| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_001096m |
| Family | GT35 |
| Protein Properties | Length: 956 Molecular Weight: 109138 Isoelectric Point: 5.0932 |
| Chromosome | Chromosome/Scaffold: 12373 Start: 57969 End: 63068 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GT35 | 164 | 949 | 0 |
| LRKLGHNLEDVARQEPDAALGNGGLGRLASCFLDSMATLNYPAWGYGLRYKYGLFKQLITKDGQEEVAESWLEMGNPWEIVRNDISYPVKFYGKVILKPD GSKAWIGGENITAVAYDVPIPGYKTKTTINLRLWSTKVAPEEFDLRAFNTGDHAKAFAAVNNAEKICYILYPGDESIEGKTLRLKQQYTLCSASLQDIIA HFERRSGESVNWEIFPDKVAVQMNDTHPTLCIPELIRILMDVKGLSWKEAWNITRRTVAYTNHTVLPEALEKWSLELLQDLLPRHVEIIKMIDEELIHTI MAEYGTEDLDLLRQKFKEMRILDNVELPDTVIPLLVKSRDSSSVDAIEYVDEVEDPDEETESAKEEEPTEEEEEKEENDVKFEPDPALPRLVRMANLCVV GGYAVNGVAEIHSEIVKNEVFNEFYKLWPEKFQNKTNGVTPRRWIRFCNPDLSKIITKWTGNEDWVLSTENLQILRKFADNENLQAEWREAKRMNKMKVA AFLKEKTGYTVNPDSMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSPEERKACYVPRVCIFGGKAFATYVQAKRIVKFITDVGATVNHDEEIGDLLKV VFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFAMNGCVLIGTLDGANVEIRQEVGEDNFFLFGARADEIAGLRKERAEGKFVADLRFEEVKAF VRSGVFGPYDYEELMGSLEGNEGYGRADYFLVGKDFPSYLECQEKVDEAYRDQKRWTRMSILNTAGSYKFSSDRTIHEYARDIWRI | |||
| Full Sequence |
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| Protein Sequence Length: 956 Download |
| MATLPFPAAQ SKSKFPSRFT HFNYRATLSK LFFTTPFLNH SRRRNLSVKN IASDQRQDLQ 60 DPVTRGDSLD TSVPDSGSIA FRIKYHAEFT PSFSPEHFEL PKAFMATAES VRDLLIINWN 120 TTFEYYVKMN VKQAYYLSME FLQGRALLNA IGNLELSGAY AEDLRKLGHN LEDVARQEPD 180 AALGNGGLGR LASCFLDSMA TLNYPAWGYG LRYKYGLFKQ LITKDGQEEV AESWLEMGNP 240 WEIVRNDISY PVKFYGKVIL KPDGSKAWIG GENITAVAYD VPIPGYKTKT TINLRLWSTK 300 VAPEEFDLRA FNTGDHAKAF AAVNNAEKIC YILYPGDESI EGKTLRLKQQ YTLCSASLQD 360 IIAHFERRSG ESVNWEIFPD KVAVQMNDTH PTLCIPELIR ILMDVKGLSW KEAWNITRRT 420 VAYTNHTVLP EALEKWSLEL LQDLLPRHVE IIKMIDEELI HTIMAEYGTE DLDLLRQKFK 480 EMRILDNVEL PDTVIPLLVK SRDSSSVDAI EYVDEVEDPD EETESAKEEE PTEEEEEKEE 540 NDVKFEPDPA LPRLVRMANL CVVGGYAVNG VAEIHSEIVK NEVFNEFYKL WPEKFQNKTN 600 GVTPRRWIRF CNPDLSKIIT KWTGNEDWVL STENLQILRK FADNENLQAE WREAKRMNKM 660 KVAAFLKEKT GYTVNPDSMF DVQVKRIHEY KRQLLNILGI VYRYKKMKEM SPEERKACYV 720 PRVCIFGGKA FATYVQAKRI VKFITDVGAT VNHDEEIGDL LKVVFVPDYN VSVAEVLIPG 780 SELSQHISTA GMEASGTSNM KFAMNGCVLI GTLDGANVEI RQEVGEDNFF LFGARADEIA 840 GLRKERAEGK FVADLRFEEV KAFVRSGVFG PYDYEELMGS LEGNEGYGRA DYFLVGKDFP 900 SYLECQEKVD EAYRDQKRWT RMSILNTAGS YKFSSDRTIH EYARDIWRID PVVLP* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 1.0e-133 | 164 | 486 | 323 | + 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 | 0 | 552 | 949 | 403 | + 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 82 | 487 | 410 | + 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 | 553 | 951 | 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. | ||
| TIGR02093 | P_ylase | 0 | 553 | 949 | 402 | + 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]. | ||
| 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 | CBI27267.1 | 0 | 1 | 955 | 1 | 933 | unnamed protein product [Vitis vinifera] |
| Swiss-Prot | P53535 | 0 | 52 | 955 | 54 | 974 | 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 | 955 | 1 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002316098.1 | 0 | 1 | 955 | 1 | 953 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512108.1 | 0 | 1 | 955 | 1 | 973 | 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 | 555 | 951 | 440 | 830 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 1z8d_A | 0 | 104 | 477 | 53 | 428 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 4el5_A | 0 | 555 | 951 | 428 | 818 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 4el5_A | 0 | 104 | 477 | 41 | 416 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 4el0_A | 0 | 555 | 951 | 428 | 818 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| 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 | ||||
|---|---|---|---|---|
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| Hit | Length | Start | End | EValue |
| HO797178 | 401 | 556 | 956 | 0 |
| HO778303 | 401 | 556 | 956 | 0 |
| HO778303 | 405 | 103 | 507 | 0 |
| HO620767 | 403 | 554 | 956 | 0 |
| HO778303 | 71 | 42 | 105 | 0.00000004 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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