ID   GLNA_AZOVI     STANDARD;      PRT;   467 AA.
AC   P22248;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   07-FEB-2006, entry version 42.
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 [GENOMIC DNA].
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: Cytoplasm.
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; M57275; AAA62673.1; -; Genomic_DNA.
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; Nucleotide-binding.
FT   CHAIN         1    467       Glutamine synthetase.
FT                                /FTId=PRO_0000153231.
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
//