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CAZyme Information: MGYG000002203_01396
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; | |||||||||||
| CAZyme ID | MGYG000002203_01396 | |||||||||||
| CAZy Family | GH5 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 6819; End: 8327 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH5 | 155 | 450 | 2.5e-93 | 0.9891304347826086 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00150 | Cellulase | 3.17e-51 | 146 | 453 | 7 | 272 | Cellulase (glycosyl hydrolase family 5). |
| COG2730 | BglC | 7.94e-25 | 129 | 451 | 45 | 361 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
| cd14948 | BACON | 1.16e-07 | 39 | 114 | 7 | 82 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
| cd19608 | GH113_mannanase-like | 5.55e-04 | 156 | 233 | 9 | 93 | Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRX62664.1 | 3.33e-187 | 20 | 502 | 23 | 513 |
| QUT35080.1 | 5.80e-179 | 20 | 502 | 22 | 517 |
| AVM57519.1 | 3.89e-178 | 4 | 501 | 53 | 562 |
| ADD61911.1 | 5.50e-174 | 33 | 502 | 4 | 485 |
| QUT88430.1 | 9.79e-172 | 30 | 502 | 123 | 598 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6WQY_A | 3.30e-154 | 122 | 477 | 18 | 375 | ChainA, Cellulase [Phocaeicola salanitronis DSM 18170] |
| 4YHE_A | 3.90e-141 | 128 | 502 | 7 | 386 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
| 4YHG_A | 3.15e-140 | 128 | 502 | 7 | 386 | NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a] |
| 2JEP_A | 9.83e-75 | 128 | 453 | 35 | 367 | Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli] |
| 3NDY_A | 7.38e-65 | 123 | 482 | 7 | 339 | Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O08342 | 3.08e-70 | 125 | 465 | 37 | 385 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
| P28623 | 3.98e-63 | 99 | 482 | 12 | 370 | Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2 |
| P28621 | 4.22e-60 | 98 | 496 | 19 | 388 | Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1 |
| Q12647 | 6.58e-60 | 119 | 466 | 16 | 347 | Endoglucanase B OS=Neocallimastix patriciarum OX=4758 GN=CELB PE=2 SV=1 |
| P10477 | 9.29e-58 | 128 | 482 | 57 | 383 | Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2 |
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 |
|---|---|---|---|---|---|
| 0.000223 | 0.053321 | 0.946285 | 0.000076 | 0.000080 | 0.000040 |