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Database: UniProt
Entry: P45627
LinkDB: P45627
Original site: P45627 
ID   GLN1A_LACDE             Reviewed;         445 AA.
AC   P45627;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   15-MAR-2017, entry version 72.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:1359838};
DE            Short=GS {ECO:0000303|PubMed:1359838};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P12425};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000250|UniProtKB:P12425};
DE   AltName: Full=Glutamine synthetase I alpha {ECO:0000250|UniProtKB:P12425};
DE            Short=GSI alpha {ECO:0000250|UniProtKB:P12425};
GN   Name=glnA {ECO:0000303|PubMed:1359838};
OS   Lactobacillus delbrueckii subsp. bulgaricus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1585;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1359838;
RA   Ishino Y., Morgenthaler P., Hottinger H., Soell D.;
RT   "Organization and nucleotide sequence of the glutamine synthetase
RT   (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus.";
RL   Appl. Environ. Microbiol. 58:3165-3169(1992).
CC   -!- FUNCTION: Glutamine synthetase (GS) is an unusual multitasking
CC       protein that functions as an enzyme, a transcription coregulator,
CC       and a chaperone in ammonium assimilation and in the regulation of
CC       genes involved in nitrogen metabolism. It catalyzes the ATP-
CC       dependent biosynthesis of glutamine from glutamate and ammonia.
CC       Feedback-inhibited GlnA also interacts with and regulates the
CC       activity of the transcriptional regulator TnrA. During nitrogen
CC       limitation, TnrA is in its DNA-binding active state and turns on
CC       the transcription of genes required for nitrogen assimilation.
CC       Under conditions of nitrogen excess, feedback-inhibited GlnA forms
CC       a stable complex with TnrA, which inhibits its DNA-binding
CC       activity. In contrast, feedback-inhibited GlnA acts as a chaperone
CC       to stabilize the DNA-binding activity of GlnR, which represses the
CC       transcription of nitrogen assimilation genes.
CC       {ECO:0000250|UniProtKB:P12425}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000250|UniProtKB:P12425}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P12425};
CC       Note=Binds 2 Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P12425};
CC   -!- ENZYME REGULATION: Inhibited by glutamine.
CC       {ECO:0000250|UniProtKB:P12425}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. In its feedback-inhibited form, interacts with TnrA in
CC       order to block its DNA-binding activity.
CC       {ECO:0000250|UniProtKB:P12425}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12425}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
DR   EMBL; D10020; BAA00910.1; -; Genomic_DNA.
DR   PIR; A48947; A48947.
DR   ProteinModelPortal; P45627; -.
DR   SMR; P45627; -.
DR   STRING; 390333.Ldb1472; -.
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:InterPro.
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   Nucleotide-binding.
FT   CHAIN         1    445       Glutamine synthetase.
FT                                /FTId=PRO_0000153241.
FT   METAL       134    134       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   METAL       136    136       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   METAL       191    191       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   METAL       198    198       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   METAL       247    247       Magnesium 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   METAL       335    335       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     186    186       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     243    243       L-glutamate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     251    251       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     300    300       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     306    306       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     318    318       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     318    318       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     323    323       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     337    337       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   SITE         63     63       Important for inhibition by glutamine.
FT                                {ECO:0000250|UniProtKB:P12425}.
SQ   SEQUENCE   445 AA;  50134 MW;  A57A9E11ABAF87E8 CRC64;
     MSKVITEEEI RKDVEEKNVR FLRLAFTDIN GTLKNLEVPV SQLDDVLGNQ TRFDGSSIDG
     FVRLEESDMV LYPDLATWLV LAWTTVEEGT IGRLVCSVHN VDGTPFEGDP RNNLKKVIAE
     MEEMGFSDFE IGFEAEFFLF KEGKNGEETT KVSDHSSYFD MASEDEGAKC RREIVETLEK
     LGFRVEAAHH EVGDGQQEID FRFDNALATA DKLQTFKMVV KTIARKYHLH ASFMAKPVEG
     LAGNGMHTNM SLLKDGKNAF YDKDGQYNLS TTALTFLNGI LEHARAITCV ANPTVNSYKR
     LIPGFEAPVY ISWASRNRSP MVRIPNANEV GTRLEMRSTD PTANPYLLLS ACLKAGLTGI
     KEGKLPMAPV TSNLFEMTDD ERKELGIKPL PSTLHNAIKA FKEDEVVKSA FSEHIVDSFL
     ELKETEWALY TQSVSEWEVK RYFNY
//
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