GLN1B_ECOLI
ID GLN1B_ECOLI Reviewed; 469 AA.
AC P0A9C5; P06711; Q2M8G7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
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}; OrderedLocusNames=b3870, JW3841;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2882477; DOI=10.1093/nar/15.6.2757;
RA Miranda-Rios J., Sanchez-Pescador R., Urdea M., Covarrubias A.A.;
RT "The complete nucleotide sequence of the glnALG operon of Escherichia coli
RT K12.";
RL Nucleic Acids Res. 15:2757-2770(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2874141; DOI=10.1016/s0021-9258(18)67425-3;
RA Colombo G., Villafranca J.J.;
RT "Amino acid sequence of Escherichia coli glutamine synthetase deduced from
RT the DNA nucleotide sequence.";
RL J. Biol. Chem. 261:10587-10591(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX PubMed=6134228; DOI=10.1007/bf00330342;
RA Covarrubias A.A., Bastarrachea F.;
RT "Nucleotide sequence of the glnA control region of Escherichia coli.";
RL Mol. Gen. Genet. 190:171-175(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=2858855; DOI=10.1073/pnas.82.7.1979;
RA Reitzer L.J., Magasanik B.;
RT "Expression of glnA in Escherichia coli is regulated at tandem promoters.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:1979-1983(1985).
RN [8]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 363-469.
RX PubMed=2865194; DOI=10.1016/0378-1119(85)90261-6;
RA Rocha M., Vazquez M., Garciarrubio A., Covarrubias A.A.;
RT "Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia
RT coli.";
RL Gene 37:91-99(1985).
RN [10]
RP PROTEIN SEQUENCE OF 387-406, SEQUENCE REVISION, AND AMPYLATION AT TYR-398.
RX PubMed=5543675; DOI=10.1016/s0021-9258(18)62436-6;
RA Heinrikson R.L., Kingdon H.S.;
RT "Primary structure of Escherichia coli glutamine synthetase. II. The
RT complete amino acid sequence of a tryptic heneicosapeptide containing
RT covalently bound adenylic acid.";
RL J. Biol. Chem. 246:1099-1106(1971).
RN [11]
RP PROTEIN SEQUENCE OF 394-406, AND AMPYLATION AT TYR-398.
RX PubMed=4904088; DOI=10.1016/s0021-9258(18)63431-3;
RA Heinrikson R.L., Kingdon H.S.;
RT "The amino acid sequence in the vicinity of the covalently bound adenylic
RT acid in glutamine synthetase from Escherichia coli.";
RL J. Biol. Chem. 245:138-142(1970).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-469.
RX PubMed=6148334; DOI=10.1128/jb.160.1.379-384.1984;
RA Ueno-Nishio S., Mango S., Reitzer L.J., Magasanik B.;
RT "Identification and regulation of the glnL operator-promoter of the complex
RT glnALG operon of Escherichia coli.";
RL J. Bacteriol. 160:379-384(1984).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={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. {ECO:0000250|UniProtKB:P9WN39};
CC -!- ACTIVITY REGULATION: The activity of this enzyme could be controlled by
CC adenylation under conditions of abundant glutamine.
CC {ECO:0000250|UniProtKB:Q3V5W6}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexameric
CC ring. {ECO:0000250|UniProtKB:P0A1P6}.
CC -!- INTERACTION:
CC P0A9C5; P0A9C5: glnA; NbExp=2; IntAct=EBI-909063, EBI-909063;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X05173; CAA28806.1; -; Genomic_DNA.
DR EMBL; M13746; AAA23879.1; -; Genomic_DNA.
DR EMBL; L19201; AAB03004.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76867.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77439.1; -; Genomic_DNA.
DR EMBL; J01618; AAA98066.1; -; Genomic_DNA.
DR EMBL; M10421; AAA23882.1; -; Genomic_DNA.
DR EMBL; K02176; AAA23880.1; -; Genomic_DNA.
DR PIR; S40815; AJECQ.
DR RefSeq; NP_418306.1; NC_000913.3.
DR RefSeq; WP_001271717.1; NZ_STEB01000017.1.
DR PDB; 7W85; EM; 2.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/U/V/W/X/Y=1-469.
DR PDBsum; 7W85; -.
DR AlphaFoldDB; P0A9C5; -.
DR SMR; P0A9C5; -.
DR BioGRID; 4262630; 46.
DR BioGRID; 852667; 1.
DR DIP; DIP-9777N; -.
DR IntAct; P0A9C5; 10.
DR STRING; 511145.b3870; -.
DR BindingDB; P0A9C5; -.
DR ChEMBL; CHEMBL3789; -.
DR MetOSite; P0A9C5; -.
DR SWISS-2DPAGE; P0A9C5; -.
DR jPOST; P0A9C5; -.
DR PaxDb; P0A9C5; -.
DR PRIDE; P0A9C5; -.
DR EnsemblBacteria; AAC76867; AAC76867; b3870.
DR EnsemblBacteria; BAE77439; BAE77439; BAE77439.
DR GeneID; 66672224; -.
DR GeneID; 948370; -.
DR KEGG; ecj:JW3841; -.
DR KEGG; eco:b3870; -.
DR PATRIC; fig|1411691.4.peg.2841; -.
DR EchoBASE; EB0378; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_017290_1_2_6; -.
DR InParanoid; P0A9C5; -.
DR OMA; PHPHEFE; -.
DR PhylomeDB; P0A9C5; -.
DR BioCyc; EcoCyc:GLUTAMINESYN-MON; -.
DR BioCyc; MetaCyc:GLUTAMINESYN-MON; -.
DR SABIO-RK; P0A9C5; -.
DR PRO; PR:P0A9C5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019676; P:ammonia assimilation cycle; IDA:EcoCyc.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0019740; P:nitrogen utilization; IDA:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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 SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..469
FT /note="Glutamine synthetase"
FT /id="PRO_0000153235"
FT DOMAIN 13..97
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 105..469
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 265..266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 266
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 272..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 322
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 328
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 360
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT MOD_RES 398
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000269|PubMed:4904088,
FT ECO:0000269|PubMed:5543675"
FT CONFLICT 90
FT /note="C -> S (in Ref. 2; AAA23879)"
FT /evidence="ECO:0000305"
FT CONFLICT 108..109
FT /note="IA -> MS (in Ref. 2; AAA23879)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="C -> S (in Ref. 2; AAA23879)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="T -> I (in Ref. 1; CAA28806)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..248
FT /note="AH -> VRN (in Ref. 1; CAA28806)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..306
FT /note="HA -> QP (in Ref. 1; CAA28806)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="DK -> KD (in Ref. 10; AA sequence and 11; AA
FT sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51904 MW; 0AFC05724CDEBA36 CRC64;
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG
INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRSTG
IADTVLFGPE PEFFLFDDIR FGSSISGSHV AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY
FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK
YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS SPKARRIEVR
FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN
ELDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV
