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CAZyme Information: MGYG000001095_01925

You are here: Home > Sequence: MGYG000001095_01925

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 Chryseobacterium gambrini
Lineage Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Chryseobacterium; Chryseobacterium gambrini
CAZyme ID MGYG000001095_01925
CAZy Family GT4
CAZyme Description Glycosyltransferase Gtf1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
228 MGYG000001095_327|CGC1 26274.42 8.5686
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001095 4128611 MAG Sweden Europe
Gene Location Start: 9034;  End: 9720  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001095_01925.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 66 212 5.7e-18 0.93125

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03809 GT4_MtfB-like 1.61e-25 1 201 120 327
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.
cd03801 GT4_PimA-like 2.08e-17 9 201 124 327
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 3.58e-17 1 201 129 336
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd01635 Glycosyltransferase_GTB-type 2.64e-10 43 177 85 220
glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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.
cd03820 GT4_AmsD-like 6.26e-10 32 177 145 288
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
QWA40252.1 1.57e-154 1 228 108 335
AZB23015.1 1.32e-101 9 228 118 337
VFB03303.1 5.28e-78 2 227 111 335
QQV03382.1 5.28e-78 2 227 111 335
AZA95113.1 8.38e-74 5 227 113 333

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4PQG_A 4.51e-06 10 178 269 435
Crystalstructure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc [Streptococcus pneumoniae TIGR4],4PQG_B Crystal structure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001095_01925.