GLNA3_RHILP
ID GLNA3_RHILP Reviewed; 435 AA.
AC P31592;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1356885};
DE Short=GS {ECO:0000303|PubMed:1356885};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:O87393};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:1356885};
DE Short=GSIII {ECO:0000305};
GN Name=glnT {ECO:0000303|PubMed:1356885};
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 PROTEIN SEQUENCE OF 1-8.
RX PubMed=1356885; DOI=10.1016/0378-1119(92)90060-3;
RA Chiurazzi M., Meza R., Lara M., Lahm A., Defez R., Iaccarino M., Espin G.;
RT "The Rhizobium leguminosarum biovar phaseoli glnT gene, encoding glutamine
RT synthetase III.";
RL Gene 119:1-8(1992).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:O87393}.
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:O87393};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O87393};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:O87393}.
CC -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSII and GSIII) can
CC be found in this nitrogen fixing bacteria, GSII is a typical eukaryotic
CC glutamine synthetase whereas GSIII is a divergent type with very low
CC sequence similarity to the type I and II enzymes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; S48357; AAB23489.1; -; Genomic_DNA.
DR PIR; JC1301; JC1301.
DR AlphaFoldDB; P31592; -.
DR SMR; P31592; -.
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; 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; IPR017536; Glutamine_synthetase_typeIII.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR03105; gln_synth_III; 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; Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding.
FT CHAIN 1..435
FT /note="Glutamine synthetase"
FT /id="PRO_0000153279"
FT DOMAIN 12..94
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 100..435
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 232
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 291
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 315
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 330
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
SQ SEQUENCE 435 AA; 48270 MW; 305FEAE2AC4A2B77 CRC64;
MTLDLAAFAR DKSIKYFMIS YTDLFGGQRA KLVPAEAIAD MQKDGAGFAG FATWLDLTPA
HPDLFAVPDA SSVIQLPWKK DVAWVAADCV MDDRPVEQAP RVVLKRLVAE AAKEGLRVKT
GVEPEFFLIS ADGSVISDQF DTAEKPCYDQ QAVMRRYDVI AEICDYMLEL GWKPYQNDHE
DANGQFEMNW EYDDVLKTAD KHSFFKFMVK SVAEKHGLRA TFMPKPFKGL TGNGCHAHIS
VWDVDGRVNA FADKEMAFGL SAQGKTFLGG IMKHAPALAA ITNPTVNSYK RINAPRTTSG
ATWSPNTVTW TGNNRTHMVR VPGPGRFELR LPDGAVNPYL LQAIIIAAGL EGIRSQADPG
QHYDIDMYAE GHLVKDAPRL PLNLLDALRA FDADEGLKAA IGAEFSSAYL KLKHLEWNAY
CSHFTQWERD STLDI
