y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30026.m001510 |
Family | GT20 |
Protein Properties | Length: 915 Molecular Weight: 103362 Isoelectric Point: 6.4122 |
Chromosome | Chromosome/Scaffold: 30026 Start: 568226 End: 577296 |
Description | trehalose-6-phosphate synthase |
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 |
GT20 | 81 | 548 | 0 |
KQRLLVVANRLPVSAVRRGEDSWQLEISVGGLVSALLGVKEFDARWIGWAGVNVHDEIGQKALTKALAEKRCIPVFLDEDVVHQYYNGYCNNILWPLFHY LGLPQEDRLATTRSFQSQFDAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEHNSNMKVGWFLHTPFPSSEIHRMLPSRTELLRSVLAADLVG FHTYDYARHFVSACTRILGLEGTPEGVEDQGKLTRVAAFPIGIDSDRFIRALELPQVQEHMKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEEFLEEN PDWRDKVVLLQIAVPTRTDVPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQAFKKGVLIL SEFAGAAQSLGAGALLVNPWNITEVAASIGYALNMPADEREKRHNHNFRHVTTHTSQEWAATFVSELN |
Full Sequence |
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Protein Sequence Length: 915 Download |
MPGNSCAPVT PRTRLERLLR DRELRKFNRI FNSNDDLGEG IVEELFANDS VLNETENSGP 60 LHEGTLLEGV DGCEWPDGHP KQRLLVVANR LPVSAVRRGE DSWQLEISVG GLVSALLGVK 120 EFDARWIGWA GVNVHDEIGQ KALTKALAEK RCIPVFLDED VVHQYYNGYC NNILWPLFHY 180 LGLPQEDRLA TTRSFQSQFD AYKKANQMFA DVVNEHYEEG DVVWCHDYHL MFLPKCLKEH 240 NSNMKVGWFL HTPFPSSEIH RMLPSRTELL RSVLAADLVG FHTYDYARHF VSACTRILGL 300 EGTPEGVEDQ GKLTRVAAFP IGIDSDRFIR ALELPQVQEH MKELKERFAG RKVMLGVDRL 360 DMIKGIPQKI LAFEEFLEEN PDWRDKVVLL QIAVPTRTDV PEYQKLTSQV HEIVGRINGR 420 FGTLTAVPIH HLDRSLDFHA LCALYAVTDV ALVTSLRDGM NLVSYEFVAC QAFKKGVLIL 480 SEFAGAAQSL GAGALLVNPW NITEVAASIG YALNMPADER EKRHNHNFRH VTTHTSQEWA 540 ATFVSELNDT IVEAQLRTRQ VLPLLPHQIA IERYLISNNR LLILGFNATL TELVDTSGRR 600 GGQIREMEPR LHPELKEPLR KLCSDEKTTV VVLSGSDRTI LDENFGEYNM WLAAENGMFL 660 RLTRGEWMTT MPENLNMDWV DSVKHVFEYF TERTPRSHFE LRETSLVWNY KYADVEFGRL 720 QARDMLQHLW TGPISNAAVD VVQGGRSVEV RAVGVTKGAA IDRILGEIVH NQGMKAPIDY 780 VLCVGHFLAK DEDIYTFFEP ELPIESPAVA RSRSPDHLVS PLPKIPCGKS RSKAHLKKQR 840 SLSTLEKSSI GSAAWRPIVR ERISVHEGSS VLDLKGENYF SCAVSRKRSN ARYLLGTSED 900 VVTLLKELAD SSSLS 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03064 | PLN03064 | 0 | 1 | 915 | 933 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PLN03063 | PLN03063 | 0 | 81 | 909 | 829 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PRK14501 | PRK14501 | 0 | 83 | 845 | 772 | + putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional | ||
TIGR02400 | trehalose_OtsA | 0 | 83 | 549 | 469 | + 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]. | ||
pfam00982 | Glyco_transf_20 | 0 | 82 | 549 | 474 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0005992 | trehalose biosynthetic 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 |
EMBL | CAA69879.1 | 0 | 1 | 913 | 1 | 940 | trehalose-6-phosphate synthase [Arabidopsis thaliana] |
RefSeq | NP_177979.1 | 0 | 1 | 913 | 1 | 940 | ATTPS1 (TREHALOSE-6-PHOSPHATE SYNTHASE); alpha,alpha-trehalose-phosphate synthase (UDP-forming)/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | XP_002305707.1 | 0 | 19 | 913 | 1 | 897 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331300.1 | 0 | 1 | 913 | 1 | 922 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522296.1 | 0 | 1 | 915 | 1 | 915 | trehalose-6-phosphate synthase, putative [Ricinus communis] |
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 | 1uqu_B | 0 | 83 | 559 | 3 | 466 | A Chain A, Trehalose-6-Phosphate From E. Coli Bound With Udp-Glucose. |
PDB | 1uqu_A | 0 | 83 | 559 | 3 | 466 | A Chain A, Trehalose-6-Phosphate From E. Coli Bound With Udp-Glucose. |
PDB | 1uqt_B | 0 | 83 | 559 | 3 | 466 | A Chain A, Trehalose-6-Phosphate From E. Coli Bound With Udp-Glucose. |
PDB | 1uqt_A | 0 | 83 | 559 | 3 | 466 | A Chain A, Trehalose-6-Phosphate From E. Coli Bound With Udp-Glucose. |
PDB | 2wtx_D | 0 | 83 | 559 | 3 | 466 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CX546763 | 304 | 71 | 372 | 0 |
DW069910 | 288 | 169 | 456 | 0 |
CV711307 | 293 | 81 | 373 | 0 |
ES813375 | 360 | 444 | 803 | 0 |
CB651133 | 280 | 110 | 389 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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