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CAZyme Information: MGYG000000042_00679

You are here: Home > Sequence: MGYG000000042_00679

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 Phocaeicola sp900066445
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900066445
CAZyme ID MGYG000000042_00679
CAZy Family GH31
CAZyme Description Alpha-xylosidase BoGH31A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
439 MGYG000000042_2|CGC2 50110.23 6.3716
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000042 3613218 Isolate United Kingdom Europe
Gene Location Start: 61582;  End: 62901  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000042_00679.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06591 GH31_xylosidase_XylS 1.59e-50 343 436 1 94
xylosidase XylS-like. XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.
pfam01055 Glyco_hydro_31 1.29e-34 326 432 2 107
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
COG1501 YicI 4.86e-27 89 432 110 345
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
cd06604 GH31_glucosidase_II_MalA 1.32e-15 343 423 1 79
Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.
cd14752 GH31_N 6.30e-14 126 193 6 82
N-terminal domain of glycosyl hydrolase family 31 (GH31). This family is found N-terminal to the glycosyl-hydrolase domain of Glycoside hydrolase family 31 (GH31). GH31 includes the glycoside hydrolases alpha-glucosidase (EC 3.2.1.20), alpha-1,3-glucosidase (EC 3.2.1.84), alpha-xylosidase (EC 3.2.1.177), sucrase-isomaltase (EC 3.2.1.48 and EC 3.2.1.10), as well as alpha-glucan lyase (EC 4.2.2.13). All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite-1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues of the catalytic domain have been identified as the catalytic nucleophile and the acid/base, respectively. A loop of the N-terminal beta-sandwich domain is part of the active site pocket.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDO68462.1 1.41e-160 26 439 32 446
BCS84774.1 2.07e-156 38 439 33 437
QUU07681.1 8.64e-153 41 439 48 450
QVJ82136.1 6.84e-150 38 439 21 402
ADE82590.1 1.09e-148 38 439 21 402

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JOU_A 3.16e-46 64 431 75 485
Bacteroidesovatus Xyloglucan PUL GH31 [Bacteroides ovatus],5JOV_A Bacteroides ovatus Xyloglucan PUL GH31 with bound 5FIdoF [Bacteroides ovatus]
2XVG_A 5.49e-42 61 436 91 518
crystalstructure of alpha-xylosidase (GH31) from Cellvibrio japonicus [Cellvibrio japonicus],2XVK_A crystal structure of alpha-xylosidase (GH31) from Cellvibrio japonicus in complex with 5-fluoro-alpha-D-xylopyranosyl fluoride [Cellvibrio japonicus],2XVL_A crystal structure of alpha-xylosidase (GH31) from Cellvibrio japonicus in complex with Pentaerythritol propoxylate (5 4 PO OH) [Cellvibrio japonicus]
7KMP_A 7.34e-39 68 436 121 521
ChainA, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306],7KNC_A Chain A, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306]
5DJW_A 2.84e-13 319 435 139 258
Crystalstructure of Family 31 alpha-glucosidase (BT_3299) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5DJW_B Crystal structure of Family 31 alpha-glucosidase (BT_3299) from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
6JR6_A 1.52e-10 309 427 224 340
Flavobacteriumjohnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR6_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A [Flavobacterium johnsoniae UW101],6JR7_A Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_B Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_C Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101],6JR7_D Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A7LXT0 1.73e-45 64 431 74 484
Alpha-xylosidase BoGH31A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02646 PE=1 SV=1
Q9P999 3.27e-38 35 429 4 298
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
Q01336 5.51e-17 122 438 128 329
Uncharacterized family 31 glucosidase ORF2 (Fragment) OS=Pseudescherichia vulneris OX=566 PE=3 SV=1
Q9F234 3.70e-11 305 423 214 330
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
A2QTU5 1.04e-09 312 436 224 350
Alpha-xylosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=axlA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000373 0.998804 0.000360 0.000154 0.000142 0.000145

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000042_00679.