ID   GLNA1_RHILV             Reviewed;         469 AA.
AC   P09826;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JUN-2009, entry version 65.
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=glnA;
OS   Rhizobium leguminosarum bv. viciae.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCC1001;
RX   MEDLINE=87174729; PubMed=2882467; DOI=10.1093/nar/15.5.1951;
RA   Colonna-Romano S., Riccio A., Guida M., Defez R., Lamberti A.,
RA   Iaccarino M., Arnold W., Priefer U., Puehler A.;
RT   "Tight linkage of glnA and a putative regulatory gene in Rhizobium
RT   leguminosarum.";
RL   Nucleic Acids Res. 15:1951-1964(1987).
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   -!- MISCELLANEOUS: Two forms of glutamine synthetase (GSI and GSII)
CC       can be found in this nitrogen fixing bacteria, GSI is a typical
CC       prokaryotic glutamine synthetase whereas GSII is similar to the
CC       eukaryotic enzyme.
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; X04880; CAA28569.1; -; Genomic_DNA.
DR   PIR; A26567; AJZRQL.
DR   HSSP; P06201; 1LGR.
DR   BRENDA; 6.3.1.2; 267396.
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:UniProtKB-KW.
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; FALSE_NEG.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Nitrogen fixation; Nucleotide-binding.
FT   CHAIN         1    469       Glutamine synthetase 1.
FT                                /FTId=PRO_0000153223.
FT   MOD_RES     398    398       O-AMP-tyrosine (By similarity).
SQ   SEQUENCE   469 AA;  52233 MW;  A1E158ECD0970FBC CRC64;
     MATASEILKQ IKENDVKFVD LRFTDRRASL QHVTMDVVCV DEDMFADGVM FDGFSIGGWK
     AINESDMVLM PDTETVHMDP FFAQSTMVIV CDILDPVSGE AYNRDRRGTA KKAEAYLKAS
     GIGDTVFVGR EAEFFVFDDV KYKADPYNTG FKLDSTELPS NDDTDYETGN LGHRPRVKGG
     YFPVPPVDSA QDMRSEMLTV LSEMGVVVEK HHHEVAAAQH DTLVRNADEL GIKFKMQIYK
     YVVHQVANAY GKTATFMPKP IFGDNGSGMH VHQSIWKGGK PTFAGDEYAG LSESCLFYIG
     GIIKHAKAIN AFTNPSTNSY KRFVPGYEAP VLLAYSARNR SASCRIPFGS NPKAKRVEVR
     FPDPTANPYL AFAAMLMAGL DGIKNKIHPG KAMDKDLYDL PPKELKKIPT VCGSLRQALE
     SLDKDRKFLT AGGVFDDDQI DAFIELKMAE VMRFEMTPHP VEYDMYYSA
//