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CAZyme Information: MGYG000003687_02421
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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 | Paenibacillus polymyxa | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa | |||||||||||
| CAZyme ID | MGYG000003687_02421 | |||||||||||
| CAZy Family | CBM26 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 55749; End: 56903 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM26 | 78 | 148 | 1.6e-23 | 0.9466666666666667 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam16738 | CBM26 | 3.37e-22 | 79 | 148 | 1 | 68 | Starch-binding module 26. CBM26 is a carbohydrate-binding module that binds starch. |
| pfam13290 | CHB_HEX_C_1 | 4.24e-18 | 179 | 245 | 1 | 67 | Chitobiase/beta-hexosaminidase C-terminal domain. |
| pfam13287 | Fn3_assoc | 3.84e-14 | 190 | 248 | 1 | 59 | Fn3 associated. |
| cd11339 | AmyAc_bac_CMD_like_2 | 1.49e-07 | 355 | 379 | 1 | 25 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. |
| pfam13290 | CHB_HEX_C_1 | 6.43e-07 | 266 | 340 | 2 | 63 | Chitobiase/beta-hexosaminidase C-terminal domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QDA28931.1 | 5.94e-262 | 1 | 379 | 1 | 379 |
| AUS27133.1 | 3.39e-261 | 1 | 379 | 1 | 379 |
| AIY07396.1 | 1.52e-256 | 1 | 379 | 1 | 376 |
| AHM66473.1 | 1.52e-256 | 1 | 379 | 1 | 376 |
| QPK54634.1 | 3.46e-253 | 1 | 379 | 1 | 378 |
Swiss-Prot Hits help
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 |
|---|---|---|---|---|---|
| 0.001117 | 0.997994 | 0.000328 | 0.000213 | 0.000169 | 0.000163 |
