ID   GLNA_AZOBR              Reviewed;         468 AA.
AC   P10583;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   01-MAY-2013, entry version 77.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
RX   PubMed=2878685; DOI=10.1016/S0300-9084(86)80062-1;
RA   Bozouklian H., Elmerich C.;
RT   "Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine
RT   synthetase structural gene.";
RL   Biochimie 68:1181-1187(1986).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- ENZYME REGULATION: The activity of this enzyme is controlled by
CC       adenylation under conditions of abundant glutamine. The fully
CC       adenylated enzyme complex is inactive (By similarity).
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR   EMBL; M26107; AAA22183.1; -; Genomic_DNA.
DR   PIR; A24714; AJKCQB.
DR   ProteinModelPortal; P10583; -.
DR   SMR; P10583; 7-468.
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; 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   SUPFAM; SSF54368; Gln_synt_beta; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN         1    468       Glutamine synthetase.
FT                                /FTId=PRO_0000153229.
FT   MOD_RES     398    398       O-AMP-tyrosine (By similarity).
SQ   SEQUENCE   468 AA;  51976 MW;  356AA3803E024F1A CRC64;
     MSDISKVFDL IKEHDVKYVD LRFTDPRGKL HHTAQHVSTI DEDVFEDGIM FDGSSIAGWK
     AINESDMILQ LDPTTAVMDP FSAQPTLNIL CDVYEPSTGQ PYARCPRGIA KAAEKYMASA
     GIADTAYFGP EAEFFVFDDV KFKVEMNKVS YEFDSEEGPY TSDKDYEDGN LGHRPGVKGG
     YFPVAPVDSG SDLRAEMLSV LAEMGVPVEK HHHEVAASQH ELGIKFDTLV RTGDNMQYYK
     YVVHNVAHAY GKTATFMPKP VFGDNGSGMH MHQSIWKEGQ PLFAGNQYAD LSELALYYIG
     GIIKHAKALN AFTNPTTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYVA SPKGKRVEVR
     FPDPSANPYL AFAALLMAGL DGIQNKIHPG EAMDKNLYDL PAEELAKVPT VCGSREALDS
     LKADSAFLQK GDVFTKDMIE SYIDLRTEEL LAFETMPHPI EYKMYYSV
//