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CAZyme Information: MGYG000000303_00661

You are here: Home > Sequence: MGYG000000303_00661

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 cambriense_A
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum cambriense_A
CAZyme ID MGYG000000303_00661
CAZy Family GH33
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1836 199634.68 6.7556
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000303 2213433 MAG Sweden Europe
Gene Location Start: 15777;  End: 21287  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.140

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH33 48 416 1.5e-72 0.9649122807017544
GH20 909 1215 2.1e-51 0.9525222551928784
CBM51 1465 1585 6.1e-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 4.64e-83 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 2.36e-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 3.70e-37 1444 1587 1 136
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 9.63e-29 923 1138 17 267
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
smart00776 NPCBM 1.65e-28 1442 1587 1 145
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 3.36e-168 720 1772 256 1302
AZR04729.1 3.36e-168 720 1772 256 1302
AZR07627.1 3.36e-168 720 1772 256 1302
AWG15845.1 3.36e-168 720 1772 256 1302
QIU85951.1 5.11e-166 720 1772 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 1.77e-132 755 1421 18 641
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 1.53e-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 4.66e-86 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 8.57e-86 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 1.16e-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 9.66e-86 29 510 29 486
Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
B2UPR7 3.29e-24 845 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 5.81e-14 784 1311 45 620
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q04786 4.80e-12 829 1273 238 778
Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
P13723 7.13e-12 857 1128 100 390
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
0.000430 0.998684 0.000197 0.000285 0.000195 0.000174

TMHMM  Annotations      download full data without filtering help

start end
13 35
1802 1824