| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os03g55090.1 |
| Family | GT35 |
| Protein Properties | Length: 592 Molecular Weight: 67205.1 Isoelectric Point: 5.3253 |
| Chromosome | Chromosome/Scaffold: 3 Start: 31332396 End: 31339163 |
| Description | Glycosyl transferase, family 35 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT35 | 186 | 586 | 0 |
| KLPRVVRMANLCVVGGHSVNGVAAIHSEIVKEDVFNSFYEMWPAKFQNKTNGVTPRRWIRFCNPELSAIISKWIGSDDWVLNTDKLAELKKFADDEDLQS EWRAAKKANKVKVVSLIREKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSAKDRINSFVPRVCIFGGKAFATYVQAKRIVKFITDVAA TVNHDPEIGDLLKVVFIPDYNVSVAEALIPASELSQHISTAGMEASGTSNMKFAMNGCILIGTLDGANVEIREEVGEENFFLFGAEAHEIAGLRKERAQG KFVPDPRFEEVKRFVRSGVFGTYNYDDLMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDKAYRDQKLWTRMSILNTASSSKFNSDRTIHEYAKDIWDI K | |||
| Full Sequence |
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| Protein Sequence Length: 592 Download |
| MNDTHPTLCI PELMRILIDV KGLSWNEAWS ITERTVAYTN HTVLPEALEK WSLDIMQKLL 60 PRHVEIIEKI DGELMNIIIS KYGTEDTSLL KKKIKEMRIL DNIDLPDSIA KLFVKPKEKK 120 ESPAKLKEKL LVKSLEPSVV VEEKTVSKVE INEDSEEVEV DSEEVVEAEN EDSEDELDPF 180 VKSDPKLPRV VRMANLCVVG GHSVNGVAAI HSEIVKEDVF NSFYEMWPAK FQNKTNGVTP 240 RRWIRFCNPE LSAIISKWIG SDDWVLNTDK LAELKKFADD EDLQSEWRAA KKANKVKVVS 300 LIREKTGYIV SPDAMFDVQV KRIHEYKRQL LNILGIVYRY KKMKEMSAKD RINSFVPRVC 360 IFGGKAFATY VQAKRIVKFI TDVAATVNHD PEIGDLLKVV FIPDYNVSVA EALIPASELS 420 QHISTAGMEA SGTSNMKFAM NGCILIGTLD GANVEIREEV GEENFFLFGA EAHEIAGLRK 480 ERAQGKFVPD PRFEEVKRFV RSGVFGTYNY DDLMGSLEGN EGYGRADYFL VGKDFPSYIE 540 CQEKVDKAYR DQKLWTRMSI LNTASSSKFN SDRTIHEYAK DIWDIKPVIL P* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 2.0e-35 | 1 | 101 | 101 | + 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 | 3.0e-41 | 1 | 102 | 102 | + 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 | 188 | 585 | 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. | ||
| pfam00343 | Phosphorylase | 0 | 189 | 587 | 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 | 189 | 585 | 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 |
| GO:0006950 | response to stress |
| GO:0008152 | metabolic process |
| GO:0009536 | plastid |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAK15695.1 | 0 | 1 | 591 | 338 | 928 | AF327055_1 alpha 1,4-glucan phosphorylase L isozyme [Oryza sativa] |
| GenBank | AAK16190.1 | 0 | 1 | 591 | 361 | 951 | AC079887_22 putative phosphorylase [Oryza sativa Japonica Group] |
| DDBJ | BAF13244.2 | 0 | 1 | 591 | 1 | 591 | Os03g0758100 [Oryza sativa Japonica Group] |
| DDBJ | BAG49328.1 | 0 | 1 | 591 | 388 | 978 | plastidial starch phosphorylase 1 [Oryza sativa Japonica Group] |
| RefSeq | NP_001051330.1 | 0 | 1 | 591 | 39 | 629 | Os03g0758100 [Oryza sativa (japonica cultivar-group)] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1qm5_B | 0 | 191 | 586 | 404 | 795 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
| PDB | 1qm5_B | 5e-23 | 1 | 78 | 305 | 382 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
| PDB | 1qm5_A | 0 | 191 | 586 | 404 | 795 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
| PDB | 1qm5_A | 5e-23 | 1 | 78 | 305 | 382 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
| PDB | 1e4o_B | 0 | 191 | 586 | 404 | 795 | A Chain A, Phosphorylase Recognition And Phosphorylysis Of Its Oligosaccharide Substrate: Answers To A Long Outstanding Question |
| 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 |
| HO797178 | 401 | 192 | 592 | 0 |
| HO778303 | 401 | 192 | 592 | 0 |
| HO778303 | 124 | 1 | 124 | 0 |
| HO620767 | 403 | 190 | 592 | 0 |
| HO613954 | 403 | 190 | 592 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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