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CAZyme Information: MGYG000001345_00834

You are here: Home > Sequence: MGYG000001345_00834

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 xylanisolvens
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides xylanisolvens
CAZyme ID MGYG000001345_00834
CAZy Family GH33
CAZyme Description Sialidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
386 MGYG000001345_31|CGC1 42750.76 5.3022
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001345 5913018 Isolate not provided not provided
Gene Location Start: 209855;  End: 211015  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001345_00834.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 49 372 1.4e-91 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 4.38e-100 48 381 3 339
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 1.02e-30 71 362 2 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam13859 BNR_3 6.99e-19 72 285 11 211
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
cd00260 Sialidase 2.09e-12 46 350 1 320
sialidases/neuraminidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases.
COG4409 NanH 7.61e-11 52 288 268 543
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT24669.1 3.79e-296 1 386 1 386
CBK69348.1 3.79e-296 1 386 1 386
QRN00956.1 1.09e-295 1 386 1 386
QUT30031.1 1.09e-295 1 386 1 386
QUR42291.1 1.09e-295 1 386 1 386

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2BF6_A 1.32e-36 59 366 23 430
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
2VK5_A 1.38e-36 59 366 23 430
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]
5TSP_A 3.02e-36 59 366 24 431
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]
6MNJ_A 8.04e-35 48 385 189 537
Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes]
6MYV_A 1.11e-33 48 385 170 520
Sialidase26co-crystallized with DANA-Gc [bacterium],6MYV_B Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_C Sialidase26 co-crystallized with DANA-Gc [bacterium],6MYV_D Sialidase26 co-crystallized with DANA-Gc [bacterium]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O35657 1.37e-34 40 382 52 405
Sialidase-1 OS=Mus musculus OX=10090 GN=Neu1 PE=1 SV=1
A5PF10 2.94e-34 40 382 59 412
Sialidase-1 OS=Sus scrofa OX=9823 GN=NEU1 PE=3 SV=1
Q99519 7.66e-34 6 382 30 411
Sialidase-1 OS=Homo sapiens OX=9606 GN=NEU1 PE=1 SV=1
Q5RAF4 7.66e-34 6 382 30 411
Sialidase-1 OS=Pongo abelii OX=9601 GN=NEU1 PE=2 SV=1
Q99PW3 1.33e-33 40 382 52 405
Sialidase-1 OS=Rattus norvegicus OX=10116 GN=Neu1 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
0.000004 0.001541 0.998485 0.000001 0.000001 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001345_00834.