ID   Q72J16_THET2            Unreviewed;       446 AA.
AC   Q72J16;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   29-MAY-2013, entry version 55.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
GN   OrderedLocusNames=TT_C0965;
OS   Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB27 / ATCC BAA-163 / DSM 7039;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA   Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA   Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA   Klenk H.-P., Overbeek R., Kramer W., Merkl R., Gottschalk G.,
RA   Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus
RT   thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE017221; AAS81307.1; -; Genomic_DNA.
DR   RefSeq; YP_004934.1; NC_005835.1.
DR   ProteinModelPortal; Q72J16; -.
DR   STRING; 262724.TTC0965; -.
DR   EnsemblBacteria; AAS81307; AAS81307; TT_C0965.
DR   GeneID; 2775922; -.
DR   KEGG; tth:TTC0965; -.
DR   PATRIC; 23952331; VBITheThe54392_0958.
DR   eggNOG; COG0174; -.
DR   KO; K01915; -.
DR   OMA; MFRTQVH; -.
DR   ProtClustDB; CLSK2761945; -.
DR   BioCyc; TTHE262724:GCAT-975-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:InterPro.
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; IPR004809; Gln_synth_I.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SUPFAM; SSF54368; Gln_synt_beta; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Ligase.
SQ   SEQUENCE   446 AA;  50557 MW;  B0816C10480EE93B CRC64;
     MGYTKAEILK ALKGENVKFL RLQITDILGV VKNVEVPESQ FEKALDGEIM FDGSSIEGFT
     RIEESDMLLR PDYNTFVILP DLVEDPKRGR VARLICDVYY PDGRPFEGDP RYVLKRQIER
     LKKLGFDNLY AGPEPEFFLF LRTPEGLPTT ETHDRAGYFD LAPIDKGEEA RRDMVNALVA
     MGFEIEAAHH EVAPGQHEID FKYADALTTA DNIATFKWVV KRIALNHGLH ATFLPKPIRG
     INGSGMHTHL SLFKDGENAF YDPNAEYQLS QTALHFIAGL LEHAAGMVAV TNPLVNSYKR
     LTPGYEAPTN IAWSASNRSA MIRIPARRGV GTRAELRMPD PSCNPYLALA VMAAAGADGI
     ERKLLPPPPI QRNIYQMTVR ERRKHKIREL PGTLREALEA LRKDPVIREA LGEHVYTHFL
     QAKQMEWDDY RVTVHQWELD RYLATY
//