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CAZyme Information: MGYG000001388_00051

You are here: Home > Sequence: MGYG000001388_00051

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 Desulfitobacterium hafniense
Lineage Bacteria; Firmicutes_B; Desulfitobacteriia; Desulfitobacteriales; Desulfitobacteriaceae; Desulfitobacterium; Desulfitobacterium hafniense
CAZyme ID MGYG000001388_00051
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
332 37086.37 6.9328
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001388 5194328 Isolate not provided not provided
Gene Location Start: 3725;  End: 4723  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001388_00051.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 219 302 1.9e-24 0.51875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 3.64e-38 13 327 15 366
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 9.56e-30 1 332 3 380
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03825 GT4_WcaC-like 6.62e-24 114 305 141 339
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
cd03808 GT4_CapM-like 4.72e-23 16 282 14 316
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
pfam00534 Glycos_transf_1 1.44e-20 220 282 69 131
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
CDX04692.1 9.25e-247 1 332 1 332
BAE86221.1 9.25e-247 1 332 1 332
ACL18954.1 2.65e-246 1 332 1 332
AET66065.1 4.37e-176 1 330 1 329
AFQ42409.1 5.91e-174 1 332 1 331

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6KIH_A 2.10e-08 223 329 317 424
Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
2R60_A 1.22e-06 222 319 347 449
Structureof apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii [Halothermothrix orenii],2R66_A Complex Structure of Sucrose Phosphate Synthase (SPS)-F6P of Halothermothrix orenii [Halothermothrix orenii H 168],2R68_A Complex Structure of Sucrose Phosphate Synthase (SPS)-S6P of Halothermothrix orenii [Halothermothrix orenii H 168]
3OKA_A 2.41e-06 22 326 42 376
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 2.48e-06 22 326 42 376
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D3Q051 1.50e-08 134 322 213 420
D-inositol 3-phosphate glycosyltransferase OS=Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 / LLR-40K-21) OX=446470 GN=mshA PE=3 SV=1
O68547 3.89e-07 134 289 137 305
Lipopolysaccharide core biosynthesis mannosyltransferase LpcC OS=Rhizobium leguminosarum bv. viciae OX=387 GN=lpcC PE=3 SV=1
C0ZUT0 6.31e-07 223 322 304 403
D-inositol 3-phosphate glycosyltransferase OS=Rhodococcus erythropolis (strain PR4 / NBRC 100887) OX=234621 GN=mshA PE=3 SV=1
P9WMZ4 2.35e-06 115 315 145 353
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=pimA PE=3 SV=1
P9WMZ5 2.35e-06 115 315 145 353
Phosphatidyl-myo-inositol mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 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
1.000070 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001388_00051.