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CAZyme Information: MGYG000001698_01520

You are here: Home > Sequence: MGYG000001698_01520

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 Marvinbryantia formatexigens
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Marvinbryantia; Marvinbryantia formatexigens
CAZyme ID MGYG000001698_01520
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
381 MGYG000001698_6|CGC2 43336.13 9.314
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001698 4516105 Isolate United States North America
Gene Location Start: 119662;  End: 120807  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001698_01520.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 205 349 8e-26 0.925

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 4.00e-62 9 377 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 3.36e-45 9 381 1 379
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03809 GT4_MtfB-like 3.53e-38 117 374 97 362
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.
cd04955 GT4-like 1.60e-37 10 376 2 378
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.
cd03821 GT4_Bme6-like 2.38e-35 23 374 14 377
Brucella melitensis Bme6 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQT55817.1 1.87e-187 7 377 5 375
AFC64059.1 1.87e-187 7 377 5 375
AQY29050.1 1.87e-187 7 377 5 375
AQY32232.1 1.87e-187 7 377 5 375
QEX01938.1 2.65e-187 7 377 5 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5D00_A 7.86e-10 23 334 17 327
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]
6EJI_A 1.01e-07 147 375 130 353
Structureof a glycosyltransferase [Campylobacter jejuni],6EJI_B Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_A Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_B Structure of a glycosyltransferase [Campylobacter jejuni]
6EJJ_A 1.01e-07 147 375 130 353
Structureof a glycosyltransferase / state 2 [Campylobacter jejuni],6EJJ_B Structure of a glycosyltransferase / state 2 [Campylobacter jejuni]
5N7Z_A 4.07e-07 138 311 117 288
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 4.08e-07 138 311 118 289
glycosyltransferaseLPS biosynthesis in complex with UDP [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 7.21e-20 8 380 1 385
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
D4GU62 1.78e-17 158 327 166 341
Low-salt glycan biosynthesis hexosyltransferase Agl9 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=agl9 PE=3 SV=1
P9WMZ1 1.70e-13 96 378 75 384
Alpha-maltose-1-phosphate synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgM PE=1 SV=1
P9WMZ0 1.70e-13 96 378 75 384
Alpha-maltose-1-phosphate synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgM PE=3 SV=1
Q65CC7 2.26e-13 103 364 88 369
Alpha-D-kanosaminyltransferase OS=Streptomyces kanamyceticus OX=1967 GN=kanE 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
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001698_01520.