Species | Arachnia massiliensis | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Arachnia; Arachnia massiliensis | |||||||||||
CAZyme ID | MGYG000001483_02455 | |||||||||||
CAZy Family | GH20 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 357865; End: 360474 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH20 | 73 | 234 | 2.2e-16 | 0.4540059347181009 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06564 | GH20_DspB_LnbB-like | 3.66e-21 | 60 | 235 | 136 | 312 | 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. |
pfam00754 | F5_F8_type_C | 7.85e-09 | 444 | 592 | 2 | 127 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
pfam00728 | Glyco_hydro_20 | 6.94e-06 | 36 | 248 | 125 | 340 | Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold. |
COG3525 | Chb | 2.53e-05 | 51 | 170 | 410 | 529 | N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]. |
pfam10633 | NPCBM_assoc | 2.70e-04 | 339 | 414 | 1 | 78 | NPCBM-associated, NEW3 domain of alpha-galactosidase. The English-language version of the first reference can be found on pages 388-399 of the above. This domain has been named NEW3 but its actual function is not known. It is found on proteins which are bacterial galactosidases. The domain is associated with the NPCBM family, pfam08305, a novel putative carbohydrate binding module found at the N-terminus of glycosyl hydrolases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AQP52241.1 | 3.00e-156 | 254 | 863 | 7 | 520 |
ALO65373.1 | 9.20e-73 | 47 | 605 | 302 | 934 |
QTO38012.1 | 1.83e-52 | 716 | 863 | 1959 | 2104 |
AQP45421.1 | 1.35e-51 | 582 | 863 | 1822 | 2071 |
AQP45642.1 | 3.50e-50 | 720 | 865 | 482 | 623 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4H04_A | 2.17e-25 | 73 | 241 | 301 | 468 | 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] |
1W8N_A | 1.86e-10 | 443 | 595 | 465 | 598 | 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] |
2BZD_A | 1.86e-10 | 443 | 595 | 465 | 598 | 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] |
1WCQ_A | 1.86e-10 | 443 | 595 | 465 | 598 | 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] |
2BER_A | 1.86e-10 | 443 | 595 | 465 | 598 | Y370GActive Site Mutant of the Sialidase from Micromonospora viridifaciens in complex with beta-Neu5Ac (sialic acid). [Micromonospora viridifaciens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q02834 | 1.08e-09 | 443 | 595 | 511 | 644 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
Q0TR53 | 1.60e-06 | 440 | 533 | 626 | 719 | O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1 |
Q8XL08 | 1.60e-06 | 440 | 533 | 626 | 719 | O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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