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CAZyme Information: MGYG000001553_00396

You are here: Home > Sequence: MGYG000001553_00396

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 Clostridium_P mediterraneense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P mediterraneense
CAZyme ID MGYG000001553_00396
CAZy Family CBM40
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
810 88736.64 6.0026
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001553 3045114 Isolate not provided not provided
Gene Location Start: 129401;  End: 131833  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 248 676 2.1e-100 0.9385964912280702
CBM40 60 229 6.4e-42 0.9608938547486033

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 5.53e-87 247 676 1 327
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 9.74e-41 1 672 1 700
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
pfam02973 Sialidase 3.28e-24 55 229 12 188
Sialidase, N-terminal domain.
pfam13088 BNR_2 6.24e-17 432 669 79 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
pfam13859 BNR_3 1.84e-10 431 611 86 249
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 1.99e-257 54 810 49 801
ATD57534.1 4.68e-246 35 810 174 949
QBJ75069.1 4.68e-246 35 810 174 949
ATD54786.1 4.68e-246 35 810 174 949
SLK16343.1 4.68e-246 35 810 174 949

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5TSP_A 3.67e-162 244 695 8 453
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 1.52e-161 244 695 7 452
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 3.86e-161 244 691 7 448
AtomicResolution Structure of the bacterial sialidase NanI from Clostridium perfringens in complex with alpha-Sialic Acid (Neu5Ac). [Clostridium perfringens]
1SLI_A 1.28e-94 54 672 6 649
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 1.36e-81 249 690 7 483
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 9.29e-243 35 810 174 948
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1
Q27701 4.76e-93 54 672 86 729
Anhydrosialidase OS=Macrobdella decora OX=6405 PE=1 SV=1
P62576 4.15e-87 63 699 132 799
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P62575 4.15e-87 63 699 132 799
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
Q54727 6.91e-56 64 695 51 697
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
0.000357 0.998909 0.000191 0.000184 0.000175 0.000159

TMHMM  Annotations      download full data without filtering help

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