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Database: UniProt
Entry: O87393
LinkDB: O87393
Original site: O87393 
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   01-MAY-2013, entry version 79.
DE   RecName: Full=Glutamine synthetase 3;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase III;
DE   AltName: Full=Glutamine synthetase III;
DE            Short=GSIII;
GN   Name=glnT; OrderedLocusNames=R00090; ORFNames=SMc02613;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
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.,
RA   Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U.,
RA   Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont
RT   Sinorhizobium 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.,
RA   Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA   Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA   Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA   Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA   Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA   Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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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   ProteinModelPortal; O87393; -.
DR   STRING; 266834.SMc02613; -.
DR   EnsemblBacteria; CAC41477; CAC41477; SMc02613.
DR   GeneID; 1231721; -.
DR   KEGG; sme:SMc02613; -.
DR   PATRIC; 23629349; VBISinMel96828_1447.
DR   eggNOG; COG0174; -.
DR   HOGENOM; HOG000005156; -.
DR   KO; K01915; -.
DR   OMA; RTHAIRI; -.
DR   ProtClustDB; CLSK864701; -.
DR   BioCyc; SMEL266834:GJF6-96-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:EC.
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   Gene3D; 3.30.590.10; -; 1.
DR   InterPro; IPR008147; Gln_synt_beta.
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   SUPFAM; SSF54368; Gln_synt_beta; 1.
DR   TIGRFAMs; TIGR03105; gln_synth_III; 1.
DR   PROSITE; PS00180; GLNA_1; FALSE_NEG.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nitrogen fixation;
KW   Nucleotide-binding.
FT   CHAIN         1    435       Glutamine synthetase 3.
FT                                /FTId=PRO_0000153227.
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
//
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