Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna15723.1-v1.0-hybrid |
Family | GT20 |
Protein Properties | Length: 961 Molecular Weight: 109446 Isoelectric Point: 6.2855 |
Chromosome | Chromosome/Scaffold: 6 Start: 23121515 End: 23128265 |
Description | trehalose-6-phosphate synthase |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT20 | 537 | 709 | 0 |
IGNKFFPIGTDSDRFIRALEVPQVQEHIRELKERFAGRKYLSTIDRGCWVMLGVDRRDMIKGIPQKILAFENFLEENPIWRDKVVLLQIAVPTRTDVPEY QKLTSQVHEIVGRINGRFGSLTAVPINHLDHSLDFHALCALYAVTDVALVTSLRDGMNLVSYEYVACQDAKRG |
Full Sequence |
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Protein Sequence Length: 961 Download |
MAEALVSVLL EQLASIIHQQ VEQHVKLVVN VEKDVANLTH NFRAIEAVLK DAEERQVKEA 60 SVKLWLDDLK DVSNEMEDVL DDWNTEILRL HIEKQEKEES GNAVDTTKKK FLTKNECSVL 120 DVQGKTKVEV PVGNKFRHLT ITSARDGPFS VCFDRRRSLR TLATFSCRIT SLDREFVSQL 180 KCVRTLNLRD NGVEELPEEV GGLVHLRYLD LSCNKWKRLP DTLCNLINLE TLRLEKCGGL 240 EELPEGMGKL ITLRHLRVKG CDRHMKLPKS IAKLTSLQTL DQVNISHDGS KASDLRNMDQ 300 LQGKLEVSWW EPVNDAAKDY AEQANLVNQK HLVSLTLNLW NGTKDSIIQE EMLNALQPNP 360 NLEALKIYNY SGTTLCGPRW LNVSLHNLRH LAFYACHGCE FVPLLVLGKL VSLEILRFRN 420 MDELKKVGHE YSLESSSSSS SSLEVTSFPN LKKLVFYYLR EWEEWEGMPA GLSKDSLASI 480 KVMPCLSTLE IDYCPKLKTL PDFLWKTPLQ NLSIDRSRIL EEGMEWHKIS HIPNIKIGNK 540 FFPIGTDSDR FIRALEVPQV QEHIRELKER FAGRKYLSTI DRGCWVMLGV DRRDMIKGIP 600 QKILAFENFL EENPIWRDKV VLLQIAVPTR TDVPEYQKLT SQVHEIVGRI NGRFGSLTAV 660 PINHLDHSLD FHALCALYAV TDVALVTSLR DGMNLVSYEY VACQDAKRGY KKGEEADRDS 720 NKLEILKFIL IGSVKVSLDS VWKEFYLVSD AMGFNTTLTE PVDTPERRGD QIKEMELKLH 780 PDLIEPLTAL CNDPNTTIVV LSGSDRAVLD ENFGKLDMWL AAENGMFLRL TKGEWMTTMP 840 EHMDMEWVES IFEYFTERTP RSHFELRVTS LMWNYKYADV DFGRLQARDM LLHLWTGPIS 900 NASVDVVQGS RSVEVRAVGV TKGAVIDRIL GEIVHSKPMT SPIDYVLCIG HFLGKCSHCT 960 * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR02400 | trehalose_OtsA | 2.0e-80 | 542 | 709 | 168 | + 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 | 7.0e-87 | 542 | 709 | 168 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PLN03063 | PLN03063 | 5.0e-103 | 752 | 955 | 207 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PLN03064 | PLN03064 | 3.0e-107 | 542 | 709 | 168 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PLN03064 | PLN03064 | 3.0e-137 | 752 | 955 | 207 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0005515 | protein binding |
GO:0005992 | trehalose biosynthetic process |
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 | 4e-23 | 587 | 705 | 258 | 376 | 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 | 4e-23 | 587 | 705 | 258 | 376 | 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 | 4e-23 | 587 | 705 | 258 | 376 | 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 | 4e-23 | 587 | 705 | 258 | 376 | 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 | 1gz5_D | 5e-23 | 587 | 705 | 257 | 375 | A Chain A, Trehalose-6-Phosphate Synthase. Otsa |
Sequence Alignments (This image is cropped. Click for full image.) |
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