Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; | |||||||||||
CAZyme ID | MGYG000000448_00435 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | Beta-hexosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 18153; End: 21350 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH43 | 29 | 307 | 1.7e-103 | 0.9928571428571429 |
GH3 | 397 | 618 | 2.2e-73 | 0.9861111111111112 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK15098 | PRK15098 | 0.0 | 330 | 1061 | 35 | 765 | beta-glucosidase BglX. |
cd18827 | GH43_XlnD-like | 6.58e-174 | 37 | 312 | 1 | 277 | Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
cd09004 | GH43_bXyl-like | 2.56e-105 | 37 | 312 | 1 | 266 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
COG1472 | BglX | 1.46e-101 | 340 | 717 | 1 | 365 | Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism]. |
pfam00933 | Glyco_hydro_3 | 1.71e-95 | 341 | 650 | 1 | 316 | Glycosyl hydrolase family 3 N terminal domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDM10595.1 | 1.66e-303 | 329 | 1050 | 30 | 750 |
QUT79182.1 | 1.66e-303 | 329 | 1050 | 30 | 750 |
QGT72545.1 | 2.44e-303 | 316 | 1061 | 17 | 761 |
QRM99629.1 | 1.97e-302 | 321 | 1061 | 22 | 761 |
QUT31653.1 | 1.59e-301 | 316 | 1061 | 17 | 761 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5XXL_A | 2.37e-275 | 321 | 1064 | 2 | 755 | Crystalstructure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5XXL_B Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5XXM_A Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron in complex with gluconolactone [Bacteroides thetaiotaomicron VPI-5482],5XXM_B Crystal structure of GH3 beta-glucosidase from Bacteroides thetaiotaomicron in complex with gluconolactone [Bacteroides thetaiotaomicron VPI-5482] |
5XXN_A | 1.35e-274 | 321 | 1064 | 2 | 755 | CrystalStructure of mutant (D286N) beta-glucosidase from Bacteroides thetaiotaomicron in complex with sophorose [Bacteroides thetaiotaomicron VPI-5482],5XXN_B Crystal Structure of mutant (D286N) beta-glucosidase from Bacteroides thetaiotaomicron in complex with sophorose [Bacteroides thetaiotaomicron VPI-5482],5XXO_A Crystal structure of mutant (D286N) GH3 beta-glucosidase from Bacteroides thetaiotaomicron in complex with sophorotriose [Bacteroides thetaiotaomicron VPI-5482],5XXO_B Crystal structure of mutant (D286N) GH3 beta-glucosidase from Bacteroides thetaiotaomicron in complex with sophorotriose [Bacteroides thetaiotaomicron VPI-5482] |
5TF0_A | 2.40e-267 | 330 | 1059 | 10 | 751 | CrystalStructure of Glycosil Hydrolase Family 3 N-Terminal Domain Protein from Bacteroides intestinalis [Bacteroides intestinalis DSM 17393],5TF0_B Crystal Structure of Glycosil Hydrolase Family 3 N-Terminal Domain Protein from Bacteroides intestinalis [Bacteroides intestinalis DSM 17393] |
6R5I_A | 2.90e-211 | 330 | 1058 | 4 | 730 | ChainA, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5I_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5N_A Chain A, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5N_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1] |
6R5O_A | 1.62e-210 | 330 | 1058 | 4 | 730 | ChainA, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5O_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5R_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5T_A Chain A, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5T_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5U_A Chain A, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5U_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5V_A Chain A, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1],6R5V_B Chain B, Periplasmic beta-glucosidase [Pseudomonas aeruginosa PAO1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q56078 | 3.59e-209 | 330 | 1059 | 35 | 763 | Periplasmic beta-glucosidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=bglX PE=3 SV=2 |
P33363 | 4.96e-206 | 330 | 1059 | 35 | 763 | Periplasmic beta-glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=bglX PE=3 SV=2 |
T2KMH0 | 5.47e-127 | 352 | 1050 | 18 | 710 | Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22130 PE=1 SV=1 |
T2KMH9 | 8.04e-105 | 333 | 1059 | 40 | 753 | Putative beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22230 PE=2 SV=1 |
A7LXU3 | 1.61e-101 | 322 | 1047 | 28 | 762 | Beta-glucosidase BoGH3B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02659 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000482 | 0.638378 | 0.360463 | 0.000238 | 0.000231 | 0.000194 |
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