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CAZyme Information: MGYG000003063_01227

You are here: Home > Sequence: MGYG000003063_01227

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 Eisenbergiella sp900544445
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900544445
CAZyme ID MGYG000003063_01227
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
319 MGYG000003063_20|CGC1 35635.11 10.0789
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003063 3890464 MAG United States North America
Gene Location Start: 12567;  End: 13526  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003063_01227.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 4 174 2.6e-29 0.9882352941176471

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1216 GT2 7.77e-54 1 282 3 302
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd04186 GT_2_like_c 1.71e-51 5 211 1 164
Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. 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.
pfam00535 Glycos_transf_2 9.15e-28 4 171 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 2.05e-24 5 198 1 151
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.
TIGR03965 mycofact_glyco 1.05e-19 4 211 77 280
mycofactocin system glycosyltransferase. Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCU01341.1 1.12e-117 2 318 3 315
QNM10256.1 8.22e-116 2 318 3 319
CBL24567.1 1.79e-111 1 318 1 314
QYX28909.1 5.61e-110 1 316 1 312
QOV20102.1 1.92e-109 2 319 3 320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3L7I_A 7.27e-07 2 88 3 93
Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A]
3L7M_A 7.27e-07 2 88 3 93
ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P9WMY2 3.07e-17 5 218 7 242
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3 3.07e-17 5 218 7 242
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
Q5HCN1 5.17e-10 4 237 50 276
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain COL) OX=93062 GN=icaA PE=3 SV=1
Q9RQP9 5.17e-10 4 237 50 276
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=icaA PE=3 SV=2
Q6GDD8 5.17e-10 4 237 50 276
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=icaA 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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003063_01227.