ID   GLNA_AZOVI     STANDARD;      PRT;   467 AA.
AC   P22248;
DT   01-AUG-1991 (Rel. 19, Created)
DT   01-AUG-1991 (Rel. 19, 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   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91035268; PubMed=1977737;
RA   Toukdarian A., Saunders G., Selman-Sosa G., Santero E., Woodley P.,
RA   Kennedy C.;
RT   "Molecular analysis of the Azotobacter vinelandii glnA gene encoding
RT   glutamine synthetase.";
RL   J. Bacteriol. 172:6529-6539(1990).
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; M57275; AAA62673.1; -.
DR   PIR; A37153; AJAVQ.
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     396    396       AMP (covalent) (By similarity).
SQ   SEQUENCE   467 AA;  51746 MW;  D4EFA6EC895E38AF CRC64;
     MSKSLQLIKE HDVKWIDLRF TDTKGKQQHV TMPARDVDDD FFEYGKMFDG SSIAGWKGIE
     ASDMILMPDD STAVLDPFTE EPTLIIVCDI IEPSTMQGYD RDPRAIARRA EEYLKSTGIG
     DTAFFGPEPE FFIFDEVKYK SDISGSMFKI FSEQAAWNTD ADFEGGNKGH RPGVKGGYFP
     VPPVDHDHEI RTAMCNALEE MGLKVEVHHH EVATAGQNEI GVSFNTLVAK ADEVQTLKYC
     VHNVADAYGK TVTFMPKPLY GDNGSGMHVH MSIAKDGKNT FAGEGYAGLS DTALYFIGGI
     IKHGKALNGF TNPSTNSYKR LVPGFEAPVM LAYSARNRSA SIRIPYVNSP KARRIEARFP
     DPSANPYLAF AALLMAGLDG IQNKIHPGDA ADKNLYDLPP EEAKEIPQVC GSLKEALEEL
     DKGRAFLTKG GVFSDDFIDA YLELKSEEEI KVRTFVHPLE YDLYYSV
//