GLNA2_RHILP
ID GLNA2_RHILP Reviewed; 326 AA.
AC Q02154; Q9R5J0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1357539};
DE Short=GS {ECO:0000303|PubMed:1357539};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P16580};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase II {ECO:0000303|PubMed:1357539};
DE Short=GSII {ECO:0000303|PubMed:1357539};
GN Name=glnII {ECO:0000303|PubMed:1357539};
OS Rhizobium leguminosarum bv. phaseoli.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=385;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=LPR1105;
RX PubMed=1357539; DOI=10.1007/bf00538692;
RA Patriarca E.J., Chiurazzi M., Manco G., Riccio A., Lamberti A., Paolis A.,
RA Rossi M., Defez R., Iaccarino M.;
RT "Activation of the Rhizobium leguminosarum glnII gene by NtrC is dependent
RT on upstream DNA sequences.";
RL Mol. Gen. Genet. 234:337-345(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-27, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=LPR1105;
RX PubMed=1355107; DOI=10.1099/00221287-138-7-1453;
RA Manco G., Rossi M., Defez R., Lamberti A., Percuoco G., Iaccarino M.;
RT "Dissociation by NH4Cl treatment of the enzymic activities of glutamine
RT synthetase II from Rhizobium leguminosarum biovar viceae.";
RL J. Gen. Microbiol. 138:1453-1460(1992).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000305|PubMed:1355107}.
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:0000250|UniProtKB:P16580};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P16580};
CC -!- ACTIVITY REGULATION: Transferase activity is inhibited by NH(4)Cl.
CC {ECO:0000269|PubMed:1355107}.
CC -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000269|PubMed:1355107}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16580}.
CC -!- INDUCTION: Up-regulated by the nitrogen regulatory protein NtrC.
CC {ECO:0000269|PubMed:1357539}.
CC -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSII) can be
CC found in this nitrogen fixing bacteria, GSI is a typical prokaryotic
CC glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.
CC {ECO:0000305|PubMed:1357539}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X67296; CAA47710.1; -; Genomic_DNA.
DR PIR; S26216; S26216.
DR AlphaFoldDB; Q02154; -.
DR SMR; Q02154; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; Nitrogen fixation; Nucleotide-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1355107"
FT CHAIN 2..326
FT /note="Glutamine synthetase"
FT /id="PRO_0000153224"
FT DOMAIN 4..85
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 83..326
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 275
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ SEQUENCE 326 AA; 36979 MW; 637AE03B83D1F840 CRC64;
MTKFKLEYIW LDGYTPVPNL RGKTQIKEFD EFPTLEQLPL WGFDGSSTMQ AEGSSDCVLK
PVAIYPDPAR TNGALVMCEV MMPDGHAHAS NARATILDDE DAWFGFEQEY FFYQNGRPLG
FPEQGYPAPQ PYYTGVGYSN VGDVAREIVE EHLDLCLAAG INHEGINAEV AKGQWEFQIF
GKGSKKAADQ IWMARYLLQR LTEKYGIDIE YHCKPLGDTD WNGSGMHCNF STKYLREVGG
KEYFEALMAS SDKNLMDHIA VYGPDNDKRL TGKHETAPWN KFSYGVADRG ASIRVPHSFI
KNDYKGYLED RRPNSQGDPY QIVRRF
