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CAZyme Information: MGYG000002300_00434
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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 cutis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides cutis | |||||||||||
| CAZyme ID | MGYG000002300_00434 | |||||||||||
| CAZy Family | GH30 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 545458; End: 546942 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH30 | 67 | 492 | 7e-149 | 0.988009592326139 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG5520 | XynC | 9.15e-55 | 60 | 493 | 28 | 429 | O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis]. |
| pfam02055 | Glyco_hydro_30 | 9.08e-43 | 82 | 422 | 3 | 345 | Glycosyl hydrolase family 30 TIM-barrel domain. |
| pfam17189 | Glyco_hydro_30C | 6.65e-17 | 428 | 490 | 1 | 63 | Glycosyl hydrolase family 30 beta sandwich domain. |
| pfam02057 | Glyco_hydro_59 | 2.09e-08 | 81 | 370 | 2 | 252 | Glycosyl hydrolase family 59. |
| pfam14587 | Glyco_hydr_30_2 | 9.40e-07 | 69 | 344 | 4 | 305 | O-Glycosyl hydrolase family 30. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QDO68126.1 | 2.48e-291 | 1 | 494 | 1 | 491 |
| ADV42636.1 | 1.28e-285 | 1 | 494 | 1 | 496 |
| QUT89171.1 | 1.51e-285 | 1 | 494 | 1 | 491 |
| ALJ59798.1 | 6.14e-285 | 1 | 494 | 1 | 491 |
| QUR49687.1 | 1.04e-250 | 39 | 492 | 25 | 478 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5NGK_A | 1.32e-234 | 39 | 494 | 37 | 492 | Theendo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron],5NGK_B The endo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron],5NGK_C The endo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron],5NGL_A The endo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron],5NGL_B The endo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron],5NGL_C The endo-beta1,6-glucanase BT3312 [Bacteroides thetaiotaomicron] |
| 2WNW_A | 1.43e-47 | 66 | 494 | 31 | 444 | Thecrystal structure of SrfJ from salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],2WNW_B The crystal structure of SrfJ from salmonella typhimurium [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2] |
| 2WKL_A | 1.85e-45 | 68 | 494 | 66 | 496 | Velaglucerasealfa [Homo sapiens],2WKL_B Velaglucerase alfa [Homo sapiens],5LVX_A Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_B Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_C Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],5LVX_D Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator [Homo sapiens],6TJK_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6TJK_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6TJQ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6TN1_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],6YTR_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],6Z3I_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_AAA Chain AAA, Lysosomal acid glucosylceramidase [Homo sapiens],7NWV_BBB Chain BBB, Lysosomal acid glucosylceramidase [Homo sapiens] |
| 3KE0_A | 2.56e-45 | 68 | 494 | 66 | 496 | ChainA, Glucosylceramidase [Homo sapiens],3KE0_B Chain B, Glucosylceramidase [Homo sapiens],3KEH_A Chain A, Glucocerebrosidase [Homo sapiens],3KEH_B Chain B, Glucocerebrosidase [Homo sapiens] |
| 1OGS_A | 4.89e-45 | 68 | 494 | 66 | 496 | humanacid-beta-glucosidase [Homo sapiens],1OGS_B human acid-beta-glucosidase [Homo sapiens],1Y7V_A Chain A, Glucosylceramidase [Homo sapiens],1Y7V_B Chain B, Glucosylceramidase [Homo sapiens],2F61_A Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2F61_B Crystal structure of partially deglycosylated acid beta-glucosidase [Homo sapiens],2J25_A Partially deglycosylated glucoceramidase [Homo sapiens],2J25_B Partially deglycosylated glucoceramidase [Homo sapiens],2NSX_A Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_B Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_C Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NSX_D Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease [Homo sapiens],2NT0_A Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_B Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_C Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT0_D Acid-beta-glucosidase low pH, glycerol bound [Homo sapiens],2NT1_A Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_B Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_C Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],2NT1_D Structure of acid-beta-glucosidase at neutral pH [Homo sapiens],3GXD_A Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_B Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_C Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXD_D Crystal structure of Apo acid-beta-glucosidase pH 4.5 [Homo sapiens],3GXF_A Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_B Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_C Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXF_D Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH [Homo sapiens],3GXI_A Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_B Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_C Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXI_D Crystal structure of acid-beta-glucosidase at pH 5.5 [Homo sapiens],3GXM_A Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_B Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_C Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3GXM_D Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition [Homo sapiens],3RIK_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIK_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_A The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_B The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_C The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],3RIL_D The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease [Homo sapiens],6MOZ_A Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6MOZ_B Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor [Homo sapiens],6Q1N_A Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1N_B Glucocerebrosidase in complex with pharmacological chaperone IMX8 [Homo sapiens],6Q1P_A Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q1P_B Glucocerebrosidase in complex with pharmacological chaperone norIMX8 [Homo sapiens],6Q6K_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6K_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569) [Homo sapiens],6Q6L_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6L_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656) [Homo sapiens],6Q6N_A Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6Q6N_B Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655) [Homo sapiens],6TJJ_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6TJJ_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YTP_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YTP_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YUT_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YUT_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6YV3_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6YV3_BBB Chain BBB, Glucosylceramidase [Homo sapiens],6Z39_AAA Chain AAA, Glucosylceramidase [Homo sapiens],6Z39_BBB Chain BBB, Glucosylceramidase [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8J0I9 | 9.49e-48 | 78 | 491 | 76 | 486 | Endo-1,6-beta-D-glucanase BGN16.3 OS=Trichoderma harzianum OX=5544 PE=1 SV=1 |
| P17439 | 1.49e-47 | 68 | 494 | 85 | 514 | Lysosomal acid glucosylceramidase OS=Mus musculus OX=10090 GN=Gba PE=1 SV=1 |
| Q4WBR2 | 3.33e-46 | 78 | 491 | 71 | 484 | Endo-1,6-beta-D-glucanase neg1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=neg1 PE=1 SV=1 |
| Q2KHZ8 | 1.00e-44 | 68 | 494 | 105 | 535 | Lysosomal acid glucosylceramidase OS=Bos taurus OX=9913 GN=GBA PE=2 SV=1 |
| Q9BDT0 | 1.91e-44 | 68 | 494 | 105 | 535 | Lysosomal acid glucosylceramidase OS=Pan troglodytes OX=9598 GN=GBA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000222 | 0.082999 | 0.916654 | 0.000038 | 0.000041 | 0.000035 |