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CAZyme Information: MGYG000003135_00793

You are here: Home > Sequence: MGYG000003135_00793

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Cutibacterium granulosum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Cutibacterium; Cutibacterium granulosum
CAZyme ID MGYG000003135_00793
CAZy Family GT4
CAZyme Description Phosphatidyl-myo-inositol mannosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
432 MGYG000003135_3|CGC1 46380.73 10.1307
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003135 2072889 MAG United States North America
Gene Location Start: 161380;  End: 162678  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003135_00793.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 239 377 1.9e-22 0.90625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 8.97e-37 38 407 1 365
phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
COG0438 RfaB 1.18e-26 38 411 2 378
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam13692 Glyco_trans_1_4 1.51e-18 241 360 1 122
Glycosyl transferases group 1.
pfam00534 Glycos_transf_1 2.24e-15 240 360 1 128
Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
cd03798 GT4_WlbH-like 2.96e-14 51 410 14 376
Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
SNV35659.1 0.0 1 432 1 432
AZZ39361.1 2.75e-156 15 417 26 424
AZZ42215.1 6.36e-155 27 417 38 424
ALN16071.1 7.85e-155 22 417 27 421
AFV89465.1 7.85e-155 22 417 27 421

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2GEJ_A 1.60e-73 35 407 19 380
CrystalStructure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155]
4N9W_A 2.03e-73 37 407 5 364
Crystalstructure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155]
3FRO_A 3.03e-11 243 412 253 432
Crystalstructure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_B Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_C Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi]
2BIS_A 3.04e-11 243 412 254 433
Structureof glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi],2BIS_B Structure of glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi],2BIS_C Structure of glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi]
3L01_A 2.16e-10 243 407 253 427
ChainA, GlgA glycogen synthase [Pyrococcus abyssi],3L01_B Chain B, GlgA glycogen synthase [Pyrococcus abyssi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D7GDZ9 3.24e-106 37 407 1 360
Phosphatidyl-myo-inositol mannosyltransferase OS=Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1) OX=754252 GN=pimA PE=1 SV=1
P9WMZ5 7.50e-77 37 407 1 364
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=pimA PE=1 SV=1
P9WMZ4 7.50e-77 37 407 1 364
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=pimA PE=3 SV=1
Q7TY88 7.50e-77 37 407 1 364
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=pimA PE=3 SV=1
A0QWG6 9.94e-73 37 407 1 360
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=pimA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000002 0.000020 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003135_00793.