| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi1g08070.1 |
| Family | GT35 |
| Protein Properties | Length: 979 Molecular Weight: 109258 Isoelectric Point: 5.3575 |
| Chromosome | Chromosome/Scaffold: 1 Start: 5684232 End: 5691628 |
| 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 | |||
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| Family | Start | End | Evalue |
| GT35 | 163 | 525 | 0 |
| ALKQLGQNLEDVASQEPDPALGNGGLGRLASCFLDSLATLNYPAWGYGLRYRYGLFKQIITKDGQEEVAENWLEMGNPWEIVRNDVSYPVKFYGKVVEGT DGRKHWIGGENIKAVAHDVPIPGYKTKTTNNLRLWSTTVPSQDFDLGAFNAGDHAKANQAHLNAEKICHVLYPGDESSEGKVLRLKQQYTLCSASLQDII SRFETRAGDSLNWEDFPSKVAVQMNDTHPTLCIPELMRILIDVKGLSWNKAWSITERTVAYTNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDGELMNG IISKYGTADISLLKQKLKEMRILDNVDLPDSIAKLFIKPKEKKESPSKSKEKLLVKSLESMAE | |||
| GT35 | 569 | 972 | 0 |
| KSDPKLPRVVRMANLCVVGGHSVNGVAEIHSEIVKQDVFNSFYEMWPAKFQNKTNGVTPRRWIRFCNPELSAIISKWIASDEWVLNTDKLAELKKFADNE DLQSEWRTTKRNNKMKVVSLIRDQTGYVVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMDAKDRIKSFVPRVCIFGGKAFATYVQAKRIVKFIT DVAATVNHDPDIGDLLKVVFVPDYNVSVAETLIPASELSQHISTAGMEASGTSNMKFSMNGCILIGTLDGANVEIREEVGEENFFLFGAEAPEIAGLRKE RAQGKFVPDPRFEEVKKYVRSGVFGTSNYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDEAYRDQKLWTRMSILNTAGSPKFSSDRTIHEYAKD IWDI | |||
| Full Sequence |
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| Protein Sequence Length: 979 Download |
| MATASPPLTL ATSYPPLAAA AGGGRLVVVG AGGGGVAPRR GPRGLAVRSV ASDREVQGPS 60 ASAEEELSSV LSSIDSSAIA SNIKHHAEFT PLFSPDHISP LKAYHATAKS VFDALIMNWN 120 ATYDYYNRMN VKQAYYLSME FLQGRALTNA IGNLELTGQY AEALKQLGQN LEDVASQEPD 180 PALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYRYGLFKQ IITKDGQEEV AENWLEMGNP 240 WEIVRNDVSY PVKFYGKVVE GTDGRKHWIG GENIKAVAHD VPIPGYKTKT TNNLRLWSTT 300 VPSQDFDLGA FNAGDHAKAN QAHLNAEKIC HVLYPGDESS EGKVLRLKQQ YTLCSASLQD 360 IISRFETRAG DSLNWEDFPS KVAVQMNDTH PTLCIPELMR ILIDVKGLSW NKAWSITERT 420 VAYTNHTVLP EALEKWSLDI MQKLLPRHVE IIETIDGELM NGIISKYGTA DISLLKQKLK 480 EMRILDNVDL PDSIAKLFIK PKEKKESPSK SKEKLLVKSL ESMAEVEEKI ESEEEENILP 540 ETAEEKAESE EIADAEKEEP EYELDPFAKS DPKLPRVVRM ANLCVVGGHS VNGVAEIHSE 600 IVKQDVFNSF YEMWPAKFQN KTNGVTPRRW IRFCNPELSA IISKWIASDE WVLNTDKLAE 660 LKKFADNEDL QSEWRTTKRN NKMKVVSLIR DQTGYVVSPD AMFDVQVKRI HEYKRQLLNI 720 LGIVYRYKKM KEMDAKDRIK SFVPRVCIFG GKAFATYVQA KRIVKFITDV AATVNHDPDI 780 GDLLKVVFVP DYNVSVAETL IPASELSQHI STAGMEASGT SNMKFSMNGC ILIGTLDGAN 840 VEIREEVGEE NFFLFGAEAP EIAGLRKERA QGKFVPDPRF EEVKKYVRSG VFGTSNYDEL 900 MGSLEGNEGY GRADYFLVGK DFPSYIECQE KVDEAYRDQK LWTRMSILNT AGSPKFSSDR 960 TIHEYAKDIW DISPVILP* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00343 | Phosphorylase | 1.0e-149 | 163 | 486 | 325 | + 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 | 575 | 972 | 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. | ||
| cd04300 | GT1_Glycogen_Phosphorylase | 0 | 82 | 487 | 411 | + 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 | 576 | 974 | 401 | + 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 | 972 | 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 | |
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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 |
| GenBank | AAK15695.1 | 0 | 48 | 978 | 1 | 928 | AF327055_1 alpha 1,4-glucan phosphorylase L isozyme [Oryza sativa] |
| GenBank | ACC59201.1 | 0 | 1 | 978 | 1 | 971 | plastid alpha-1,4-glucan phosphorylase [Triticum aestivum] |
| DDBJ | BAG49328.1 | 0 | 1 | 978 | 1 | 978 | plastidial starch phosphorylase 1 [Oryza sativa Japonica Group] |
| GenBank | EEC76210.1 | 0 | 1 | 978 | 1 | 964 | hypothetical protein OsI_13605 [Oryza sativa Indica Group] |
| GenBank | EEE59962.1 | 0 | 1 | 978 | 1 | 977 | hypothetical protein OsJ_12655 [Oryza sativa Japonica Group] |
| 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 | 2azd_B | 0 | 578 | 970 | 404 | 792 | A Chain A, The Crystal Structure Of Pgip (Polygalacturonase Inhibiting Protein), A Leucine Rich Repeat Protein Involved In Plant Defense |
| PDB | 2azd_B | 0 | 130 | 456 | 57 | 375 | A Chain A, The Crystal Structure Of Pgip (Polygalacturonase Inhibiting Protein), A Leucine Rich Repeat Protein Involved In Plant Defense |
| PDB | 2azd_A | 0 | 578 | 970 | 404 | 792 | A Chain A, The Crystal Structure Of Pgip (Polygalacturonase Inhibiting Protein), A Leucine Rich Repeat Protein Involved In Plant Defense |
| PDB | 2azd_A | 0 | 130 | 456 | 57 | 375 | A Chain A, The Crystal Structure Of Pgip (Polygalacturonase Inhibiting Protein), A Leucine Rich Repeat Protein Involved In Plant Defense |
| PDB | 2aw3_B | 0 | 578 | 970 | 404 | 792 | A Chain A, The Crystal Structure Of Pgip (Polygalacturonase Inhibiting Protein), A Leucine Rich Repeat Protein Involved In Plant Defense |
| Metabolic Pathways | |||
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| 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 | 579 | 979 | 0 |
| HO778303 | 401 | 579 | 979 | 0 |
| HO778303 | 397 | 103 | 499 | 0 |
| HO620767 | 403 | 577 | 979 | 0 |
| HO613954 | 403 | 577 | 979 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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