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CAZyme Information: MGYG000000105_00831

You are here: Home > Sequence: MGYG000000105_00831

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 Bacteroides clarus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides clarus
CAZyme ID MGYG000000105_00831
CAZy Family GH98
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
934 MGYG000000105_1|CGC14 105013.35 5.492
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000105 3966085 Isolate Canada North America
Gene Location Start: 883493;  End: 886297  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH98 224 536 5.9e-114 0.9877675840978594
CBM35 824 920 2e-17 0.7899159663865546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam08306 Glyco_hydro_98M 1.57e-122 224 536 6 328
Glycosyl hydrolase family 98. This domain is the putative catalytic domain of glycosyl hydrolase family 98 proteins.
cd04083 CBM35_Lmo2446-like 4.30e-19 803 931 1 125
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.
pfam16378 DUF4988 2.62e-17 40 211 12 181
Domain of unknown function. This family around 200 residues locates in the N-terminal of some uncharacterized proteins in various Bacteroides and Alistipes species. The function of this family remains unknown. The N-terminus of this model has been clipped by ~30 residues as it was capturing parts of collagen sequences, pfam01391.
pfam08307 Glyco_hydro_98C 3.21e-15 541 773 1 268
Glycosyl hydrolase family 98 C-terminal domain. This putative domain is found at the C-terminus of glycosyl hydrolase family 98 proteins. This domain is not expected to form part of the catalytic activity.
cd04082 CBM35_pectate_lyase-like 8.73e-10 830 920 22 114
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ55178.1 0.0 13 932 14 937
SCV07742.1 0.0 13 932 22 945
ALJ48334.1 0.0 13 932 14 937
EDO10800.1 0.0 13 932 22 945
QDH54066.1 0.0 13 932 14 937

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WMI_A 9.79e-18 255 721 69 514
Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 in complex with the A-trisaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71],2WMJ_A Crystal structure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 (Sp3GH98) in complex with the B-trisaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71],2WMJ_B Crystal structure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 (Sp3GH98) in complex with the B-trisaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71]
4D6D_A 3.86e-17 255 721 46 491
Crystalstructure of a family 98 glycoside hydrolase catalytic module (Sp3GH98) in complex with the blood group A-trisaccharide (X02 mutant) [Streptococcus pneumoniae SP3-BS71]
2WMI_B 3.93e-17 255 721 69 514
Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 in complex with the A-trisaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71]
2WMK_A 5.19e-17 255 721 69 514
Crystalstructure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 (Sp3GH98) in complex with the A-LewisY pentasaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71],2WMK_B Crystal structure of the catalytic module of a family 98 glycoside hydrolase from Streptococcus pneumoniae SP3-BS71 (Sp3GH98) in complex with the A-LewisY pentasaccharide blood group antigen. [Streptococcus pneumoniae SP3-BS71]
4D6E_A 1.17e-16 255 721 46 491
Crystalstructure of a family 98 glycoside hydrolase catalytic module (Sp3GH98) in complex with the blood group A-trisaccharide (X01 mutant) [Streptococcus pneumoniae SP3-BS71]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q6RUF5 1.29e-16 255 719 262 705
Blood-group-substance endo-1,4-beta-galactosidase OS=Clostridium perfringens OX=1502 GN=eabC PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000001 0.000041 1.000038 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000105_00831.