Species | UBA4372 sp900766785 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; UBA4372; UBA4372 sp900766785 | |||||||||||
CAZyme ID | MGYG000003420_00649 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3183; End: 6455 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 344 | 660 | 1.4e-116 | 0.993485342019544 |
GH43 | 74 | 310 | 9.2e-76 | 0.9914163090128756 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01301 | Glyco_hydro_35 | 2.64e-154 | 343 | 657 | 1 | 313 | Glycosyl hydrolases family 35. |
cd08983 | GH43_Bt3655-like | 2.98e-73 | 57 | 323 | 1 | 260 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. 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 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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. |
PLN03059 | PLN03059 | 5.07e-56 | 343 | 916 | 36 | 715 | beta-galactosidase; Provisional |
COG1874 | GanA | 3.44e-42 | 342 | 917 | 6 | 593 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
cd08978 | GH_F | 2.29e-11 | 77 | 313 | 1 | 239 | Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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 |
---|---|---|---|---|---|
AGB27610.1 | 0.0 | 337 | 1088 | 32 | 796 |
QVJ81893.1 | 0.0 | 337 | 1088 | 24 | 786 |
ADE83089.1 | 0.0 | 337 | 1088 | 24 | 786 |
BCS84536.1 | 0.0 | 337 | 1088 | 30 | 778 |
VEH15027.1 | 0.0 | 324 | 1088 | 17 | 783 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EON_A | 1.03e-293 | 334 | 1088 | 25 | 772 | GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482] |
3D3A_A | 3.37e-237 | 332 | 946 | 3 | 605 | Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
4MAD_A | 5.06e-128 | 341 | 914 | 21 | 578 | ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans] |
3WF3_A | 4.03e-113 | 343 | 930 | 41 | 634 | 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 | 4.06e-113 | 343 | 930 | 17 | 610 | 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 |
---|---|---|---|---|---|---|
P16278 | 4.17e-112 | 343 | 930 | 40 | 633 | Beta-galactosidase OS=Homo sapiens OX=9606 GN=GLB1 PE=1 SV=2 |
Q95LV1 | 6.02e-112 | 344 | 956 | 39 | 649 | Beta-galactosidase-1-like protein OS=Macaca fascicularis OX=9541 GN=GLB1L PE=2 SV=1 |
Q60HF6 | 1.80e-111 | 344 | 930 | 41 | 633 | Beta-galactosidase OS=Macaca fascicularis OX=9541 GN=GLB1 PE=2 SV=1 |
Q6UWU2 | 2.27e-111 | 340 | 956 | 35 | 649 | Beta-galactosidase-1-like protein OS=Homo sapiens OX=9606 GN=GLB1L PE=2 SV=1 |
P48982 | 2.54e-110 | 336 | 896 | 29 | 572 | Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.260979 | 0.677977 | 0.059980 | 0.000365 | 0.000286 | 0.000388 |
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