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CAZyme Information: MGYG000001518_02329

You are here: Home > Sequence: MGYG000001518_02329

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 Gorillibacterium timonense
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Gorillibacterium; Gorillibacterium timonense
CAZyme ID MGYG000001518_02329
CAZy Family GH67
CAZyme Description Xylan alpha-(1->2)-glucuronosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
672 MGYG000001518_6|CGC10 76806.45 5.5956
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001518 5263339 Isolate not provided not provided
Gene Location Start: 858116;  End: 860134  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.139 3.2.1.131

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH67 5 669 5.7e-289 0.9955156950672646

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3661 AguA2 0.0 3 672 6 682
Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488 Glyco_hydro_67M 0.0 118 445 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 1.31e-144 447 670 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 9.78e-09 7 115 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
ANY73872.1 0.0 2 672 3 699
QOT09613.1 0.0 1 672 1 692
ACX68300.1 0.0 2 672 3 692
AVV55991.1 0.0 2 672 3 696
AWP30526.1 0.0 2 672 3 696

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1MQP_A 1.25e-312 13 672 33 678
TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1MQR_A 3.57e-312 13 672 33 678
ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9D_A 7.19e-312 13 672 33 678
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]
1K9E_A 7.19e-312 13 672 33 678
ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus]
1GQI_A 6.61e-159 5 662 4 668
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q09LY5 6.85e-312 13 672 33 678
Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105 4.64e-250 8 672 7 673
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
B8NGU1 1.70e-187 5 669 22 691
Probable alpha-glucuronidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aguA PE=3 SV=1
Q5AQZ4 3.44e-186 100 669 126 699
Alpha-glucuronidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aguA PE=1 SV=1
O42814 4.56e-185 13 669 57 692
Alpha-glucuronidase A OS=Aspergillus tubingensis OX=5068 GN=aguA 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
1.000041 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001518_02329.