| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000145828 |
| Family | GT35 |
| Protein Properties | Length: 1014 Molecular Weight: 115662 Isoelectric Point: 7.0543 |
| Chromosome | Chromosome/Scaffold: 002480238 Start: 2215 End: 7188 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
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| Family | Start | End | Evalue |
| GT35 | 219 | 1009 | 0 |
| ALKTLGHNLEDVARQEPDAALGNGGLGRLASCFLDSLATQNYPAWGYGLRYKYGLFKQHITKDGQEEVAENWLENTFPYQMGNPWEIPRNDVSYPVKFYG EVVSGLDGKKTWIGGENVMAVAYDVPIPGYKTKTTINLRLWSTKVAPEEFDLHAFNTGDHAKAYAALKNAEKICYILYPGDESMEGKSLRLKQQYTLCSA SLQDIVARFERRSGESVKWEEFPEKVAVQMNDTHPTLCIPELIRILMDVKGLSWTEAWDITRRTVAYTNHTVLPEALEKWSLQLIQELLPRHVEIIKTID EELIHTIIAEYGTEDLNLLEQKLREMRILDNIDLPDSVIGILCKSEESSAVDHVEEVDFSDEEAKTTDEVGQSKGLDTNTKNEVTFEPDPKLPKTVRMAN LCIAGGHAVNGVAEIHSEIVKNEVFNDFYKLWPEKFQNKTNGVTPRRWIRFCNPGLSKIITKWIGTDDWVRNTXMLVTLRKFADNEDLQSEWREAKRXNK IKVASFLKEKTGXLVNPDAMFDVQVKRIHEYKRQLLNILGIIYRYKXMKEMSPEERKAKFVPRVCIFGGKAFATYIQAKRIVKFITDVGATVNNDRDIGD LLKVVFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFAMNGCVQIGTLDGANVEXREEVGEDNFFLFGAHAHEIAGLRKERSEGKFVPDPRFEE VKAYVRTGVFGPYNYDELMGSLEGNEGYGRADYFLVGKDFPSYLDCQDKVDEAYRDQKRWTRKSILNTAGSYKFSSDRTIHEYARDIWKIE | |||
| Full Sequence |
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| Protein Sequence Length: 1014 Download |
| MAALPFSAKS TPSKFVSSFI HSNRIRRNSR PFFITTTTCS RSRARRQLRV KNVETDEKDV 60 AXXTQQEFWL QRAFFIKVKR FDAFIVKCIS TFYPSQLRRP IVVXXKMLLX KALQLKSVFL 120 KASSLATIPP DSSFIASNIK YHAEFTPSFS IESFALPKAF YXTAESVRDM LIVNWNATYE 180 YHDRLNVKQA YYLSMEFLQG RALLNAIGNL ELSGAYAHAL KTLGHNLEDV ARQEPDAALG 240 NGGLGRLASC FLDSLATQNY PAWGYGLRYK YGLFKQHITK DGQEEVAENW LENTFPYQMG 300 NPWEIPRNDV SYPVKFYGEV VSGLDGKKTW IGGENVMAVA YDVPIPGYKT KTTINLRLWS 360 TKVAPEEFDL HAFNTGDHAK AYAALKNAEK ICYILYPGDE SMEGKSLRLK QQYTLCSASL 420 QDIVARFERR SGESVKWEEF PEKVAVQMND THPTLCIPEL IRILMDVKGL SWTEAWDITR 480 RTVAYTNHTV LPEALEKWSL QLIQELLPRH VEIIKTIDEE LIHTIIAEYG TEDLNLLEQK 540 LREMRILDNI DLPDSVIGIL CKSEESSAVD HVEEVDFSDE EAKTTDEVGQ SKGLDTNTKN 600 EVTFEPDPKL PKTVRMANLC IAGGHAVNGV AEIHSEIVKN EVFNDFYKLW PEKFQNKTNG 660 VTPRRWIRFC NPGLSKIITK WIGTDDWVRN TXMLVTLRKF ADNEDLQSEW REAKRXNKIK 720 VASFLKEKTG XLVNPDAMFD VQVKRIHEYK RQLLNILGII YRYKXMKEMS PEERKAKFVP 780 RVCIFGGKAF ATYIQAKRIV KFITDVGATV NNDRDIGDLL KVVFVPDYNV SVAEVLIPGS 840 ELSQHISTAG MEASGTSNMK FAMNGCVQIG TLDGANVEXR EEVGEDNFFL FGAHAHEIAG 900 LRKERSEGKF VPDPRFEEVK AYVRTGVFGP YNYDELMGSL EGNEGYGRAD YFLVGKDFPS 960 YLDCQDKVDE AYRDQKRWTR KSILNTAGSY KFSSDRTIHE YARDIWKIEP VVLQ 1020 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 5.0e-129 | 219 | 548 | 330 | + 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-180 | 136 | 549 | 418 | + 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. | ||
| COG0058 | GlgP | 0 | 163 | 1010 | 856 | + Glucan phosphorylase [Carbohydrate transport and metabolism] | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 611 | 1008 | 407 | + 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 | 612 | 1010 | 404 | + 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 | |
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| GO Term | Description |
| GO:0004645 | phosphorylase activity |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI27267.1 | 0 | 84 | 1013 | 38 | 932 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P53535 | 0 | 124 | 1013 | 71 | 973 | PHSL2_SOLTU RecName: Full=Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic; AltName: Full=Starch phosphorylase L-2; Flags: Precursor |
| RefSeq | XP_002274575.1 | 0 | 1 | 1013 | 1 | 980 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316098.1 | 0 | 1 | 1013 | 1 | 952 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512108.1 | 0 | 1 | 1013 | 1 | 972 | glycogen phosphorylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1xoi_B | 0 | 160 | 1014 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 1xoi_A | 0 | 160 | 1014 | 52 | 833 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Chloroindoloyl Glycine Amide |
| PDB | 2zb2_B | 0 | 160 | 1014 | 55 | 836 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
| PDB | 2zb2_A | 0 | 160 | 1014 | 55 | 836 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
| PDB | 3cem_B | 0 | 160 | 1010 | 30 | 807 | A Chain A, Human Liver Glycogen Phosphorylase A Complexed With Glcose And 5- Chloro-N-[4-(1,2-Dihydroxyethyl)phenyl]-1h-Indole-2-Carboxamide |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO778303 | 868 | 159 | 1013 | 0 |
| HO797178 | 399 | 615 | 1013 | 0 |
| HO613954 | 509 | 502 | 1010 | 0 |
| HO418036 | 587 | 351 | 934 | 0 |
| HO778303 | 39 | 122 | 160 | 0.0001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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