| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G133966_T01 |
| Family | GT20 |
| Protein Properties | Length: 375 Molecular Weight: 41350.9 Isoelectric Point: 7.4122 |
| Chromosome | Chromosome/Scaffold: 6 Start: 159247083 End: 159249932 |
| Description | trehalose-6-phosphate synthase |
| 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 |
| GT20 | 101 | 374 | 0 |
| MKQRLLVVANRLPVSANRRGEDHWSLEISAGGLVSALLGVKDVDAKWIGWAGVNVPDEIGQRALTKALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFH YLGLPQEDRLATTRNFESQFDAYKRANQMFADVVYQHYQEGDVIWCHDYHLMFLPKCLKDHDINMKVGWFLHTPFPSSEIYRTLPSRLELLRSVLCADLV GFHTYDYARHFVSACTRILGLEGTPEGVEDQGRLTRVAAFPIGIDSDRFKRALELPAVKRHINELTQRFAGRKV | |||
| Full Sequence |
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| Protein Sequence Length: 375 Download |
| MPTSSPFVGD SGTAGSPIRA ERAVGEHGRR YDVFASDAMD TDAAEAASAS AGAFALDGVH 60 SPGRASPANM EDAGGAAAGH AARPPLAGSR SGFRRLGLRG MKQRLLVVAN RLPVSANRRG 120 EDHWSLEISA GGLVSALLGV KDVDAKWIGW AGVNVPDEIG QRALTKALAE KRCIPVFLDE 180 EIVHQYYNGY CNNILWPLFH YLGLPQEDRL ATTRNFESQF DAYKRANQMF ADVVYQHYQE 240 GDVIWCHDYH LMFLPKCLKD HDINMKVGWF LHTPFPSSEI YRTLPSRLEL LRSVLCADLV 300 GFHTYDYARH FVSACTRILG LEGTPEGVED QGRLTRVAAF PIGIDSDRFK RALELPAVKR 360 HINELTQRFA GRKV* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd03788 | GT1_TPS | 3.0e-112 | 104 | 374 | 273 | + Trehalose-6-Phosphate Synthase (TPS) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain. | ||
| pfam00982 | Glyco_transf_20 | 2.0e-122 | 103 | 373 | 276 | + Glycosyltransferase family 20. Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex. | ||
| TIGR02400 | trehalose_OtsA | 2.0e-122 | 104 | 374 | 273 | + alpha,alpha-trehalose-phosphate synthase [UDP-forming]. This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., PMID:12890033) [Cellular processes, Adaptations to atypical conditions]. | ||
| PLN03063 | PLN03063 | 8.0e-174 | 102 | 374 | 273 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
| PLN03064 | PLN03064 | 0 | 102 | 374 | 273 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0005992 | trehalose biosynthetic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABF70084.1 | 0 | 85 | 374 | 87 | 376 | trehalose-6-phosphate synthase, putative [Musa balbisiana] |
| GenBank | ACI16353.1 | 0 | 101 | 374 | 1 | 274 | trehalose-6-P synthase [Triticum aestivum] |
| GenBank | EAY98715.1 | 0 | 101 | 374 | 1 | 274 | hypothetical protein OsI_20647 [Oryza sativa Indica Group] |
| RefSeq | NP_001123593.2 | 0 | 1 | 374 | 1 | 364 | trehalose-6-phosphate synthase [Zea mays] |
| RefSeq | XP_002440086.1 | 0 | 1 | 374 | 24 | 399 | hypothetical protein SORBIDRAFT_09g025790 [Sorghum bicolor] |
| 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 | 2wtx_D | 9e-28 | 104 | 345 | 3 | 229 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 2wtx_C | 9e-28 | 104 | 345 | 3 | 229 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 2wtx_B | 9e-28 | 104 | 345 | 3 | 229 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 2wtx_A | 9e-28 | 104 | 345 | 3 | 229 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 1uqu_B | 1e-27 | 104 | 345 | 3 | 229 | A Chain A, Trehalose-6-Phosphate From E. Coli Bound With Udp-Glucose. |
| Hydropathy |
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