GLN1B_MYCTU
ID GLN1B_MYCTU Reviewed; 478 AA.
AC P9WN39; L0TAJ3; P0A590; Q10377;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:7937767};
DE Short=GS {ECO:0000303|PubMed:7937767};
DE EC=6.3.1.2 {ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000305};
DE Short=GSI beta {ECO:0000305};
GN Name=glnA1 {ECO:0000303|PubMed:7937767}; Synonyms=glnA;
GN OrderedLocusNames=Rv2220; ORFNames=MTCY190.31, MTCY427.01;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=9278431; DOI=10.1074/jbc.272.36.22728;
RA Harth G., Horwitz M.A.;
RT "Expression and efficient export of enzymatically active Mycobacterium
RT tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence
RT that the information for export is contained within the protein.";
RL J. Biol. Chem. 272:22728-22735(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=7937767; DOI=10.1073/pnas.91.20.9342;
RA Harth G., Clemens D.L., Horwitz M.A.;
RT "Glutamine synthetase of Mycobacterium tuberculosis: extracellular release
RT and characterization of its enzymatic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=10618433; DOI=10.1073/pnas.97.1.418;
RA Harth G., Zamecnik P.C., Tang J.Y., Tabatadze D., Horwitz M.A.;
RT "Treatment of Mycobacterium tuberculosis with antisense oligonucleotides to
RT glutamine synthetase mRNA inhibits glutamine synthetase activity, formation
RT of the poly-L-glutamate/glutamine cell wall structure, and bacterial
RT replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:418-423(2000).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=12496196; DOI=10.1128/iai.71.1.456-464.2003;
RA Harth G., Horwitz M.A.;
RT "Inhibition of Mycobacterium tuberculosis glutamine synthetase as a novel
RT antibiotic strategy against tuberculosis: demonstration of efficacy in
RT vivo.";
RL Infect. Immun. 71:456-464(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=12819079; DOI=10.1128/iai.71.7.3927-3936.2003;
RA Tullius M.V., Harth G., Horwitz M.A.;
RT "Glutamine synthetase GlnA1 is essential for growth of Mycobacterium
RT tuberculosis in human THP-1 macrophages and guinea pigs.";
RL Infect. Immun. 71:3927-3936(2003).
RN [7]
RP AMPYLATION AT TYR-406, MUTAGENESIS OF TYR-406, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=15037612; DOI=10.1074/jbc.m401652200;
RA Mehta R., Pearson J.T., Mahajan S., Nath A., Hickey M.J., Sherman D.R.,
RA Atkins W.M.;
RT "Adenylylation and catalytic properties of Mycobacterium tuberculosis
RT glutamine synthetase expressed in Escherichia coli versus mycobacteria.";
RL J. Biol. Chem. 279:22477-22482(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-478, ACTIVITY REGULATION,
RP AMPYLATION AT TYR-406, AND SUBUNIT.
RX PubMed=12146952; DOI=10.1021/bi020254s;
RA Gill H.S., Pfluegl G.M., Eisenberg D.;
RT "Multicopy crystallographic refinement of a relaxed glutamine synthetase
RT from Mycobacterium tuberculosis highlights flexible loops in the enzymatic
RT mechanism and its regulation.";
RL Biochemistry 41:9863-9872(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE
RP ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, AMPYLATION AT TYR-406, REACTION
RP MECHANISM, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=16027359; DOI=10.1073/pnas.0502248102;
RA Krajewski W.W., Jones T.A., Mowbray S.L.;
RT "Structure of Mycobacterium tuberculosis glutamine synthetase in complex
RT with a transition-state mimic provides functional insights.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10499-10504(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE
RP ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RX PubMed=19695264; DOI=10.1016/j.jmb.2009.08.028;
RA Nilsson M.T., Krajewski W.W., Yellagunda S., Prabhumurthy S.,
RA Chamarahally G.N., Siddamadappa C., Srinivasa B.R., Yahiaoui S., Larhed M.,
RA Karlen A., Jones T.A., Mowbray S.L.;
RT "Structural basis for the inhibition of Mycobacterium tuberculosis
RT glutamine synthetase by novel ATP-competitive inhibitors.";
RL J. Mol. Biol. 393:504-513(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE
RP ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX PubMed=22369127; DOI=10.1021/jm201212h;
RA Gising J., Nilsson M.T., Odell L.R., Yahiaoui S., Lindh M., Iyer H.,
RA Sinha A.M., Srinivasa B.R., Larhed M., Mowbray S.L., Karlen A.;
RT "Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine
RT synthetase inhibitors.";
RL J. Med. Chem. 55:2894-2898(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE
RP ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX DOI=10.1039/C2MD00310D;
RA Nordqvist A., Nilsson M.T., Lagerlund O., Muthas D., Gising J.,
RA Yahiaoui S., Odell L.R., Srinivasa B.R., Larhed M., Mowbray S.L.,
RA Karlen A.;
RT "Synthesis, biological evaluation and X-Ray crystallographic studies of
RT imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine
RT synthetase inhibitors.";
RL Med. Chem. Commun. 3:620-626(2012).
CC -!- FUNCTION: Involved in nitrogen metabolism via ammonium assimilation.
CC Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate
CC and ammonia (PubMed:7937767, PubMed:12819079). Also able to use GTP
CC (PubMed:7937767). D-glutamate is a poor substrate, and DL-glutamate
CC shows about 50% of the standard specific activity (PubMed:7937767).
CC Also plays a key role in controlling the ammonia levels within infected
CC host cells and so contributes to the pathogens capacity to inhibit
CC phagosome acidification and phagosome-lysosome fusion (PubMed:7937767,
CC PubMed:12819079). Involved in cell wall biosynthesis via the production
CC of the major component poly-L-glutamine (PLG) (PubMed:7937767,
CC PubMed:10618433). PLG synthesis in the cell wall occurs only in
CC nitrogen limiting conditions and on the contrary high nitrogen
CC conditions inhibit PLG synthesis (Probable).
CC {ECO:0000269|PubMed:10618433, ECO:0000269|PubMed:12819079,
CC ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:9278431}.
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:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16027359, ECO:0000269|PubMed:19695264,
CC ECO:0000269|PubMed:22369127, ECO:0000269|Ref.13};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:16027359,
CC ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
CC ECO:0000269|Ref.13};
CC -!- ACTIVITY REGULATION: When cellular nitrogen levels are high, the C-
CC terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent
CC transfer of an adenylyl group from ATP to Tyr-406 (PubMed:15037612).
CC Conversely, when nitrogen levels are low, the N-terminal adenylyl
CC removase (AR) of GlnE activates GlnA by removing the adenylyl group by
CC phosphorolysis (PubMed:15037612). The fully adenylated enzyme complex
CC is inactive (Probable). Also inhibited by the diketopurine analog 1-
CC [(3,4-dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-
CC dione, EDTA, and by L-methionine-SR-sulfoximine (MSO) (PubMed:7937767,
CC PubMed:12496196, PubMed:19695264). {ECO:0000269|PubMed:12496196,
CC ECO:0000269|PubMed:15037612, ECO:0000269|PubMed:19695264,
CC ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:12146952}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for ATP {ECO:0000269|PubMed:19695264};
CC KM=2.7 mM for L-glutamate {ECO:0000269|PubMed:7937767};
CC KM=2.9 mM for L-glutamine {ECO:0000269|PubMed:7937767};
CC KM=10.8 mM for ammonium {ECO:0000269|PubMed:19695264};
CC KM=21.6 mM for L-glutamate {ECO:0000269|PubMed:19695264};
CC Vmax=110 umol/min/mg enzyme {ECO:0000269|PubMed:7937767};
CC pH dependence:
CC Optimum pH is 7.5 in the presence of magnesium and cobalt ions
CC (PubMed:7937767, PubMed:19695264). Optimum pH is 7 in the presence of
CC manganese ions (PubMed:7937767). {ECO:0000269|PubMed:19695264,
CC ECO:0000269|PubMed:7937767};
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two hexagons.
CC {ECO:0000269|PubMed:12146952, ECO:0000269|PubMed:16027359,
CC ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264,
CC ECO:0000305|PubMed:22369127, ECO:0000305|Ref.13}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9278431}.
CC -!- INDUCTION: Repressed by phosphorothioate modified antisense
CC oligodeoxyribonucleotides (PS-ODNs), which acts against the mRNA of
CC glutamine synthetase. {ECO:0000269|PubMed:10618433}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show a detectable
CC glutamine synthetase activity and is auxotrophic for L-glutamine. This
CC mutant is also attenuated for intracellular growth in human THP-1
CC macrophages and avirulent in the highly susceptible guinea pig model of
CC pulmonary tuberculosis. {ECO:0000269|PubMed:12819079}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; U87280; AAB70038.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44998.1; -; Genomic_DNA.
DR PIR; H70775; H70775.
DR RefSeq; NP_216736.1; NC_000962.3.
DR RefSeq; WP_003411475.1; NZ_NVQJ01000008.1.
DR PDB; 1HTO; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-478.
DR PDB; 1HTQ; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-478.
DR PDB; 2BVC; X-ray; 2.10 A; A/B/C/D/E/F=2-478.
DR PDB; 2WGS; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J/K/L=2-478.
DR PDB; 2WHI; X-ray; 2.20 A; A/B/C/D/E/F=2-478.
DR PDB; 3ZXR; X-ray; 2.15 A; A/B/C/D/E/F=2-478.
DR PDB; 3ZXV; X-ray; 2.26 A; A/B/C/D/E/F=2-478.
DR PDB; 4ACF; X-ray; 2.00 A; A/B/C/D/E/F=2-478.
DR PDB; 4XYC; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-478.
DR PDBsum; 1HTO; -.
DR PDBsum; 1HTQ; -.
DR PDBsum; 2BVC; -.
DR PDBsum; 2WGS; -.
DR PDBsum; 2WHI; -.
DR PDBsum; 3ZXR; -.
DR PDBsum; 3ZXV; -.
DR PDBsum; 4ACF; -.
DR PDBsum; 4XYC; -.
DR AlphaFoldDB; P9WN39; -.
DR SMR; P9WN39; -.
DR STRING; 83332.Rv2220; -.
DR DrugBank; DB04272; Citric acid.
DR PaxDb; P9WN39; -.
DR DNASU; 888383; -.
DR GeneID; 45426197; -.
DR GeneID; 888383; -.
DR KEGG; mtu:Rv2220; -.
DR TubercuList; Rv2220; -.
DR eggNOG; COG0174; Bacteria.
DR OMA; PHPHEFE; -.
DR PhylomeDB; P9WN39; -.
DR BRENDA; 6.3.1.2; 3445.
DR PHI-base; PHI:7587; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0006542; P:glutamine biosynthetic process; IMP:MTBBASE.
DR GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:CAFA.
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; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7937767"
FT CHAIN 2..478
FT /note="Glutamine synthetase"
FT /id="PRO_0000153246"
FT DOMAIN 16..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 108..478
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0007744|PDB:2BVC"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 230..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0007744|PDB:2BVC"
FT BINDING 271..272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
FT ECO:0000305|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 272
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P12425"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
FT ECO:0000305|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 329
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
FT ECO:0000305|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 335
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P0A1P6"
FT BINDING 347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19695264,
FT ECO:0000305|PubMed:22369127, ECO:0007744|PDB:2WHI,
FT ECO:0007744|PDB:3ZXR"
FT BINDING 347
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
FT ECO:0000305|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:22369127, ECO:0000305|Ref.13,
FT ECO:0007744|PDB:2BVC, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P77961"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16027359,
FT ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
FT ECO:0000269|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT BINDING 368
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000305|PubMed:16027359,
FT ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
FT ECO:0000305|Ref.13, ECO:0007744|PDB:2BVC,
FT ECO:0007744|PDB:2WHI, ECO:0007744|PDB:3ZXR,
FT ECO:0007744|PDB:3ZXV, ECO:0007744|PDB:4ACF"
FT MOD_RES 406
FT /note="O-AMP-tyrosine"
FT /evidence="ECO:0000269|PubMed:15037612,
FT ECO:0000305|PubMed:12146952, ECO:0000305|PubMed:16027359"
FT MUTAGEN 406
FT /note="Y->F: Unable to be adenylylated."
FT /evidence="ECO:0000269|PubMed:15037612"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1HTQ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:4ACF"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 108..122
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4ACF"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4ACF"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 235..255
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 300..320
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1HTQ"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:4ACF"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:4ACF"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 376..392
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 445..458
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:4ACF"
FT HELIX 469..475
FT /evidence="ECO:0007829|PDB:4ACF"
SQ SEQUENCE 478 AA; 53570 MW; 576E30073484136D CRC64;
MTEKTPDDVF KLAKDEKVEY VDVRFCDLPG IMQHFTIPAS AFDKSVFDDG LAFDGSSIRG
FQSIHESDML LLPDPETARI DPFRAAKTLN INFFVHDPFT LEPYSRDPRN IARKAENYLI
STGIADTAYF GAEAEFYIFD SVSFDSRANG SFYEVDAISG WWNTGAATEA DGSPNRGYKV
RHKGGYFPVA PNDQYVDLRD KMLTNLINSG FILEKGHHEV GSGGQAEINY QFNSLLHAAD
DMQLYKYIIK NTAWQNGKTV TFMPKPLFGD NGSGMHCHQS LWKDGAPLMY DETGYAGLSD
TARHYIGGLL HHAPSLLAFT NPTVNSYKRL VPGYEAPINL VYSQRNRSAC VRIPITGSNP
KAKRLEFRSP DSSGNPYLAF SAMLMAGLDG IKNKIEPQAP VDKDLYELPP EEAASIPQTP
TQLSDVIDRL EADHEYLTEG GVFTNDLIET WISFKRENEI EPVNIRPHPY EFALYYDV
