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CAZyme Information: MGYG000000775_00171

You are here: Home > Sequence: MGYG000000775_00171

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 Bifidobacterium sp900551485
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium sp900551485
CAZyme ID MGYG000000775_00171
CAZy Family GH33
CAZyme Description Sialidase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
757 MGYG000000775_1|CGC6 83205.26 4.4045
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000775 1891758 MAG Japan Asia
Gene Location Start: 204428;  End: 206701  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 316 744 4.5e-83 0.9415204678362573

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 1.07e-77 316 752 1 339
Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
pfam13088 BNR_2 3.11e-23 498 737 79 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4409 NanH 3.61e-10 293 645 228 606
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam02210 Laminin_G_2 2.18e-04 180 286 1 117
Laminin G domain. This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
cd00110 LamG 0.008 153 277 2 124
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOL55771.1 0.0 12 755 11 754
BAQ32396.1 0.0 13 755 12 751
AYZ21300.1 0.0 8 756 3 755
AHJ18498.1 0.0 12 755 11 754
AQM42305.1 0.0 12 755 11 754

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 1.69e-66 307 740 2 430
Crystalstructure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124],5TSP_B Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES [Clostridium perfringens ATCC 13124]
2BF6_A 8.91e-66 307 740 1 429
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 9.62e-66 307 740 1 429
TheStructure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK6_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_A The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens],2VK7_B The Structure Of Clostridium Perfringens Nani Sialidase And Its Catalytic Intermediates [Clostridium perfringens]
3H72_A 9.20e-65 309 745 4 457
Crystalstructure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H72_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA [Streptococcus pneumoniae R6],3H73_A Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6],3H73_B Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with DANA [Streptococcus pneumoniae R6]
2W20_A 1.10e-64 313 745 4 453
Structureof the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6],2W20_B Structure of the catalytic domain of the native NanA sialidase from Streptococcus pneumoniae [Streptococcus pneumoniae R6]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P62575 8.12e-64 164 745 142 773
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
P62576 8.12e-64 164 745 142 773
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P29767 5.84e-61 164 756 212 826
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
Q27701 2.07e-28 249 741 206 730
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
Q02834 2.26e-26 309 756 47 401
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA 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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000775_00171.