| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma10g34080.1 |
| Family | GH13 |
| Protein Properties | Length: 952 Molecular Weight: 105650 Isoelectric Point: 6.3215 |
| Chromosome | Chromosome/Scaffold: 10 Start: 42262334 End: 42279064 |
| Description | limit dextrinase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 354 | 758 | 7.3e-30 |
| GVLHLKKLSSAGITHVHLLPTFQFAGVDDQKEDWRFVDTSILESLPPDSDQQQALITAIQNFDGYNWGYNPVLWGVPKGSYASNPNGPYRTIEFRKMVMA LNHIGLRVVLDVVYNHLQGSGPFDEHSVLDKIVPGYYLRRNSDGLIEHSTCINNTASEHFMVERLILDDLVHWAVNYKIDGFRFDLMGHIMKSTMVKAKT ALQCLTKEKDGLDGSSIYIYGEGWDFGEVAKNGRGVNASQFNLPGTQIGSFNDRIRDAILGGSPFGHPLQQGFVTGLLLQPNGHDHGTEANAKSMLAASM DHIQIGMAANLKDFVLTNSEGEEVKGSEILTYGGTPVAYASCPIETINYVSAHDNETLFDIVSLKTPMDISVSERCRINHLATSIIALSQGIPFFHSGDE ILRSK | |||
| Full Sequence |
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| Protein Sequence Length: 952 Download |
| MHLLASSSSL SPSLPSSFPR PSLHLHLHFP SQTTQLRLHT PPPLSCSLNS SSSSSYVEQS 60 ASSSQMQNGL LYSRAYWVAE SLIAWDVDVG NGFSCYLLAS KNASLTIANC QIQGEDLKIK 120 LQEDRVGLPA NVVEKFPHIR GHKVFSLPPT LDVKPLLKFR LAVVICDSDG ECMNCTGLQL 180 PGVLDDLFSY SGPLGALFSE EAVSLYLWAP TAQAVHAYIY KDPSGDDPIE IVCLEEENGV 240 WRTKGPKSWE GCYYVYEVCV YHPSTMRIEK CYTSDPYARG LSSDGRRSFL LNLDSVKLKP 300 DGWDNLANKK PTIHSFSDIS IYEMHIRDFS ASDLSVQPEF RGGYLAFTLQ DSAGVLHLKK 360 LSSAGITHVH LLPTFQFAGV DDQKEDWRFV DTSILESLPP DSDQQQALIT AIQNFDGYNW 420 GYNPVLWGVP KGSYASNPNG PYRTIEFRKM VMALNHIGLR VVLDVVYNHL QGSGPFDEHS 480 VLDKIVPGYY LRRNSDGLIE HSTCINNTAS EHFMVERLIL DDLVHWAVNY KIDGFRFDLM 540 GHIMKSTMVK AKTALQCLTK EKDGLDGSSI YIYGEGWDFG EVAKNGRGVN ASQFNLPGTQ 600 IGSFNDRIRD AILGGSPFGH PLQQGFVTGL LLQPNGHDHG TEANAKSMLA ASMDHIQIGM 660 AANLKDFVLT NSEGEEVKGS EILTYGGTPV AYASCPIETI NYVSAHDNET LFDIVSLKTP 720 MDISVSERCR INHLATSIIA LSQGIPFFHS GDEILRSKSL DRDSYNSGDW FNRLDFTYNS 780 NNWGVGLPPQ EKNEKNWPLI KPRLANPSFR PQKTDILATV DNFLNLLRIR YSSPLFRLKT 840 ANTIQERVRF HNTGPSWVCG VIVMSIEDGH NGFPGLSQLD PIYSFIVVVF NASPKEVSFV 900 SPALQLRNLQ LHPIQVSSSD DLVKSSRYEA SSGCFVVPRR TTAVFVEPRK T* 960 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG1523 | PulA | 2.0e-94 | 186 | 945 | 800 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02104 | pulA_typeI | 4.0e-136 | 185 | 915 | 747 | + 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 | 1.0e-169 | 318 | 782 | 475 | + 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 | 65 | 949 | 885 | + alpha-amylase/limit dextrinase | ||
| TIGR02103 | pullul_strch | 0 | 69 | 949 | 916 | + 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 | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI31395.1 | 0 | 21 | 950 | 16 | 955 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_196056.2 | 0 | 57 | 949 | 72 | 963 | ATLDA (LIMIT DEXTRINASE); alpha-amylase/ limit dextrinase/ pullulanase [Arabidopsis thaliana] |
| RefSeq | XP_002271820.1 | 0 | 66 | 950 | 23 | 906 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315334.1 | 0 | 62 | 949 | 6 | 893 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532780.1 | 0 | 6 | 949 | 22 | 964 | pullulanase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4aio_A | 0 | 73 | 949 | 6 | 883 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 2y5e_A | 0 | 73 | 949 | 6 | 883 | A Chain A, Crystal Structure Of The Nasturtium Seedling Mutant Xyloglucanase Isoform Nxg1-Delta-Yniig |
| PDB | 2y4s_A | 0 | 73 | 949 | 6 | 883 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhf_A | 0 | 51 | 949 | 155 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2fhc_A | 0 | 51 | 949 | 155 | 1070 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| Metabolic Pathways | |||
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| 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 |
| GO872243 | 341 | 575 | 915 | 0 |
| CO128344 | 287 | 385 | 671 | 0 |
| EH773847 | 282 | 606 | 887 | 0 |
| DV135457 | 264 | 564 | 827 | 0 |
| BQ509860 | 263 | 601 | 863 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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