| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_002614m |
| Family | GT35 |
| Protein Properties | Length: 714 Molecular Weight: 80091.7 Isoelectric Point: 7.1403 |
| Chromosome | Chromosome/Scaffold: 11341 Start: 911272 End: 917791 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 25 | 217 | 0 |
| ALTKLGHDLESVARHEPDAALGNGGLGRLASCFLDSMATLNYPAWGYGLRYKYGLFKQRIAKDGQEEVAEDWLEMGNPWEIVRNDISYPVKFYGKVVSGS DGKKHWIGGEDIIAVAYDLPIPGYKTKSTINLRLWSTKAPAEDLDLYAFNAGKHTKAYEALANAEKICYILYPGDDSLEGKILRLKQHFRHSI | |||
| GT35 | 310 | 707 | 0 |
| PPKLVRMANLCVVGGHAVNGVAEIHSEIVKDEVFNAFYELWPNKFQNKTNGVTPRRWIRFCNPDLSKIITEWTGSEEWVLNTEKLAELRKFADNEDFQTQ WRAAKKSNKMKVASLLKEKTGYSVSADAMFDIQVKRIHEYKRQLLNILGIVYRYKKMKEMSAVERKAKYVPRVCIFGGKAFATYAQAKRIVKFITDVGAT VNHDPEIGDLLKVVFVPDYNVSVAELLIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIRQEVGEDNFFLFGAKAHEIAGLRKERVMGK FVPDPRFEEVKDFVRTGVFGCKYDEMLGSLEGNEGFGCGDYFLVGKDFPSYIECQEKVDEAYQDQRRWTNMSIMNTAGSYKFSSDRTIHEYAKDIWNI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 714 Download |
| MEFLQGRALL NAIGNLELTG AYAEALTKLG HDLESVARHE PDAALGNGGL GRLASCFLDS 60 MATLNYPAWG YGLRYKYGLF KQRIAKDGQE EVAEDWLEMG NPWEIVRNDI SYPVKFYGKV 120 VSGSDGKKHW IGGEDIIAVA YDLPIPGYKT KSTINLRLWS TKAPAEDLDL YAFNAGKHTK 180 AYEALANAEK ICYILYPGDD SLEGKILRLK QHFRHSILQL VNFIVCKYGK ADPNIFEKKL 240 KEMRILENVD LPSTFAGLTL KPKESSAAAI SEASKLNVKD EVDSGDEPQS KGEPKSKGTQ 300 KKEEVMAEPP PKLVRMANLC VVGGHAVNGV AEIHSEIVKD EVFNAFYELW PNKFQNKTNG 360 VTPRRWIRFC NPDLSKIITE WTGSEEWVLN TEKLAELRKF ADNEDFQTQW RAAKKSNKMK 420 VASLLKEKTG YSVSADAMFD IQVKRIHEYK RQLLNILGIV YRYKKMKEMS AVERKAKYVP 480 RVCIFGGKAF ATYAQAKRIV KFITDVGATV NHDPEIGDLL KVVFVPDYNV SVAELLIPAS 540 ELSQHISTAG MEASGTSNMK FAMNGCILIG TLDGANVEIR QEVGEDNFFL FGAKAHEIAG 600 LRKERVMGKF VPDPRFEEVK DFVRTGVFGC KYDEMLGSLE GNEGFGCGDY FLVGKDFPSY 660 IECQEKVDEA YQDQRRWTNM SIMNTAGSYK FSSDRTIHEY AKDIWNIRPT ILP* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 1.0e-68 | 25 | 213 | 189 | + 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 4.0e-87 | 1 | 213 | 217 | + 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 | 1 | 707 | 753 | + 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 | 0 | 305 | 707 | 409 | + 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. | ||
| pfam00343 | Phosphorylase | 0 | 305 | 709 | 411 | + 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. | ||
| 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 | 1 | 707 | 92 | 834 | starch phosphorylase type H [Citrus hybrid cultivar] |
| Swiss-Prot | Q9LKJ3 | 0 | 1 | 713 | 81 | 832 | PHSH_WHEAT RecName: Full=Alpha-glucan phosphorylase, H isozyme; AltName: Full=Starch phosphorylase H |
| RefSeq | XP_002280732.1 | 0 | 1 | 713 | 93 | 843 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520435.1 | 0 | 1 | 713 | 98 | 849 | glycogen phosphorylase, putative [Ricinus communis] |
| RefSeq | XP_002526085.1 | 0 | 219 | 713 | 468 | 977 | 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 | 1 | 710 | 88 | 831 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2ffr_A | 0 | 1 | 710 | 76 | 819 | A Chain A, Crystallographic Studies On N-Azido-Beta-D-Glucopyranosylamine, An Inhibitor Of Glycogen Phosphorylase: Comparison With N-Acetyl-Beta-D- Glucopyranosylam |
| PDB | 1ygp_B | 0 | 1 | 710 | 104 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1ygp_A | 0 | 1 | 710 | 104 | 878 | A Chain A, Phosphorylated Form Of Yeast Glycogen Phosphorylase With Phosphate Bound In The Active Site. |
| PDB | 1abb_D | 0 | 1 | 710 | 78 | 821 | 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 |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO778303 | 509 | 219 | 714 | 0 |
| HO778303 | 235 | 1 | 235 | 0 |
| HO797178 | 401 | 315 | 714 | 0 |
| HO620767 | 403 | 313 | 714 | 0 |
| HO613954 | 403 | 313 | 714 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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