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CAZyme Information: MGYG000002428_00312

You are here: Home > Sequence: MGYG000002428_00312

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 Campylobacter_A concisus_W
Lineage Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter_A; Campylobacter_A concisus_W
CAZyme ID MGYG000002428_00312
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
342 38824.08 9.2289
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002428 1937734 Isolate South Africa Africa
Gene Location Start: 41077;  End: 42105  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002428_00312.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 7 126 1.5e-29 0.7294117647058823

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00761 Glyco_tranf_GTA_type 2.99e-30 9 158 2 156
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.
PRK10073 PRK10073 8.60e-29 5 158 7 164
putative glycosyl transferase; Provisional
pfam00535 Glycos_transf_2 5.29e-28 7 114 1 112
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.
cd02525 Succinoglycan_BP_ExoA 1.35e-25 5 117 1 118
ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.
cd06423 CESA_like 3.12e-23 9 184 2 180
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALF48163.1 7.75e-235 1 342 1 342
QPI03486.1 1.56e-234 1 342 1 342
QPH88537.1 1.56e-234 1 342 1 342
QPH86818.1 1.23e-231 1 342 1 342
QPH99922.1 8.29e-230 1 342 1 342

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 2.11e-24 3 253 4 250
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]
3BCV_A 1.27e-21 5 209 6 225
Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
6P61_A 2.52e-20 6 140 15 148
Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]
5TZE_C 3.52e-19 4 206 1 201
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 8.42e-19 4 206 1 201
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2URH7 1.19e-25 5 246 6 253
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
E0U4V7 3.31e-23 4 330 1 332
Poly(ribitol-phosphate) beta-glucosyltransferase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarQ PE=1 SV=1
A0A0H3JPC6 4.62e-18 4 206 2 202
Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=tarS PE=1 SV=1
A0A0H3JVA1 4.62e-18 4 206 2 202
Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain MW2) OX=196620 GN=tarS PE=1 SV=1
P11290 1.81e-17 5 112 7 117
Uncharacterized glycosyltransferase YibD OS=Escherichia coli (strain K12) OX=83333 GN=yibD PE=3 SV=2

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
1.000054 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002428_00312.