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CAZyme Information: MGYG000003891_00957
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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 | UBA11524 sp000437595 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UBA11524; UBA11524 sp000437595 | |||||||||||
| CAZyme ID | MGYG000003891_00957 | |||||||||||
| CAZy Family | CE2 | |||||||||||
| CAZyme Description | Cellulase/esterase CelE | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 6394; End: 7464 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE2 | 134 | 344 | 3.4e-53 | 0.9952153110047847 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17996 | CE2_N | 2.13e-34 | 20 | 128 | 1 | 108 | Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum. |
| cd01831 | Endoglucanase_E_like | 3.94e-16 | 134 | 318 | 1 | 138 | Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| cd01827 | sialate_O-acetylesterase_like1 | 4.18e-05 | 231 | 318 | 66 | 138 | sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
| pfam13472 | Lipase_GDSL_2 | 8.36e-04 | 227 | 299 | 56 | 119 | GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657. |
| cd01836 | FeeA_FeeB_like | 0.004 | 176 | 295 | 28 | 122 | SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBL12376.1 | 4.65e-115 | 11 | 352 | 39 | 384 |
| CBL10431.1 | 6.56e-114 | 11 | 352 | 3 | 348 |
| AEN97395.1 | 1.61e-112 | 9 | 351 | 3 | 349 |
| VCV21230.1 | 2.14e-112 | 11 | 352 | 3 | 348 |
| BBF42855.1 | 1.08e-111 | 6 | 353 | 389 | 739 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2WAO_A | 2.20e-21 | 14 | 345 | 7 | 328 | ChainA, ENDOGLUCANASE E [Acetivibrio thermocellus] |
| 2WAB_A | 5.65e-21 | 14 | 345 | 7 | 328 | ChainA, ENDOGLUCANASE E [Acetivibrio thermocellus] |
| 2WAA_A | 9.37e-13 | 11 | 353 | 13 | 341 | Structureof a family two carbohydrate esterase from Cellvibrio japonicus [Cellvibrio japonicus] |
| 3U37_A | 9.67e-09 | 132 | 344 | 165 | 400 | AnAcetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_B An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_C An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_D An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_E An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_F An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_G An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],3U37_H An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316] |
| 4DEV_A | 3.04e-08 | 132 | 318 | 165 | 371 | AnAcetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_B An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_C An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_D An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_E An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_F An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_G An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316],4DEV_H An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus. [Butyrivibrio proteoclasticus B316] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P10477 | 4.65e-20 | 3 | 345 | 482 | 809 | 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 |
| B3PIB0 | 7.33e-12 | 11 | 340 | 32 | 348 | Acetylxylan esterase / glucomannan deacetylase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=axe2C PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000052 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |