| Basic Information | |
|---|---|
| Species | Ricinus communis |
| Cazyme ID | 29630.m000793 |
| Family | GT35 |
| Protein Properties | Length: 977 Molecular Weight: 111023 Isoelectric Point: 6.4876 |
| Chromosome | Chromosome/Scaffold: 29630 Start: 104770 End: 113523 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 173 | 972 | 0 |
| ALTKLGHNLENVARQEPDAALGNGGLGRLASCFLDSLATLNYPAWGYGLRYKYGLFKQRITKDGQEEVAEDWLEMGNPWEIVRNDVAYPVKFYGKVVSGS DGRKHWIGGEDIKAVAYDVPIPGYKTKSTINLRLWSTKAPAEDLDLSAFNSGDHTKAYETLANAEKICHILYPGDDSVEGKILRLKQQYTLCSASLQDII VRFERRSGSHVKWEEFPEKVAVQMNDTHPTLCIPELMRILMDLKGLSWKEAWNITQRTVAYTNHTVLPEALEKWSLDLMQKLLPRHVEIIEMIDEELIRT IVSEYGREDLDLLNKKLKEMRILENVDLPDAFADLIIKTKESSAASTTKEPEDADDEIKLVNEKDELESKEESENKDEAERKDELENKNTQKKEKAVVEP PPKMVRMANLCVVGGHAVNGVAEIHSEIVKDEVFNVFYQLWPKKFQNKTNGVTPRRWIRFCNPDLSKIITDWTGSEDWVLNTEKLAELRKFSDNEDLQTQ WRAAKRSNKMKVVQLIKEKTGYSVSTDAMFDIQVKRIHEYKRQLLNILGIVYRYKKMKEMSAAERKKEYVPRVCIFGGKAFATYLQAKRIVKFITDVGAT VNHDPEIGDLLKVVFVPNYNVSVAELLIPASELSQHISTAGMEASGTSNMKFSMNGCVLIGTLDGANVEIRKEVGEDNFFLFGAKAHEIAGLRKERAEGK FVPDPRFEEVKEFVRSGVFGTYDYDELLGSLEGNEGFGRGDYFLVGKDFPSYLECQEKVDKAYRDQKRWTKMSIMNTAGSYYFSSDRTIHEYARDIWNIE | |||
| Full Sequence |
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| Protein Sequence Length: 977 Download |
| MASSSGTGSH LCRSWQCSGV SRFVHFGAKS SSKWRSNLLL IRTFRSRPVS TSFSVRNVST 60 EPKTKIVDSL SHEAAPSNRS LFNLDSSSIA SSIKYHAEFT PSFSPEQFEL PKAFFATAQS 120 VRDSLIINWN STYEYYEKLN VKQAYYMSME FLQGRALLNA VGNLELTGAY AEALTKLGHN 180 LENVARQEPD AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ RITKDGQEEV 240 AEDWLEMGNP WEIVRNDVAY PVKFYGKVVS GSDGRKHWIG GEDIKAVAYD VPIPGYKTKS 300 TINLRLWSTK APAEDLDLSA FNSGDHTKAY ETLANAEKIC HILYPGDDSV EGKILRLKQQ 360 YTLCSASLQD IIVRFERRSG SHVKWEEFPE KVAVQMNDTH PTLCIPELMR ILMDLKGLSW 420 KEAWNITQRT VAYTNHTVLP EALEKWSLDL MQKLLPRHVE IIEMIDEELI RTIVSEYGRE 480 DLDLLNKKLK EMRILENVDL PDAFADLIIK TKESSAASTT KEPEDADDEI KLVNEKDELE 540 SKEESENKDE AERKDELENK NTQKKEKAVV EPPPKMVRMA NLCVVGGHAV NGVAEIHSEI 600 VKDEVFNVFY QLWPKKFQNK TNGVTPRRWI RFCNPDLSKI ITDWTGSEDW VLNTEKLAEL 660 RKFSDNEDLQ TQWRAAKRSN KMKVVQLIKE KTGYSVSTDA MFDIQVKRIH EYKRQLLNIL 720 GIVYRYKKMK EMSAAERKKE YVPRVCIFGG KAFATYLQAK RIVKFITDVG ATVNHDPEIG 780 DLLKVVFVPN YNVSVAELLI PASELSQHIS TAGMEASGTS NMKFSMNGCV LIGTLDGANV 840 EIRKEVGEDN FFLFGAKAHE IAGLRKERAE GKFVPDPRFE EVKEFVRSGV FGTYDYDELL 900 GSLEGNEGFG RGDYFLVGKD FPSYLECQEK VDKAYRDQKR WTKMSIMNTA GSYYFSSDRT 960 IHEYARDIWN IEPVILP 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 2.0e-137 | 173 | 477 | 306 | + 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 | 576 | 971 | 401 | + 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 | 90 | 477 | 392 | + 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 | 577 | 973 | 402 | + 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 | 576 | 971 | 401 | + 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 - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1z8d_A | 0 | 564 | 973 | 427 | 830 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 1z8d_A | 0 | 114 | 496 | 53 | 433 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_B | 0 | 575 | 969 | 402 | 792 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_B | 0 | 140 | 476 | 57 | 384 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| PDB | 2azd_A | 0 | 575 | 969 | 402 | 792 | A Chain A, Crystal Structure Of Human Muscle Glycogen Phosphorylase A With Amp And Glucose |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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