ID   GLNA3_RHIME             Reviewed;         435 AA.
AC   O87393;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:8093245};
DE            Short=GS {ECO:0000303|PubMed:8093245};
DE            EC=6.3.1.2 {ECO:0000269|PubMed:8093245};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:8093245};
DE            Short=GSIII {ECO:0000303|PubMed:8093245};
GN   Name=glnT {ECO:0000303|PubMed:8093245}; OrderedLocusNames=R00090;
GN   ORFNames=SMc02613;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RA   Powers E.L., Vuyyuru V., Kahn M.L.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=104A14;
RX   PubMed=8093245; DOI=10.1016/s0021-9258(18)54175-2;
RA   Shatters R.G., Liu Y., Kahn M.L.;
RT   "Isolation and characterization of a novel glutamine synthetase from
RT   Rhizobium meliloti.";
RL   J. Biol. Chem. 268:469-475(1993).
CC   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC       glutamate and ammonia. {ECO:0000269|PubMed:8093245}.
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:0000269|PubMed:8093245};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:8093245};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425};
CC   -!- ACTIVITY REGULATION: Inhibited by methionine sulfoximine, ADP and
CC       pyrophosphate, but not by various nitrogen-containing metabolites that
CC       inhibit other GS enzymes. {ECO:0000269|PubMed:8093245}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.3 mM for glutamate {ECO:0000269|PubMed:8093245};
CC         KM=33 mM for ammonium {ECO:0000269|PubMed:8093245};
CC       pH dependence:
CC         Optimum pH is 6.8. {ECO:0000269|PubMed:8093245};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:8093245};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:8093245}.
CC   -!- MISCELLANEOUS: Can grow, in the absence of GSI and GSII glutamine
CC       synthetases, without a glutamine supplement in minimal medium that
CC       contains both ammonium and glutamate. However, given the high glutamate
CC       and ammonium substrate Km values, glutamine synthase is probably a
CC       secondary activity of GlnT. {ECO:0000305|PubMed:8093245}.
CC   -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSIII) can be
CC       found in this nitrogen fixing bacteria, GSI is a typical prokaryotic
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; AF055582; AAC62223.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC41477.1; -; Genomic_DNA.
DR   RefSeq; NP_384196.1; NC_003047.1.
DR   RefSeq; WP_003532529.1; NC_003047.1.
DR   AlphaFoldDB; O87393; -.
DR   SMR; O87393; -.
DR   EnsemblBacteria; CAC41477; CAC41477; SMc02613.
DR   GeneID; 61601571; -.
DR   KEGG; sme:SMc02613; -.
DR   PATRIC; fig|266834.11.peg.1447; -.
DR   eggNOG; COG0174; Bacteria.
DR   HOGENOM; CLU_017290_1_3_5; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase 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; 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; IPR017536; Glutamine_synthetase_typeIII.
DR   NCBIfam; TIGR03105; gln_synth_III; 1.
DR   PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR   PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR   Pfam; PF00120; Gln-synt_C; 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; 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; Ligase; Magnesium; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153227"
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;  48481 MW;  90DE8275496E5400 CRC64;
     MTLDLSTFAR EKGVKYFMIS YTDLFGGQRA KLVPAEAIAD MQKGGAGFAG FATWFDLTPA
     HPDLFALPDA SAVIQLPWKK DVAWVAADCI MDDAPVEQAP RVVLKKLVAE AAQEGLRVKT
     GVEPEFFLIS PDGSKISDTF DTAEKPCYDQ QAIMRRYDVI AEICDYMLEL GWKPYQNDHE
     DANGQFEMNW EYDDALRTAD KHSFFKFMVK SIAEKHGLRA TFMPKPFKGL TGNGCHCHIS
     VWDLAGEVNA FADNKAEFGL SAEGRHFLGG IMKHASALAA VTNPTVNSYK RINAPRTISG
     ATWAPNSVTW TGNNRTHMVR VPGPGRFELR LPDGAVNPYL LQAIIIAAGL SGVRSKADPG
     RHYDIDMYKD GHKVTDAPKL PLNLLDALRE YNRDEELQEA LGREFSAAYL KLKQGEWNTY
     CSQFTEWEHQ TTLDV
//