| Basic Information | |
|---|---|
| Species | Phaseolus vulgaris |
| Cazyme ID | Phvul.007G139400.1 |
| Family | GH13 |
| Protein Properties | Length: 958 Molecular Weight: 106570 Isoelectric Point: 6.2632 |
| Chromosome | Chromosome/Scaffold: 07 Start: 34315056 End: 34334394 |
| Description | limit dextrinase |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 363 | 764 | 2.1e-31 |
| HLKRLSSAGITHVHLLPSFQFAGVDDQKENWRYVDNSILESLPPDSDQQQALITAIQNFDGYNWGYNPVLWGVPKGSYASNPNGPYRTIEFRKMVKALNH IGLRVVLDVVYNHLQGSGPLEEHSVLDKIVPGYYLRRNRDGFIENSTCINNTASEHFMVERLILDDLVHWALNYKIDGFRFDLMGHIMKRTMVKAKTALH SLTKEKDGVDGSSIYIYGEGWDFGEVAKNGRGINASQFNLPGTQIGSFNDRIRDAILGGSPFGHPLQQGFVTGLLLQPNGHDHGTEANAKSMLDTSMDHI QIGMAANLQDFVLTNCEGEEVKGSEILTYDGTPVAYASCPIETINYVSAHDNETLFDIVSLKTPMDVTVTERCRINHLATSIVALSQGIPFFHSGDEILR SK | |||
| Full Sequence |
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| Protein Sequence Length: 958 Download |
| MLLLASSSSS PSLSLPSLSH LHHSLPSSFP RHSLRLHFPS QATPLHLRTP PPLSCSINAS 60 SSVEQSASLS QMQNSLLYSR AYWVTEFLIA WNVDVANGSS CHLIASKNAS LTIANCQIQG 120 EDLKIELQED RAGLPANVVE KFPHIRGYKA FKLPSTLDVK PLLKSQLAVA IYDSDDKCRN 180 CTGLQLPGVL DELFSYDGPL GALFSEEAVS LYLWAPTAQA VRAYIYKDPS GDDPIEIVCL 240 EEENGVWRTK GRKSWEHCYY VYEVCVYHHS TLRVEKCYAN DPYARGLSSD GGRTFLLNLD 300 SDDLKPDGWD NLANEKPTIH SFTDISIYEM HIRDFSASDL SVQPSFRGGY LAFTLLDSAG 360 VLHLKRLSSA GITHVHLLPS FQFAGVDDQK ENWRYVDNSI LESLPPDSDQ QQALITAIQN 420 FDGYNWGYNP VLWGVPKGSY ASNPNGPYRT IEFRKMVKAL NHIGLRVVLD VVYNHLQGSG 480 PLEEHSVLDK IVPGYYLRRN RDGFIENSTC INNTASEHFM VERLILDDLV HWALNYKIDG 540 FRFDLMGHIM KRTMVKAKTA LHSLTKEKDG VDGSSIYIYG EGWDFGEVAK NGRGINASQF 600 NLPGTQIGSF NDRIRDAILG GSPFGHPLQQ GFVTGLLLQP NGHDHGTEAN AKSMLDTSMD 660 HIQIGMAANL QDFVLTNCEG EEVKGSEILT YDGTPVAYAS CPIETINYVS AHDNETLFDI 720 VSLKTPMDVT VTERCRINHL ATSIVALSQG IPFFHSGDEI LRSKSLDRDS YNSGDWFNRL 780 DFTYNSNNWG VGLPPQEKNE KNWPLMKPRL ANPSFRPEKI HILAAVDNLL NLLRIRYSSP 840 LFRLKTENAI KQRVSFHNTG PSWVCGVIVM SIEDGHDGFP GLSQLDPIYS FIVVVVNASP 900 KEVSFVSPAL QSRSLQLHPI QVSSSDDLVK SSRYETSSGC FVVPQRTTAV FVEPRKT* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1523 | PulA | 4.0e-92 | 192 | 951 | 813 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 2.0e-132 | 191 | 909 | 735 | + 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 | 4.0e-169 | 323 | 788 | 476 | + 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 | 71 | 955 | 885 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 76 | 955 | 915 | + 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:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| 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 | CAA58803.1 | 0 | 53 | 955 | 61 | 962 | pullulanase [Spinacia oleracea] |
| EMBL | CBI31395.1 | 0 | 26 | 956 | 16 | 955 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002271820.1 | 0 | 72 | 956 | 23 | 906 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315334.1 | 0 | 68 | 955 | 6 | 893 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532780.1 | 0 | 52 | 955 | 61 | 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 | 79 | 955 | 6 | 883 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2y5e_A | 0 | 79 | 955 | 6 | 883 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 2y4s_A | 0 | 79 | 955 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 138 | 955 | 232 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 138 | 955 | 232 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| CO128344 | 287 | 391 | 677 | 0 |
| GO872243 | 341 | 581 | 921 | 0 |
| EH773847 | 282 | 612 | 893 | 0 |
| DV135457 | 264 | 570 | 833 | 0 |
| AM733410 | 287 | 632 | 918 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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