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Database: UniProt
Entry: P43518
LinkDB: P43518
Original site: P43518 
ID   GLN1B_RHOSH             Reviewed;         467 AA.
AC   P43518;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   12-APR-2017, entry version 76.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GS {ECO:0000250|UniProtKB:P0A1P6};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P0A1P6};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P0A1P6};
GN   Name=glnA {ECO:0000250|UniProtKB:P0A1P6};
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; DOI=10.1099/13500872-140-8-2143;
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   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine
CC       from glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WN39};
CC       Note=Binds 2 Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P9WN39};
CC   -!- ENZYME REGULATION: The activity of this enzyme could be controlled
CC       by adenylation under conditions of abundant glutamine.
CC       {ECO:0000250|UniProtKB:Q3V5W6}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexameric ring. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
DR   EMBL; X71659; CAA50651.1; -; Genomic_DNA.
DR   PIR; S33181; S33181.
DR   ProteinModelPortal; P43518; -.
DR   SMR; P43518; -.
DR   STRING; 349102.Rsph17025_1344; -.
DR   eggNOG; ENOG4105C5F; Bacteria.
DR   eggNOG; COG0174; LUCA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_b-grasp.
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   SMART; SM01230; Gln-synt_C; 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; Magnesium; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    467       Glutamine synthetase.
FT                                /FTId=PRO_0000153256.
FT   NP_BIND     272    274       ATP. {ECO:0000250|UniProtKB:P0A1P6}.
FT   REGION      265    266       L-glutamate binding.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   METAL       131    131       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       133    133       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       214    214       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       221    221       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       270    270       Magnesium 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       356    356       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     209    209       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     266    266       L-glutamate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     274    274       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     320    320       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     326    326       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     338    338       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     338    338       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     343    343       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     358    358       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   MOD_RES     396    396       O-AMP-tyrosine.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
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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