You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002937_01607
You are here: Home > Sequence: MGYG000002937_01607
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Sporolactobacillus sp900543345 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_G; Sporolactobacillaceae; Sporolactobacillus; Sporolactobacillus sp900543345 | |||||||||||
| CAZyme ID | MGYG000002937_01607 | |||||||||||
| CAZy Family | GH43 | |||||||||||
| CAZyme Description | Beta-xylosidase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 6422; End: 7861 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH43 | 1 | 242 | 1.4e-97 | 0.791095890410959 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3507 | XynB2 | 0.0 | 1 | 476 | 81 | 549 | Beta-xylosidase [Carbohydrate transport and metabolism]. |
| cd09000 | GH43_SXA-like | 5.83e-133 | 1 | 242 | 59 | 290 | Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA. This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These 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. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. 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. |
| cd08989 | GH43_XYL-like | 9.10e-71 | 1 | 237 | 59 | 272 | Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). 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 | 6.35e-69 | 5 | 242 | 62 | 281 | 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. |
| pfam17851 | GH43_C2 | 1.82e-66 | 273 | 474 | 2 | 203 | Beta xylosidase C-terminal Concanavalin A-like domain. This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGT14431.1 | 5.61e-303 | 1 | 476 | 63 | 538 |
| SQG82162.1 | 5.61e-303 | 1 | 476 | 63 | 538 |
| QOX68184.1 | 2.28e-302 | 1 | 476 | 63 | 538 |
| ANN47934.1 | 2.28e-302 | 1 | 476 | 63 | 538 |
| BAN07996.1 | 2.28e-302 | 1 | 476 | 63 | 538 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1Y7B_A | 2.83e-160 | 1 | 475 | 64 | 534 | Beta-d-xylosidase,A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_B Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_C Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824],1Y7B_D Beta-d-xylosidase, A Family 43 Glycoside Hydrolase [Clostridium acetobutylicum ATCC 824] |
| 3C2U_A | 7.06e-160 | 1 | 477 | 63 | 538 | Structureof the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_B Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_C Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium],3C2U_D Structure of the two subsite D-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane [Selenomonas ruminantium] |
| 1YI7_A | 3.24e-159 | 2 | 475 | 65 | 534 | Beta-d-xylosidase(selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_B Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_C Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824],1YI7_D Beta-d-xylosidase (selenomethionine) XYND from Clostridium Acetobutylicum [Clostridium acetobutylicum ATCC 824] |
| 6IFE_A | 4.67e-151 | 1 | 477 | 81 | 552 | AGlycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus],6IFE_B A Glycoside Hydrolase Family 43 beta-Xylosidase [Bacillus pumilus] |
| 5ZQJ_A | 1.27e-150 | 1 | 475 | 63 | 532 | Crystalstructure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus],5ZQJ_B Crystal structure of beta-xylosidase from Bacillus pumilus [Bacillus pumilus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P07129 | 5.75e-150 | 1 | 475 | 63 | 532 | Beta-xylosidase OS=Bacillus pumilus OX=1408 GN=xynB PE=1 SV=2 |
| P94489 | 1.08e-149 | 1 | 475 | 63 | 532 | Beta-xylosidase OS=Bacillus subtilis (strain 168) OX=224308 GN=xynB PE=1 SV=2 |
| P77713 | 3.66e-143 | 1 | 476 | 63 | 536 | Putative beta-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yagH PE=3 SV=1 |
| A9ZND1 | 5.35e-87 | 1 | 475 | 65 | 534 | Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1 |
| A7LXU0 | 2.33e-43 | 1 | 477 | 88 | 529 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.999946 | 0.000083 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |