Species | UMGS2055 sp900557635 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS2055; UMGS2055 sp900557635 | |||||||||||
CAZyme ID | MGYG000003996_00669 | |||||||||||
CAZy Family | GH43 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4076; End: 6847 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH43 | 185 | 422 | 1.1e-53 | 0.9887640449438202 |
CBM66 | 755 | 911 | 3.5e-19 | 0.9161290322580645 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08991 | GH43_HoAraf43-like | 4.17e-76 | 176 | 431 | 1 | 283 | Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) 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. |
pfam04616 | Glyco_hydro_43 | 1.29e-45 | 157 | 421 | 1 | 276 | Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
cd18608 | GH43_F5-8_typeC-like | 1.55e-37 | 175 | 422 | 1 | 269 | Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 domain. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8), and beta-galactosidase (EC 3.2.1.145) activities, and some as F5/8 type C domain (also known as the discoidin (DS) domain)-containing proteins. Most contain a F5/8 type C domain C-terminal to the GH43 domain. 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. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. 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. |
cd08978 | GH_F | 6.18e-36 | 177 | 400 | 2 | 249 | 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. |
cd09004 | GH43_bXyl-like | 2.34e-31 | 177 | 423 | 2 | 260 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASK62826.1 | 2.47e-126 | 144 | 912 | 35 | 834 |
ASS67957.1 | 1.08e-122 | 157 | 910 | 24 | 816 |
QMV41051.1 | 1.55e-122 | 157 | 922 | 39 | 829 |
ANY76047.1 | 2.15e-121 | 151 | 923 | 3 | 783 |
AZN38608.1 | 2.72e-120 | 140 | 882 | 28 | 779 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4QQS_A | 7.15e-29 | 156 | 438 | 4 | 312 | Crystalstructure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168],4QQS_B Crystal structure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168] |
5A8C_A | 2.45e-10 | 177 | 340 | 39 | 229 | ChainA, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus],5A8D_A Chain A, CARBOHYDRATE BINDING FAMILY 6 [Acetivibrio thermocellus] |
3VSF_A | 4.12e-10 | 180 | 388 | 63 | 286 | ChainA, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405] |
5JOW_A | 1.12e-08 | 157 | 441 | 13 | 306 | Bacteroidesovatus Xyloglucan PUL GH43A [Bacteroides ovatus ATCC 8483],5JOW_B Bacteroides ovatus Xyloglucan PUL GH43A [Bacteroides ovatus ATCC 8483],5JOX_A Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraDNJ [Bacteroides ovatus],5JOX_B Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraDNJ [Bacteroides ovatus],5JOY_A Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraLOG [Bacteroides ovatus],5JOY_B Bacteroides ovatus Xyloglucan PUL GH43A in complex with AraLOG [Bacteroides ovatus] |
7ERL_A | 1.17e-08 | 175 | 391 | 38 | 289 | ChainA, Beta-xylanase [Bacteroides intestinalis],7ERL_B Chain B, Beta-xylanase [Bacteroides intestinalis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A7LXT8 | 3.58e-08 | 152 | 441 | 18 | 316 | Non-reducing end alpha-L-arabinofuranosidase BoGH43A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02654 PE=1 SV=1 |
A7LXU0 | 2.48e-07 | 156 | 612 | 26 | 511 | Non-reducing end alpha-L-arabinofuranosidase BoGH43B OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02656 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999747 | 0.000293 | 0.000006 | 0.000000 | 0.000000 | 0.000001 |
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