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CAZyme Information: MGYG000000488_00136

You are here: Home > Sequence: MGYG000000488_00136

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 Anaeroplasma sp900767915
Lineage Bacteria; Firmicutes; Bacilli; Acholeplasmatales; Anaeroplasmataceae; Anaeroplasma; Anaeroplasma sp900767915
CAZyme ID MGYG000000488_00136
CAZy Family GH43
CAZyme Description Non-reducing end alpha-L-arabinofuranosidase BoGH43A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
492 56613.69 7.3985
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000488 1945837 MAG Fiji Oceania
Gene Location Start: 148353;  End: 149831  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000488_00136.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 5 273 4.6e-86 0.992619926199262

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09001 GH43_FsAxh1-like 1.57e-108 3 276 2 270
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) 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. 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. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). 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 4.39e-49 3 273 1 281
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.
cd08989 GH43_XYL-like 2.06e-39 5 266 1 269
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.
cd18617 GH43_XynB-like 1.56e-38 5 274 1 284
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases 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. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. 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.
COG3507 XynB2 2.02e-33 1 320 19 360
Beta-xylosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHW58600.1 1.05e-126 3 491 39 540
AXB58263.1 2.69e-124 3 491 33 529
QSB28907.1 8.31e-124 3 476 33 515
QCK13289.1 5.39e-123 3 492 38 542
QPH38248.1 1.85e-122 3 490 38 540

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MLY_A 2.23e-34 5 490 23 511
ChainA, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_B Chain B, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_C Chain C, Bifunctional GH43-CE protein [Bacteroides eggerthii],6MLY_D Chain D, Bifunctional GH43-CE protein [Bacteroides eggerthii]
5Z5D_A 1.06e-30 1 475 1 492
Crystalstructure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 [Geobacillus thermoleovorans],5Z5F_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose [Geobacillus thermoleovorans],5Z5H_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with D-xylose [Geobacillus thermoleovorans],5Z5I_A Crystal structure of a thermostable glycoside hydrolase family 43 {beta}-1,4-xylosidase from Geobacillus thermoleovorans IT-08 in complex with L-arabinose and D-xylose [Geobacillus thermoleovorans]
6MS3_A 4.32e-28 3 323 30 357
Crystalstructure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580],6MS3_B Crystal structure of the GH43 protein BlXynB mutant (K247S) from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
6MS2_A 7.87e-28 3 323 30 357
Crystalstructure of the GH43 BlXynB protein from Bacillus licheniformis [Bacillus licheniformis DSM 13 = ATCC 14580]
3C2U_A 2.11e-26 5 320 5 347
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9WXE8 2.37e-63 13 397 46 414
Putative beta-xylosidase OS=Prevotella ruminicola OX=839 PE=3 SV=2
T2KN85 7.34e-37 3 480 51 573
Beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22160 PE=1 SV=1
A7LXT8 2.34e-22 3 490 23 519
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 2.46e-21 5 397 29 423
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
A9ZND1 1.93e-20 5 328 7 357
Xylan 1,3-beta-xylosidase OS=Vibrio sp. OX=678 GN=xloA PE=1 SV=1

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
1.000050 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000488_00136.