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Literature summary extracted from

  • Sancho-Vaello, E.; Albesa-Jove, D.; Rodrigo-Unzueta, A.; Guerin, M.
    Structural basis of phosphatidyl-myo-inositol mannosides biosynthesis in mycobacteria (2017), Biochim. Biophys. Acta, 1862, 1355-1367 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.265 E200A site-directed mutagenesis, inactive enzyme mutant Mycobacterium tuberculosis
2.3.1.265 E200A site-directed mutagenesis, inactive enzyme mutant Mycolicibacterium smegmatis
2.3.1.265 H126A site-directed mutagenesis, inactive enzyme mutant Mycobacterium tuberculosis
2.3.1.265 H126A site-directed mutagenesis, inactive enzyme mutant Mycolicibacterium smegmatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.265 inner membrane
-
 Mycobacterium tuberculosis
-
-
2.3.1.265 inner membrane
-
 Mycolicibacterium smegmatis
-
-
2.3.1.265 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
-
-
2.3.1.265 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
-
-
2.3.1.265 plasma membrane
-
 Mycobacterium tuberculosis 5886
-
2.3.1.265 plasma membrane
-
 Mycolicibacterium smegmatis 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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

EC Number Organism UniProt Comment Textmining
2.3.1.265 Mycobacterium tuberculosis P9WMB5
-
-
2.3.1.265 Mycobacterium tuberculosis ATCC 25618 P9WMB5
-
-
2.3.1.265 Mycobacterium tuberculosis H37Rv P9WMB5
-
-
2.3.1.265 Mycolicibacterium smegmatis A0QWG5 i.e. Mycobacterium smegmatis
-
2.3.1.265 Mycolicibacterium smegmatis ATCC 700084 A0QWG5 i.e. Mycobacterium smegmatis
-
2.3.1.265 Mycolicibacterium smegmatis mc(2)155 A0QWG5 i.e. Mycobacterium smegmatis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.265 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 ?
-
-
2.3.1.265 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 ?
-
-
2.3.1.265 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 ?
-
-
2.3.1.265 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 ?
-
-
2.3.1.265 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 ?
-
-
2.3.1.265 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 ?
-
-
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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
-
 ?
2.3.1.265 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

EC Number Subunits Comment Organism
2.3.1.265 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
2.3.1.265 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

EC Number Synonyms Comment Organism
2.3.1.265 acyltransferase PatA
-
 Mycobacterium tuberculosis
2.3.1.265 acyltransferase PatA
-
 Mycolicibacterium smegmatis
2.3.1.265 MSMEG_2934
-
 Mycolicibacterium smegmatis
2.3.1.265 PatA ambiguous Mycobacterium tuberculosis
2.3.1.265 PatA ambiguous Mycolicibacterium smegmatis
2.3.1.265 phosphatidylinositol mannoside acyltransferase UniProt Mycobacterium tuberculosis
2.3.1.265 phosphatidylinositol mannoside acyltransferase UniProt Mycolicibacterium smegmatis
2.3.1.265 PIM acyltransferase
-
 Mycobacterium tuberculosis
2.3.1.265 PIM acyltransferase
-
 Mycolicibacterium smegmatis
2.3.1.265 Rv2611c
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.265 malfunction disruption of gene MSMEG_2934 severely affects the groth of Mycobacterium smegmatis Mycolicibacterium smegmatis
2.3.1.265 malfunction disruption of gene Rv2611c abolishes the growth of Mycobacterium tuberculosis Mycobacterium tuberculosis
2.3.1.265 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
2.3.1.265 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
2.3.1.265 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
2.3.1.265 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