| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb03g040350.1 |
| Family | CBM20 |
| Protein Properties | Length: 374 Molecular Weight: 40281.9 Isoelectric Point: 4.3291 |
| Chromosome | Chromosome/Scaffold: 3 Start: 67984070 End: 67986060 |
| 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 | 124 | 208 | 1.6e-28 |
| VRVKFVLRKQCAFGQQFLVVGDDAALGLWDPAKAIALNWSEGHVWTATTDLPANRSIEFKFLLRDASGHVRWQHGTNRTLQITET | |||
| Full Sequence |
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| Protein Sequence Length: 374 Download |
| MHPASSKPME VAAVACRAGL LARARPGSRP RTRRFAVGPA PSAARRRLLV ASLGVGEPLP 60 AQSLLCEEAV ALEVGVGEPL PARSLGEDAV ALEVGEDDDL DSLVSAENLL PPAAAADVPE 120 DRTVRVKFVL RKQCAFGQQF LVVGDDAALG LWDPAKAIAL NWSEGHVWTA TTDLPANRSI 180 EFKFLLRDAS GHVRWQHGTN RTLQITETPN TMVVHEDWDH GNKQKVSEEE ELSIGAEDVV 240 FSEDLEGTNG AMPVDNNPQK HENLETDRSA VVVADAPLQW EMVAANGTDQ PQLMLDKHQT 300 ILEEVPGEQN GPPSAGDYAG NGDDDDDDTT LYQGGDLLQN RPTSIFENDL AWAGKAMQQL 360 LRILGFQIGT TRT* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd02856 | E_set_GDE_Isoamylase_N | 6.0e-16 | 122 | 218 | 102 | + 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. | ||
| cd02853 | E_set_MTHase_like_N | 5.0e-19 | 136 | 218 | 83 | + N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins. E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase 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 | 4.0e-20 | 124 | 207 | 88 | + Starch binding domain. | ||
| pfam00686 | CBM_20 | 2.0e-25 | 123 | 208 | 89 | + Starch binding domain. | ||
| cd05467 | CBM20 | 1.0e-31 | 125 | 218 | 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:2001070 | starch binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ACN25201.1 | 0 | 9 | 373 | 1 | 351 | unknown [Zea mays] |
| GenBank | EAY76546.1 | 0 | 12 | 373 | 5 | 387 | hypothetical protein OsI_04489 [Oryza sativa Indica Group] |
| RefSeq | NP_001044849.1 | 0 | 12 | 373 | 5 | 379 | Os01g0856900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001152198.1 | 0 | 9 | 373 | 1 | 348 | starch binding domain containing protein [Zea mays] |
| RefSeq | XP_002456661.1 | 0 | 1 | 373 | 1 | 373 | hypothetical protein SORBIDRAFT_03g040350 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1ded_B | 0.00000002 | 124 | 218 | 587 | 684 | A Chain A, Apo Form Of A Mutant Of Glycogenin In Which Asp159 Is Replaced By Asn |
| PDB | 1ded_A | 0.00000002 | 124 | 218 | 587 | 684 | A Chain A, Apo Form Of A Mutant Of Glycogenin In Which Asp159 Is Replaced By Asn |
| PDB | 1d7f_B | 0.00000002 | 124 | 218 | 587 | 684 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
| PDB | 1d7f_A | 0.00000002 | 124 | 218 | 587 | 684 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
| PDB | 1uks_B | 0.00000002 | 124 | 218 | 587 | 684 | 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 |
| CD213553 | 221 | 1 | 221 | 0 |
| DR817309 | 249 | 36 | 276 | 0 |
| EE037858 | 254 | 9 | 256 | 0 |
| DR789445 | 247 | 9 | 251 | 0 |
| DT939906 | 247 | 9 | 251 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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