Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s240_110V6.1 |
Family | GT20 |
Protein Properties | Length: 854 Molecular Weight: 96006.2 Isoelectric Point: 6.8649 |
Chromosome | Chromosome/Scaffold: 240 Start: 643987 End: 652014 |
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 | 155 | 629 | 0 |
IHRSAQRLLVVANRLPVSATRLDGDKWDLQLSAGGLVSALLGVKQIFETRWIGWAGVSVHDERGRASLTEALALKGCVPVFLDDDTVDQYYNGYCNNVLW PLFHYIGLPQADRLAATRSLDSQYAAYQHANKLFAQVVFSQYQEGDVVWCHDYHLMCLPQELKTLNPRMKVGWFLHTPFPSSEIYRTLPLRSELLKAVLT ADLIGFHTYDYARHFVSACTRILGLEGTPEGVEDQGKLTRVAAFPIGIDPERFIQALETEQVKLHVKELLRFFAGRKVMLGVDRLDMIKGIPQKLLAFEM FLEKNPEWREKVMLVQIAVPTRTDVHEYQRLTSQVHEIVGRINGRYGTVTFVPIHHLDRSLAFHELCALYASTDVALVTSLRDGMNLVSYEYVACQNFKN TEGVLVLSEFAGAAQSLGAGAILVNPWNIREMYIAIEEALKMSDEERKERHRHNFTHVTTHTAQAWAHNFVSELY |
Full Sequence |
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Protein Sequence Length: 854 Download |
MPYSLTTKAS QKSKQLWEGD ESSGPSSTPQ RRFSLSSLGE LNYRPSNLTR TTSLTEEEVK 60 HDLSTPKVTP TPSVTSARVE RLVRERQLRR SGSCYTLGDE VDAKSEVLGG NGGMVGGSGD 120 RMGEWWAATE PQSSHSKAGA HTDNYESSRN LNDKIHRSAQ RLLVVANRLP VSATRLDGDK 180 WDLQLSAGGL VSALLGVKQI FETRWIGWAG VSVHDERGRA SLTEALALKG CVPVFLDDDT 240 VDQYYNGYCN NVLWPLFHYI GLPQADRLAA TRSLDSQYAA YQHANKLFAQ VVFSQYQEGD 300 VVWCHDYHLM CLPQELKTLN PRMKVGWFLH TPFPSSEIYR TLPLRSELLK AVLTADLIGF 360 HTYDYARHFV SACTRILGLE GTPEGVEDQG KLTRVAAFPI GIDPERFIQA LETEQVKLHV 420 KELLRFFAGR KVMLGVDRLD MIKGIPQKLL AFEMFLEKNP EWREKVMLVQ IAVPTRTDVH 480 EYQRLTSQVH EIVGRINGRY GTVTFVPIHH LDRSLAFHEL CALYASTDVA LVTSLRDGMN 540 LVSYEYVACQ NFKNTEGVLV LSEFAGAAQS LGAGAILVNP WNIREMYIAI EEALKMSDEE 600 RKERHRHNFT HVTTHTAQAW AHNFVSELYD TIVEAELRTL NEPPNLPVDS AKESFLNSKN 660 RLLVFGFNST ITATVEAPRR DQIKESKLGL HPGIKECLGT LCSDPNTDVV ILSGSKRDTL 720 EEVFGGFNIW LAAENGMYLR DLIGKWMPTM EHLNMDWKDS VQLVFDYFCA RTPRSFVEKR 780 ETSLVWNYKY ADLEFGRVQA RNMLQHLWTG PISNAAVDVV QGQKSVEVRP IGVSKVIFPA 840 RAPLFHRLGV DLA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN03063 | PLN03063 | 0 | 153 | 835 | 684 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
PLN03064 | PLN03064 | 0 | 138 | 835 | 701 | + alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional | ||
pfam00982 | Glyco_transf_20 | 0 | 160 | 630 | 476 | + 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. | ||
PRK14501 | PRK14501 | 0 | 161 | 835 | 677 | + putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional | ||
TIGR02400 | trehalose_OtsA | 0 | 161 | 630 | 471 | + 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]. |
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 |
GenBank | AAD00829.1 | 0 | 72 | 835 | 36 | 780 | SL-TPS/P [Selaginella lepidophylla] |
GenBank | ABO61742.1 | 0 | 160 | 835 | 91 | 767 | trehalose-phosphate synthase 1 [Solanum lycopersicum] |
RefSeq | XP_001769595.1 | 0 | 143 | 835 | 2 | 706 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001778505.1 | 0 | 161 | 835 | 1 | 675 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002531237.1 | 0 | 152 | 835 | 82 | 765 | 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 | 1gz5_D | 0 | 161 | 628 | 2 | 450 | A Chain A, Trehalose-6-Phosphate Synthase. Otsa |
PDB | 1gz5_C | 0 | 161 | 628 | 2 | 450 | A Chain A, Trehalose-6-Phosphate Synthase. Otsa |
PDB | 1gz5_B | 0 | 161 | 628 | 2 | 450 | A Chain A, Trehalose-6-Phosphate Synthase. Otsa |
PDB | 1gz5_A | 0 | 161 | 628 | 2 | 450 | A Chain A, Trehalose-6-Phosphate Synthase. Otsa |
PDB | 2wtx_D | 0 | 161 | 632 | 3 | 455 | 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 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
trehalose biosynthesis I | TREHALOSE6PSYN-RXN | EC-2.4.1.15 | α,α-trehalose-phosphate synthase (UDP-forming) |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC341849 | 267 | 384 | 650 | 0 |
FC390642 | 241 | 595 | 835 | 0 |
FC331811 | 240 | 418 | 657 | 0 |
DW069910 | 288 | 248 | 535 | 0 |
BJ946404 | 220 | 616 | 835 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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