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Conserved domains on  [gi|1040222710|ref|XP_017197971|]
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glycerophosphodiester phosphodiesterase 1 isoform X3 [Oryctolagus cuniculus]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171153)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens glycerophosphodiester phosphodiesterase 1 (GDE1) that hydrolyzes the phosphodiester bond of glycerophosphodiesters such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine (GroPEth), to yield a glycerol phosphate and an alcohol

EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-213 1.11e-118

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


:

Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 338.08  E-value: 1.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLKNNLTIFFDVKGHANMATDALKKMY 80
Cdd:cd08573    45 MHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSSRFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  81 MEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALTHRPWSLSHTGD-GKPRYSSFWRQAVFVGLDILLDWSMHNVLWYLC 159
Cdd:cd08573   125 KKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWRPWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFL 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040222710 160 GVSAFLMQKDFVSPDYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSM 213
Cdd:cd08573   205 GVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTEKQYFAKTLNVPYITDSL 258
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-213 1.11e-118

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 338.08  E-value: 1.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLKNNLTIFFDVKGHANMATDALKKMY 80
Cdd:cd08573    45 MHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSSRFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  81 MEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALTHRPWSLSHTGD-GKPRYSSFWRQAVFVGLDILLDWSMHNVLWYLC 159
Cdd:cd08573   125 KKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWRPWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFL 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040222710 160 GVSAFLMQKDFVSPDYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSM 213
Cdd:cd08573   205 GVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTEKQYFAKTLNVPYITDSL 258
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-196 4.31e-25

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 98.40  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHrlrnDFPDEKIPTLREaVAECLKNNLTIFFDVKGHANMATDALKKMY 80
Cdd:COG0584    49 FHDPTLDRTTNGTGRVADLTLAELRQLDAGSGP----DFAGERIPTLEE-VLELVPGDVGLNIEIKSPPAAEPDLAEAVA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  81 --MEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALthrpwsLSHTGDGKPRYSSFWRQAVFVGLDIlldwsmhnvlwyl 158
Cdd:COG0584   124 alLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGL------LVEELPADPLELARALGADGVGPDY------------- 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1040222710 159 cgvsaflmqkDFVSPDYLKKWSAKGIQVVGWTVNTFDE 196
Cdd:COG0584   185 ----------DLLTPELVAAAHAAGLKVHVWTVNDPEE 212
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 1-196 1.83e-16

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.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 75.51  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHrlRNDFPDEK--IPTLREAVAECLKNNLTIFFDVkghanmatdalkK 78
Cdd:pfam03009  42 LHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGN--SGPLSGERvpFPTLEEVLEFDWDVGFNIEIKI------------K 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  79 MYMEFPQLYNSSMV---CSFLPEVIYKMRQTDQNVITalTHRPWSLSHTGDGKPRYSsfwRQAVFVGLDILLDWSMHNVL 155
Cdd:pfam03009 108 PYVEAIAPEEGLIVkdlLLSVDEILAKKADPRRVIFS--SFNPDELKRLRELAPKLP---LVFLSSGRAYAEADLLERAA 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1040222710 156 WYLcGVSAFLMQ---KDFVSPDYLKKWSAKGIQVVGWTVNTFDE 196
Cdd:pfam03009 183 AFA-GAPALLGEvalVDEALPDLVKRAHARGLVVHVWTVNNEDE 225
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 1-59 1.86e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.49  E-value: 1.86e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRndFPDEKIPTLREAVAECLKNNL 59
Cdd:PRK09454   54 LHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA--FAGEPLPTLSQVAARCRAHGM 110
 
Name Accession Description Interval E-value
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-213 1.11e-118

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE1 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE1 (also known as MIR16, membrane interacting protein of RGS16) and their metazoan homologs. GDE1 is widely expressed in mammalian tissues, including the heart, brain, liver, and kidney. It shows sequence homology to bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyzes the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. GDE1 has been characterized as GPI-GDE (EC 3.1.4.44) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate glycerol phosphate and inositol. It functions as an integral membrane-bound glycoprotein interacting with regulator of G protein signaling protein RGS16, and is modulated by G protein-coupled receptor (GPCR) signaling. In addition, GDE1 may interact with PRA1 domain family, member 2 (PRAF2, also known as JM4), which is an interacting protein of the G protein-coupled chemokine receptor CCR5. The catalytic activity, which is dependent on the integrity of the GDPD domain, is required for GDE1 cellular function.


Pssm-ID: 176515 [Multi-domain]  Cd Length: 258  Bit Score: 338.08  E-value: 1.11e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLREAVAECLKNNLTIFFDVKGHANMATDALKKMY 80
Cdd:cd08573    45 MHDDTVDRTTDGTGLVAELTWEELRKLNAAAKHRLSSRFPGEKIPTLEEAVKECLENNLRMIFDVKSNSSKLVDALKNLF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  81 MEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALTHRPWSLSHTGD-GKPRYSSFWRQAVFVGLDILLDWSMHNVLWYLC 159
Cdd:cd08573   125 KKYPGLYDKAIVCSFNPIVIYKVRKADPKILTGLTWRPWFLSYTDDeGGPRRKSGWKHFLYSMLDVILEWSLHSWLPYFL 204

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1040222710 160 GVSAFLMQKDFVSPDYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITDSM 213
Cdd:cd08573   205 GVSALLIHKDDISSAYVRYWRARGIRVIAWTVNTPTEKQYFAKTLNVPYITDSL 258
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-196 4.31e-25

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 98.40  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHrlrnDFPDEKIPTLREaVAECLKNNLTIFFDVKGHANMATDALKKMY 80
Cdd:COG0584    49 FHDPTLDRTTNGTGRVADLTLAELRQLDAGSGP----DFAGERIPTLEE-VLELVPGDVGLNIEIKSPPAAEPDLAEAVA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  81 --MEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALthrpwsLSHTGDGKPRYSSFWRQAVFVGLDIlldwsmhnvlwyl 158
Cdd:COG0584   124 alLKRYGLEDRVIVSSFDPEALRRLRELAPDVPLGL------LVEELPADPLELARALGADGVGPDY------------- 184

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1040222710 159 cgvsaflmqkDFVSPDYLKKWSAKGIQVVGWTVNTFDE 196
Cdd:COG0584   185 ----------DLLTPELVAAAHAAGLKVHVWTVNDPEE 212
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 1-210 1.82e-24

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176524 [Multi-domain]  Cd Length: 233  Bit Score: 96.61  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHrlRNDFPDEKIPTLREAVAECLKNNLTIFFDVKGHAN--MATDALKK 78
Cdd:cd08582    45 VHDPTLKRTSGGDGAVSDLTLAELRKLDIGSWK--GESYKGEKVPTLEEYLAIVPKYGKKLFIEIKHPRRgpEAEEELLK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  79 MYMEFPQLYNSSMVCSFLPEVIYKMRQTDQNVITALTHRPWslSHTGDGKPRYssfwRQAVFVGLDILLDWSMHnvlwyl 158
Cdd:cd08582   123 LLKESGLLPEQIVIISFDAEALKRVRELAPTLETLWLRNYK--SPKEDPRPLA----KSGGAAGLDLSYEKKLN------ 190

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1040222710 159 cgvsaflmqkdfvsPDYLKKWSAKGIQVVGWTVNTFDE-KSYYEshLGSSYIT 210
Cdd:cd08582   191 --------------PAFIKALRDAGLKLNVWTVDDAEDaKRLIE--LGVDSIT 227
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 1-211 4.86e-18

Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 79.14  E-value: 4.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNpaANHRLRNDFPDEKIPTLREaVAECLKN-----NLTIFFDVKGHANMAtDA 75
Cdd:cd08563    47 IHDETVDRTTNGKGYVKDLTLEELKKLD--AGSWFDEKFTGEKIPTLEE-VLDLLKDkdlllNIEIKTDVIHYPGIE-KK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  76 LKKMYMEFpQLYNSSMVCSFLPEVIYKMRQTDQNVITALthrpwsLSHTGdgkprYSSFWRQAVFVGLDilldwSMHnvL 155
Cdd:cd08563   123 VLELVKEY-NLEDRVIFSSFNHESLKRLKKLDPKIKLAL------LYETG-----LQDPKDYAKKIGAD-----SLH--P 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1040222710 156 WYlcgvsaflmqkDFVSPDYLKKWSAKGIQVVGWTVNTFDEKSYYESHLGSSYITD 211
Cdd:cd08563   184 DF-----------KLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITN 228
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 1-111 1.34e-16

Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (AtGDE, EC 3.1.4.46) and its uncharacterized eukaryotic homolgoues. Members in this family shows high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. AtGDE exists as a hexamer that is a trimer of dimers, which is unique among current known GDPD family members. However, it remains unclear if the hexamer plays a physiological role in AtGDE enzymatic function.


Pssm-ID: 176509 [Multi-domain]  Cd Length: 240  Bit Score: 75.80  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLnpaanhRLRNDFP---DEKIPTLREAVAEClKNNLTIFFDVK-GHANMATDAL 76
Cdd:cd08566    47 MHDDTLDRTTNGKGKVSDLTLAEIRKL------RLKDGDGevtDEKVPTLEEALAWA-KGKILLNLDLKdADLDEVIALV 119

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1040222710  77 KKMYMEfpqlyNSSMVCSFLPEVIYKMRQTDQNVI 111
Cdd:cd08566   120 KKHGAL-----DQVIFKSYSEEQAKELRALAPEVM 149
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 1-196 1.83e-16

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.


Pssm-ID: 397241 [Multi-domain]  Cd Length: 244  Bit Score: 75.51  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHrlRNDFPDEK--IPTLREAVAECLKNNLTIFFDVkghanmatdalkK 78
Cdd:pfam03009  42 LHDFNLDRTTDGAGYVRDLTLEELKRLDIGAGN--SGPLSGERvpFPTLEEVLEFDWDVGFNIEIKI------------K 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  79 MYMEFPQLYNSSMV---CSFLPEVIYKMRQTDQNVITalTHRPWSLSHTGDGKPRYSsfwRQAVFVGLDILLDWSMHNVL 155
Cdd:pfam03009 108 PYVEAIAPEEGLIVkdlLLSVDEILAKKADPRRVIFS--SFNPDELKRLRELAPKLP---LVFLSSGRAYAEADLLERAA 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1040222710 156 WYLcGVSAFLMQ---KDFVSPDYLKKWSAKGIQVVGWTVNTFDE 196
Cdd:pfam03009 183 AFA-GAPALLGEvalVDEALPDLVKRAHARGLVVHVWTVNNEDE 225
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 44-211 3.07e-15

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.


Pssm-ID: 176499 [Multi-domain]  Cd Length: 189  Bit Score: 70.76  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  44 IPTLREAVAEClKNNLTIFFDVKGHANMATDA--LKKMYMEFPqLYNSSMVCSFLPEVIYKMRQTDQNVITALTHRPWSL 121
Cdd:cd08556    48 IPTLEEVLELV-KGGVGLNIELKEPTRYPGLEakVAELLREYG-LEERVVVSSFDHEALRALKELDPEVPTGLLVDKPPL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710 122 SHTGDGKPRYssfwrqavfvgldilldwsmhnvlwylCGVSAFLMQKDFVSPDYLKKWSAKGIQVVGWTVNTFDEKSYYE 201
Cdd:cd08556   126 DPLLAELARA---------------------------LGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDARRLL 178

                         170
                  ....*....|
gi 1040222710 202 SHLGSSYITD 211
Cdd:cd08556   179 ALGVDGIITD 188
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 1-105 8.16e-15

Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase UgpQ and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46), UgpQ, 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 distinct GP-GDEs. UgpQ gene from the E. coli ugp operon codes for a cytosolic phosphodiesterase GlpQ, which is the prototype of this family. Various glycerophosphodiesters, such as glycerophosphocholine (GPC), glycerophosphoethanolanmine (GPE), glycerophosphoglycerol (GPG), glycerophosphoinositol (GPI), and glycerophosphoserine (GPS), can only be hydrolyzed by UgpQ during transport at the inner side of the cytoplasmic membrane to alcohols and G3P, which is a source of phosphate. In contrast to Ca2+-dependent periplasmic phosphodiesterase GlpQ, cytosolic phosphodiesterase UgpQ requires divalent cations, such as Mg2+, Co2+, or Mn2+, for its enzyme activity.


Pssm-ID: 176505 [Multi-domain]  Cd Length: 229  Bit Score: 70.71  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNpaANHRLRNDFPDEKIPTLREAVAECLKNNLTIFFDVK---GHANMATDALK 77
Cdd:cd08562    45 IHDDTLDRTTNGSGAVTELTWAELAQLD--AGSWFSPEFAGEPIPTLADVLELARELGLGLNLEIKpdpGDEALTARVVA 122

                          90       100
                  ....*....|....*....|....*...
gi 1040222710  78 KMYMEFPQLYNSSMVCSFLPEVIYKMRQ 105
Cdd:cd08562   123 AALRELWPHASKLLLSSFSLEALRAARR 150
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 1-196 6.21e-13

Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic phosphodiesterases UgpQ2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized cytoplasmic phosphodiesterases which predominantly exist in bacteria. The prototype of this family is a putative cytoplasmic phosphodiesterase encoded by gene ulpQ2 (SCO1419) in the Streptomyces coelicolor genome. It is distantly related to the Escherichia coli cytoplasmic phosphodiesterases UgpQ that catalyzes the hydrolysis of glycerophosphodiesters at the inner side of the cytoplasmic membrane to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176504 [Multi-domain]  Cd Length: 249  Bit Score: 65.74  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRN--DFP----DEKIPTLREaVAECLKnNLTIFFDVKGHANMATD 74
Cdd:cd08561    45 IHDETLDRTTDGTGPVADLTLAELRRLDAGYHFTDDGgrTYPyrgqGIRIPTLEE-LFEAFP-DVRLNIEIKDDGPAAAA 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  75 ALKKMYMEFpQLYNSSMVCSFLPEVIYKMRQTDQNVITALThrpwslshTGDGkpryssfwrqAVFVGLDILLDWSmhnv 154
Cdd:cd08561   123 ALADLIERY-GAQDRVLVASFSDRVLRRFRRLCPRVATSAG--------EGEV----------AAFVLASRLGLGS---- 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1040222710 155 lWYLCGVSAFLM---QKDF--VSPDYLKKWSAKGIQVVGWTVNTFDE 196
Cdd:cd08561   180 -LYSPPYDALQIpvrYGGVplVTPRFVRAAHAAGLEVHVWTVNDPAE 225
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 1-59 1.86e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 61.49  E-value: 1.86e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRndFPDEKIPTLREAVAECLKNNL 59
Cdd:PRK09454   54 LHDDTLERTSNGWGVAGELTWQDLAQLDAGSWFSAA--FAGEPLPTLSQVAARCRAHGM 110
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 2-69 1.51e-09

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176523 [Multi-domain]  Cd Length: 229  Bit Score: 55.80  E-value: 1.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   2 HDNTVDRTTDGSGRLCDLTFEQIRKLNPAANHRLRNDFPDEKIPTLrEAVAECLKNN--LTIFFDVKGHA 69
Cdd:cd08581    46 HDDTLLRLTGVEGLLHELEDAELDSLRVAEPARFGSRFAGEPLPSL-AAVVQWLAQHpqVTLFVEIKTES 114
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 1-109 1.12e-08

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial glycerophosphodiester phosphodiesterases. In addition to a C-terminal GDPD domain, most members in this family have an N-terminus that functions as a membrane anchor.


Pssm-ID: 176521 [Multi-domain]  Cd Length: 220  Bit Score: 53.32  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLNpaanhrLRNDFPDEKIPTLREAVAECLKNNLTIFFDVKGHANMATDALKKmy 80
Cdd:cd08579    45 MHDANLKRLAGVNKKVWDLTLEELKKLT------IGENGHGAKIPSLDEYLALAKGLKQKLLIELKPHGHDSPDLVEK-- 116

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1040222710  81 meFPQLY------NSSMVCSFLPEVIYKMRQTDQN 109
Cdd:cd08579   117 --FVKLYkqnlieNQHQVHSLDYRVIEKVKKLDPK 149
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 2-193 2.40e-07

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity with Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176527 [Multi-domain]  Cd Length: 237  Bit Score: 49.63  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   2 HDNTVDRTTDGSGRLCDLTFEQIRKLnpaanhRLRNDfpDEKIPTLREaVAECLKNNLTIFFDVKGHANMATD---ALKK 78
Cdd:cd08585    53 HDDNLKRLTGVEGRVEELTAAELRAL------RLLGT--DEHIPTLDE-VLELVAGRVPLLIELKSCGGGDGGlerRVLA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710  79 MYMEFPQLYnssMVCSFLPEVIYKMRQTDQNVITALTHRPWSLShtgdgkpRYSSFWRQAVFVGLdilldwsmhnvlwyl 158
Cdd:cd08585   124 ALKDYKGPA---AIMSFDPRVVRWFRKLAPGIPRGQLSEGSNDE-------ADPAFWNEALLSAL--------------- 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1040222710 159 cgVSAFLMQKDFVS--PDYLKKWSAK------GIQVVGWTVNT 193
Cdd:cd08585   179 --FSNLLTRPDFIAyhLDDLPNPFVTlarallGMPVIVWTVRT 219
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 1-123 2.28e-06

Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Agrobacterium tumefaciens glycerophosphodiester phosphodiesterase (pAtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176508 [Multi-domain]  Cd Length: 235  Bit Score: 47.01  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1040222710   1 MHDNTVDRTTDGSGRLCDLTFEQIRKLnpaanhRLRNDFpDEKIPTLREaVAECLKNNLTIFfdvkgHANMATDALKKMY 80
Cdd:cd08565    45 IHDPTLDRTTHGTGAVRDLTLAERKAL------RLRDSF-GEKIPTLEE-VLALFAPSGLEL-----HVEIKTDADGTPY 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1040222710  81 MEFPQ----------LYNSSMVCSFLPEVIYKMRqtdqnvitALTHRP--WSLSH 123
Cdd:cd08565   112 PGAAAlaaatlrrhgLLERSVLTSFDPAVLTEVR--------KHPGVRtlGSVDE 158
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 1-49 6.22e-06

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.


Pssm-ID: 176543 [Multi-domain]  Cd Length: 256  Bit Score: 45.77  E-value: 6.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1040222710   1 MHDNTVDRTTDGS--GRLCDLTFEQIRKL------NPAANHRLRNDFPDEKIPTLRE 49
Cdd:cd08601    47 MHDETLDRTTNIErpGPVKDYTLAEIKQLdagswfNKAYPEYARESYSGLKVPTLEE 103
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 1-49 5.15e-04

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.


Pssm-ID: 176502 [Multi-domain]  Cd Length: 296  Bit Score: 39.95  E-value: 5.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1040222710   1 MHDNTVDRTTD------------GSGRLCDLTFEQIRKLN--PAANHRLRNDFPDE----KIPTLRE 49
Cdd:cd08559    47 RHDPTLDRTTNvaehfpfrgrkdTGYFVIDFTLAELKTLRagSWFNQRYPERAPSYyggfKIPTLEE 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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