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CAZyme Information: MGYG000004698_00461

You are here: Home > Sequence: MGYG000004698_00461

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 Prevotella sp000436695
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000436695
CAZyme ID MGYG000004698_00461
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
258 MGYG000004698_8|CGC1 30175.44 9.353
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004698 3424026 MAG Denmark Europe
Gene Location Start: 31290;  End: 32066  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004698_00461.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 10 139 3.4e-31 0.7588235294117647

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06433 GT_2_WfgS_like 1.52e-84 10 217 1 202
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.
cd00761 Glyco_tranf_GTA_type 4.52e-28 11 123 1 113
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.
pfam00535 Glycos_transf_2 9.89e-28 10 165 1 160
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.
PRK10063 PRK10063 3.17e-27 9 217 3 204
colanic acid biosynthesis glycosyltransferase WcaE.
cd06423 CESA_like 8.19e-23 11 175 1 173
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
QYR11074.1 1.39e-113 8 256 2 251
QUB48550.1 1.14e-107 8 256 2 250
QUB51590.1 3.27e-107 8 256 2 250
ATV32369.1 9.33e-107 8 256 2 250
ATV41222.1 9.33e-107 8 256 2 250

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z86_A 2.02e-08 9 129 377 496
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]
2Z87_A 2.02e-08 9 129 376 495
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]
1H7L_A 3.25e-08 8 142 2 126
dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis]
5TZE_C 9.11e-08 8 137 2 117
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]
3BCV_A 9.76e-08 8 122 6 118
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P71239 1.21e-16 10 217 4 204
Putative colanic acid biosynthesis glycosyl transferase WcaE OS=Escherichia coli (strain K12) OX=83333 GN=wcaE PE=4 SV=2
A1KMV1 6.48e-15 10 223 7 215
PGL/p-HBAD biosynthesis glycosyltransferase BCG_2978 OS=Mycobacterium bovis (strain BCG / Pasteur 1173P2) OX=410289 GN=BCG_2978 PE=3 SV=2
P0A5A0 6.48e-15 10 223 7 215
PGL/p-HBAD biosynthesis glycosyltransferase Mb2981 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB2981 PE=3 SV=1
A5U6W5 6.48e-15 10 223 7 215
PGL/p-HBAD biosynthesis glycosyltransferase MRA_2984 OS=Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra) OX=419947 GN=MRA_2984 PE=3 SV=2
P9WMX6 6.48e-15 10 223 7 215
PGL/p-HBAD biosynthesis glycosyltransferase MT3031 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3031 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
1.000052 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004698_00461.