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CAZyme Information: MGYG000000273_00076

You are here: Home > Sequence: MGYG000000273_00076

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 Phocaeicola coprophilus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprophilus
CAZyme ID MGYG000000273_00076
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
319 MGYG000000273_1|CGC2 37647.18 8.0842
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000273 3492533 Isolate China Asia
Gene Location Start: 76389;  End: 77348  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000273_00076.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 7 167 1.4e-30 0.9823529411764705

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00535 Glycos_transf_2 3.22e-30 7 165 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.
cd00761 Glyco_tranf_GTA_type 1.59e-27 8 118 1 112
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 4.22e-25 4 115 6 117
putative glycosyl transferase; Provisional
COG0463 WcaA 2.92e-21 2 263 1 258
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd02525 Succinoglycan_BP_ExoA 7.95e-21 5 175 1 181
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALO47937.1 3.26e-82 6 296 16 310
QCY56824.1 1.90e-70 4 295 3 296
AST54053.1 1.90e-70 4 295 3 296
QKH97959.1 1.90e-70 4 295 3 296
QRO16476.1 1.90e-70 4 295 3 296

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 1.02e-29 6 216 7 226
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 3.14e-20 4 205 5 224
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 8.75e-19 4 122 13 132
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]
6H1J_A 3.25e-14 6 197 22 219
ChainA, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315]
2Z86_A 1.58e-12 4 98 375 469
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
P71057 2.63e-28 1 250 1 254
Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2URH7 1.02e-22 6 121 7 122
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P71059 1.53e-22 4 227 3 231
Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
A0A0H2UR96 4.06e-22 6 121 5 121
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1
P46918 1.63e-18 7 243 11 253
Minor teichoic acid biosynthesis protein GgaB OS=Bacillus subtilis (strain 168) OX=224308 GN=ggaB 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
1.000050 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000273_00076.