| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma01g28520.2 |
| Family | CBM20 |
| Protein Properties | Length: 393 Molecular Weight: 43498.6 Isoelectric Point: 4.0871 |
| Chromosome | Chromosome/Scaffold: 01 Start: 38386524 End: 38389414 |
| Description | Carbohydrate-binding-like fold |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM20 | 93 | 177 | 1e-24 |
| VRVSFQLEKNCNFGEQFLIVGDDPVLGSWDPLEALPMTWFEGHVWAVELDMPAGKSFQFKFILKGKGGDIIWQPGLDRMIHTWET | |||
| Full Sequence |
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| Protein Sequence Length: 393 Download |
| MKALTSSCSK TVVDTLGPFS PRVCLRVSYR PEFCFTLRSK NEKKSCNSLL LKLVRNKGVV 60 YPVHAVPPKN QVDLDTAEPQ AQQSEQTNES KFVRVSFQLE KNCNFGEQFL IVGDDPVLGS 120 WDPLEALPMT WFEGHVWAVE LDMPAGKSFQ FKFILKGKGG DIIWQPGLDR MIHTWETMNR 180 IIVLEDWENA ELQKIIEEDQ LAEPNEEPQV DLEVPTLAET LENPQEELDS NASEISAVED 240 TQIHAEEKPL AEPVMQQNTD TISSSIEKPM AIVAENISSS EDLINSTSQK SNKKNIILQP 300 KEESADSPGN DDIIHDLGHN GNAASLENQE KTIVESSLFD LEGGPVLVPG LIIEPTEPTD 360 QAGQSEVQEM TNTDTSVGAF ETQDQNIPEV NA* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd05818 | CBM20_water_dikinase | 4.0e-13 | 93 | 172 | 80 | + Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. | ||
| cd02856 | E_set_GDE_Isoamylase_N | 9.0e-14 | 93 | 187 | 99 | + N-terminal Early set domain associated with the catalytic domain of Glycogen debranching enzyme and bacterial isoamylase (also called glycogen 6-glucanohydrolase). E or "early" set domains are associated with the catalytic domain of the glycogen debranching enzyme at the N-terminal end. Glycogen debranching enzymes have both 4-alpha-glucanotransferase and amylo-1,6-glucosidase activities. As a transferase, it transfers a segment of the 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase, it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Bacterial isoamylases are also included in this subfamily. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of glycogen debranching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. | ||
| smart01065 | CBM_2 | 6.0e-17 | 93 | 176 | 88 | + Starch binding domain. | ||
| pfam00686 | CBM_20 | 3.0e-18 | 93 | 177 | 88 | + Starch binding domain. | ||
| cd05467 | CBM20 | 7.0e-25 | 94 | 187 | 97 | + The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:2001070 | starch binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACU23169.1 | 0 | 1 | 391 | 2 | 391 | unknown [Glycine max] |
| EMBL | CAN60108.1 | 0 | 60 | 389 | 29 | 352 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002308216.1 | 0 | 87 | 387 | 24 | 315 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002322974.1 | 0 | 1 | 281 | 1 | 287 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002528119.1 | 0 | 88 | 390 | 15 | 321 | catalytic, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1cyg_A | 0.00000006 | 3 | 189 | 487 | 680 | A Chain A, Cyclodextrin Glucanotransferase (E.C.2.4.1.19) (Cgtase) |
| PDB | 1uks_B | 0.0001 | 105 | 174 | 600 | 672 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| PDB | 1uks_A | 0.0001 | 105 | 174 | 600 | 672 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| PDB | 1ded_B | 0.0001 | 106 | 174 | 601 | 672 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| PDB | 1ded_A | 0.0001 | 106 | 174 | 601 | 672 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EV280388 | 237 | 91 | 327 | 0 |
| EV276083 | 250 | 70 | 318 | 0 |
| BW659263 | 187 | 1 | 187 | 0 |
| FG986698 | 225 | 1 | 225 | 0 |
| BM525430 | 190 | 90 | 279 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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