00021364, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN Name=glnA {ECO:0000313|EMBL:KNG95419.1};
GN ORFNames=ATO11_02100 {ECO:0000313|EMBL:KNG95419.1};
OS Pseudaestuariivita atlantica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudaestuariivita.
OX NCBI_TaxID=1317121 {ECO:0000313|EMBL:KNG95419.1, ECO:0000313|Proteomes:UP000036938};
RN [1] {ECO:0000313|EMBL:KNG95419.1, ECO:0000313|Proteomes:UP000036938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z3 {ECO:0000313|EMBL:KNG95419.1,
RC ECO:0000313|Proteomes:UP000036938};
RA Li G., Lai Q., Du Y., Liu X., Sun F., Shao Z.;
RT "Aestuariivita atlantica sp. nov., isolated from deep sea sediment of the
RT Atlantic Ocean.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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 hexagons.
CC {ECO:0000256|RuleBase:RU000387}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000256|ARBA:ARBA00011258}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000387}.
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:KNG95419.1}.
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DR EMBL; AQQZ01000001; KNG95419.1; -; Genomic_DNA.
DR RefSeq; WP_050529152.1; NZ_AQQZ01000001.1.
DR AlphaFoldDB; A0A0L1JUF7; -.
DR STRING; 1317121.ATO11_02100; -.
DR PATRIC; fig|1317121.7.peg.423; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000036938; 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: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; IPR001637; Gln_synth_I_adenylation_site.
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; PS00182; GLNA_ADENYLATION; 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|RuleBase:RU000387};
KW Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:KNG95419.1};
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:UP000036938}.
FT DOMAIN 13..97
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 105..468
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 264..265
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 321
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 327
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 339
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2"
FT BINDING 359
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1"
FT MOD_RES 397
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604809-50"
SQ SEQUENCE 468 AA; 52228 MW; DFE97362A2DBBDDC CRC64;
MSVDNVLKTI KDEDVEYVDI RFTDPRGKLQ HVTVMSDQVD ADFLEEGFMF DGSSIAGWKS
IEASDMKLMP DTESAYIDPF YAEKTLCVHC SVVEPDTGEA YDRDPRGTAE KAEAYLKSSG
IGDTAFFGPE AEFFLFDDVK FSTAMNKVSY EVDATDASWN TDTDYEMGNM GHRPGVKGGY
FPVNPTDEAQ DLRSEMLSTM KRIGMKVDKH HHEVASCQHE LGLIFDSLTK QADELQKYKY
IIHNVAHAYG KSATFMPKPI AGDNGTGMHC NMSIWKDGKP LFAGDKYADL SQEALYFIGG
ILKHAKALNA FTNPSTNSYK RLIPGFEAPV LRAYSARNRS GCVRIPWTES PKAKRVEARF
PDPSANPYLC FAALLMAGLD GIKNKIDPGE AMDKNLYDLP AEELADIPTV CGSLREALEE
LEADMDFLLA GDVFTKDQIA GYIDLKMEEI EAYEHTPHPM EFQLYYSC
//
