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Information on EC 2.4.1.346 - phosphatidyl-myo-inositol dimannoside synthase
for references in articles please use BRENDA:EC2.4.1.346
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.346 phosphatidyl-myo-inositol dimannoside synthase
IUBMB Comments
Requires Mg2+. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.4.1.346
- mycobacterium
- tuberculosis
- mannosides
- corynebacterium
-
lipomannan
- glycolipids
- lipoarabinomannan
- glutamicum
- envelope
-
lipoglycans
- smegmatis
-
mannosylated
- lm
Reaction Schemes
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Synonyms
pimb', ncgl2106, rv2188c, mannosyltransferase pimb, rv0557, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.4.1.57
-
-
formerly, part transferred
-
GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase
guanosine diphosphomannose-phosphatidyl-inositol alpha-mannosyltransferase
-
-
ambiguous
-
mannoslytransferase PimB'
mannosyltransferase PimB
-
-
-
-
MgtA
MSMEG_4253
NCgl2106
PimB
pimB'
Rv0557
Rv2188c
GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase
-
GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase
-
-
PimB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol = GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(2)
-
-
-
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol = GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
(1)
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosphatidylinositol mannoside biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
GDP-alpha-D-mannose:2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol 6-alpha-D-mannosyltransferase (configuration-retaining)
Requires Mg2+. The enzyme, found in Corynebacteriales, is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIMs).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannopyranose + phosphatidyl-myo-inositol
GDP + ?
Substrates: attaches mannosyl selectively to the 6-OH of the inositol moiety
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-Man + phosphatidyl-myo-inositol
?
Substrates: assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH
Products: -
Products: -
?
GDP-Man + phosphatidyl-myo-inositol
?
Substrates: assay at pH 7.5, 37°C, reaction stopped with CHCl3/CH3OH
Products: -
Products: -
?
additional information
?
-
-
Substrates: PimB attaches the mannosyl moiety selectively to the 6-OH of the inositol moiety of phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
Substrates: PimB attaches the mannosyl moiety selectively to the 6-OH of the inositol moiety of phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
Substrates: PimB attaches the mannosyl moiety selectively to the 6-OH of the inositol moiety of phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme accepts 1,2-di-O-C16/C18:1-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-glycerol as equally efficient substrate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme accepts 1,2-di-O-C16/C18:1-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-glycerol as equally efficient substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme accepts 1,2-di-O-C16/C18:1-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-glycerol as equally efficient substrate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme accepts 1,2-di-O-C16/C18:1-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-glycerol as equally efficient substrate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme accepts 1,2-di-O-C16/C18:1-(1->4)-(alpha-D-glucopyranosyluronic acid)-(1->3)-glycerol as equally efficient substrate
Products: -
Products: -
?
additional information
?
-
Substrates: PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
Substrates: PimB specifically catalyzes the transfer of a mannopyranosyl residue to the 6-position of the myo-inositol ring of phosphatidylinositol
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-(6-O-acyl-alpha-D-mannosyl)-1-phosphatidyl-1D-myo-inositol
GDP + 2-O-(6-O-acyl-alpha-D-mannosyl)-6-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 2-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
GDP + 2,6-di-O-alpha-D-mannosyl-1-phosphatidyl-1D-myo-inositol
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-mannosamine
does not bind directly or efficiently to the active site of the enzyme, but interferes indirectly with the enzymes access to GDP-Man
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Analysis of a new mannosyltransferase required for the synthesis of phosphatidylinositol mannosides and lipoarbinomannan reveals two lipomannan pools in corynebacterineae.
Tuberculosis
Characterization of the Corynebacterium glutamiucm{Delta}pimB'{Delta}mgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologoues Rv2188c and Rv0557 in glycolipid biosynthesis.
Tuberculosis
Inactivation of Mycobacterium tuberculosis mannosyltransferase pimB reduces cell wall lipoarabinomannan and lipomannan content and increases the rate of bacterial-induced human macrophage cell death.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
disruption of gene NCgl2106 results in a mutant devoid of monoacylated phosphatidyl-myo-inositol dimannoside (Ac1PIM2) resulting in the accumulation of monoacylated phosphatidyl-myo-inositol monomannoside Ac1PIM1 and cessation of phosphatidyl-myo-inositol based lipomannan and lipoarabinomannan biosynthesis. The mutant syntheses a single novel lipoglycan possessing an alpha-D-glucopyranosyluronic acid-(1->3)-glycerol (GlcAGroAc2) based anchor which is then further glycosylated by 822 mannose residues, with Man1220GlcAGroAC2 molecular species being the most abundant
physiological function
characterization of a PimB MgtA double deletion mutant. Gene product of Rv2188c acts as an Ac1PIM1:mannosyltransferase PimB and the product of Rv0557 acts as a GlcAGroAc2:mannosyltransferase MgtA
physiological function
both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB'
physiological function
-
disruption of gene NCgl2106 results in a mutant devoid of monoacylated phosphatidyl-myo-inositol dimannoside (Ac1PIM2) resulting in the accumulation of monoacylated phosphatidyl-myo-inositol monomannoside Ac1PIM1 and cessation of phosphatidyl-myo-inositol based lipomannan and lipoarabinomannan biosynthesis. The mutant syntheses a single novel lipoglycan possessing an alpha-D-glucopyranosyluronic acid-(1->3)-glycerol (GlcAGroAc2) based anchor which is then further glycosylated by 822 mannose residues, with Man1220GlcAGroAC2 molecular species being the most abundant
-
physiological function
-
both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol as a lipid acceptor. PimA specifically catalyzes the transfer of a mannopyranosyl residue to the 2-position of the myo-inositol ring of phosphatidylinositol, whereas PimB' exclusively transfers to the 6-position. PimB' can catalyze the transfer of a mannopyranosyl residue onto the phosphatidylinositol-monomannoside (PIM1) product of PimA, while PimA is unable in vitro to transfer mannopyranosyl onto the PIM1 product of PimB'
-
physiological function
-
characterization of a PimB MgtA double deletion mutant. Gene product of Rv2188c acts as an Ac1PIM1:mannosyltransferase PimB and the product of Rv0557 acts as a GlcAGroAc2:mannosyltransferase MgtA
-
Show AA Sequence and Transmembrane Helices (1134 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of mannosyltransferase PimB in complex with nucleotide to a resolution of 2.0 A. Both the nucleotide conformation as well as the structural framework of the active site display flexibility
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D13A
D13N
D13Y
E290D
E290N
E290Q
G123P
G20W
G291S
H118S
H120S
I21A
I21S
K211Q
N12A
Q22A
R206S
R210S
S205G
G123P
86.6% of wild type activity (blank has 0.5% activity)
H120S
81.2% of wild type activity (blank has 0.5% activity)
S205G
119.6% of wild type activity (blank has 0.5% activity)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guerin, M.E.; Kaur, D.; Somashekar, B.S.; Gibbs, S.; Gest, P.; Chatterjee, D.; Brennan, P.J.; Jackson, M.
New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB is an essential enzyme of Mycobacterium smegmatis
J. Biol. Chem.
284
25687-25696
2009
Mycolicibacterium smegmatis (A0R043), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R043)
brenda
Batt, S.M.; Jabeen, T.; Mishra, A.K.; Veerapen, N.; Krumbach, K.; Eggeling, L.; Besra, G.S.; Fuetterer, K.
Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB
J. Biol. Chem.
285
37741-37752
2010
Corynebacterium glutamicum, Corynebacterium glutamicum (Q8NNK8), Corynebacterium glutamicum DSM 20300 (Q8NNK8)
brenda
Mishra, A.; Klein, C.; Gurcha, S.; Alderwick, L.; Babu, P.; Hitchen, P.; Morris, H.; Dell, A.; Besra, G.; Eggeling, L.
Structural characterization and functional properties of a novel lipomannan variant isolated from a Corynebacterium glutamicum pimB' mutant
Antonie van Leeuwenhoek
94
277-287
2008
Corynebacterium glutamicum (Q8NNK8), Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20300 (Q8NNK8)
brenda
Mishra, A.K.; Batt, S.; Krumbach, K.; Eggeling, L.; Besra, G.S.
Characterization of the Corynebacterium glutamicum deltapimB deltamgtA double deletion mutant and the role of Mycobacterium tuberculosis orthologues Rv2188c and Rv0557 in glycolipid biosynthesis
J. Bacteriol.
191
4465-4472
2009
Mycobacterium tuberculosis (P9WMY5), Mycobacterium tuberculosis (P9WMZ3), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WMY5), Mycobacterium tuberculosis ATCC 25618 (P9WMZ3)
brenda
Schaeffer, M.L.; Khoo, K.H.; Besra, G.S.; Chatterjee, D.; Brennan, P.J.; Belisle, J.T.; Inamine, J.M.
The pimB gene of Mycobacterium tuberculosis encodes a mannosyltransferase involved in lipoarabinomannan biosynthesis
J. Biol. Chem.
274
31625-31631
1999
Mycobacterium tuberculosis (P9WMY5), Mycobacterium tuberculosis H37Rv (P9WMY5)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.346)
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