ID   GLNA_AZOBR     STANDARD;      PRT;   468 AA.
AC   P10583;
DT   01-JUL-1989 (Rel. 11, Created)
DT   01-JUL-1989 (Rel. 11, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Glutamine synthetase (EC 6.3.1.2) (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.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=87076765; PubMed=2878685;
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: Cytoplasmic.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M26107; AAA22183.1; -.
DR   PIR; A24714; AJKCQB.
DR   HSSP; P06201; 1LGR.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR008146; Gln_synt_C.
DR   InterPro; IPR004809; GlnA.
DR   InterPro; IPR001637; GlnA_adenyltn_S.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   ProDom; PD001057; Gln_synt_C; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
KW   Ligase; Nitrogen fixation.
FT   BINDING     398    398       AMP (covalent) (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
//