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CAZyme Information: MGYG000004222_01320

You are here: Home > Sequence: MGYG000004222_01320

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 CAG-269 sp900556345
Lineage Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269; CAG-269 sp900556345
CAZyme ID MGYG000004222_01320
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
365 MGYG000004222_6|CGC1 41793.19 8.8091
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004222 1526338 MAG United Kingdom Europe
Gene Location Start: 17194;  End: 18291  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004222_01320.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 194 339 2.9e-27 0.93125

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 1.73e-51 4 364 6 366
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.
cd04955 GT4-like 7.45e-43 1 363 4 378
glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases. 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 in certain bacteria and Archaea.
COG0438 RfaB 1.64e-39 1 365 4 376
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03809 GT4_MtfB-like 9.04e-33 6 361 8 362
glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
cd03820 GT4_AmsD-like 1.44e-31 12 358 13 348
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QFJ53915.1 8.06e-151 1 364 5 370
CBK75177.1 3.77e-149 1 364 5 370
QEX01938.1 7.64e-147 1 364 10 375
AQT55817.1 7.64e-147 1 364 10 375
QRN07016.1 7.64e-147 1 364 10 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5D00_A 9.43e-08 12 301 17 306
Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]
2F9F_A 3.15e-07 196 294 24 122
CrystalStructure of the Putative Mannosyl Transferase (wbaZ-1)from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR29A. [Archaeoglobus fulgidus DSM 4304]
5N7Z_A 1.56e-06 199 342 184 333
glycosyltransferasein LPS biosynthesis [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],6Y6G_A Chain A, Lipopolysaccharide 1,6-galactosyltransferase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
5N80_A 1.57e-06 199 342 185 334
glycosyltransferaseLPS biosynthesis in complex with UDP [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
6Y6I_A 1.57e-06 199 342 186 335
ChainA, Lipopolysaccharide 1,6-galactosyltransferase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q59002 7.78e-15 8 364 12 382
Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1
Q58577 4.89e-14 12 365 17 348
Uncharacterized glycosyltransferase MJ1178 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1178 PE=3 SV=1
Q4JAK2 1.12e-08 195 364 179 349
Archaeal glycosylation protein 16 OS=Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) OX=330779 GN=agl16 PE=3 SV=1
P42982 5.14e-07 12 301 15 304
N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=bshA PE=1 SV=2
P26470 1.63e-06 148 361 142 373
Lipopolysaccharide 1,2-N-acetylglucosaminetransferase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=waaK 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
1.000055 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004222_01320.