ID   GLNA1_STRVR             Reviewed;         469 AA.
AC   Q05542;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Glutamine synthetase 1;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamine synthetase I;
DE            Short=GSI;
DE   AltName: Full=Glutamate--ammonia ligase I;
GN   Name=glnI; Synonyms=glnA;
OS   Streptomyces viridochromogenes.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93219414; PubMed=8096645; DOI=10.1073/pnas.90.7.3009;
RA   Kumada Y., Benson D.R., Hillemann D., Hosted T.J., Rocheford D.A.,
RA   Thompson C.J., Wohlleben W., Tateno Y.;
RT   "Evolution of the glutamine synthetase gene, one of the oldest
RT   existing and functioning genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:3009-3013(1993).
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; X70924; CAA50272.1; -; Genomic_DNA.
DR   PIR; S32024; S32024.
DR   HSSP; P06201; 1LGR.
DR   BRENDA; 6.3.1.2; 39938.
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:InterPro.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat.
DR   InterPro; IPR008146; Gln_synth_cat.
DR   InterPro; IPR004809; Gln_synth_I.
DR   InterPro; IPR001637; Gln_synth_I_adenyltn_S.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    469       Glutamine synthetase 1.
FT                                /FTId=PRO_0000153269.
FT   MOD_RES     397    397       O-AMP-tyrosine (By similarity).
SQ   SEQUENCE   469 AA;  52248 MW;  2F152E5A5A4283E4 CRC64;
     MFQNADEAKK LIADEDVKFI DVRFCDLPGV MQHFTIPASA FDPAEELAFD GSSIRGFQAI
     HESDMAVRAD LSTARVDPFR RDKTVNINFF IHDPITGEQY SRDPRNVAKK AEAYLASTGI
     GDTGYFGPEA EFYVFDSVRL ANSATESFYH IDSEAGAWNT GALENNRGYK VRYKGGYFPV
     PPVDHFADLR AQISLELDRA GLQVERHDHE VGTAGQAEIN YKFNTLLAAA DDLQLFKYIV
     KNVAWQNGKT ATFMPKPIFG DNGSGMHVHQ SLWTGGQALF YDEAGYAGLS DTARYYMGGI
     LKHAPSLLAF TNPTVNSYHR LVPGFEAPVN LVYSQRNRSA AMRIPITGSN PKAKRVEFRA
     PDSSGNPYLA FSALLLAGLD GIKNKIEPAE PIDKDLYELA PEEHAGVPQV PTSLPAVLDR
     LEADHEFLLA GDVFTPDLIE TWIDYKRTNE IAPLQLRPHP YEYEQYYDV
//