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CAZyme Information: MGYG000003806_00582

You are here: Home > Sequence: MGYG000003806_00582

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
Lineage Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium;
CAZyme ID MGYG000003806_00582
CAZy Family GT4
CAZyme Description GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000003806_10|CGC2 42105.08 6.3448
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003806 2539854 MAG Canada North America
Gene Location Start: 37115;  End: 38275  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 193 339 5.1e-31 0.8875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 2.27e-60 3 372 1 366
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 6.74e-45 5 372 4 375
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam13692 Glyco_trans_1_4 5.69e-33 193 339 1 138
Glycosyl transferases group 1.
cd03807 GT4_WbnK-like 3.22e-31 122 363 119 353
Shigella dysenteriae WbnK and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
pfam00534 Glycos_transf_1 1.67e-30 194 353 3 158
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACP33286.1 2.28e-254 1 386 1 387
QQU92599.1 2.28e-254 1 386 1 387
QQU94539.1 4.59e-254 1 386 1 387
QPS59308.1 2.94e-220 1 375 1 376
SQH99384.1 2.94e-220 1 375 1 376

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3OKA_A 8.17e-154 3 374 6 379
Crystalstructure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum]
3OKC_A 1.28e-153 3 374 6 379
Crystalstructure of Corynebacterium glutamicum PimB' bound to GDP (orthorhombic crystal form) [Corynebacterium glutamicum],3OKP_A Crystal structure of Corynebacterium glutamicum PimB' bound to GDP-Man (orthorhombic crystal form) [Corynebacterium glutamicum]
4N9W_A 2.91e-16 16 376 19 369
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]
2GEJ_A 3.19e-16 16 376 35 385
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]
3C4Q_A 2.13e-14 131 367 159 398
Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8NNK8 4.48e-153 3 374 6 379
GDP-mannose-dependent monoacylated alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=pimB PE=1 SV=1
A0R043 4.14e-124 5 371 2 373
GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=pimB PE=1 SV=1
P9WMZ3 1.35e-115 1 374 1 381
GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=pimB PE=1 SV=1
P9WMZ2 1.35e-115 1 374 1 381
GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=pimB PE=3 SV=1
D5UJ42 4.48e-17 126 370 184 435
D-inositol 3-phosphate glycosyltransferase OS=Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / NCIMB 8073 / NRS 134) OX=446466 GN=mshA PE=3 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
1.000075 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003806_00582.