Protein : Qrob_P0321590.2 Q. robur
Protein Identifier  ? Qrob_P0321590.2 Organism . Name  Quercus robur
Score  100.0 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: 348  
Kegg Orthology  K01087
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0008152 metabolic process The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
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.

32 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pxb:103958159 1 338 + 338 Gaps:18 94.37 373 69.89 4e-163 probable trehalose-phosphate phosphatase 4
blastp_kegg lcl|mdm:103439858 1 338 + 338 Gaps:18 93.62 376 69.60 9e-163 probable trehalose-phosphate phosphatase 4
blastp_kegg lcl|pper:PRUPE_ppa026983mg 1 338 + 338 Gaps:18 96.99 365 69.21 2e-161 hypothetical protein
blastp_kegg lcl|pmum:103333663 1 338 + 338 Gaps:21 94.41 376 69.01 5e-159 probable trehalose-phosphate phosphatase C
blastp_kegg lcl|pxb:103948101 1 338 + 338 Gaps:18 75.54 466 69.03 1e-158 probable trehalose-phosphate phosphatase 4
blastp_kegg lcl|cit:102629242 1 322 + 322 Gaps:13 90.14 365 69.30 1e-157 probable trehalose-phosphate phosphatase D-like
blastp_kegg lcl|cic:CICLE_v10006768mg 1 322 + 322 Gaps:13 94.00 350 69.30 1e-157 hypothetical protein
blastp_kegg lcl|rcu:RCOM_1580260 1 334 + 334 Gaps:12 90.41 365 70.30 3e-156 trehalose-6-phosphate synthase putative (EC:3.1.3.12)
blastp_kegg lcl|mdm:103445424 1 338 + 338 Gaps:18 94.37 373 67.33 1e-155 probable trehalose-phosphate phosphatase C
blastp_kegg lcl|pxb:103943455 1 338 + 338 Gaps:18 94.37 373 66.19 2e-152 probable trehalose-phosphate phosphatase C
blastp_pdb 1u02_A 71 283 + 213 Gaps:39 77.82 239 27.42 6e-07 mol:protein length:239 trehalose-6-phosphate phosphatase related pro
blastp_uniprot_sprot sp|Q9FWQ2|TPP2_ORYSJ 31 330 + 300 Gaps:13 79.84 382 54.43 6e-111 Probable trehalose-phosphate phosphatase 2 OS Oryza sativa subsp. japonica GN TPP2 PE 1 SV 1
blastp_uniprot_sprot sp|Q6ZGP8|TPP4_ORYSJ 44 340 + 297 Gaps:21 77.38 367 57.39 4e-109 Probable trehalose-phosphate phosphatase 4 OS Oryza sativa subsp. japonica GN TPP4 PE 2 SV 1
blastp_uniprot_sprot sp|Q67XC9|TPPD_ARATH 44 329 + 286 Gaps:15 75.61 369 56.63 9e-108 Probable trehalose-phosphate phosphatase D OS Arabidopsis thaliana GN TPPD PE 2 SV 1
blastp_uniprot_sprot sp|Q6ZAL2|TPP6_ORYSJ 46 322 + 277 Gaps:14 73.24 370 58.30 1e-107 Probable trehalose-phosphate phosphatase 6 OS Oryza sativa subsp. japonica GN TPP6 PE 2 SV 1
blastp_uniprot_sprot sp|Q6H5L4|TPP7_ORYSJ 40 322 + 283 Gaps:12 74.40 375 55.91 5e-107 Probable trehalose-phosphate phosphatase 7 OS Oryza sativa subsp. japonica GN TPP7 PE 2 SV 2
blastp_uniprot_sprot sp|F4KFG5|TPPI_ARATH 37 327 + 291 Gaps:14 77.24 369 53.68 1e-105 Probable trehalose-phosphate phosphatase I OS Arabidopsis thaliana GN TPPI PE 2 SV 1
blastp_uniprot_sprot sp|Q7XI41|TPP3_ORYSJ 41 322 + 282 Gaps:9 76.78 366 55.16 1e-105 Probable trehalose-phosphate phosphatase 3 OS Oryza sativa subsp. japonica GN TPP3 PE 2 SV 1
blastp_uniprot_sprot sp|Q9C9S4|TPPB_ARATH 32 329 + 298 Gaps:15 77.81 374 53.61 2e-104 Trehalose-phosphate phosphatase B OS Arabidopsis thaliana GN TPPB PE 1 SV 1
blastp_uniprot_sprot sp|O64896|TPPA_ARATH 17 322 + 306 Gaps:25 78.70 385 54.46 2e-103 Trehalose-phosphate phosphatase A OS Arabidopsis thaliana GN TPPA PE 1 SV 1
blastp_uniprot_sprot sp|Q0D6F4|TPP10_ORYSJ 44 332 + 289 Gaps:7 81.89 359 51.36 9e-102 Probable trehalose-phosphate phosphatase 10 OS Oryza sativa subsp. japonica GN TPP10 PE 2 SV 1
rpsblast_cdd gnl|CDD|178192 43 322 + 280 Gaps:6 73.96 384 56.69 1e-105 PLN02580 PLN02580 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|178591 44 327 + 284 Gaps:14 75.96 366 54.68 3e-90 PLN03017 PLN03017 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|177812 32 322 + 291 Gaps:17 79.66 354 53.55 2e-85 PLN02151 PLN02151 trehalose-phosphatase.
rpsblast_cdd gnl|CDD|145482 73 313 + 241 Gaps:34 100.00 235 39.57 3e-53 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|161997 67 324 + 258 Gaps:36 100.00 244 34.43 1e-37 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|32061 66 323 + 258 Gaps:32 89.47 266 28.57 1e-34 COG1877 OtsB Trehalose-6-phosphatase [Carbohydrate transport and metabolism].
rpsblast_cdd gnl|CDD|184712 67 323 + 257 Gaps:42 32.37 726 31.49 1e-31 PRK14501 PRK14501 putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB Provisional.
rpsblast_cdd gnl|CDD|182291 73 331 + 259 Gaps:42 88.35 266 27.23 4e-12 PRK10187 PRK10187 trehalose-6-phosphate phosphatase Provisional.
rpsblast_cdd gnl|CDD|162385 71 284 + 214 Gaps:33 96.57 204 23.86 9e-12 TIGR01484 HAD-SF-IIB HAD-superfamily hydrolase subfamily IIB. This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685) plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences eukaryotic phosphomannomutase (pfam03332) a large subfamily ("Cof-like hydrolases" TIGR00099) containing many closely related bacterial sequences a hypothetical equivalog containing the E. coli YedP protein as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear.

8 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 41 342 302 PTHR10788 none none none
SUPERFAMILY 71 323 253 SSF56784 none none IPR023214
TIGRFAM 67 323 257 TIGR00685 none T6PP: trehalose-phosphatase IPR003337
Pfam 73 312 240 PF02358 none Trehalose-phosphatase IPR003337
TIGRFAM 72 288 217 TIGR01484 "Reactome:REACT_17015" HAD-SF-IIB: HAD hydrolase, family IIB IPR006379
PANTHER 41 342 302 PTHR10788:SF19 none none none
Gene3D 70 143 74 G3DSA:3.40.50.1000 none none IPR023214
Gene3D 236 329 94 G3DSA:3.40.50.1000 none none IPR023214

0 Localization

8 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2004_QTL4_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,45 0 27,45 lod 4,5 10,6
Bourran_2000_2002_QTL7_Delta.F Qrob_Chr09 9 v_5944_442 s_1BA1PC_866 23.51 10,96 35,74 lod 4.1466 0.041
Bourran2_2003_QTL11_peak_Bud_burst_3P Qrob_Chr09 9 s_1CGP2H_273 v_15801_330 27,16 4,16 48,16 lod 2,3 5,1
Bourran2_2003_QTL13_peak_Bud_burst_A4 Qrob_Chr09 9 s_1AP8MN_635 s_1A3QQ_692 18,18 10,88 25,88 lod 3,4 7,2
Bourran2_2004_QTL14_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 10,33 22,33 lod 3,8 9
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4
Bourran2_2002_QTL12_peak_Bud_burst_A4 Qrob_Chr09 9 s_1BY6BQ_440 s_1AOIKO_756 16,83 4,33 33,33 lod 6,5 9,1

0 Targeting