| Species | Alkalihalobacillus alcalophilus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_H; Bacillaceae_D; Alkalihalobacillus; Alkalihalobacillus alcalophilus | |||||||||||
| CAZyme ID | MGYG000002326_01224 | |||||||||||
| CAZy Family | GH67 | |||||||||||
| CAZyme Description | Xylan alpha-(1->2)-glucuronosidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11588; End: 13648 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH67 | 10 | 683 | 0 | 0.9970104633781763 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3661 | AguA2 | 0.0 | 11 | 686 | 8 | 682 | Alpha-glucuronidase [Carbohydrate transport and metabolism]. |
| pfam07488 | Glyco_hydro_67M | 0.0 | 132 | 459 | 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 | 1.33e-143 | 461 | 684 | 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 | 1.27e-19 | 13 | 128 | 1 | 119 | 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). |
| NF033535 | lass_lactam_cya | 7.19e-04 | 532 | 679 | 346 | 499 | lasso peptide isopeptide bond-forming cyclase. Members of this family are the isopeptide bond-forming cyclase of lasso peptide biosynthesis systems, from a subgroup that contains primarily cyanobacterial examples. These proteins resemble the glutamine-hydrolyzing asparagine synthase AsnB (EC 6.3.5.4). |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BAB04780.1 | 0.0 | 11 | 686 | 8 | 680 |
| QDP42219.1 | 0.0 | 9 | 686 | 8 | 690 |
| ARA99631.1 | 0.0 | 13 | 686 | 8 | 683 |
| QNU31482.1 | 0.0 | 13 | 686 | 8 | 683 |
| ATO35839.1 | 0.0 | 13 | 686 | 8 | 683 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1K9D_A | 0.0 | 13 | 686 | 8 | 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 | 0.0 | 13 | 686 | 8 | 678 | ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus] |
| 1MQP_A | 0.0 | 13 | 686 | 8 | 678 | TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus] |
| 1MQR_A | 0.0 | 13 | 686 | 8 | 678 | ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus] |
| 1GQI_A | 5.26e-171 | 9 | 676 | 2 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q09LY5 | 0.0 | 13 | 686 | 8 | 678 | Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1 |
| P96105 | 4.69e-266 | 94 | 686 | 83 | 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 | 1.23e-185 | 11 | 683 | 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 | 3.10e-182 | 13 | 683 | 23 | 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 |
| Q2UFP4 | 4.85e-181 | 11 | 683 | 22 | 687 | Probable alpha-glucuronidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aguA PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000039 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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