GLNA2_BRADU
ID GLNA2_BRADU Reviewed; 344 AA.
AC P04772;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glutamine synthetase {ECO:0000303|Ref.1};
DE Short=GS {ECO:0000303|Ref.1};
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|Ref.1};
DE Short=GSII {ECO:0000303|Ref.1};
GN Name=glnII {ECO:0000303|Ref.1}; OrderedLocusNames=blr4169;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RA Carlson T.A., Chelm B.K.;
RT "Apparent eukaryotic origin of glutamine synthetase II from the bacterium
RT Bradyrhizobium japonicum.";
RL Nature 322:568-570(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:Q02154}.
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 -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000250|UniProtKB:Q02154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16580}.
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|Ref.1}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X04187; CAA27779.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC49434.1; -; Genomic_DNA.
DR PIR; A24155; AJZJQ2.
DR RefSeq; NP_770809.1; NC_004463.1.
DR RefSeq; WP_011086942.1; NZ_CP011360.1.
DR AlphaFoldDB; P04772; -.
DR SMR; P04772; -.
DR STRING; 224911.27352431; -.
DR EnsemblBacteria; BAC49434; BAC49434; BAC49434.
DR GeneID; 64023900; -.
DR KEGG; bja:blr4169; -.
DR PATRIC; fig|224911.44.peg.3887; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_036762_1_0_5; -.
DR InParanoid; P04772; -.
DR OMA; DRRPNAN; -.
DR PhylomeDB; P04772; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..344
FT /note="Glutamine synthetase"
FT /id="PRO_0000153220"
FT DOMAIN 4..86
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 89..344
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 278
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT CONFLICT 37..38
FT /note="QL -> HV (in Ref. 1; CAA27779)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..344
FT /note="ASQILKTISSVPTEKKAVA -> VRRS (in Ref. 1; CAA27779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38366 MW; 5462522D03DC51B2 CRC64;
MTKYKLEYIW LDGYTPTPNL RGKTQIKEFA SFPTLEQLPL WGFDGSSTQQ AEGHSSDCVL
KPVAVFPDAA RTNGVLVMCE VMMPDGKTPH ASNKRATILD DAGAWFGFEQ EYFFYKDGRP
LGFPTSGYPA PQGPYYTGVG FSNVGDVARK IVEEHLDLCL AAGINHEGIN AEVAKGQWEF
QIFGKGSKKA ADEMWMARYL MLRLTEKYGI DIEFHCKPLG DTDWNGSGMH ANFSTEYMRT
VGGKEYFEAL MAAFDKNLMD HIAVYGPDND KRLTGKHETA PWNKFSYGVA DRGASIRVPH
SFVNNGYKGY LEDRRPNSQG DPYQIASQIL KTISSVPTEK KAVA
