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Database: UniProt
Entry: P45627
LinkDB: P45627
Original site: P45627 
ID   GLNA_LACDE              Reviewed;         445 AA.
AC   P45627;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   16-OCT-2013, entry version 62.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA;
OS   Lactobacillus delbrueckii subsp. bulgaricus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1359838;
RA   Ishino Y., Morgenthaler P., Hottinger H., Soell D.;
RT   "Organization and nucleotide sequence of the glutamine synthetase
RT   (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus.";
RL   Appl. Environ. Microbiol. 58:3165-3169(1992).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- ENZYME REGULATION: Does not seem to be regulated by adenylation.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR   EMBL; D10020; BAA00910.1; -; Genomic_DNA.
DR   PIR; A48947; A48947.
DR   ProteinModelPortal; P45627; -.
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:UniProtKB-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; SSF54368; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    445       Glutamine synthetase.
FT                                /FTId=PRO_0000153241.
SQ   SEQUENCE   445 AA;  50134 MW;  A57A9E11ABAF87E8 CRC64;
     MSKVITEEEI RKDVEEKNVR FLRLAFTDIN GTLKNLEVPV SQLDDVLGNQ TRFDGSSIDG
     FVRLEESDMV LYPDLATWLV LAWTTVEEGT IGRLVCSVHN VDGTPFEGDP RNNLKKVIAE
     MEEMGFSDFE IGFEAEFFLF KEGKNGEETT KVSDHSSYFD MASEDEGAKC RREIVETLEK
     LGFRVEAAHH EVGDGQQEID FRFDNALATA DKLQTFKMVV KTIARKYHLH ASFMAKPVEG
     LAGNGMHTNM SLLKDGKNAF YDKDGQYNLS TTALTFLNGI LEHARAITCV ANPTVNSYKR
     LIPGFEAPVY ISWASRNRSP MVRIPNANEV GTRLEMRSTD PTANPYLLLS ACLKAGLTGI
     KEGKLPMAPV TSNLFEMTDD ERKELGIKPL PSTLHNAIKA FKEDEVVKSA FSEHIVDSFL
     ELKETEWALY TQSVSEWEVK RYFNY
//
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