Species | Alistipes sp900549305 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900549305 | |||||||||||
CAZyme ID | MGYG000004290_02486 | |||||||||||
CAZy Family | GH18 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 268; End: 1710 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06542 | GH18_EndoS-like | 2.90e-40 | 190 | 456 | 1 | 254 | Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B. |
pfam08522 | DUF1735 | 1.16e-14 | 45 | 157 | 5 | 115 | Domain of unknown function (DUF1735). This domain of unknown function is found in a number of bacterial proteins including acylhydrolases. The structure of this domain has a beta-sandwich fold. |
pfam00704 | Glyco_hydro_18 | 1.41e-13 | 191 | 391 | 1 | 182 | Glycosyl hydrolases family 18. |
smart00636 | Glyco_18 | 8.62e-08 | 261 | 391 | 63 | 191 | Glyco_18 domain. |
cd02871 | GH18_chitinase_D-like | 1.04e-05 | 257 | 318 | 66 | 125 | GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QIU94417.1 | 7.31e-163 | 16 | 479 | 17 | 472 |
BBL07593.1 | 1.16e-144 | 4 | 479 | 1 | 465 |
QQT26426.1 | 4.70e-100 | 15 | 479 | 16 | 469 |
QQS96497.1 | 1.47e-98 | 15 | 479 | 16 | 469 |
QMI80605.1 | 1.06e-90 | 4 | 476 | 1 | 475 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6T8I_A | 3.16e-66 | 27 | 367 | 2 | 343 | Crystalstructure of wild type EndoBT-3987 from Bacteroides thetaiotamicron VPI-5482 [Bacteroides thetaiotaomicron VPI-5482],6T8K_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8K_B Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc product in P1 [Bacteroides thetaiotaomicron VPI-5482],6T8L_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man9GlcNAc product in P212121 [Bacteroides thetaiotaomicron VPI-5482],6TCW_A Crystal structure of Bacteroides thetaiotamicron EndoBT-3987 with Man5GlcNAc product [Bacteroides thetaiotaomicron VPI-5482],7NWF_A Chain A, Endo-beta-N-acetylglucosaminidase F1 [Bacteroides thetaiotaomicron VPI-5482] |
6TCV_B | 7.01e-64 | 27 | 367 | 2 | 343 | Crystalstructure of Bacteroides thetaiotamicron EndoBT-3987 in complex with Man9GlcNAc2Asn substrate [Bacteroides thetaiotaomicron VPI-5482] |
3POH_A | 9.82e-64 | 27 | 367 | 2 | 343 | Crystalstructure of an endo-beta-N-acetylglucosaminidase (BT_3987) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.55 A resolution [Bacteroides thetaiotaomicron VPI-5482] |
2EBN_A | 3.50e-55 | 195 | 479 | 15 | 289 | CRYSTALSTRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F1, AN ALPHA(SLASH)BETA-BARREL ENZYME ADAPTED FOR A COMPLEX SUBSTRATE [Elizabethkingia meningoseptica] |
1EDT_A | 2.32e-47 | 189 | 462 | 8 | 269 | ChainA, ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, ENDO H [Streptomyces plicatus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P36911 | 5.42e-54 | 164 | 479 | 35 | 339 | Endo-beta-N-acetylglucosaminidase F1 OS=Elizabethkingia meningoseptica OX=238 GN=endOF1 PE=1 SV=1 |
P04067 | 3.90e-46 | 189 | 462 | 50 | 311 | Endo-beta-N-acetylglucosaminidase H OS=Streptomyces plicatus OX=1922 PE=1 SV=1 |
P80036 | 1.60e-35 | 179 | 460 | 44 | 311 | Endo-beta-N-acetylglucosaminidase OS=Flavobacterium sp. (strain SK1022) OX=148444 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000002 | 0.001113 | 0.998944 | 0.000000 | 0.000001 | 0.000000 |
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