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CAZyme Information: MGYG000000152_04899

You are here: Home > Sequence: MGYG000000152_04899

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 Lacrimispora sp902363835
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lacrimispora; Lacrimispora sp902363835
CAZyme ID MGYG000000152_04899
CAZy Family GH67
CAZyme Description Xylan alpha-(1->2)-glucuronosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
650 MGYG000000152_31|CGC1 74487.99 6.034
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000152 6260407 Isolate United Kingdom Europe
Gene Location Start: 8722;  End: 10674  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 64 646 5.1e-261 0.8759342301943199

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3661 AguA2 0.0 66 649 92 682
Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488 Glyco_hydro_67M 0.0 105 422 10 324
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 9.42e-122 424 647 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 5.09e-04 8 94 1 118
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
SET65514.1 0.0 1 650 2 651
QIK51557.1 6.62e-301 5 649 3 650
ATF73792.1 3.13e-292 3 649 2 651
AYJ46832.1 4.44e-292 3 649 2 651
QGN31111.1 1.47e-290 3 649 2 651

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1MQP_A 1.04e-249 81 649 106 678
TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1K9D_A 2.10e-249 81 649 106 678
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]
1MQR_A 2.97e-249 81 649 106 678
ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9E_A 5.97e-249 81 649 106 678
ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus]
1GQI_A 2.09e-134 66 641 93 670
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 5.71e-249 81 649 106 678
Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105 5.49e-215 56 649 74 673
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
Q5AQZ4 9.58e-164 68 646 113 699
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
A2R3X3 2.21e-160 68 646 113 692
Probable alpha-glucuronidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aguA PE=3 SV=1
Q96WX9 3.12e-160 68 646 113 692
Probable alpha-glucuronidase A OS=Aspergillus niger OX=5061 GN=aguA PE=2 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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000152_04899.