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CAZyme Information: MGYG000000574_02592
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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; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; ; | |||||||||||
| CAZyme ID | MGYG000000574_02592 | |||||||||||
| CAZy Family | GH78 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2788; End: 4041 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH78 | 3 | 382 | 9.5e-86 | 0.746031746031746 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17389 | Bac_rhamnosid6H | 3.34e-20 | 5 | 338 | 4 | 339 | Bacterial alpha-L-rhamnosidase 6 hairpin glycosidase domain. This family consists of bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria. |
| COG3408 | GDB1 | 1.18e-07 | 82 | 206 | 335 | 465 | Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism]. |
| pfam06202 | GDE_C | 2.34e-07 | 82 | 209 | 80 | 217 | Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33). |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRQ48848.1 | 1.66e-137 | 4 | 412 | 286 | 697 |
| QUT45325.1 | 2.34e-137 | 4 | 412 | 286 | 697 |
| QIK55686.1 | 1.94e-135 | 4 | 388 | 291 | 675 |
| AXP80063.1 | 2.62e-135 | 4 | 401 | 279 | 674 |
| QUT83668.1 | 3.10e-135 | 4 | 382 | 300 | 678 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3CIH_A | 3.02e-127 | 4 | 401 | 301 | 697 | Crystalstructure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
| 4XHC_A | 1.62e-28 | 9 | 338 | 211 | 541 | ChainA, Alpha-L-rhamnosidase [Klebsiella oxytoca],4XHC_B Chain B, Alpha-L-rhamnosidase [Klebsiella oxytoca] |
| 1V7V_A | 3.60e-08 | 83 | 248 | 422 | 601 | Crystalstructure of Vibrio proteolyticus chitobiose phosphorylase [Vibrio proteolyticus],1V7W_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc [Vibrio proteolyticus],1V7X_A Crystal structure of Vibrio proteolyticus chitobiose phosphorylase in complex with GlcNAc and sulfate [Vibrio proteolyticus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| T2KM26 | 5.78e-09 | 6 | 371 | 732 | 1102 | Bifunctional sulfatase/alpha-L-rhamnosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22250 PE=1 SV=2 |
| Q76IQ9 | 1.97e-07 | 83 | 248 | 422 | 601 | N,N'-diacetylchitobiose phosphorylase OS=Vibrio proteolyticus OX=671 GN=chbP PE=1 SV=1 |
| P9WF03 | 6.27e-07 | 7 | 377 | 472 | 853 | Alpha-L-rhamnosidase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_34 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 |
|---|---|---|---|---|---|
| 1.000071 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |