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Database: UniProt
Entry: P43518
LinkDB: P43518
Original site: P43518 
ID   GLNA_RHOSH              Reviewed;         467 AA.
AC   P43518;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   29-OCT-2014, entry version 66.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA;
OS   Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2R;
RX   PubMed=7921264;
RA   Zinchenko V.V., Churin Y., Shestopalov V.I., Shestakov S.V.;
RT   "Nucleotide sequence and characterization of the Rhodobacter
RT   sphaeroides glnB and glnA genes.";
RL   Microbiology 140:2143-2151(1994).
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       {ECO:0000250}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; X71659; CAA50651.1; -; Genomic_DNA.
DR   PIR; S33181; S33181.
DR   ProteinModelPortal; P43518; -.
DR   SMR; P43518; 5-466.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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; Nitrogen fixation; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    467       Glutamine synthetase.
FT                                /FTId=PRO_0000153256.
FT   MOD_RES     396    396       O-AMP-tyrosine. {ECO:0000250}.
SQ   SEQUENCE   467 AA;  51964 MW;  BA93A04250BFB978 CRC64;
     MSKVADALKL MKDEEVEYVD IRFTDPRGKL QHVTLVADLV DEDFFEEGFM FDGSSIAGWK
     SIDQSDMKLI PDAGSVYIDP FYAEKTLCVH CNVVEPDTGE AYSRDPRGAA VKAEAYLKAS
     GIGDVAYFGP EAEFFIFDDV RYSVTPAKVA YQIDADAGAW NTDSEYEMGN LAHRAGHKGG
     YFPVNPIDEA QDLRGEMLST MKRMGMKVDK HHHEVATCQH ELGLIFGGLT EQADNILKYK
     YVIHNVAGMH GKTVTFMPKP MKGDNGSGMH VNMSIWKEQA LFAGDKYADL SQEALWFIGG
     ILKQPSVNAL TNPATNSYKR LIPGFEAPVL RAYSARNRSG CVRIPWTESP NAKRVEARFP
     DPSANPYLAF AALLMAGLDG IKNKIDPGPA SDKDLYDLPP EELAAIPTVC GSLREALEEL
     EKDHDFLLAG DVFTKDQLEG YMALKWEEVY AYEHTPHPVE YQMYYSC
//
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