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CAZyme Information: MGYG000000008_00198

You are here: Home > Sequence: MGYG000000008_00198

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 Lactobacillus johnsonii
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus johnsonii
CAZyme ID MGYG000000008_00198
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
664 MGYG000000008_1|CGC2 76175.62 9.643
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000008 1971706 Isolate United Kingdom Europe
Gene Location Start: 207203;  End: 209197  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000008_00198.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 280 392 6.9e-27 0.6588235294117647

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00761 Glyco_tranf_GTA_type 3.00e-25 281 367 1 87
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
pfam00535 Glycos_transf_2 3.56e-25 280 443 1 164
Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd06423 CESA_like 2.57e-21 281 370 1 91
CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
cd06433 GT_2_WfgS_like 8.01e-20 280 445 1 156
WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
COG0463 WcaA 2.75e-19 278 536 4 289
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEB93804.1 0.0 1 664 1 664
AZZ68074.1 0.0 1 664 1 664
AYN50070.1 0.0 1 664 1 664
AOG26129.1 0.0 1 664 1 664
AAS09506.1 0.0 1 664 1 664

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 2.82e-11 279 449 7 179
CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
5TZE_C 2.57e-08 278 463 2 172
Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A 3.98e-08 278 463 2 172
Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]
5MLZ_A 1.44e-07 268 429 14 165
Dolichylphosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638]
2Z86_A 1.51e-06 274 370 372 467
Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_C Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_D Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q1RIM7 8.17e-11 275 407 289 415
Uncharacterized glycosyltransferase RBE_0706 OS=Rickettsia bellii (strain RML369-C) OX=336407 GN=RBE_0706 PE=3 SV=1
A0A0H2UR96 2.91e-10 279 408 5 131
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
P46918 3.72e-10 280 418 11 150
Minor teichoic acid biosynthesis protein GgaB OS=Bacillus subtilis (strain 168) OX=224308 GN=ggaB PE=3 SV=1
P71054 5.55e-10 278 375 6 104
Putative glycosyltransferase EpsE OS=Bacillus subtilis (strain 168) OX=224308 GN=epsE PE=2 SV=2
B5L3F2 1.01e-09 279 495 6 211
UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfgD OS=Escherichia coli OX=562 GN=wfgD 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
1.000006 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
9 28
33 52
65 87
91 108
115 132
136 158
165 183
193 215
222 241
251 273