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CAZyme Information: MGYG000000224_00087

You are here: Home > Sequence: MGYG000000224_00087

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 sp003545565
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp003545565
CAZyme ID MGYG000000224_00087
CAZy Family GH67
CAZyme Description Extracellular xylan exo-alpha-(1->2)-glucuronosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
667 MGYG000000224_1|CGC2 76695.26 7.3408
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000224 3747034 Isolate China Asia
Gene Location Start: 118515;  End: 120518  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.139 3.2.1.131 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH67 50 633 5.6e-266 0.9013452914798207

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3661 AguA2 0.0 21 630 4 674
Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488 Glyco_hydro_67M 0.0 108 408 1 324
Glycosyl hydrolase family 67 middle domain. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuronidase.
pfam07477 Glyco_hydro_67C 6.76e-135 410 636 1 223
Glycosyl hydrolase family 67 C-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C terminal region of alpha-glucuronidase which is mainly alpha-helical. It wraps around the catalytic domain (pfam07488), making additional interactions both with the N-terminal domain (pfam03648) of its parent monomer and also forming the majority of the dimer-surface with the equivalent C-terminal domain of the other monomer of the dimer.
pfam03648 Glyco_hydro_67N 3.39e-04 27 105 1 120
Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ48276.1 0.0 1 667 1 669
QUT46117.1 0.0 1 667 26 694
QDO69417.1 0.0 4 667 3 676
EDV05062.1 0.0 4 667 3 676
QUU00908.1 0.0 1 667 1 668

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1GQI_A 5.12e-234 22 643 1 683
Structureof Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQI_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQJ_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQJ_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQK_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQK_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQL_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus],1GQL_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus]
1H41_A 4.14e-233 22 643 1 683
Pseudomonascellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid [Cellvibrio japonicus],1H41_B Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid [Cellvibrio japonicus]
1MQP_A 5.03e-173 38 629 25 669
TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1MQR_A 1.42e-172 38 629 25 669
ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9D_A 2.01e-172 38 629 25 669
The1.7 A crystal structure of alpha-D-glucuronidase, a family-67 glycoside hydrolase from Bacillus stearothermophilus T-1 [Geobacillus stearothermophilus],1L8N_A The 1.5A crystal structure of alpha-D-glucuronidase from Bacillus stearothermophilus T-1, complexed with 4-O-methyl-glucuronic acid and xylotriose [Geobacillus stearothermophilus],1MQQ_A THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM BACILLUS STEAROTHERMOPHILUS T-1 COMPLEXED WITH GLUCURONIC ACID [Geobacillus stearothermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B3PC73 6.32e-233 22 643 25 707
Extracellular xylan exo-alpha-(1->2)-glucuronosidase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=gla67A PE=1 SV=1
Q09LY5 2.75e-172 38 629 25 669
Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105 4.28e-167 61 630 70 665
Xylan alpha-(1->2)-glucuronosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=aguA PE=1 SV=2
A1CC12 9.38e-140 73 629 109 686
Probable alpha-glucuronidase A OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=aguA PE=3 SV=1
A1DD80 1.32e-139 20 629 18 686
Probable alpha-glucuronidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aguA PE=3 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
0.000918 0.998254 0.000248 0.000194 0.000181 0.000187

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000224_00087.