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CAZyme Information: MGYG000004290_01238

You are here: Home > Sequence: MGYG000004290_01238

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 Alistipes sp900549305
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900549305
CAZyme ID MGYG000004290_01238
CAZy Family GH33
CAZyme Description Sialidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
378 MGYG000004290_58|CGC1 41579.7 8.033
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004290 3325933 MAG China Asia
Gene Location Start: 12075;  End: 13211  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004290_01238.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 26 367 3.2e-96 0.9590643274853801

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 5.80e-108 25 372 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 3.22e-34 49 349 1 280
BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases.
COG4409 NanH 4.77e-15 20 363 257 711
Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd00260 Sialidase 3.41e-08 32 344 9 327
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.
pfam15902 Sortilin-Vps10 0.002 258 326 378 431
Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDT42616.1 3.39e-118 25 370 39 375
QDV50699.1 5.66e-118 25 370 43 379
QQL50302.1 7.32e-116 19 371 28 372
BBD46002.1 3.06e-114 27 376 39 375
AYQ36531.1 2.72e-113 6 372 13 366

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1EUR_A 1.12e-43 30 354 17 346
Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens]
6MYV_A 1.51e-42 31 353 174 505
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]
6MRV_A 2.18e-42 31 353 195 526
Sialidase26co-crystallized with DANA [bacterium],6MRV_B Sialidase26 co-crystallized with DANA [bacterium],6MRX_A Sialidase26 apo [bacterium],6MRX_B Sialidase26 apo [bacterium],6MRX_C Sialidase26 apo [bacterium],6MRX_D Sialidase26 apo [bacterium]
1W8N_A 2.78e-42 30 354 13 342
Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens]
4J9T_A 3.03e-42 30 354 13 342
Crystalstructure of a putative, de novo designed unnatural amino acid dependent metalloprotein, northeast structural genomics consortium target OR61 [Micromonospora viridifaciens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q02834 4.49e-41 30 354 59 388
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
P31206 1.23e-37 31 353 196 527
Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2
P62575 7.47e-34 23 372 325 790
Sialidase A OS=Streptococcus pneumoniae OX=1313 GN=nanA PE=1 SV=1
P62576 7.47e-34 23 372 325 790
Sialidase A OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=nanA PE=1 SV=1
P29767 4.55e-30 19 378 376 833
Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1

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
0.000607 0.717088 0.281399 0.000379 0.000265 0.000233

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004290_01238.