Protein : Qrob_P0003690.2 Q. robur
Protein Identifier  ? Qrob_P0003690.2 Organism . Name  Quercus robur
Score  0.0 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: 273  
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.

28 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|tcc:TCM_011524 50 269 + 220 Gaps:41 65.91 396 67.82 4e-120 PLC-like phosphodiesterases superfamily protein
blastp_kegg lcl|pxb:103930605 50 269 + 220 Gaps:41 66.41 393 66.67 2e-117 probable glycerophosphoryl diester phosphodiesterase 2
blastp_kegg lcl|mdm:103437892 50 269 + 220 Gaps:41 67.97 384 67.05 5e-117 probable glycerophosphoryl diester phosphodiesterase 3
blastp_kegg lcl|ath:AT5G08030 50 271 + 222 Gaps:41 70.70 372 66.16 1e-116 glycerophosphoryl diester phosphodiesterase
blastp_kegg lcl|pxb:103937763 50 269 + 220 Gaps:41 66.92 390 66.67 4e-116 probable glycerophosphoryl diester phosphodiesterase 3
blastp_kegg lcl|vvi:100260480 50 272 + 223 Gaps:41 66.84 395 66.67 6e-116 glycerophosphoryl diester phosphodiesterase-like
blastp_kegg lcl|pper:PRUPE_ppa006823mg 50 269 + 220 Gaps:41 66.24 394 65.90 7e-116 hypothetical protein
blastp_kegg lcl|aly:ARALYDRAFT_660662 50 271 + 222 Gaps:41 70.70 372 65.40 1e-115 hypothetical protein
blastp_kegg lcl|tcc:TCM_014275 51 272 + 222 Gaps:41 65.26 403 66.16 2e-115 PLC-like phosphodiesterases superfamily protein isoform 1
blastp_kegg lcl|mdm:103415331 50 269 + 220 Gaps:41 63.35 412 66.28 3e-115 probable glycerophosphoryl diester phosphodiesterase 3
blastp_pdb 1ydy_B 58 257 + 200 Gaps:57 63.76 356 29.07 2e-11 mol:protein length:356 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1ydy_A 58 257 + 200 Gaps:57 63.76 356 29.07 2e-11 mol:protein length:356 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_D 58 257 + 200 Gaps:57 67.56 336 29.07 3e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_C 58 257 + 200 Gaps:57 67.56 336 29.07 3e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_B 58 257 + 200 Gaps:57 67.56 336 29.07 3e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_pdb 1t8q_A 58 257 + 200 Gaps:57 67.56 336 29.07 3e-11 mol:protein length:336 Glycerophosphoryl diester phosphodiesterase
blastp_uniprot_sprot sp|P09394|GLPQ_ECOLI 58 257 + 200 Gaps:57 63.41 358 29.07 7e-11 Glycerophosphoryl diester phosphodiesterase OS Escherichia coli (strain K12) GN glpQ PE 1 SV 2
rpsblast_cdd gnl|CDD|176544 50 258 + 209 Gaps:62 79.94 309 46.56 4e-73 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 71 258 + 188 Gaps:37 65.20 296 48.19 1e-52 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|182992 73 258 + 186 Gaps:52 58.03 355 31.07 1e-18 PRK11143 glpQ glycerophosphodiester phosphodiesterase Provisional.
rpsblast_cdd gnl|CDD|176542 26 258 + 233 Gaps:68 75.16 318 33.05 1e-17 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|176513 71 257 + 187 Gaps:22 61.26 302 27.03 3e-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 68 262 + 195 Gaps:60 67.58 256 32.95 3e-13 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|202508 58 259 + 202 Gaps:39 73.53 238 22.86 4e-13 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|30929 59 267 + 209 Gaps:48 71.21 257 28.96 5e-12 COG0584 UgpQ Glycerophosphoryl diester phosphodiesterase [Energy production and conversion].
rpsblast_cdd gnl|CDD|176546 71 264 + 194 Gaps:28 62.00 300 26.88 1e-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.
rpsblast_cdd gnl|CDD|176499 75 257 + 183 Gaps:55 75.13 189 30.28 3e-10 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_kog gnl|CDD|37469 30 271 + 242 Gaps:33 69.50 341 24.89 5e-26 KOG2258 KOG2258 KOG2258 Glycerophosphoryl diester phosphodiesterase [Energy production and conversion].

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 53 262 210 G3DSA:3.20.20.190 none none IPR017946
ProSiteProfiles 1 265 265 PS51704 none GP-PDE domain profile. IPR030395
SUPERFAMILY 60 263 204 SSF51695 none none IPR017946
Pfam 55 259 205 PF03009 none Glycerophosphoryl diester phosphodiesterase family IPR030395
PANTHER 54 271 218 PTHR23344:SF7 none none none
PANTHER 54 271 218 PTHR23344 none none IPR004129

0 Localization

14 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_nLBD*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 34,91 16,12 53,62 lod 2,4961 5,2
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC*_A4 Qrob_Chr08 8 v_12498_318 v_12364_308 35,77 14,11 55,31 lod 2,9413 6,2
Bourran2_2015_nEpiBC_3P Qrob_Chr12 12 s_1B73S5_217 v_7050_211 28,31 26,37 28,45 lod 4.5 11.6
Bourran_2000_2002_QTL3_Delta.F Qrob_Chr08 8 s_1A3EF7_1406 s_1AIWYC_607 30.17 21,01 40,21 lod 6.8553 0.055
Bourran2_2014_aSeqBC_A4 Qrob_Chr08 8 v_15999_278 v_AP13YL15_395 32,52 4,22 57,22 lod 2,7561 6,7
Bourran2_2014_nFork*_A4 Qrob_Chr08 8 PIE175 s_1CD7GJ_1398 31,22 5,24 57,24 lod 2,6724 6,8
Bourran2_2014_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2014_nPriLBD_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,36 0 30,43 lod 2,5806 5,1
Bourran2_2014_nPriLBD_A4 Qrob_Chr08 8 PIE175 v_9164_159 31,85 15,39 48,29 lod 2,8308 6,8
Bourran2_2015_rEpiBC_3P Qrob_Chr08 8 s_A9TNV_543 v_11837_70 9,93 9,83 11,15 lod 3.3 7.3
Champenoux_2015_nSeqBC_A4 Qrob_Chr08 8 v_AD7YD13_501 s_1A7IED_780 43,44 43,42 43,99 lod 3.7 8.9
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL3_d13Cf Qrob_Chr08 8 v_5216_549 v_11625_20 37.08 12,26 54,9 lod 6.5888 0.04

0 Targeting