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CAZyme Information: MGYG000003893_00773
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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 | Prevotella multisaccharivorax | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella multisaccharivorax | |||||||||||
| CAZyme ID | MGYG000003893_00773 | |||||||||||
| CAZy Family | GH99 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 489; End: 1709 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH99 | 53 | 372 | 5.7e-69 | 0.9850299401197605 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11575 | GH99_GH71_like_3 | 2.17e-141 | 45 | 399 | 1 | 376 | Uncharacterized glycoside hydrolase family 99-like domain. This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism. |
| cd11573 | GH99_GH71_like | 2.74e-28 | 107 | 357 | 5 | 270 | Glycoside hydrolase families 71, 99, and related domains. This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity. |
| cd11574 | GH99 | 1.85e-20 | 59 | 349 | 7 | 319 | Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase. This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear. |
| pfam16317 | Glyco_hydro_99 | 3.89e-10 | 84 | 349 | 43 | 319 | Glycosyl hydrolase family 99. This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer. |
| cd11577 | GH71 | 5.49e-10 | 200 | 356 | 97 | 261 | Glycoside hydrolase family 71. This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUB83810.1 | 9.54e-194 | 19 | 404 | 19 | 404 |
| QKH89593.1 | 6.34e-193 | 6 | 404 | 7 | 404 |
| QUB65436.1 | 6.34e-193 | 6 | 404 | 7 | 404 |
| QUB56050.1 | 1.28e-192 | 3 | 404 | 4 | 404 |
| QUB58645.1 | 1.28e-192 | 3 | 404 | 4 | 404 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4ACZ_A | 3.82e-09 | 93 | 340 | 83 | 338 | Structureof the GH99 endo-alpha-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],4AD0_A Structure of the GH99 endo-alpha-mannosidase from Bacteriodes thetaiotaomicron in complex with BIS-TRIS-Propane [Bacteroides thetaiotaomicron VPI-5482],4AD0_B Structure of the GH99 endo-alpha-mannosidase from Bacteriodes thetaiotaomicron in complex with BIS-TRIS-Propane [Bacteroides thetaiotaomicron VPI-5482],4AD0_C Structure of the GH99 endo-alpha-mannosidase from Bacteriodes thetaiotaomicron in complex with BIS-TRIS-Propane [Bacteroides thetaiotaomicron VPI-5482],4AD0_D Structure of the GH99 endo-alpha-mannosidase from Bacteriodes thetaiotaomicron in complex with BIS-TRIS-Propane [Bacteroides thetaiotaomicron VPI-5482] |
| 4ACZ_B | 3.82e-09 | 93 | 340 | 83 | 338 | Structureof the GH99 endo-alpha-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 4ACY_A | 2.12e-08 | 93 | 340 | 83 | 338 | Selenomethioninederivative of the GH99 endo-alpha-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],4ACY_B Selenomethionine derivative of the GH99 endo-alpha-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
Swiss-Prot Hits help
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 |
|---|---|---|---|---|---|
| 0.000361 | 0.121787 | 0.877594 | 0.000097 | 0.000094 | 0.000072 |