| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_001626m |
| Family | GT35 |
| Protein Properties | Length: 847 Molecular Weight: 95777 Isoelectric Point: 7.1165 |
| Chromosome | Chromosome/Scaffold: 06512 Start: 2036044 End: 2045162 |
| Description | alpha-glucan phosphorylase 2 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 119 | 841 | 0 |
| ALNNLGHKLEEIIEQEKDAALGNGGLGRLASCFLDSMATLDLPAWGYGLRYRYGLFKQRITKEGQEEIAEDWLEKFSPWEVVRHDVVFPVRFFGHVQVNP DGSRKWVGGEIVQALAYDVPIPGYKTKNTINLRLWEARASAEDFNLFQFNDGQYESAAQLHSRAQQICAVLYPGDATEEGKLLRLKQQFFLCSASLQDII MRFKERRTGKGSWKWSEFPSKVAVQLNDTHPTLAIPELMRILMDDEGLGWDEAWDVITRTIAYTNHTVLPEALEKWSQTVMRKLLPRHMEIIEEIDKRFI AMIRGSRTDLEGKLPSMCILDNNPQKPVVRMANLCVVSSHTVNGVAQLHSDILKSELFADYVSIWPKKFQNKTNGITPRRWLRFCSPELSNIITKWLKTD QWITNLDLLAGLQKFADNAEFQTAWGSAKMANKQRLAQYILRVTGVSIDPNSLFDIQVKRIHEYKRQLLNILGAVYRYKKLKEMSAEERKNTTPRTVMIG GKAFATYTNAKRIVKLVNDVGAVVNSDPEVNSYLKVVFVPNYNVSVAEMLIPGSELSQHISTAGMEASGTSNMKFALNGCLIIGTLDGANVEIREEIGEE NFFLFGATADQVPRLRKERENGLFKPDHRFEEAKQFIRSGVFGSYDYNPLLDSLEGNSGYGRGDYFLVGHDFPSYLDAQKRVDEAYKDSKRWLKMSILSA AGSGKFSSDRTIAQYAKEIWNIE | |||
| Full Sequence |
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| Protein Sequence Length: 847 Download |
| MATEEATNGT SATVSAVFSK IPAAANPLAE DPLKIASNIS YHAQYSPHFS PSKFEPEQAF 60 YATAESVRDR LIQQWNETYL HYHKVDPKQT YYLSMEYLQG RALTNAIGNL DIQGAYADAL 120 NNLGHKLEEI IEQEKDAALG NGGLGRLASC FLDSMATLDL PAWGYGLRYR YGLFKQRITK 180 EGQEEIAEDW LEKFSPWEVV RHDVVFPVRF FGHVQVNPDG SRKWVGGEIV QALAYDVPIP 240 GYKTKNTINL RLWEARASAE DFNLFQFNDG QYESAAQLHS RAQQICAVLY PGDATEEGKL 300 LRLKQQFFLC SASLQDIIMR FKERRTGKGS WKWSEFPSKV AVQLNDTHPT LAIPELMRIL 360 MDDEGLGWDE AWDVITRTIA YTNHTVLPEA LEKWSQTVMR KLLPRHMEII EEIDKRFIAM 420 IRGSRTDLEG KLPSMCILDN NPQKPVVRMA NLCVVSSHTV NGVAQLHSDI LKSELFADYV 480 SIWPKKFQNK TNGITPRRWL RFCSPELSNI ITKWLKTDQW ITNLDLLAGL QKFADNAEFQ 540 TAWGSAKMAN KQRLAQYILR VTGVSIDPNS LFDIQVKRIH EYKRQLLNIL GAVYRYKKLK 600 EMSAEERKNT TPRTVMIGGK AFATYTNAKR IVKLVNDVGA VVNSDPEVNS YLKVVFVPNY 660 NVSVAEMLIP GSELSQHIST AGMEASGTSN MKFALNGCLI IGTLDGANVE IREEIGEENF 720 FLFGATADQV PRLRKERENG LFKPDHRFEE AKQFIRSGVF GSYDYNPLLD SLEGNSGYGR 780 GDYFLVGHDF PSYLDAQKRV DEAYKDSKRW LKMSILSAAG SGKFSSDRTI AQYAKEIWNI 840 EGCRVP* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 36 | 840 | 813 | + 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. | ||
| TIGR02093 | P_ylase | 0 | 39 | 840 | 810 | + 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]. | ||
| pfam00343 | Phosphorylase | 0 | 119 | 841 | 728 | + 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. | ||
| PRK14985 | PRK14985 | 0 | 92 | 838 | 752 | + maltodextrin phosphorylase; Provisional | ||
| COG0058 | GlgP | 0 | 36 | 841 | 810 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
| 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 |
| GenBank | AAM29154.1 | 0 | 15 | 845 | 12 | 839 | starch phosphorylase type H [Citrus hybrid cultivar] |
| DDBJ | BAG31926.1 | 0 | 1 | 846 | 1 | 843 | alpha-1,4-glucan phosphorylase H isozyme [Cucurbita maxima] |
| RefSeq | XP_002280732.1 | 0 | 1 | 846 | 1 | 843 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002313399.1 | 0 | 10 | 846 | 16 | 853 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002520435.1 | 0 | 1 | 846 | 1 | 849 | 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 | 1z8d_A | 0 | 29 | 844 | 22 | 832 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 1ygp_B | 0 | 59 | 841 | 68 | 876 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1ygp_A | 0 | 59 | 841 | 68 | 876 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 2ffr_A | 0 | 29 | 844 | 10 | 820 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| PDB | 2gj4_A | 0 | 29 | 844 | 10 | 820 | A Chain A, Structure Of Rabbit Muscle Glycogen Phosphorylase In Complex With Ligand |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1826 | EC-2.4.1.1 | phosphorylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO782200 | 412 | 175 | 586 | 0 |
| HO418036 | 539 | 245 | 762 | 0 |
| HO586252 | 552 | 293 | 843 | 0 |
| HO613954 | 499 | 398 | 847 | 0 |
| GO871118 | 324 | 149 | 472 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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