logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004314_00012

You are here: Home > Sequence: MGYG000004314_00012

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 Varibaculum timonense
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum timonense
CAZyme ID MGYG000004314_00012
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1831 MGYG000004314_1|CGC1 199145.2 6.7135
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004314 2027678 MAG Israel Asia
Gene Location Start: 17014;  End: 22509  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.140

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 48 413 5.6e-73 0.956140350877193
GH20 909 1215 2e-51 0.9525222551928784
CBM51 1465 1585 3.1e-33 0.8731343283582089

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd15482 Sialidase_non-viral 2.60e-84 46 417 2 339
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.
cd06564 GH20_DspB_LnbB-like 1.26e-58 909 1215 2 326
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam08305 NPCBM 3.09e-36 1446 1587 3 136
NPCBM/NEW2 domain. This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins. This domain has also been called the NEW2 domain (Naumoff DG. Phylogenetic analysis of alpha-galactosidases of the GH27 family. Molecular Biology (Engl Transl). (2004)38:388-399.)
pfam00728 Glyco_hydro_20 4.43e-29 923 1138 17 267
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
smart00776 NPCBM 1.88e-28 1451 1587 10 145
This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWG03116.1 6.64e-164 720 1771 256 1302
AZR04729.1 6.64e-164 720 1771 256 1302
AZR07627.1 6.64e-164 720 1771 256 1302
AWG15845.1 6.64e-164 720 1771 256 1302
QIU85951.1 1.89e-161 720 1771 250 1296

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4H04_A 4.43e-132 765 1421 28 641
Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
1EUT_A 6.97e-86 51 510 18 444
Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens]
1WCQ_A 2.13e-85 51 510 14 440
Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens]
2BZD_A 3.91e-85 51 510 14 440
Galactoserecognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_B Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_C Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens]
1W8N_A 5.30e-85 51 510 14 440
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q02834 4.38e-85 29 510 29 486
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
B2UPR7 5.16e-23 845 1193 169 545
Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P49008 1.72e-13 784 1157 45 429
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q04786 9.37e-13 842 1227 253 734
Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
P13723 3.10e-12 857 1129 100 391
Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 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
0.000431 0.998657 0.000196 0.000286 0.000195 0.000174

TMHMM  Annotations      download full data without filtering help

start end
13 35
1801 1823