| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_004771m |
| Family | GH13 |
| Protein Properties | Length: 559 Molecular Weight: 62160.6 Isoelectric Point: 6.4619 |
| Chromosome | Chromosome/Scaffold: 00224 Start: 15930 End: 35895 |
| Description | limit dextrinase |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 16 | 364 | 6.6e-29 |
| ITAFQNDDGYNWGYNPVLWGVPKGSYASNPNGSCRTIEFRKMVQAINRIGLRVVLDVVYNHLHGSGPFDENSVLDKVVPGYYLRRNSDGFIENSTCVNNT ASEHYMVERLIVDDLLSWAVNYKIDGFRFDLMGHMMKSTMVKAKDALLSLTKERNGVDGSSIYLYGEGWDFGEVAKNARGINASQFNLGGTGIGSFNDRI RDAMHGGSPFGHPLQQGFVTGLMLQPNGHDHGGKDVEEHMLTIAKDHIQAGMAANLREFVLINSEGKEVKGSEILTYGGEPLAYALCPTETINYVSAHDN ETLFDVVCMKTPMQISVDERCRLNYLATNMIALAQGIPFFHAGDEMLRS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 559 Download |
| MLEKLPPDSA EQQAHITAFQ NDDGYNWGYN PVLWGVPKGS YASNPNGSCR TIEFRKMVQA 60 INRIGLRVVL DVVYNHLHGS GPFDENSVLD KVVPGYYLRR NSDGFIENST CVNNTASEHY 120 MVERLIVDDL LSWAVNYKID GFRFDLMGHM MKSTMVKAKD ALLSLTKERN GVDGSSIYLY 180 GEGWDFGEVA KNARGINASQ FNLGGTGIGS FNDRIRDAMH GGSPFGHPLQ QGFVTGLMLQ 240 PNGHDHGGKD VEEHMLTIAK DHIQAGMAAN LREFVLINSE GKEVKGSEIL TYGGEPLAYA 300 LCPTETINYV SAHDNETLFD VVCMKTPMQI SVDERCRLNY LATNMIALAQ GIPFFHAGDE 360 MLRSKSLDRD SYNSGDWFNR LDFSYNSNNW GVGLPPKGKN EGNWPLMKPR LADPSFKPQK 420 SHILATVDNF LDVLQIRYSS PLFRLTTANA IQERVRFHNT GPSWVPGVIV MSIEDGHEGF 480 PGLSQLDPIY SYIVVIFNTC PNEILFACPP LRARGFQLHP VQVKSTDKVV KKSAYEPLSG 540 CFTVPPMTTS VFVEPRKI* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam11852 | DUF3372 | 8.0e-85 | 384 | 556 | 173 | + Domain of unknown function (DUF3372). This domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This presumed domain is about 170 amino acids in length. | ||
| TIGR02104 | pulA_typeI | 9.0e-93 | 22 | 509 | 493 | + pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. | ||
| cd11341 | AmyAc_Pullulanase_LD-like | 2.0e-141 | 20 | 389 | 373 | + Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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. | ||
| PLN02877 | PLN02877 | 0 | 1 | 556 | 556 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 1 | 556 | 560 | + alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102) [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI31395.1 | 0 | 1 | 558 | 399 | 956 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_196056.2 | 0 | 1 | 556 | 408 | 963 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
| RefSeq | XP_002271820.1 | 0 | 1 | 558 | 350 | 907 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315334.1 | 0 | 1 | 556 | 338 | 893 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532780.1 | 0 | 1 | 556 | 409 | 964 | pullulanase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4aio_A | 0 | 2 | 556 | 329 | 883 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
| PDB | 2y5e_A | 0 | 2 | 556 | 329 | 883 | A Chain A, Crystal Structure Of The R3 Form Of Pectate Lyase A, Erwinia Chrysanthemi |
| PDB | 2y4s_A | 0 | 2 | 556 | 329 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 8 | 556 | 538 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 8 | 556 | 538 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1824 | EC-3.2.1.41 | pullulanase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CO128344 | 278 | 1 | 278 | 0 |
| DV135457 | 264 | 171 | 434 | 0 |
| GO872243 | 341 | 182 | 522 | 0 |
| EH773847 | 282 | 213 | 494 | 0 |
| AM733410 | 287 | 233 | 519 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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