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CAZyme Information: MGYG000000765_00456
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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 | Porphyromonas_A bennonis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A bennonis | |||||||||||
| CAZyme ID | MGYG000000765_00456 | |||||||||||
| CAZy Family | GH2 | |||||||||||
| CAZyme Description | Exo-beta-D-glucosaminidase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 77854; End: 80343 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH2 | 37 | 688 | 1.5e-74 | 0.6343085106382979 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3250 | LacZ | 5.91e-80 | 52 | 824 | 40 | 799 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
| PRK10150 | PRK10150 | 1.51e-10 | 81 | 386 | 69 | 352 | beta-D-glucuronidase; Provisional |
| pfam17753 | Ig_mannosidase | 2.78e-10 | 752 | 824 | 1 | 78 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
| pfam18368 | Ig_GlcNase | 0.001 | 788 | 815 | 65 | 92 | Exo-beta-D-glucosaminidase Ig-fold domain. This domain can be found in 2 glycoside hydrolase subfamily of beta-glucosaminidases (EC:3.2.1.165) such as CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. It has an immunoglobulin-like topology. |
| pfam02837 | Glyco_hydro_2_N | 0.004 | 80 | 145 | 68 | 134 | Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRM70633.1 | 7.40e-199 | 45 | 816 | 48 | 842 |
| QKH84210.1 | 1.48e-198 | 45 | 816 | 48 | 842 |
| QCQ54654.1 | 2.94e-198 | 45 | 816 | 48 | 842 |
| AAO75565.1 | 3.76e-198 | 45 | 816 | 55 | 850 |
| QMW87505.1 | 3.76e-198 | 45 | 816 | 55 | 850 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2VJX_A | 7.90e-200 | 45 | 816 | 30 | 825 | Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482] |
| 2JE8_A | 8.40e-200 | 45 | 816 | 32 | 827 | Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 7OP6_A | 8.67e-200 | 45 | 816 | 32 | 827 | ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482] |
| 2WBK_A | 2.30e-199 | 45 | 816 | 30 | 825 | Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482] |
| 2VQU_A | 9.91e-198 | 45 | 816 | 30 | 825 | Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| I2C092 | 1.84e-96 | 27 | 808 | 12 | 839 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
| Q5B7W2 | 1.42e-89 | 33 | 652 | 20 | 658 | Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2 |
| Q2TXB7 | 3.73e-87 | 31 | 808 | 18 | 828 | Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3 |
| Q0CCA0 | 5.08e-87 | 32 | 652 | 19 | 656 | Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2 |
| B8NW36 | 7.17e-87 | 31 | 808 | 18 | 828 | Beta-mannosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=mndB PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.013121 | 0.985066 | 0.000846 | 0.000336 | 0.000291 | 0.000307 |