| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_025456m |
| Family | GT35 |
| Protein Properties | Length: 251 Molecular Weight: 27490.5 Isoelectric Point: 4.6397 |
| Chromosome | Chromosome/Scaffold: 04851 Start: 440087 End: 444118 |
| Description | alpha-glucan phosphorylase 2 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 5 | 244 | 0 |
| DRRNVVPRVCIIGGKAAPGYEIAKKIIKLCHAVAEKINNDPDIGDLLKLVFIPDYNITVAELVIPGADLSQHLSTAGHEASGTGCMKFLMNGCLLLATAD GSTIEIIEEIGADNMFLFGAKVSEVPVLRKKAPNLKVPLQFARVTMILNDLTAASRMVRNGYFGFEDYFESLCDSVEVDNDFYLLGADFESYLEAQAAAD KAFIDEEKWTQMSILSTAGSGRFSSDRTIDDYAEKTWGIE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 251 Download |
| MEKKDRRNVV PRVCIIGGKA APGYEIAKKI IKLCHAVAEK INNDPDIGDL LKLVFIPDYN 60 ITVAELVIPG ADLSQHLSTA GHEASGTGCM KFLMNGCLLL ATADGSTIEI IEEIGADNMF 120 LFGAKVSEVP VLRKKAPNLK VPLQFARVTM ILNDLTAASR MVRNGYFGFE DYFESLCDSV 180 EVDNDFYLLG ADFESYLEAQ AAADKAFIDE EKWTQMSILS TAGSGRFSSD RTIDDYAEKT 240 WGIERCRCPA * 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0058 | GlgP | 3.0e-69 | 6 | 245 | 247 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
| PRK14985 | PRK14985 | 2.0e-75 | 8 | 245 | 240 | + maltodextrin phosphorylase; Provisional | ||
| pfam00343 | Phosphorylase | 6.0e-98 | 1 | 245 | 247 | + Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin. | ||
| TIGR02093 | P_ylase | 9.0e-100 | 9 | 243 | 237 | + glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 2.0e-115 | 7 | 243 | 241 | + This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004645 | phosphorylase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN84047.1 | 0 | 1 | 250 | 190 | 448 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI30609.1 | 0 | 1 | 250 | 575 | 814 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002273615.1 | 0 | 1 | 250 | 579 | 818 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002305114.1 | 0 | 1 | 249 | 579 | 817 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002509431.1 | 0 | 1 | 249 | 710 | 948 | glycogen phosphorylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1c50_A | 0 | 1 | 250 | 578 | 824 | A Chain A, Identification And Structural Characterization Of A Novel Allosteric Binding Site Of Glycogen Phosphorylase B |
| PDB | 1abb_D | 0 | 1 | 250 | 581 | 827 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1abb_C | 0 | 1 | 250 | 581 | 827 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1abb_B | 0 | 1 | 250 | 581 | 827 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1abb_A | 0 | 1 | 250 | 581 | 827 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
| Hydropathy |
|---|
 |
| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO802292 | 249 | 1 | 249 | 0 |
| CF228074 | 220 | 6 | 225 | 0 |
| AI730831 | 218 | 7 | 224 | 0 |
| EL689312 | 233 | 1 | 233 | 0 |
| JK498909 | 212 | 13 | 224 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
|---|
 |
