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CAZyme Information: MGYG000002328_01229

You are here: Home > Sequence: MGYG000002328_01229

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 Enterocloster asparagiformis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster asparagiformis
CAZyme ID MGYG000002328_01229
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
472 MGYG000002328_66|CGC1 54850.49 6.6503
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002328 6168028 Isolate not provided not provided
Gene Location Start: 18703;  End: 20121  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002328_01229.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 171 5e-38 0.9823529411764705

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10032 UDG-F6_HDG 1.16e-67 298 435 2 141
Uracil DNA glycosylase family 6, includes hypoxanthine-DNA glycosylase and similar proteins. Uracil DNA glycosylase family 6 hypoxanthine-DNA glycosylase (HDG) lacks any detectable UDG activity; it excises hypoxanthine, a deamination product of adenine, from double-stranded DNA. Uracil-DNA glycosylase (UDGs) initiates repair of uracils in DNA. Uracil in DNA can arise as a result of misincorporation of dUMP residues by DNA polymerase or via deamination of cytosine. Uracil in DNA mispaired with guanine is one of the major pro-mutagenic events, causing G:C->A:T mutations. Thus, UDG is an essential enzyme for maintaining the integrity of genetic information. UDGs have been classified into various families on the basis of their substrate specificity, conserved motifs, and structural similarities. Although these families demonstrate different substrate specificities, often the function of one enzyme can be complemented by the other.
TIGR04274 hypoxanDNAglyco 2.80e-41 299 446 2 150
hypoxanthine-DNA glycosylase. Members of this protein family represent family 6 of the uracil-DNA glycosylase superfamily, where the five previously described families all act as uracil-DNA glycosylase (EC 3.2.2.27) per se. This family, instead, acts as a hypoxanthine-DNA glycosylase, where hypoxanthine results from deamination of adenine. Activity was shown directly for members from Methanosarcina barkeri and Methanosarcina acetivorans.
pfam00535 Glycos_transf_2 1.68e-39 5 169 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 1.76e-33 7 116 2 113
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.
COG3663 Mug 1.60e-30 298 446 1 157
G:T/U-mismatch repair DNA glycosylase [Replication, recombination and repair].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJU21468.1 1.70e-264 1 446 1 446
ASN94231.1 5.67e-263 1 446 1 446
QRP41091.1 5.67e-263 1 446 1 446
QIX92878.1 3.12e-260 1 446 1 446
ANU48636.1 3.63e-259 1 446 1 446

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 6.54e-29 3 219 6 225
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 5.18e-25 1 209 4 224
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]
5TZE_C 1.21e-21 5 221 4 215
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 4.52e-21 5 221 4 215
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]
2Z87_A 6.80e-21 1 143 373 505
Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli],2Z87_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc 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
P71059 7.82e-40 1 224 2 226
Uncharacterized glycosyltransferase EpsJ OS=Bacillus subtilis (strain 168) OX=224308 GN=epsJ PE=2 SV=1
P71057 9.17e-33 2 259 4 259
Putative glycosyltransferase EpsH OS=Bacillus subtilis (strain 168) OX=224308 GN=epsH PE=2 SV=1
A0A0H2URH7 9.84e-33 4 314 7 309
Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1
P11290 2.66e-23 4 198 8 210
Uncharacterized glycosyltransferase YibD OS=Escherichia coli (strain K12) OX=83333 GN=yibD PE=3 SV=2
A0A0H2UR96 1.17e-22 3 221 4 226
Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG 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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002328_01229.