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CAZyme Information: MGYG000002585_00566

You are here: Home > Sequence: MGYG000002585_00566

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000002585_00566
CAZy Family GH10
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
908 MGYG000002585_7|CGC2 100700.23 5.0762
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002585 2701793 MAG China Asia
Gene Location Start: 48337;  End: 51063  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002585_00566.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 399 693 4.7e-114 0.9928825622775801
GH10 33 370 1.3e-102 0.9867986798679867

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18617 GH43_XynB-like 2.04e-164 399 695 1 285
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.
pfam00331 Glyco_hydro_10 2.74e-111 33 364 1 303
Glycosyl hydrolase family 10.
smart00633 Glyco_10 9.88e-103 76 364 1 258
Glycosyl hydrolase family 10.
COG3507 XynB2 8.70e-99 399 906 23 534
Beta-xylosidase [Carbohydrate transport and metabolism].
cd09000 GH43_SXA-like 3.60e-92 399 693 1 290
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALJ61536.1 0.0 1 905 31 927
QUT92894.1 0.0 19 905 3 882
QDO69420.1 0.0 1 906 1 898
EDV05059.1 0.0 1 906 1 909
QCD38829.1 5.95e-207 375 902 30 547

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7ERL_A 6.13e-115 399 902 31 538
ChainA, Beta-xylanase [Bacteroides intestinalis],7ERL_B Chain B, Beta-xylanase [Bacteroides intestinalis]
4PMU_A 6.38e-93 32 375 2 355
Crystalstructure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_B Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_C Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_D Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_E Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_F Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306]
4PMV_A 6.59e-93 32 375 3 356
Crystalstructure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P43212) [Xanthomonas citri pv. citri str. 306],4PMV_B Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P43212) [Xanthomonas citri pv. citri str. 306]
6FHE_A 5.38e-92 31 364 11 333
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
1UQY_A 2.59e-91 30 363 24 359
XylanaseXyn10B mutant (E262S) from Cellvibrio mixtus in complex with xylopentaose [Cellvibrio mixtus],1UQZ_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with 4-O-methyl glucuronic acid [Cellvibrio mixtus],1UR1_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with arabinofuranose alpha-1,3 linked to xylobiose [Cellvibrio mixtus],1UR2_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with arabinofuranose alpha 1,3 linked to xylotriose [Cellvibrio mixtus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P49942 3.15e-171 1 370 1 369
Endo-1,4-beta-xylanase A OS=Bacteroides ovatus OX=28116 GN=xylI PE=2 SV=1
P48789 2.90e-114 30 370 23 365
Endo-1,4-beta-xylanase A OS=Prevotella ruminicola OX=839 GN=xynA PE=3 SV=1
P45982 1.25e-84 398 904 5 499
Xylosidase/arabinosidase OS=Butyrivibrio fibrisolvens OX=831 GN=xylB PE=3 SV=1
A7LXT8 1.14e-79 392 902 18 501
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 1.57e-74 399 908 29 514
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 LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000093 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002585_00566.