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Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta)

 GLN1B_MYCTU             Reviewed;         478 AA.
P9WN39; L0TAJ3; P0A590; Q10377;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-FEB-2018, entry version 29.
RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:7937767};
Short=GS {ECO:0000303|PubMed:7937767};
EC=6.3.1.2 {ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:19695264};
AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
AltName: Full=Glutamine synthetase I beta {ECO:0000305};
Short=GSI beta {ECO:0000305};
Name=glnA1 {ECO:0000303|PubMed:7937767}; Synonyms=glnA;
OrderedLocusNames=Rv2220; ORFNames=MTCY190.31, MTCY427.01;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=9278431; DOI=10.1074/jbc.272.36.22728;
Harth G., Horwitz M.A.;
"Expression and efficient export of enzymatically active Mycobacterium
tuberculosis glutamine synthetase in Mycobacterium smegmatis and
evidence that the information for export is contained within the
protein.";
J. Biol. Chem. 272:22728-22735(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[3]
PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE
SPECIFICITY, AND SUBUNIT.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=7937767; DOI=10.1073/pnas.91.20.9342;
Harth G., Clemens D.L., Horwitz M.A.;
"Glutamine synthetase of Mycobacterium tuberculosis: extracellular
release and characterization of its enzymatic activity.";
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994).
[4]
FUNCTION, AND INDUCTION.
PubMed=10618433; DOI=10.1073/pnas.97.1.418;
Harth G., Zamecnik P.C., Tang J.Y., Tabatadze D., Horwitz M.A.;
"Treatment of Mycobacterium tuberculosis with antisense
oligonucleotides to glutamine synthetase mRNA inhibits glutamine
synthetase activity, formation of the poly-L-glutamate/glutamine cell
wall structure, and bacterial replication.";
Proc. Natl. Acad. Sci. U.S.A. 97:418-423(2000).
[5]
ENZYME REGULATION.
PubMed=12496196; DOI=10.1128/IAI.71.1.456-464.2003;
Harth G., Horwitz M.A.;
"Inhibition of Mycobacterium tuberculosis glutamine synthetase as a
novel antibiotic strategy against tuberculosis: demonstration of
efficacy in vivo.";
Infect. Immun. 71:456-464(2003).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=12819079; DOI=10.1128/IAI.71.7.3927-3936.2003;
Tullius M.V., Harth G., Horwitz M.A.;
"Glutamine synthetase GlnA1 is essential for growth of Mycobacterium
tuberculosis in human THP-1 macrophages and guinea pigs.";
Infect. Immun. 71:3927-3936(2003).
[7]
AMPYLATION AT TYR-406, MUTAGENESIS OF TYR-406, AND ENZYME REGULATION.
STRAIN=ATCC 27294 / TMC 102 / H37Rv;
PubMed=15037612; DOI=10.1074/jbc.M401652200;
Mehta R., Pearson J.T., Mahajan S., Nath A., Hickey M.J.,
Sherman D.R., Atkins W.M.;
"Adenylylation and catalytic properties of Mycobacterium tuberculosis
glutamine synthetase expressed in Escherichia coli versus
mycobacteria.";
J. Biol. Chem. 279:22477-22482(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[9]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-478, ENZYME REGULATION,
AMPYLATION AT TYR-406, AND SUBUNIT.
PubMed=12146952; DOI=10.1021/bi020254s;
Gill H.S., Pfluegl G.M., Eisenberg D.;
"Multicopy crystallographic refinement of a relaxed glutamine
synthetase from Mycobacterium tuberculosis highlights flexible loops
in the enzymatic mechanism and its regulation.";
Biochemistry 41:9863-9872(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-478 IN COMPLEX WITH
SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, AMPYLATION AT
TYR-406, REACTION MECHANISM, COFACTOR, AND SUBUNIT.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=16027359; DOI=10.1073/pnas.0502248102;
Krajewski W.W., Jones T.A., Mowbray S.L.;
"Structure of Mycobacterium tuberculosis glutamine synthetase in
complex with a transition-state mimic provides functional insights.";
Proc. Natl. Acad. Sci. U.S.A. 102:10499-10504(2005).
[11]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH
SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, AND
SUBUNIT.
PubMed=19695264; DOI=10.1016/j.jmb.2009.08.028;
Nilsson M.T., Krajewski W.W., Yellagunda S., Prabhumurthy S.,
Chamarahally G.N., Siddamadappa C., Srinivasa B.R., Yahiaoui S.,
Larhed M., Karlen A., Jones T.A., Mowbray S.L.;
"Structural basis for the inhibition of Mycobacterium tuberculosis
glutamine synthetase by novel ATP-competitive inhibitors.";
J. Mol. Biol. 393:504-513(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-478 IN COMPLEX WITH
SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, AND
SUBUNIT.
PubMed=22369127; DOI=10.1021/jm201212h;
Gising J., Nilsson M.T., Odell L.R., Yahiaoui S., Lindh M., Iyer H.,
Sinha A.M., Srinivasa B.R., Larhed M., Mowbray S.L., Karlen A.;
"Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine
synthetase inhibitors.";
J. Med. Chem. 55:2894-2898(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-478 IN COMPLEX WITH
SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, AND
SUBUNIT.
DOI=10.1039/C2MD00310D;
Nordqvist A., Nilsson M.T., Lagerlund O., Muthas D., Gising J.,
Yahiaoui S., Odell L.R., Srinivasa B.R., Larhed M., Mowbray S.L.,
Karlen A.;
"Synthesis, biological evaluation and X-Ray crystallographic studies
of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine
synthetase inhibitors.";
Med. Chem. Commun. 3:620-626(2012).
-!- FUNCTION: Involved in nitrogen metabolism via ammonium
assimilation. Catalyzes the ATP-dependent biosynthesis of
glutamine from glutamate and ammonia (PubMed:7937767,
PubMed:12819079). Also able to use GTP (PubMed:7937767). D-
glutamate is a poor substrate, and DL-glutamate shows about 50% of
the standard specific activity (PubMed:7937767). Also plays a key
role in controlling the ammonia levels within infected host cells
and so contributes to the pathogens capacity to inhibit phagosome
acidification and phagosome-lysosome fusion (PubMed:7937767,
PubMed:12819079). Involved in cell wall biosynthesis via the
production of the major component poly-L-glutamine (PLG)
(PubMed:7937767, PubMed:10618433). PLG synthesis in the cell wall
occurs only in nitrogen limiting conditions and on the contrary
high nitrogen conditions inhibit PLG synthesis (Probable).
{ECO:0000269|PubMed:10618433, ECO:0000269|PubMed:12819079,
ECO:0000269|PubMed:7937767, ECO:0000305|PubMed:9278431}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
L-glutamine. {ECO:0000269|PubMed:7937767,
ECO:0000305|PubMed:19695264}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13};
Note=Binds 2 Mg(2+) ions per subunit.
{ECO:0000269|PubMed:16027359, ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127, ECO:0000269|Ref.13};
-!- ENZYME REGULATION: When cellular nitrogen levels are high, the C-
terminal adenylyl transferase (AT) of GlnE inhibits GlnA by
covalent transfer of an adenylyl group from ATP to Tyr-406
(PubMed:15037612). Conversely, when nitrogen levels are low, the
N-terminal adenylyl removase (AR) of GlnE activates GlnA by
removing the adenylyl group by phosphorolysis (PubMed:15037612).
The fully adenylated enzyme complex is inactive (Probable). Also
inhibited by the diketopurine analog 1-[(3,4-
dichlorophenyl)methyl]-3,7-dimethyl-8-morpholin-4-yl-purine-2,6-
dione, EDTA, and by L-methionine-SR-sulfoximine (MSO)
(PubMed:7937767, PubMed:12496196, PubMed:19695264).
{ECO:0000269|PubMed:12496196, ECO:0000269|PubMed:15037612,
ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:7937767,
ECO:0000305|PubMed:12146952}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.5 mM for ATP {ECO:0000269|PubMed:19695264};
KM=2.7 mM for L-glutamate {ECO:0000269|PubMed:7937767};
KM=2.9 mM for L-glutamine {ECO:0000269|PubMed:7937767};
KM=10.8 mM for ammonium {ECO:0000269|PubMed:19695264};
KM=21.6 mM for L-glutamate {ECO:0000269|PubMed:19695264};
Vmax=110 umol/min/mg enzyme {ECO:0000269|PubMed:7937767};
pH dependence:
Optimum pH is 7.5 in the presence of magnesium and cobalt ions
(PubMed:7937767, PubMed:19695264). Optimum pH is 7 in the
presence of manganese ions (PubMed:7937767).
{ECO:0000269|PubMed:19695264, ECO:0000269|PubMed:7937767};
-!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
hexagons. {ECO:0000269|PubMed:12146952,
ECO:0000269|PubMed:16027359, ECO:0000269|PubMed:7937767,
ECO:0000305|PubMed:19695264, ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9278431}.
-!- INDUCTION: Repressed by phosphorothioate modified antisense
oligodeoxyribonucleotides (PS-ODNs), which acts against the mRNA
of glutamine synthetase. {ECO:0000269|PubMed:10618433}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show a
detectable glutamine synthetase activity and is auxotrophic for L-
glutamine. This mutant is also attenuated for intracellular growth
in human THP-1 macrophages and avirulent in the highly susceptible
guinea pig model of pulmonary tuberculosis.
{ECO:0000269|PubMed:12819079}.
-!- SIMILARITY: Belongs to the glutamine synthetase family.
{ECO:0000305}.
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EMBL; U87280; AAB70038.1; -; Genomic_DNA.
EMBL; AL123456; CCP44998.1; -; Genomic_DNA.
PIR; H70775; H70775.
RefSeq; NP_216736.1; NC_000962.3.
RefSeq; WP_003411475.1; NZ_KK339370.1.
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.
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.
PDB; 2BVC; X-ray; 2.10 A; A/B/C/D/E/F=2-478.
PDB; 2WGS; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J/K/L=2-478.
PDB; 2WHI; X-ray; 2.20 A; A/B/C/D/E/F=2-478.
PDB; 3ZXR; X-ray; 2.15 A; A/B/C/D/E/F=2-478.
PDB; 3ZXV; X-ray; 2.26 A; A/B/C/D/E/F=2-478.
PDB; 4ACF; X-ray; 2.00 A; A/B/C/D/E/F=2-478.
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.
PDBsum; 1HTO; -.
PDBsum; 1HTQ; -.
PDBsum; 2BVC; -.
PDBsum; 2WGS; -.
PDBsum; 2WHI; -.
PDBsum; 3ZXR; -.
PDBsum; 3ZXV; -.
PDBsum; 4ACF; -.
PDBsum; 4XYC; -.
ProteinModelPortal; P9WN39; -.
SMR; P9WN39; -.
STRING; 83332.Rv2220; -.
PaxDb; P9WN39; -.
EnsemblBacteria; CCP44998; CCP44998; Rv2220.
GeneID; 888383; -.
KEGG; mtu:Rv2220; -.
TubercuList; Rv2220; -.
eggNOG; ENOG4105C5F; Bacteria.
eggNOG; COG0174; LUCA.
KO; K01915; -.
OMA; IEAAWNT; -.
PhylomeDB; P9WN39; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:MTBBASE.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035375; F:zymogen binding; IPI:CAFA.
GO; GO:0020012; P:evasion or tolerance of host immune response; IDA:MTBBASE.
GO; GO:0006542; P:glutamine biosynthetic process; IMP:MTBBASE.
GO; GO:0040007; P:growth; IMP:MTBBASE.
GO; GO:0044044; P:interaction with host via substance in symbiont surface; IDA:CAFA.
GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IMP:MTBBASE.
GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:CAFA.
Gene3D; 3.10.20.70; -; 1.
InterPro; IPR008147; Gln_synt_b-grasp.
InterPro; IPR036651; Gln_synt_N.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
InterPro; IPR008146; Gln_synth_cat_dom.
InterPro; IPR027303; Gln_synth_gly_rich_site.
InterPro; IPR004809; Gln_synth_I.
InterPro; IPR001637; Gln_synth_I_adenylation_site.
InterPro; IPR027302; Gln_synth_N_conserv_site.
Pfam; PF00120; Gln-synt_C; 1.
Pfam; PF03951; Gln-synt_N; 1.
SMART; SM01230; Gln-synt_C; 1.
SUPFAM; SSF54368; SSF54368; 1.
SUPFAM; SSF55931; SSF55931; 1.
TIGRFAMs; TIGR00653; GlnA; 1.
PROSITE; PS00180; GLNA_1; 1.
PROSITE; PS00182; GLNA_ADENYLATION; 1.
PROSITE; PS00181; GLNA_ATP; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Ligase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Virulence.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7937767}.
CHAIN 2 478 Glutamine synthetase.
/FTId=PRO_0000153246.
NP_BIND 230 232 ATP. {ECO:0000244|PDB:2BVC,
ECO:0000305|PubMed:16027359}.
NP_BIND 278 280 ATP. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
REGION 271 272 L-glutamate binding.
{ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
METAL 133 133 Magnesium 1. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
METAL 135 135 Magnesium 2. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
METAL 219 219 Magnesium 2. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
METAL 227 227 Magnesium 2. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
METAL 276 276 Magnesium 1; via pros nitrogen.
{ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
METAL 366 366 Magnesium 1. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000269|PubMed:16027359,
ECO:0000269|PubMed:19695264,
ECO:0000269|PubMed:22369127,
ECO:0000269|Ref.13}.
BINDING 214 214 ATP. {ECO:0000244|PDB:2BVC,
ECO:0000305|PubMed:16027359}.
BINDING 272 272 L-glutamate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P12425}.
BINDING 280 280 ATP. {ECO:0000250|UniProtKB:P77961}.
BINDING 329 329 L-glutamate. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
BINDING 335 335 L-glutamate.
{ECO:0000250|UniProtKB:P0A1P6}.
BINDING 347 347 ATP. {ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127}.
BINDING 347 347 L-glutamate. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
BINDING 352 352 ATP. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
BINDING 361 361 ATP. {ECO:0000250|UniProtKB:P77961}.
BINDING 368 368 L-glutamate. {ECO:0000244|PDB:2BVC,
ECO:0000244|PDB:2WHI,
ECO:0000244|PDB:3ZXR,
ECO:0000244|PDB:3ZXV,
ECO:0000244|PDB:4ACF,
ECO:0000305|PubMed:16027359,
ECO:0000305|PubMed:19695264,
ECO:0000305|PubMed:22369127,
ECO:0000305|Ref.13}.
MOD_RES 406 406 O-AMP-tyrosine.
{ECO:0000269|PubMed:15037612,
ECO:0000305|PubMed:12146952,
ECO:0000305|PubMed:16027359}.
MUTAGEN 406 406 Y->F: Unable to be adenylylated.
{ECO:0000269|PubMed:15037612}.
HELIX 6 15 {ECO:0000244|PDB:4ACF}.
STRAND 20 26 {ECO:0000244|PDB:4ACF}.
STRAND 28 30 {ECO:0000244|PDB:4ACF}.
STRAND 32 38 {ECO:0000244|PDB:4ACF}.
HELIX 39 41 {ECO:0000244|PDB:4ACF}.
HELIX 44 48 {ECO:0000244|PDB:4ACF}.
STRAND 51 54 {ECO:0000244|PDB:4ACF}.
HELIX 55 57 {ECO:0000244|PDB:4ACF}.
STRAND 58 62 {ECO:0000244|PDB:1HTQ}.
HELIX 64 66 {ECO:0000244|PDB:4ACF}.
STRAND 68 73 {ECO:0000244|PDB:4ACF}.
HELIX 75 77 {ECO:0000244|PDB:4ACF}.
STRAND 88 96 {ECO:0000244|PDB:4ACF}.
TURN 98 100 {ECO:0000244|PDB:4ACF}.
HELIX 108 122 {ECO:0000244|PDB:4ACF}.
STRAND 126 134 {ECO:0000244|PDB:4ACF}.
STRAND 136 146 {ECO:0000244|PDB:4ACF}.
STRAND 151 156 {ECO:0000244|PDB:4ACF}.
HELIX 161 163 {ECO:0000244|PDB:4ACF}.
STRAND 186 188 {ECO:0000244|PDB:4ACF}.
TURN 190 192 {ECO:0000244|PDB:4ACF}.
HELIX 196 208 {ECO:0000244|PDB:4ACF}.
STRAND 213 218 {ECO:0000244|PDB:4ACF}.
TURN 222 224 {ECO:0000244|PDB:4ACF}.
STRAND 225 230 {ECO:0000244|PDB:4ACF}.
HELIX 235 255 {ECO:0000244|PDB:4ACF}.
STRAND 259 261 {ECO:0000244|PDB:4ACF}.
STRAND 275 283 {ECO:0000244|PDB:4ACF}.
STRAND 286 290 {ECO:0000244|PDB:4ACF}.
HELIX 295 297 {ECO:0000244|PDB:4ACF}.
HELIX 300 320 {ECO:0000244|PDB:4ACF}.
HELIX 326 329 {ECO:0000244|PDB:4ACF}.
STRAND 330 333 {ECO:0000244|PDB:1HTQ}.
STRAND 334 336 {ECO:0000244|PDB:4ACF}.
STRAND 338 340 {ECO:0000244|PDB:4ACF}.
STRAND 342 344 {ECO:0000244|PDB:4ACF}.
STRAND 349 353 {ECO:0000244|PDB:4ACF}.
TURN 360 362 {ECO:0000244|PDB:4ACF}.
STRAND 365 367 {ECO:0000244|PDB:4ACF}.
STRAND 372 374 {ECO:0000244|PDB:4ACF}.
HELIX 376 392 {ECO:0000244|PDB:4ACF}.
HELIX 405 407 {ECO:0000244|PDB:4ACF}.
HELIX 410 414 {ECO:0000244|PDB:4ACF}.
HELIX 423 432 {ECO:0000244|PDB:4ACF}.
HELIX 435 438 {ECO:0000244|PDB:4ACF}.
HELIX 439 441 {ECO:0000244|PDB:4ACF}.
HELIX 445 458 {ECO:0000244|PDB:4ACF}.
HELIX 460 464 {ECO:0000244|PDB:4ACF}.
HELIX 469 475 {ECO:0000244|PDB:4ACF}.
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


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