GLN1B_BRADU
ID GLN1B_BRADU Reviewed; 469 AA.
AC P05457;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P0A1P6};
DE Short=GS {ECO:0000250|UniProtKB:P0A1P6};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P0A1P6};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P0A1P6};
DE Short=GSI beta {ECO:0000250|UniProtKB:P0A1P6};
GN Name=glnA {ECO:0000250|UniProtKB:P0A1P6}; Synonyms=glnI;
GN OrderedLocusNames=blr4949;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
RX PubMed=2859270; DOI=10.1128/jb.162.2.698-703.1985;
RA Carlson T.A., Guerinot M.L., Chelm B.K.;
RT "Characterization of the gene encoding glutamine synthetase I (glnA) from
RT Bradyrhizobium japonicum.";
RL J. Bacteriol. 162:698-703(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2793830; DOI=10.1128/jb.171.10.5638-5645.1989;
RA Martin G.B., Thomashow M.F., Chelm B.K.;
RT "Bradyrhizobium japonicum glnB, a putative nitrogen-regulatory gene, is
RT regulated by NtrC at tandem promoters.";
RL J. Bacteriol. 171:5638-5645(1989).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}.
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:P0A1P6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WN39};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
CC -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC adenylation under conditions of abundant glutamine.
CC {ECO:0000250|UniProtKB:Q3V5W6}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000250|UniProtKB:P0A1P6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
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}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; BA000040; BAC50214.1; -; Genomic_DNA.
DR EMBL; M10926; AAA26213.1; -; Genomic_DNA.
DR EMBL; M26753; AAA26215.1; -; Genomic_DNA.
DR PIR; B33600; B33600.
DR RefSeq; NP_771589.1; NC_004463.1.
DR RefSeq; WP_011087712.1; NZ_CP011360.1.
DR AlphaFoldDB; P05457; -.
DR SMR; P05457; -.
DR STRING; 224911.27353214; -.
DR PRIDE; P05457; -.
DR EnsemblBacteria; BAC50214; BAC50214; BAC50214.
DR GeneID; 64024710; -.
DR KEGG; bja:blr4949; -.
DR PATRIC; fig|224911.44.peg.4803; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_2_5; -.
DR InParanoid; P05457; -.
DR OMA; PHPHEFE; -.
DR PhylomeDB; P05457; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; 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 GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central.
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; IPR004809; Gln_synth_I.
DR InterPro; IPR001637; Gln_synth_I_adenylation_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 TIGRFAMs; TIGR00653; GlnA; 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; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="Glutamine synthetase"
FT /id="PRO_0000153219"
FT DOMAIN 14..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 106..469
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 265..266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 272..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 322
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 328
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 360
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT MOD_RES 398
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ SEQUENCE 469 AA; 52315 MW; DCFA18CAA64F4B80 CRC64;
MKTAKDVLKS IKDNDVKYVD LRFTDPRGKW QHVTFDVSMI DEDIFAEGTM FDGSSIAGWK
AINESDMCLM PDPVTATIDP FFAETTMVIT CDVLEPTTGE PYNRDPRGIA KKAEAMVKSM
GVGDTVFVGP EAEFFVFDDV RFSSSPYNTG FRLDSSELPT NTDTEYEGGN LGHRVRTKGG
YFPVPPQDSV QDMRSEMLGA MAKMGVKVEK HHHEVASAQH ELGMKFDTLT LMADHLQIYK
YCIHQVAHIY GKTATFMPKP VYGDNGSGMH VHQSIWKDGK PVFAGNKYAD LSETCLHYIG
GIIKHAKAIN AFTNPSTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYTA SPKAKRVEVR
FPDPLANPYL GFAAMLMAGL DGIKNKIDPG PAMDKDLYDL PKEELKQIPT VCGSLREALE
NLDKDRAFLK AGGVFDDDFI DSYIELKMTE VERFEMTPHP VEFDMYYSG
