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CAZyme Information: MGYG000000325_02544

You are here: Home > Sequence: MGYG000000325_02544

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
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-95;
CAZyme ID MGYG000000325_02544
CAZy Family GH67
CAZyme Description Xylan alpha-(1->2)-glucuronosidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
664 75740.31 4.8266
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000325 3194566 MAG Sweden Europe
Gene Location Start: 1337;  End: 3331  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 6 661 5.7e-272 0.9940209267563528

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3661 AguA2 0.0 6 664 9 682
Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488 Glyco_hydro_67M 0.0 112 438 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 2.25e-140 440 662 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 1.33e-05 7 109 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
AOZ95219.1 0.0 4 664 6 662
ADL32927.1 0.0 4 664 6 668
BCJ97914.1 1.96e-298 8 664 7 668
ABX43513.1 7.22e-293 8 664 24 684
CUH91818.1 4.31e-289 4 664 3 673

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1K9D_A 1.14e-247 8 664 9 678
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]
1MQP_A 2.30e-247 75 664 83 678
TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1MQR_A 6.55e-247 75 664 83 678
ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9E_A 1.32e-246 75 664 83 678
ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus]
1GQI_A 3.29e-144 7 654 6 668
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 1.26e-246 75 664 83 678
Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105 6.48e-243 81 664 86 673
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 2.20e-166 36 662 53 700
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
Q0CJP9 1.59e-161 8 662 26 694
Probable alpha-glucuronidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aguA PE=3 SV=1
B8NGU1 2.98e-161 81 662 112 692
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

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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000325_02544.