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CAZyme Information: MGYG000000001_01867

You are here: Home > Sequence: MGYG000000001_01867

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 GCA-900066495 sp902362365
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; GCA-900066495; GCA-900066495 sp902362365
CAZyme ID MGYG000000001_01867
CAZy Family CBM40
CAZyme Description Sialidase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
803 MGYG000000001_27|CGC2 89420.61 4.6326
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000001 3219617 Isolate United Kingdom Europe
Gene Location Start: 20135;  End: 22546  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 247 676 1e-104 0.956140350877193
CBM40 55 227 6.7e-48 0.9832402234636871

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 1.78e-93 246 677 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.
COG4409 NanH 8.68e-47 105 667 129 703
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam02973 Sialidase 1.35e-29 49 227 2 188
Sialidase, N-terminal domain.
pfam13088 BNR_2 5.71e-19 422 661 79 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam13859 BNR_3 6.20e-10 270 566 9 211
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJA08933.1 0.0 3 803 2 801
ATD57534.1 1.38e-296 37 801 178 947
QBJ75069.1 1.38e-296 37 801 178 947
ATD54786.1 1.38e-296 37 801 178 947
SLK16343.1 1.38e-296 37 801 178 947

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 2.39e-213 238 687 3 453
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]
2VK5_A 9.85e-213 238 687 2 452
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]
2BF6_A 2.51e-212 238 682 2 447
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
1SLI_A 6.85e-99 66 683 22 667
LeechIntramolecular Trans-Sialidase Complexed With Dana [Macrobdella decora],1SLL_A Sialidase L From Leech Macrobdella Decora [Macrobdella decora],2SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac, The Reaction Product [Macrobdella decora],3SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2,7- Anhydro-Neu5ac Prepared By Soaking With 3'-Sialyllactose [Macrobdella decora],4SLI_A Leech Intramolecular Trans-Sialidase Complexed With 2- Propenyl-Neu5ac, An Inactive Substrate Analogue [Macrobdella decora]
4X6K_A 9.42e-89 249 687 9 481
Crystalstructure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B [[Ruminococcus] gnavus CC55_001C]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P29767 2.62e-292 72 801 213 946
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
P62575 1.42e-97 46 681 116 789
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
P62576 1.42e-97 46 681 116 789
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
Q27701 2.69e-97 66 683 102 747
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
Q54727 2.64e-54 66 688 55 691
Sialidase B OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=nanB PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.272626 0.724683 0.001488 0.000430 0.000363 0.000374

TMHMM  Annotations      download full data without filtering help

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