logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004479_00704

You are here: Home > Sequence: MGYG000004479_00704

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 mediterraneensis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola mediterraneensis
CAZyme ID MGYG000004479_00704
CAZy Family GH31
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
357 MGYG000004479_6|CGC1 40729.4 4.7683
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004479 3712458 MAG Israel Asia
Gene Location Start: 52974;  End: 54047  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004479_00704.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06591 GH31_xylosidase_XylS 8.63e-53 246 355 1 109
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.
COG1501 YicI 7.07e-42 91 352 82 361
Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
pfam01055 Glyco_hydro_31 3.22e-38 227 354 1 128
Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
cd14752 GH31_N 7.26e-22 143 246 8 122
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.
cd06593 GH31_xylosidase_YicI 3.66e-19 246 352 1 106
alpha-xylosidase YicI-like. YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). 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 YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALJ61510.1 7.71e-145 19 357 16 353
QUT92920.1 7.71e-145 19 357 16 353
QUU00762.1 3.84e-130 30 357 30 353
QUT65260.1 3.84e-130 30 357 30 353
QMI79564.1 3.94e-130 30 357 30 353

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2XVG_A 5.11e-39 218 354 397 532
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 1.25e-38 218 353 400 534
ChainA, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306],7KNC_A Chain A, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306]
5JOU_A 3.93e-36 75 353 74 503
Bacteroidesovatus Xyloglucan PUL GH31 [Bacteroides ovatus],5JOV_A Bacteroides ovatus Xyloglucan PUL GH31 with bound 5FIdoF [Bacteroides ovatus]
6DRU_A 1.08e-12 149 352 141 344
Xylosidasefrom Aspergillus niger [Aspergillus niger],6DRU_B Xylosidase from Aspergillus niger [Aspergillus niger]
4B9Y_A 1.89e-08 226 330 234 340
CrystalStructure of Apo Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31 [Cellvibrio japonicus],4B9Z_A Crystal Structure of Agd31B, alpha-transglucosylase, complexed with Acarbose [Cellvibrio japonicus],4BA0_A Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF [Cellvibrio japonicus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9P999 6.69e-57 39 352 1 317
Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
A7LXT0 2.15e-35 75 353 73 502
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
Q01336 2.02e-22 74 352 44 339
Uncharacterized family 31 glucosidase ORF2 (Fragment) OS=Pseudescherichia vulneris OX=566 PE=3 SV=1
Q9F234 3.00e-22 42 329 43 332
Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
A2QTU5 6.00e-12 149 352 159 362
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.574337 0.417053 0.005428 0.001232 0.000647 0.001311

TMHMM  Annotations      download full data without filtering help

start end
7 29