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CAZyme Information: MGYG000002273_01622

You are here: Home > Sequence: MGYG000002273_01622

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 Bacteroides stercorirosoris
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides stercorirosoris
CAZyme ID MGYG000002273_01622
CAZy Family GH10
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
642 MGYG000002273_8|CGC4 72176.63 5.1334
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002273 6091524 Isolate China Asia
Gene Location Start: 97271;  End: 99199  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002273_01622.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH10 30 368 3.5e-102 0.9900990099009901
GH43 410 638 1.6e-83 0.7615658362989324

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd18617 GH43_XynB-like 1.38e-120 411 638 1 219
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 4.30e-114 30 368 1 310
Glycosyl hydrolase family 10.
smart00633 Glyco_10 1.95e-105 73 361 1 258
Glycosyl hydrolase family 10.
COG3693 XynA 6.32e-94 53 368 47 339
Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd08989 GH43_XYL-like 1.72e-72 411 638 1 213
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
EDV05059.1 0.0 1 636 1 636
ALJ61536.1 0.0 1 636 31 655
QDO69420.1 0.0 1 636 1 625
QUT92894.1 0.0 16 636 1 610
ALJ61519.1 1.16e-204 14 370 15 371

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4PMU_A 1.62e-100 29 367 2 350
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 1.67e-100 29 367 3 351
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 7.16e-93 28 361 11 333
Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
2CNC_A 3.73e-90 30 368 36 376
Family10 xylanase [Cellvibrio mixtus]
1UQY_A 8.10e-90 30 368 27 367
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 5.12e-173 1 368 1 370
Endo-1,4-beta-xylanase A OS=Bacteroides ovatus OX=28116 GN=xylI PE=2 SV=1
P48789 2.49e-128 28 368 24 366
Endo-1,4-beta-xylanase A OS=Prevotella ruminicola OX=839 GN=xynA PE=3 SV=1
Q12603 1.38e-76 28 368 33 351
Beta-1,4-xylanase OS=Dictyoglomus thermophilum OX=14 GN=xynA PE=3 SV=1
O69231 9.15e-74 28 360 6 322
Endo-1,4-beta-xylanase B OS=Paenibacillus barcinonensis OX=198119 GN=xynB PE=1 SV=1
D5EY13 1.65e-71 1 366 1 366
Endo-1,4-beta-xylanase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=xyn10D-fae1A PE=1 SV=1

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 1.000035 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002273_01622.