Family Search for PF11896 (GlgE_dom_N_S)
April 2024: GapMind for amino acid biosynthesis has been updated to include newly-discovered enzymes and comparative genomics predictions (see details)
Running HMMer for PF11896
PF11896 hits 44 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.
GLGE1_STRCO / Q9L1K2 Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1; GMPMT 1; (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 1; EC 2.4.99.16 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see paper)
Q9L1K2 starch synthase (maltosyl-transferring) (EC 2.4.99.16) from Streptomyces coelicolor (see 3 papers)
Aligns to 19:206 / 675 (27.9%), covers 100.0% of PF11896, 214.7 bits
- function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE- catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
catalytic activity: [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate (RHEA:42692)
subunit: Homodimer.
F2R411 starch synthase (maltosyl-transferring) (EC 2.4.99.16) from Streptomyces venezuelae (see paper)
Aligns to 33:221 / 692 (27.3%), covers 100.0% of PF11896, 214.3 bits
GLGE2_STRCO / Q9KY04 Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 2; GMPMT 2; (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase 2; EC 2.4.99.16 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see paper)
Aligns to 10:197 / 669 (28.1%), covers 100.0% of PF11896, 213.6 bits
- function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE- catalyzed polymerization with M1P. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
catalytic activity: [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate (RHEA:42692)
subunit: Homodimer.
GLGE_MYCS2 / Q9RP48 Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase; GMPMT; (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase; EC 2.4.99.16 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see 3 papers)
Q9RP48 starch synthase (maltosyl-transferring) (EC 2.4.99.16) from Mycolicibacterium smegmatis (see paper)
Aligns to 8:222 / 697 (30.8%), covers 100.0% of PF11896, 187.3 bits
- function: Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is also able to catalyze the reverse reaction in vitro. Cannot use glucose 1-phosphate as substrate. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
catalytic activity: [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate (RHEA:42692)
subunit: Homodimer.
disruption phenotype: Cells lacking this gene display M1P accumulation and trehalose sensitivity. These phenotypes are suppressed in mutants lacking both glgE and treS or both glgE and mak. Deletion of glgE does not increase glycogen content.
glgE / P9WQ17 starch synthase (maltosyl-transferring) monomer (EC 2.4.99.16) from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
GLGE_MYCTU / P9WQ17 Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase; GMPMT; (1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase; (1->4)-alpha-D-glucan:phosphate alpha-D-maltosyltransferase; EC 2.4.99.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
P9WQ17 starch synthase (maltosyl-transferring) (EC 2.4.99.16) from Mycobacterium tuberculosis (see 2 papers)
Aligns to 16:226 / 701 (30.1%), covers 100.0% of PF11896, 181.9 bits
- function: Essential maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)- glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP5 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Exhibits an alpha-retaining catalytic mechanism. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.
catalytic activity: [(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate = [(1->4)-alpha-D-glucosyl](n+2) + phosphate (RHEA:42692)
subunit: Homodimer.
disruption phenotype: GlgE inactivation causes rapid death of M.tuberculosis in vitro and in mice through a self-poisoning accumulation of maltose 1-phosphate, driven by a self-amplifying feedback stress response.
Or search for genetic data about PF11896 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory