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Database: UniProt
Entry: P10583
LinkDB: P10583
Original site: P10583 
ID   GLN1B_AZOBR             Reviewed;         468 AA.
AC   P10583;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   12-APR-2017, entry version 91.
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   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
RX   PubMed=2878685; DOI=10.1016/S0300-9084(86)80062-1;
RA   Bozouklian H., Elmerich C.;
RT   "Nucleotide sequence of the Azospirillum brasilense Sp7 glutamine
RT   synthetase structural gene.";
RL   Biochimie 68:1181-1187(1986).
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; M26107; AAA22183.1; -; Genomic_DNA.
DR   PIR; A24714; AJKCQB.
DR   ProteinModelPortal; P10583; -.
DR   SMR; P10583; -.
DR   STRING; 1064539.AZOBR_100228; -.
DR   PRIDE; P10583; -.
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; IPR001637; Gln_synth_I_adenylation_site.
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; PS00182; GLNA_ADENYLATION; 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    468       Glutamine synthetase.
FT                                /FTId=PRO_0000153229.
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       358    358       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     209    209       ATP. {ECO:0000250|UniProtKB:P0A1P6}.
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     322    322       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     328    328       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     340    340       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     340    340       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     345    345       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     353    353       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     360    360       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   MOD_RES     398    398       O-AMP-tyrosine.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
SQ   SEQUENCE   468 AA;  51976 MW;  356AA3803E024F1A CRC64;
     MSDISKVFDL IKEHDVKYVD LRFTDPRGKL HHTAQHVSTI DEDVFEDGIM FDGSSIAGWK
     AINESDMILQ LDPTTAVMDP FSAQPTLNIL CDVYEPSTGQ PYARCPRGIA KAAEKYMASA
     GIADTAYFGP EAEFFVFDDV KFKVEMNKVS YEFDSEEGPY TSDKDYEDGN LGHRPGVKGG
     YFPVAPVDSG SDLRAEMLSV LAEMGVPVEK HHHEVAASQH ELGIKFDTLV RTGDNMQYYK
     YVVHNVAHAY GKTATFMPKP VFGDNGSGMH MHQSIWKEGQ PLFAGNQYAD LSELALYYIG
     GIIKHAKALN AFTNPTTNSY KRLVPGYEAP VLLAYSARNR SASCRIPYVA SPKGKRVEVR
     FPDPSANPYL AFAALLMAGL DGIQNKIHPG EAMDKNLYDL PAEELAKVPT VCGSREALDS
     LKADSAFLQK GDVFTKDMIE SYIDLRTEEL LAFETMPHPI EYKMYYSV
//
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