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Literature summary for 2.3.1.265 extracted from
- Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria (2017), Biochim. Biophys. Acta, 1862, 1355-1367 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E200A | site-directed mutagenesis, inactive enzyme mutant | Mycobacterium tuberculosis |
| E200A | site-directed mutagenesis, inactive enzyme mutant | Mycolicibacterium smegmatis |
| H126A | site-directed mutagenesis, inactive enzyme mutant | Mycobacterium tuberculosis |
| H126A | site-directed mutagenesis, inactive enzyme mutant | Mycolicibacterium smegmatis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inner membrane | - |
Mycobacterium tuberculosis | - |
- |
| inner membrane | - |
Mycolicibacterium smegmatis | - |
- |
| additional information | the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins | Mycobacterium tuberculosis | - |
- |
| additional information | the enzyme shows a highly polarized electrostatic surface potential, which seems essential for the correct orientation of the enzyme to the cytosolic side of the plasma membrane, a key characteristic for peripheral and monotopic membrane proteins | Mycolicibacterium smegmatis | - |
- |
| plasma membrane | - |
Mycobacterium tuberculosis | 5886 | - |
| plasma membrane | - |
Mycolicibacterium smegmatis | 5886 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? |  |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis ATCC 700084 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis H37Rv | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis ATCC 25618 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis mc(2)155 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis ATCC 700084 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis H37Rv | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycobacterium tuberculosis ATCC 25618 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | Mycolicibacterium smegmatis mc(2)155 | - |
CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mycobacterium tuberculosis | P9WMB5 | - |
- |
| Mycobacterium tuberculosis ATCC 25618 | P9WMB5 | - |
- |
| Mycobacterium tuberculosis H37Rv | P9WMB5 | - |
- |
| Mycolicibacterium smegmatis | A0QWG5 | i.e. Mycobacterium smegmatis | - |
| Mycolicibacterium smegmatis ATCC 700084 | A0QWG5 | i.e. Mycobacterium smegmatis | - |
| Mycolicibacterium smegmatis mc(2)155 | A0QWG5 | i.e. Mycobacterium smegmatis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycobacterium tuberculosis | ? | - |
- |
|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycolicibacterium smegmatis | ? | - |
- |
|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycolicibacterium smegmatis ATCC 700084 | ? | - |
- |
|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycobacterium tuberculosis H37Rv | ? | - |
- |
|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycobacterium tuberculosis ATCC 25618 | ? | - |
- |
|
| additional information | the active site of PatA comprises a catalytic triad consisting of the acceptor O6 atom of Manp, the imidazole ring of His126, and the carboxylate group of Glu200. In the proposed reaction mechanism, His126 acts initially as a general base to deprotonate the acceptor hydroxyl group, facilitating the nucleophilic attack on the thioester bond of palmitoyl-CoA. The carboxylic group of Glu200 contributes to the correct positioning of the imidazole ring of His126 and is involved in a charge relay system that increases the nucleophilicity of the acceptor Manp hydroxyl and modulates the pKa of His126 to act as a base in the first step and as an acid in the second step, providing protonic assistance to the departing CoA leaving group | Mycolicibacterium smegmatis mc(2)155 | ? | - |
- |
|
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis ATCC 700084 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis H37Rv | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis ATCC 25618 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis mc(2)155 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis ATCC 700084 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis H37Rv | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycobacterium tuberculosis ATCC 25618 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
| palmitoyl-CoA + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol | - |
Mycolicibacterium smegmatis mc(2)155 | CoA + 2-O-(6-O-palmitoyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis | Mycobacterium tuberculosis |
| More | enzyme PatA displays an alpha/beta architecture, with an acyl-binding pocket that runs along the enzyme's core and perpendicular to a long groove that contains the reaction center. The crystal structure provides unique insight into membrane association, acyl-donor recognition and catalysis | Mycolicibacterium smegmatis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acyltransferase PatA | - |
Mycobacterium tuberculosis |
| acyltransferase PatA | - |
Mycolicibacterium smegmatis |
| MSMEG_2934 | - |
Mycolicibacterium smegmatis |
| PatA | ambiguous | Mycobacterium tuberculosis |
| PatA | ambiguous | Mycolicibacterium smegmatis |
| phosphatidylinositol mannoside acyltransferase | UniProt | Mycobacterium tuberculosis |
| phosphatidylinositol mannoside acyltransferase | UniProt | Mycolicibacterium smegmatis |
| PIM acyltransferase | - |
Mycobacterium tuberculosis |
| PIM acyltransferase | - |
Mycolicibacterium smegmatis |
| Rv2611c | - |
Mycobacterium tuberculosis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis | Mycolicibacterium smegmatis |
| malfunction | disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis | Mycobacterium tuberculosis |
| metabolism | the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit | Mycobacterium tuberculosis |
| metabolism | the enzyme is part of the PIM biosynthetic pathway in mycobacteria, detailed overview. Ac1PIM6 and Ac2PIM6 seems to be located in the outer leaflet of the inner membrane. Palmitic acid (C16:0) and 10-methyloctadecanoic acid (i.e. tuberculostearic acid) are the major fatty acid constituents of the biochemically isolated inner membrane. PIM2 is composed of two mannose (Man) residues attached to positions 2 and 6 of the myo-inositol ring of phosphatidyl-1D-myo-inositol (PI), whereas PIM6 is composed of a pentamannosyl group, t-alpha-Man(1->2)-alpha-Man(1->2)-alpha-Man(1->6)-alpha-Man(1->6)-alpha-Man(1->, attached to position 6 of the myo-inositol ring), in addition to the Manp residue present at position 2. The triacylated forms of PIM2 and PIM6 (Ac1PIM2 and Ac1PIM6) show major acyl forms containing two palmitic acid residues (C16) and one tuberculostearic acid residue (10-methyloctadecanoate, C19), where one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol, and two fatty acyl chains are located on the glycerol moiety. The tetraacylated forms, Ac2PIM2 and Ac2PIM6, are present predominantly as two populations bearing either three C16/one C19 or two C16/two C19. Two fatty acyl chains are located on the glycerol moiety, one fatty acyl chain is linked to the Manp residue attached to position 2 of myo-inositol and one fatty acyl chain is attached to position 3 of the myo-inositol unit | Mycolicibacterium smegmatis |
| physiological function | the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2 | Mycobacterium tuberculosis |
| physiological function | the PIM acyltransferase (PatA) is an essential membrane associated acyltransferase, it transfers a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to 2-position of inositol in PIM1/PIM2 resulting in Ac1PIM1 and Ac1PIM2 | Mycolicibacterium smegmatis |
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