Species | Bacteroides sp900555635 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900555635 | |||||||||||
CAZyme ID | MGYG000004899_00934 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 391977; End: 395291 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 357 | 666 | 2e-116 | 0.9869706840390879 |
GH43 | 52 | 307 | 4.1e-101 | 0.9878048780487805 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18825 | GH43_CtGH43-like | 2.97e-160 | 44 | 323 | 1 | 285 | Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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. |
pfam01301 | Glyco_hydro_35 | 1.98e-154 | 355 | 664 | 1 | 313 | Glycosyl hydrolases family 35. |
cd08985 | GH43_CtGH43-like | 5.53e-119 | 44 | 323 | 1 | 273 | Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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. |
cd18826 | GH43_CtGH43-like | 4.51e-110 | 44 | 323 | 1 | 269 | Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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. |
cd18822 | GH43_CtGH43-like | 5.51e-107 | 44 | 323 | 1 | 266 | Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT33927.1 | 0.0 | 1 | 1104 | 1 | 1106 |
QUT64844.1 | 0.0 | 1 | 1104 | 1 | 1106 |
QUT62346.1 | 0.0 | 1 | 1104 | 1 | 1106 |
QQA30849.1 | 0.0 | 1 | 1104 | 1 | 1106 |
QUU00371.1 | 0.0 | 1 | 1104 | 1 | 1106 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EON_A | 0.0 | 346 | 1103 | 25 | 778 | GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482] |
3D3A_A | 3.15e-266 | 346 | 953 | 5 | 605 | Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
4MAD_A | 1.33e-144 | 355 | 921 | 23 | 578 | ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans] |
3WF3_A | 9.74e-115 | 353 | 905 | 39 | 605 | Crystalstructure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_B Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_C Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF3_D Crystal structure of human beta-galactosidase mutant I51T in complex with Galactose [Homo sapiens],3WF4_A Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_B Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_C Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens],3WF4_D Crystal structure of human beta-galactosidase mutant I51T in complex with 6S-NBI-DGJ [Homo sapiens] |
3THC_A | 9.77e-115 | 353 | 905 | 15 | 581 | Crystalstructure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_B Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_C Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_D Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THD_A Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_B Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_C Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_D Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48982 | 9.91e-118 | 356 | 904 | 37 | 573 | Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1 |
P16278 | 1.01e-113 | 353 | 905 | 38 | 604 | Beta-galactosidase OS=Homo sapiens OX=9606 GN=GLB1 PE=1 SV=2 |
Q95LV1 | 7.62e-113 | 356 | 962 | 39 | 645 | Beta-galactosidase-1-like protein OS=Macaca fascicularis OX=9541 GN=GLB1L PE=2 SV=1 |
Q5R7P4 | 2.78e-112 | 356 | 905 | 41 | 604 | Beta-galactosidase OS=Pongo abelii OX=9601 GN=GLB1 PE=2 SV=1 |
Q6UWU2 | 4.00e-112 | 352 | 962 | 35 | 645 | Beta-galactosidase-1-like protein OS=Homo sapiens OX=9606 GN=GLB1L PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000651 | 0.830232 | 0.168271 | 0.000322 | 0.000263 | 0.000233 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.