GLNA3_RHIME
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 03-AUG-2022, entry version 116.
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; Proteobacteria; 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 STRING; 266834.SMc02613; -.
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 OMA; RLDINMY; -.
DR Proteomes; UP000001976; Chromosome.
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; 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
