UniProtKB - P9WN39 (GLN1B_MYCTU)
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>sp|P9WN39|GLN1B_MYCTU Glutamine synthetase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glnA1 PE=1 SV=1 MTEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAFDGSSIRG FQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKAENYLI STGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTGAATEADGSPNRGYKV RHKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAAD DMQLYKYIIKNTAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSD TARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNP KAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEEAASIPQTP TQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEPVNIRPHPYEFALYYDVHelp videoAdd a publicationFeedback
Protein
Glutamine synthetase
Gene
glnA1
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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).1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.1"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."
Harth G., Horwitz M.A.
J. Biol. Chem. 272:22728-22735(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT. - Ref.4"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."
Harth G., Zamecnik P.C., Tang J.Y., Tabatadze D., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 97:418-423(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION. - Ref.6"Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs."
Tullius M.V., Harth G., Horwitz M.A.
Infect. Immun. 71:3927-3936(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- ATPEC:6.3.1.2
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Manual assertion inferred by curator fromi
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
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Manual assertion inferred by curator fromi
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
Source: Rhea- Search for this reaction in UniProtKB.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mg2+
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Manual assertion based on experiment ini
- Ref.10"Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights."
Krajewski W.W., Jones T.A., Mowbray S.L.
Proc. Natl. Acad. Sci. U.S.A. 102:10499-10504(2005) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBUNIT. - Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT. - Ref.12"Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
J. Med. Chem. 55:2894-2898(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT. - Ref.13"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
Med. Chem. Commun. 3:620-626(2012)Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.10"Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights."
Krajewski W.W., Jones T.A., Mowbray S.L.
Proc. Natl. Acad. Sci. U.S.A. 102:10499-10504(2005) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBUNIT. - Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT. - Ref.12"Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
J. Med. Chem. 55:2894-2898(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT. - Ref.13"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
Med. Chem. Commun. 3:620-626(2012)Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
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).1 Publication
Manual assertion inferred by curator fromi
- Ref.9"Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation."
Gill H.S., Pfluegl G.M., Eisenberg D.
Biochemistry 41:9863-9872(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-478, ACTIVITY REGULATION, AMPYLATION AT TYR-406, SUBUNIT.
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT. - Ref.5"Inhibition of Mycobacterium tuberculosis glutamine synthetase as a novel antibiotic strategy against tuberculosis: demonstration of efficacy in vivo."
Harth G., Horwitz M.A.
Infect. Immun. 71:456-464(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION. - Ref.7"Adenylylation and catalytic properties of Mycobacterium tuberculosis glutamine synthetase expressed in Escherichia coli versus mycobacteria."
Mehta R., Pearson J.T., Mahajan S., Nath A., Hickey M.J., Sherman D.R., Atkins W.M.
J. Biol. Chem. 279:22477-22482(2004) [PubMed] [Europe PMC] [Abstract]Cited for: AMPYLATION AT TYR-406, MUTAGENESIS OF TYR-406, ACTIVITY REGULATION. - Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=0.5 mM for ATP1 Publication
Manual assertion based on experiment ini
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
- KM=2.7 mM for L-glutamate1 Publication
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
- KM=2.9 mM for L-glutamine1 Publication
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
- KM=10.8 mM for ammonium1 Publication
Manual assertion based on experiment ini
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
- KM=21.6 mM for L-glutamate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
- Vmax=110 µmol/min/mg enzyme1 Publication
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
pH dependencei
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).2 Publications
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT. - Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 133 | Magnesium 1Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 135 | Magnesium 2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 214 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 219 | Magnesium 2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 227 | Magnesium 2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 272 | L-glutamate; via carbonyl oxygenBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 276 | Magnesium 1; via pros nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 280 | ATPBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Binding sitei | 329 | L-glutamateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 335 | L-glutamateBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Binding sitei | 347 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 347 | L-glutamateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 352 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 361 | ATPBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 366 | Magnesium 1Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 368 | L-glutamateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion inferred by curator fromi
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 230 – 232 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
| 3 | |
| Nucleotide bindingi | 278 – 280 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion inferred by curator fromi
| 3 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- fibronectin binding Source: CAFA
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
- glutamate-ammonia ligase activity Source: MTBBASE
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "Cloning and expression of mycobacterial glutamine synthetase gene in Escherichia coli."
Singh J., Joshi M.C., Bhatnagar R.
Biochem. Biophys. Res. Commun. 317:634-638(2004) [PubMed] [Europe PMC] [Abstract] - "All four Mycobacterium tuberculosis glnA genes encode glutamine synthetase activities but only GlnA1 is abundantly expressed and essential for bacterial homeostasis."
Harth G., Maslesa-Galic S., Tullius M.V., Horwitz M.A.
Mol. Microbiol. 58:1157-1172(2005) [PubMed] [Europe PMC] [Abstract]
- metal ion binding Source: UniProtKB-KW
- zymogen binding Source: CAFAInferred from physical interactioni
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
GO - Biological processi
- glutamine biosynthetic process Source: MTBBASE
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Protection elicited by two glutamine auxotrophs of Mycobacterium tuberculosis and in vivo growth phenotypes of the four unique glutamine synthetase mutants in a murine model."
Lee S., Jeon B.Y., Bardarov S., Chen M., Morris S.L., Jacobs W.R. Jr.
Infect. Immun. 74:6491-6495(2006) [PubMed] [Europe PMC] [Abstract]
- nitrogen utilization Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- pathogenesis Source: MTBBASEInferred from mutant phenotypei
- Ref.6"Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs."
Tullius M.V., Harth G., Horwitz M.A.
Infect. Immun. 71:3927-3936(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.
- positive regulation of plasminogen activation Source: CAFAInferred from direct assayi
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Ligase |
| Biological process | Virulence |
| Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Glutamine synthetase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
Short name: GS1 Publication Manual assertion based on opinion ini
Alternative name(s): Glutamate--ammonia ligaseCurated Glutamine synthetase I betaCurated Short name: GSI betaCurated |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:glnA11 Publication Manual assertion based on opinion ini
Synonyms:glnA Ordered Locus Names:Rv2220 ORF Names:MTCY190.31, MTCY427.01 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83332 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium tuberculosis |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Mycobacterium tuberculosis strain H37Rv genome database More...TubercuListi | Rv2220 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
- Cytoplasm 1 Publication
Manual assertion inferred by curator fromi
- Ref.1"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."
Harth G., Horwitz M.A.
J. Biol. Chem. 272:22728-22735(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
GO - Cellular componenti
- cell wall Source: MTBBASEInferred from high throughput direct assayi
- "Proteomic definition of the cell wall of Mycobacterium tuberculosis."
Wolfe L.M., Mahaffey S.B., Kruh N.A., Dobos K.M.
J. Proteome Res. 9:5816-5826(2010) [PubMed] [Europe PMC] [Abstract]
- cytoplasm Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- cytosol Source: MTBBASEInferred from high throughput direct assayi
- "Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling."
Mawuenyega K.G., Forst C.V., Dobos K.M., Belisle J.T., Chen J., Bradbury E.M., Bradbury A.R., Chen X.
Mol. Biol. Cell 16:396-404(2005) [PubMed] [Europe PMC] [Abstract]
- extracellular region Source: CAFAInferred from direct assayi
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
- membrane Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- plasma membrane Source: MTBBASEInferred from high throughput direct assayi
- "Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain."
Gu S., Chen J., Dobos K.M., Bradbury E.M., Belisle J.T., Chen X.
Mol. Cell Proteomics 2:1284-1296(2003) [PubMed] [Europe PMC] [Abstract] - "Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling."
Mawuenyega K.G., Forst C.V., Dobos K.M., Belisle J.T., Chen J., Bradbury E.M., Bradbury A.R., Chen X.
Mol. Biol. Cell 16:396-404(2005) [PubMed] [Europe PMC] [Abstract]
Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
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.1 Publication
Manual assertion based on experiment ini
- Ref.6"Glutamine synthetase GlnA1 is essential for growth of Mycobacterium tuberculosis in human THP-1 macrophages and guinea pigs."
Tullius M.V., Harth G., Horwitz M.A.
Infect. Immun. 71:3927-3936(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 406 | Y → F: Unable to be adenylylated. 1 Publication Manual assertion based on experiment ini
| 1 |
Miscellaneous databases
Pathogen-Host Interaction database More...PHI-basei | PHI:7587 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04272, Citric acid |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000153246 | 2 – 478 | Glutamine synthetaseAdd BLAST | 477 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 406 | O-AMP-tyrosine2 Publications Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P9WN39 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Repressed by phosphorothioate modified antisense oligodeoxyribonucleotides (PS-ODNs), which acts against the mRNA of glutamine synthetase.1 Publication
Manual assertion based on experiment ini
- Ref.4"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."
Harth G., Zamecnik P.C., Tang J.Y., Tabatadze D., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 97:418-423(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Oligomer of 12 subunits arranged in the form of two hexagons.
3 PublicationsManual assertion inferred by curator fromi
- Ref.11"Structural basis for the inhibition of Mycobacterium tuberculosis glutamine synthetase by novel ATP-competitive inhibitors."
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.
J. Mol. Biol. 393:504-513(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT. - Ref.12"Trisubstituted imidazoles as Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
J. Med. Chem. 55:2894-2898(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT. - Ref.13"Synthesis, biological evaluation and X-Ray crystallographic studies of imidazo(1,2-A)pyridine-based Mycobacterium tuberculosis glutamine synthetase inhibitors."
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.
Med. Chem. Commun. 3:620-626(2012)Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-478 IN COMPLEX WITH SUBSTRATE ANALOG; ATP ANALOG AND 2 MAGNESIUM IONS, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.3"Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity."
Harth G., Clemens D.L., Horwitz M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:9342-9346(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT. - Ref.9"Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation."
Gill H.S., Pfluegl G.M., Eisenberg D.
Biochemistry 41:9863-9872(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-478, ACTIVITY REGULATION, AMPYLATION AT TYR-406, SUBUNIT. - Ref.10"Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights."
Krajewski W.W., Jones T.A., Mowbray S.L.
Proc. Natl. Acad. Sci. U.S.A. 102:10499-10504(2005) [PubMed] [Europe PMC] [Abstract]Cited for: 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, SUBUNIT.
GO - Molecular functioni
- fibronectin binding Source: CAFAInferred from physical interactioni
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
- zymogen binding Source: CAFAInferred from physical interactioni
- "Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis."
Xolalpa W., Vallecillo A.J., Lara M., Mendoza-Hernandez G., Comini M., Spallek R., Singh M., Espitia C.
Proteomics 7:3332-3341(2007) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
STRING: functional protein association networks More...STRINGi | 83332.Rv2220 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 6 – 15 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 20 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 28 – 30 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 32 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 39 – 41 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 44 – 48 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 51 – 54 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 55 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 58 – 62 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 64 – 66 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 68 – 73 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 75 – 77 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 88 – 96 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 98 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 108 – 122 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| Beta strandi | 126 – 134 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 136 – 146 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 151 – 156 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 161 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 186 – 188 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 190 – 192 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 196 – 208 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 213 – 218 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 222 – 224 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 225 – 230 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 235 – 255 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| Beta strandi | 259 – 261 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 275 – 283 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 286 – 290 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 295 – 297 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 300 – 320 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
| Helixi | 326 – 329 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 330 – 333 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 334 – 336 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 338 – 340 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 342 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 349 – 353 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 360 – 362 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 365 – 367 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 372 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 376 – 392 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| Helixi | 405 – 407 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 410 – 414 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 423 – 432 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 435 – 438 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 439 – 441 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 445 – 458 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| Helixi | 460 – 464 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 469 – 475 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P9WN39 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 271 – 272 | L-glutamate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion inferred by curator fromi
| 2 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the glutamine synthetase family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0174, Bacteria |
KEGG Orthology (KO) More...KOi | K01915 |
Identification of Orthologs from Complete Genome Data More...OMAi | PHPHEFE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P9WN39 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.20.70, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR008147, Gln_synt_b-grasp IPR036651, Gln_synt_N IPR014746, Gln_synth/guanido_kin_cat_dom IPR008146, Gln_synth_cat_dom IPR027303, Gln_synth_gly_rich_site IPR004809, Gln_synth_I IPR001637, Gln_synth_I_adenylation_site IPR027302, Gln_synth_N_conserv_site |
Pfam protein domain database More...Pfami | View protein in Pfam PF00120, Gln-synt_C, 1 hit PF03951, Gln-synt_N, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01230, Gln-synt_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54368, SSF54368, 1 hit SSF55931, SSF55931, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00653, GlnA, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00180, GLNA_1, 1 hit PS00182, GLNA_ADENYLATION, 1 hit PS00181, GLNA_ATP, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P9WN39-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MTEKTPDDVF KLAKDEKVEY VDVRFCDLPG IMQHFTIPAS AFDKSVFDDG
60 70 80 90 100
LAFDGSSIRG FQSIHESDML LLPDPETARI DPFRAAKTLN INFFVHDPFT
110 120 130 140 150
LEPYSRDPRN IARKAENYLI STGIADTAYF GAEAEFYIFD SVSFDSRANG
160 170 180 190 200
SFYEVDAISG WWNTGAATEA DGSPNRGYKV RHKGGYFPVA PNDQYVDLRD
210 220 230 240 250
KMLTNLINSG FILEKGHHEV GSGGQAEINY QFNSLLHAAD DMQLYKYIIK
260 270 280 290 300
NTAWQNGKTV TFMPKPLFGD NGSGMHCHQS LWKDGAPLMY DETGYAGLSD
310 320 330 340 350
TARHYIGGLL HHAPSLLAFT NPTVNSYKRL VPGYEAPINL VYSQRNRSAC
360 370 380 390 400
VRIPITGSNP KAKRLEFRSP DSSGNPYLAF SAMLMAGLDG IKNKIEPQAP
410 420 430 440 450
VDKDLYELPP EEAASIPQTP TQLSDVIDRL EADHEYLTEG GVFTNDLIET
460 470
WISFKRENEI EPVNIRPHPY EFALYYDV
Length:478
Mass (Da):53,570
Last modified:April 16, 2014 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i576E30073484136D
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U87280 Genomic DNA Translation: AAB70038.1 AL123456 Genomic DNA Translation: CCP44998.1 |
Protein sequence database of the Protein Information Resource More...PIRi | H70775 |
NCBI Reference Sequences More...RefSeqi | NP_216736.1, NC_000962.3 WP_003411475.1, NZ_NVQJ01000008.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | CCP44998; CCP44998; Rv2220 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23491584 888383 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | mtu:Rv2220 mtv:RVBD_2220 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WN39 | Glutamine synthetase | 478 | UniRef100_P0A591 | |||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| +7 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WN39 | Glutamine synthetase | 478 | UniRef90_P0A591 | |||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 478 | |||||
| +77 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P9WN39 | Glutamine synthetase | 478 | UniRef50_P0A591 | |||
| Glutamine synthetase | 478 | |||||
| Glutamine synthetase | 474 | |||||
| Glutamine synthetase | 469 | |||||
| Glutamine synthetase | 469 | |||||
| +5858 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U87280 Genomic DNA Translation: AAB70038.1 AL123456 Genomic DNA Translation: CCP44998.1 |
| PIRi | H70775 |
| RefSeqi | NP_216736.1, NC_000962.3 WP_003411475.1, NZ_NVQJ01000008.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1HTO | X-ray | 2.40 | 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 | [»] | |
| 1HTQ | X-ray | 2.40 | 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 | [»] | |
| 2BVC | X-ray | 2.10 | A/B/C/D/E/F | 2-478 | [»] | |
| 2WGS | X-ray | 2.55 | A/B/C/D/E/F/G/H/I/J/K/L | 2-478 | [»] | |
| 2WHI | X-ray | 2.20 | A/B/C/D/E/F | 2-478 | [»] | |
| 3ZXR | X-ray | 2.15 | A/B/C/D/E/F | 2-478 | [»] | |
| 3ZXV | X-ray | 2.26 | A/B/C/D/E/F | 2-478 | [»] | |
| 4ACF | X-ray | 2.00 | A/B/C/D/E/F | 2-478 | [»] | |
| 4XYC | X-ray | 3.30 | 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 | [»] | |
| SMRi | P9WN39 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| STRINGi | 83332.Rv2220 |
Chemistry databases
| DrugBanki | DB04272, Citric acid |
Proteomic databases
| PaxDbi | P9WN39 |
Genome annotation databases
| EnsemblBacteriai | CCP44998; CCP44998; Rv2220 |
| GeneIDi | 23491584 888383 |
| KEGGi | mtu:Rv2220 mtv:RVBD_2220 |
Organism-specific databases
| TubercuListi | Rv2220 |
Phylogenomic databases
| eggNOGi | COG0174, Bacteria |
| KOi | K01915 |
| OMAi | PHPHEFE |
| PhylomeDBi | P9WN39 |
Miscellaneous databases
| PHI-basei | PHI:7587 |
Family and domain databases
| Gene3Di | 3.10.20.70, 1 hit |
| InterProi | View protein in InterPro IPR008147, Gln_synt_b-grasp IPR036651, Gln_synt_N IPR014746, Gln_synth/guanido_kin_cat_dom IPR008146, Gln_synth_cat_dom IPR027303, Gln_synth_gly_rich_site IPR004809, Gln_synth_I IPR001637, Gln_synth_I_adenylation_site IPR027302, Gln_synth_N_conserv_site |
| Pfami | View protein in Pfam PF00120, Gln-synt_C, 1 hit PF03951, Gln-synt_N, 1 hit |
| SMARTi | View protein in SMART SM01230, Gln-synt_C, 1 hit |
| SUPFAMi | SSF54368, SSF54368, 1 hit SSF55931, SSF55931, 1 hit |
| TIGRFAMsi | TIGR00653, GlnA, 1 hit |
| PROSITEi | View protein in PROSITE PS00180, GLNA_1, 1 hit PS00182, GLNA_ADENYLATION, 1 hit PS00181, GLNA_ATP, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | GLN1B_MYCTU | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P9WN39Primary (citable) accession number: P9WN39 Secondary accession number(s): L0TAJ3, P0A590, Q10377 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
| Last sequence update: | April 16, 2014 | |
| Last modified: | October 7, 2020 | |
| This is version 41 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
