Protein : Qrob_P0359370.2 Q. robur
Protein Identifier  ? Qrob_P0359370.2 Organism . Name  Quercus robur
Score  73.1 Score Type  egn
Protein Description  (M=5) K01126 - glycerophosphoryl diester phosphodiesterase [EC:3.1.4.46] Code Enzyme  EC:3.1.4.46
Gene Prediction Quality  validated Protein length 

Sequence

Length: 314  
Kegg Orthology  K01126
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0006629 lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
GO:0008081 phosphoric diester hydrolase activity Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group.
GO:0006071 glycerol metabolic process The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
GO:0008889 glycerophosphodiester phosphodiesterase activity Catalysis of the reaction: a glycerophosphodiester + H2O = an alcohol + sn-glycerol 3-phosphate.

31 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa006823mg 1 313 + 313 Gaps:3 78.93 394 79.10 1e-139 hypothetical protein
blastp_kegg lcl|pmum:103338572 1 313 + 313 Gaps:1 78.83 392 78.96 2e-139 probable glycerophosphoryl diester phosphodiesterase 3
blastp_kegg lcl|fve:101311863 1 313 + 313 Gaps:1 78.83 392 78.32 9e-139 glycerophosphoryl diester phosphodiesterase-like
blastp_kegg lcl|vvi:100260480 7 312 + 306 Gaps:3 77.47 395 79.74 3e-138 glycerophosphoryl diester phosphodiesterase-like
blastp_kegg lcl|gmx:100778145 1 311 + 311 Gaps:4 80.36 392 76.83 5e-138 PHYTASE glycerophosphoryl diester phosphodiesterase-like
blastp_kegg lcl|mdm:103437892 1 313 + 313 Gaps:9 78.39 384 78.74 2e-137 probable glycerophosphoryl diester phosphodiesterase 3
blastp_kegg lcl|tcc:TCM_014275 4 311 + 308 Gaps:3 75.19 403 78.22 3e-137 PLC-like phosphodiesterases superfamily protein isoform 1
blastp_kegg lcl|mdm:103455560 68 313 + 246 Gaps:1 77.53 316 77.14 2e-135 uncharacterized LOC103455560
blastp_kegg lcl|pxb:103930605 1 313 + 313 Gaps:2 78.88 393 76.77 3e-135 probable glycerophosphoryl diester phosphodiesterase 2
blastp_kegg lcl|cam:101511486 1 311 + 311 Gaps:1 78.72 390 74.92 2e-134 glycerophosphoryl diester phosphodiesterase-like
blastp_pdb 1ydy_B 70 274 + 205 Gaps:44 58.71 356 31.10 2e-11 mol:protein length:356 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1ydy_A 70 274 + 205 Gaps:44 58.71 356 31.10 2e-11 mol:protein length:356 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_D 70 274 + 205 Gaps:44 62.20 336 31.10 2e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_C 70 274 + 205 Gaps:44 62.20 336 31.10 2e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_B 70 274 + 205 Gaps:44 62.20 336 31.10 2e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_A 70 274 + 205 Gaps:44 62.20 336 31.10 2e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_uniprot_sprot sp|P09394|GLPQ_ECOLI 70 274 + 205 Gaps:44 58.38 358 31.10 7e-11 Glycerophosphoryl diester phosphodiesterase OS Escherichia coli (strain K12) GN glpQ PE 1 SV 2
blastp_uniprot_sprot sp|Q06282|GLPQ_HAEIN 74 274 + 201 Gaps:43 56.59 364 32.52 7e-09 Glycerophosphoryl diester phosphodiesterase OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN glpQ PE 1 SV 1
blastp_uniprot_sprot sp|Q7Y208|GLPQ3_ARATH 76 274 + 199 Gaps:26 36.04 763 26.91 7e-07 Probable glycerophosphoryl diester phosphodiesterase 3 OS Arabidopsis thaliana GN GPDL3 PE 1 SV 2
blastp_uniprot_sprot sp|Q9FJ62|GLPQ1_ARATH 170 300 + 131 Gaps:8 16.58 766 29.13 3e-06 Probable glycerophosphoryl diester phosphodiesterase 1 OS Arabidopsis thaliana GN GPDL1 PE 1 SV 1
rpsblast_cdd gnl|CDD|176544 73 275 + 203 Gaps:21 64.72 309 54.00 4e-77 cd08602 GDPD_ScGlpQ1_like Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of putative bacterial and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDE EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ as well as plant glycerophosphodiester phosphodiesterases (GP-PDEs) all of which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. The prototypes of this family include putative secreted phosphodiesterase encoded by gene glpQ1 (SCO1565) from the pho regulon in Streptomyces coelicolor genome and in plants two distinct Arabidopsis thaliana genes AT5G08030 and AT1G74210 coding putative GP-PDEs from the cell walls and vacuoles respectively.
rpsblast_cdd gnl|CDD|176502 68 275 + 208 Gaps:21 66.55 296 46.19 9e-63 cd08559 GDPD_periplasmic_GlpQ_like Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in bacterial and eukaryotic glycerophosphodiester phosphodiesterase (GP-GDE EC 3.1.4.46) similar to Escherichia coli periplasmic phosphodiesterase GlpQ. GP-GDEs are involved in glycerol metabolism and catalyze the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols which are major sources of carbon and phosphate. In E. coli there are two major G3P uptake systems: Glp and Ugp which contain genes coding for two different GP-GDEs. GlpQ gene from the glp operon codes for a periplasmic phosphodiesterase GlpQ. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters such as glycerophosphocholine (GPC) glycerophosphoethanolanmine (GPE) glycerophosphoglycerol (GPG) glycerophosphoinositol (GPI) and glycerophosphoserine (GPS) to the corresponding alcohols and G3P which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for GlpQ enzymatic activity. This subfamily also includes some GP-GDEs in higher plants and their eukaryotic homologs which show very high sequence similarities with bacterial periplasmic GP-GDEs.
rpsblast_cdd gnl|CDD|176542 74 275 + 202 Gaps:33 64.47 318 32.68 5e-21 cd08600 GDPD_EcGlpQ_like Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli periplasmic glycerophosphodiester phosphodiesterase (GP-GDE EC 3.1.4.46) GlpQ and similar proteins. GP-GDE plays an essential role in the metabolic pathway of E. coli. It catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols which are major sources of carbon and phosphate. E. coli possesses two major G3P uptake systems: Glp and Ugp which contain genes coding for two different GP-GDEs. GlpQ gene from the E. coli glp operon codes for a periplasmic phosphodiesterase GlpQ which is the prototype of this family. GlpQ is a dimeric enzyme that hydrolyzes periplasmic glycerophosphodiesters such as glycerophosphocholine (GPC) glycerophosphoethanolanmine (GPE) glycerophosphoglycerol (GPG) glycerophosphoinositol (GPI) and glycerophosphoserine (GPS) to the corresponding alcohols and G3P which is subsequently transported into the cell through the GlpT transport system. Ca2+ is required for the enzymatic activity of GlpQ. This family also includes a surface-exposed lipoprotein protein D (HPD) from Haemophilus influenza Type b and nontypeable strains which shows very high sequence similarity with E. coli GlpQ. HPD has been characterized as a human immunoglobulin D-binding protein with glycerophosphodiester phosphodiesterase activity. It can hydrolyze phosphatidylcholine from host membranes to produce free choline on the lipopolysaccharides on the surface of pathogenic bacteria.
rpsblast_cdd gnl|CDD|182992 70 275 + 206 Gaps:38 59.15 355 31.90 8e-21 PRK11143 glpQ glycerophosphodiester phosphodiesterase Provisional.
rpsblast_cdd gnl|CDD|202508 49 276 + 228 Gaps:81 99.58 238 18.99 3e-17 pfam03009 GDPD Glycerophosphoryl diester phosphodiesterase family. E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388 which suggests that this family may adopt a TIM barrel fold.
rpsblast_cdd gnl|CDD|176513 73 274 + 202 Gaps:26 60.93 302 28.80 2e-16 cd08571 GDPD_SHV3_plant Glycerophosphodiester phosphodiesterase domain of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase (GDPD) domain present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs) which may play an important role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both SHV3 and SVLs have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition the two tandem repeats show low sequence similarity to each other suggesting they have different biochemical function. Most members of this family are Arabidopsis-specific gene products. To date SHV3 orthologues are only found in Physcomitrella patens.
rpsblast_cdd gnl|CDD|176543 46 278 + 233 Gaps:116 97.27 256 26.91 3e-16 cd08601 GDPD_SaGlpQ_like Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE EC 3.1.4.46) from Staphylococcus aureus Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.
rpsblast_cdd gnl|CDD|176499 47 274 + 228 Gaps:80 99.47 189 29.26 2e-14 cd08556 GDPD Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota and similar proteins. The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs EC 3.1.4.46) and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D EC 3.1.4.41) from spider venom SMases D-like proteins and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs EC 3.1.4.11). Both GDPD related proteins and PI-PLCs belong to the superfamily of PI-PLC-like phosphodiesterases.
rpsblast_cdd gnl|CDD|30929 42 274 + 233 Gaps:94 94.55 257 26.34 1e-12 COG0584 UgpQ Glycerophosphoryl diester phosphodiesterase [Energy production and conversion].
rpsblast_cdd gnl|CDD|176546 76 281 + 206 Gaps:28 61.33 300 26.09 3e-11 cd08604 GDPD_SHV3_repeat_2 Glycerophosphodiester phosphodiesterase domain repeat 2 of glycerophosphodiester phosphodiesterase-like protein SHV3 and SHV3-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) repeat 2 present in glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs) which may play important an role in cell wall organization. The prototype of this family is a glycosylphosphatidylinositol (GPI) anchored protein SHV3 encoded by shaven3 (shv3) gene from Arabidopsis thaliana. Members in this family show sequence homology to bacterial GP-GDEs (EC 3.1.4.46) that catalyze the hydrolysis of various glycerophosphodiesters and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Both SHV3 and SVLs have two tandemly repeated GDPD domains whose biochemical functions remain unclear. The residues essential for interactions with the substrates and calcium ions in bacterial GP-GDEs are not conserved in SHV3 and SVLs which suggests that the function of GDPD domains in these proteins might be distinct from those in typical bacterial GP-GDEs. In addition the two tandem repeats show low sequence similarity to each other suggesting they have different biochemical function. Most of the members of this family are Arabidopsis-specific gene products. To date SHV3 orthologues are only found in Physcomitrella patens. This CD includes domain II (the second GDPD domain of SHV3 and SVLs) which is necessary for SHV3 function.

12 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Phobius 22 313 292 NON_CYTOPLASMIC_DOMAIN none Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. none
Phobius 18 21 4 SIGNAL_PEPTIDE_C_REGION none C-terminal region of a signal peptide. none
Gene3D 68 279 212 G3DSA:3.20.20.190 none none IPR017946
ProSiteProfiles 1 282 282 PS51704 none GP-PDE domain profile. IPR030395
Phobius 1 5 5 SIGNAL_PEPTIDE_N_REGION none N-terminal region of a signal peptide. none
Gene3D 35 65 31 G3DSA:3.20.20.190 none none IPR017946
Phobius 6 17 12 SIGNAL_PEPTIDE_H_REGION none Hydrophobic region of a signal peptide. none
SUPERFAMILY 43 281 239 SSF51695 none none IPR017946
PANTHER 26 307 282 PTHR23344 none none IPR004129
Pfam 72 276 205 PF03009 none Glycerophosphoryl diester phosphodiesterase family IPR030395
Phobius 1 21 21 SIGNAL_PEPTIDE none Signal peptide region none
PANTHER 26 307 282 PTHR23344:SF7 none none none

1 Localization

Analysis Start End Length
SignalP_EUK 1 21 20

16 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2003_QTL2_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 87 lod 3,3 8,7
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL2_d13Cf Qrob_Chr02 2 s_1AQA4Z_1644 s_1AK5QX_947 53.67 14,01 79,68 lod 5.6594 0.03
Bourran1_2004_QTL2_peak_Bud_burst_3P Qrob_Chr02 2 s_1AW12F_382 s_1A77MR_223 42 6 64 lod 3,6 9,6
Bourran2_2002_QTL9_peak_Bud_burst_A4 Qrob_Chr02 2 s_1BFNDA_375 s_1A3VA1_2139 32,5 17 62 lod 3,1 4,2
Bourran2_2003_QTL8_peak_Bud_burst_3P Qrob_Chr02 2 s_1ANG6_1446 v_11270_161 40 0 72 lod 4,4 9,9
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2015_nP_A4 Qrob_Chr02 2 s_1A0FUE_1868 s_1A1UAI_500 20,64 20,47 21,36 lod 5.8 10.9
Bourran2_2015_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 24,87 24,63 26,18 lod 3.8 7
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran1_2003_QTL1_peak_Bud_burst_3P Qrob_Chr02 2 s_1AR8KI_1183 s_1B0QB1_473 22 6 41 lod 4,2 11,5
Bourran1_2004_QTL3_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 46 lod 2,9 6,4
Bourran2_2015_nEpiBC_A4 Qrob_Chr07 7 s_1DP9TW_798 v_8128_173 22,61 22,14 22,73 lod 3.1 8.5
Champenoux_2015_nEpis_A4 Qrob_Chr02 2 s_1BAGIZ_823 s_1BN4CB_644 23,06 23,06 23,06 lod 4.9 11
Champenoux_2015_nP_A4 Qrob_Chr02 2 s_1BN4CB_644 v_508_128 23,76 23,06 24,51 lod 2.8 6.2
Champenoux_2015_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 25,35 24,63 26,18 lod 4.0 8.7
Champenoux_2015_nSecLBD_A4 Qrob_Chr02 2 s_1AN4ZM_1665 v_8587_238 18,52 18,89 18,27 lod 3.2 7.4

0 Targeting