Protein : Qrob_P0341260.2 Q. robur
Protein Identifier  ? Qrob_P0341260.2 Organism . Name  Quercus robur
Score  0.0 Score Type  egn
Protein Description  (M=4) K01087 - trehalose-phosphatase [EC:3.1.3.12] Code Enzyme  EC:3.1.3.12
Gene Prediction Quality  validated Protein length 

Sequence

Length: 219  
Kegg Orthology  K01087
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0 Synonyms

2 GO Terms

Identifier Name Description
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0005992 trehalose biosynthetic process The chemical reactions and pathways resulting in the formation of trehalose, a disaccharide isomeric with sucrose and obtained from certain lichens and fungi.

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103959771 1 201 + 201 Gaps:36 75.00 316 58.65 4e-85 probable trehalose-phosphate phosphatase 2
blastp_kegg lcl|mdm:103404566 1 201 + 201 Gaps:36 75.00 316 59.07 5e-85 probable trehalose-phosphate phosphatase 2
blastp_kegg lcl|pxb:103965858 1 201 + 201 Gaps:36 75.00 316 58.23 4e-83 probable trehalose-phosphate phosphatase 2
blastp_kegg lcl|gmx:100799466 1 201 + 201 Gaps:37 76.04 313 54.20 3e-78 probable trehalose-phosphate phosphatase 3-like
blastp_kegg lcl|pvu:PHAVU_010G112900g 1 205 + 205 Gaps:39 77.32 313 52.89 6e-77 hypothetical protein
blastp_kegg lcl|cic:CICLE_v10023731mg 1 203 + 203 Gaps:36 73.54 325 53.56 1e-76 hypothetical protein
blastp_kegg lcl|cit:102627037 1 203 + 203 Gaps:27 72.61 314 53.95 1e-72 probable trehalose-phosphate phosphatase D-like
blastp_kegg lcl|pper:PRUPE_ppa026983mg 1 218 + 218 Gaps:38 70.14 365 47.27 1e-71 hypothetical protein
blastp_kegg lcl|pxb:103958159 1 200 + 200 Gaps:35 63.00 373 49.36 2e-71 probable trehalose-phosphate phosphatase 4
blastp_kegg lcl|mdm:103439858 1 200 + 200 Gaps:35 62.50 376 48.94 2e-71 probable trehalose-phosphate phosphatase 4
blastp_uniprot_sprot sp|Q6ZGP8|TPP4_ORYSJ 1 200 + 200 Gaps:21 59.67 367 46.12 2e-61 Probable trehalose-phosphate phosphatase 4 OS Oryza sativa subsp. japonica GN TPP4 PE 2 SV 1
blastp_uniprot_sprot sp|Q6H5L4|TPP7_ORYSJ 1 200 + 200 Gaps:28 60.80 375 43.42 6e-60 Probable trehalose-phosphate phosphatase 7 OS Oryza sativa subsp. japonica GN TPP7 PE 2 SV 2
blastp_uniprot_sprot sp|Q7XI41|TPP3_ORYSJ 1 199 + 199 Gaps:31 62.84 366 43.48 7e-58 Probable trehalose-phosphate phosphatase 3 OS Oryza sativa subsp. japonica GN TPP3 PE 2 SV 1
blastp_uniprot_sprot sp|Q6ZAL2|TPP6_ORYSJ 1 200 + 200 Gaps:26 61.08 370 43.36 9e-58 Probable trehalose-phosphate phosphatase 6 OS Oryza sativa subsp. japonica GN TPP6 PE 2 SV 1
blastp_uniprot_sprot sp|Q67XC9|TPPD_ARATH 1 200 + 200 Gaps:25 60.98 369 42.67 1e-56 Probable trehalose-phosphate phosphatase D OS Arabidopsis thaliana GN TPPD PE 2 SV 1
blastp_uniprot_sprot sp|Q75WV3|TPP1_ORYSJ 1 200 + 200 Gaps:29 61.19 371 44.05 2e-56 Probable trehalose-phosphate phosphatase 1 OS Oryza sativa subsp. japonica GN TPP1 PE 1 SV 1
blastp_uniprot_sprot sp|Q5HZ05|TPPJ_ARATH 1 200 + 200 Gaps:28 61.08 370 46.02 3e-56 Probable trehalose-phosphate phosphatase J OS Arabidopsis thaliana GN TPPJ PE 1 SV 1
blastp_uniprot_sprot sp|O64896|TPPA_ARATH 1 203 + 203 Gaps:42 62.08 385 41.84 2e-55 Trehalose-phosphate phosphatase A OS Arabidopsis thaliana GN TPPA PE 1 SV 1
blastp_uniprot_sprot sp|Q9SUW0|TPPG_ARATH 1 200 + 200 Gaps:36 62.60 377 43.22 6e-54 Probable trehalose-phosphate phosphatase G OS Arabidopsis thaliana GN TPPG PE 2 SV 1
blastp_uniprot_sprot sp|Q9C9S4|TPPB_ARATH 1 200 + 200 Gaps:25 60.16 374 42.67 8e-54 Trehalose-phosphate phosphatase B OS Arabidopsis thaliana GN TPPB PE 1 SV 1
rpsblast_cdd gnl|CDD|178192 1 200 + 200 Gaps:36 61.46 384 42.37 3e-59 PLN02580 PLN02580 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|178591 1 200 + 200 Gaps:36 61.75 366 43.36 7e-49 PLN03017 PLN03017 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|177812 1 200 + 200 Gaps:27 63.56 354 43.11 2e-48 PLN02151 PLN02151 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|145482 1 186 + 186 Gaps:28 90.21 235 26.89 3e-28 pfam02358 Trehalose_PPase Trehalose-phosphatase. This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes. Trehalose is a common disaccharide of bacteria fungi and invertebrates that appears to play a major role in desiccation tolerance.
rpsblast_cdd gnl|CDD|32061 1 196 + 196 Gaps:14 78.20 266 18.75 2e-16 COG1877 OtsB Trehalose-6-phosphatase [Carbohydrate transport and metabolism].
rpsblast_cdd gnl|CDD|161997 1 197 + 197 Gaps:38 88.11 244 24.65 1e-15 TIGR00685 T6PP trehalose-phosphatase. Trehalose a neutral disaccharide of two glucose residues is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species including E. coli Saccharomyces cerevisiae and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme trehalose-phosphatase removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified roughly half of these are of the fungal type with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes.
rpsblast_cdd gnl|CDD|184712 1 197 + 197 Gaps:34 28.51 726 25.12 3e-08 PRK14501 PRK14501 putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB Provisional.
rpsblast_kog gnl|CDD|36268 1 206 + 206 Gaps:51 35.11 732 22.96 7e-25 KOG1050 KOG1050 KOG1050 Trehalose-6-phosphate synthase component TPS1 and related subunits [Carbohydrate transport and metabolism].

7 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 1 215 215 PTHR10788 none none none
SUPERFAMILY 2 198 197 SSF56784 none none IPR023214
Pfam 1 153 153 PF02358 none Trehalose-phosphatase IPR003337
Gene3D 127 201 75 G3DSA:3.40.50.1000 none none IPR023214
Gene3D 1 48 48 G3DSA:3.40.50.1000 none none IPR023214
PANTHER 1 215 215 PTHR10788:SF19 none none none
TIGRFAM 6 156 151 TIGR00685 none T6PP: trehalose-phosphatase IPR003337

0 Localization

0 Qtllist

0 Targeting