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Conserved domains on  [gi|1472785098|gb|RHV35320|]
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glycerophosphodiester phosphodiesterase [Ruminococcus sp. OM05-10BH]

Protein Classification

glycerophosphodiester phosphodiesterase( domain architecture ID 10171165)

glycerophosphodiester phosphodiesterase catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 39-268 8.93e-94

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: 276.51  E-value: 8.93e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLHDLSLGIPENTMAAFRRAVEHGYGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGTAEH 118
Cdd:cd08585     7 IAHRGLHDRDAGIPENSLSAFRAAAEAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLGTDEH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 119 IPLFQDVLDLVDGKVPLLVEIK--YKHVGsSICRKAAELLDHYSGSYCIESFHPVALMWFRKYRPYTVRGQLGMNFHKDD 196
Cdd:cd08585    87 IPTLDEVLELVAGRVPLLIELKscGGGDG-GLERRVLAALKDYKGPAAIMSFDPRVVRWFRKLAPGIPRGQLSEGSNDEA 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098 197 GRVHPVYYFPRHLLTNFLTKPDFIAYDHHARSALSLTICRVVFGIPCFAWTVKSPREYYACEHVFDYFIFEG 268
Cdd:cd08585   166 DPAFWNEALLSALFSNLLTRPDFIAYHLDDLPNPFVTLARALLGMPVIVWTVRTEEDIARLKQYADNIIFEG 237
 
Name Accession Description Interval E-value
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 39-268 8.93e-94

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: 276.51  E-value: 8.93e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLHDLSLGIPENTMAAFRRAVEHGYGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGTAEH 118
Cdd:cd08585     7 IAHRGLHDRDAGIPENSLSAFRAAAEAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLGTDEH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 119 IPLFQDVLDLVDGKVPLLVEIK--YKHVGsSICRKAAELLDHYSGSYCIESFHPVALMWFRKYRPYTVRGQLGMNFHKDD 196
Cdd:cd08585    87 IPTLDEVLELVAGRVPLLIELKscGGGDG-GLERRVLAALKDYKGPAAIMSFDPRVVRWFRKLAPGIPRGQLSEGSNDEA 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098 197 GRVHPVYYFPRHLLTNFLTKPDFIAYDHHARSALSLTICRVVFGIPCFAWTVKSPREYYACEHVFDYFIFEG 268
Cdd:cd08585   166 DPAFWNEALLSALFSNLLTRPDFIAYHLDDLPNPFVTLARALLGMPVIVWTVRTEEDIARLKQYADNIIFEG 237
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
39-254 8.11e-52

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.28  E-value: 8.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVL---- 113
Cdd:COG0584     6 IAHRGA---SGLAPENTLAAFRAALELGaDGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGsgpd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 114 GTAEHIPLFQDVLDLVDGKVPLLVEIK-YKHVGSSICRKAAELLD--HYSGSYCIESFHPVALMWFRKYRPYTVRGQLGM 190
Cdd:COG0584    83 FAGERIPTLEEVLELVPGDVGLNIEIKsPPAAEPDLAEAVAALLKryGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 191 NFHKDD----GRVHPVYYFPRHLLTNfltkPDFIAYDHHArsalslticrvvfGIPCFAWTVKSPREY 254
Cdd:COG0584   163 ELPADPlelaRALGADGVGPDYDLLT----PELVAAAHAA-------------GLKVHVWTVNDPEEM 213
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 41-255 8.83e-25

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: 99.40  E-value: 8.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  41 HRGLHDLslgIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL--------P 111
Cdd:pfam03009   1 HRGASGS---YPENTLASFRKAAEAGAdYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLdigagnsgP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 112 VLGTAEHIPLFQDVLDLVDGkVPLLVEIKYKHVGSSICRK--------AAELLDHYSGSYC-----IESFHPVALMWFRK 178
Cdd:pfam03009  78 LSGERVPFPTLEEVLEFDWD-VGFNIEIKIKPYVEAIAPEeglivkdlLLSVDEILAKKADprrviFSSFNPDELKRLRE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 179 YRPytvRGQLGMNFHKDDgrvhPVYYFPRHLLTNFLTKPDFIAYDHHARSALSLTICRV-VFGIPCFAWTVKSPREYY 255
Cdd:pfam03009 157 LAP---KLPLVFLSSGRA----YAEADLLERAAAFAGAPALLGEVALVDEALPDLVKRAhARGLVVHVWTVNNEDEMK 227
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 40-110 1.12e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 63.42  E-value: 1.12e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL 110
Cdd:PRK09454   12 AHRGGGKLA---PENTLAAIDVGARYGHrMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQL 80
 
Name Accession Description Interval E-value
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 39-268 8.93e-94

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: 276.51  E-value: 8.93e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLHDLSLGIPENTMAAFRRAVEHGYGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGTAEH 118
Cdd:cd08585     7 IAHRGLHDRDAGIPENSLSAFRAAAEAGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAELRALRLLGTDEH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 119 IPLFQDVLDLVDGKVPLLVEIK--YKHVGsSICRKAAELLDHYSGSYCIESFHPVALMWFRKYRPYTVRGQLGMNFHKDD 196
Cdd:cd08585    87 IPTLDEVLELVAGRVPLLIELKscGGGDG-GLERRVLAALKDYKGPAAIMSFDPRVVRWFRKLAPGIPRGQLSEGSNDEA 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098 197 GRVHPVYYFPRHLLTNFLTKPDFIAYDHHARSALSLTICRVVFGIPCFAWTVKSPREYYACEHVFDYFIFEG 268
Cdd:cd08585   166 DPAFWNEALLSALFSNLLTRPDFIAYHLDDLPNPFVTLARALLGMPVIVWTVRTEEDIARLKQYADNIIFEG 237
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
39-254 8.11e-52

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 169.28  E-value: 8.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVL---- 113
Cdd:COG0584     6 IAHRGA---SGLAPENTLAAFRAALELGaDGIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAELRQLDAGsgpd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 114 GTAEHIPLFQDVLDLVDGKVPLLVEIK-YKHVGSSICRKAAELLD--HYSGSYCIESFHPVALMWFRKYRPYTVRGQLGM 190
Cdd:COG0584    83 FAGERIPTLEEVLELVPGDVGLNIEIKsPPAAEPDLAEAVAALLKryGLEDRVIVSSFDPEALRRLRELAPDVPLGLLVE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 191 NFHKDD----GRVHPVYYFPRHLLTNfltkPDFIAYDHHArsalslticrvvfGIPCFAWTVKSPREY 254
Cdd:COG0584   163 ELPADPlelaRALGADGVGPDYDLLT----PELVAAAHAA-------------GLKVHVWTVNDPEEM 213
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 37-263 2.64e-36

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: 129.21  E-value: 2.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  37 KFYAHRGlhdlSLGI-PENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL---- 110
Cdd:cd08563     2 LIFAHRG----YSGTaPENTLLAFKKAIEAGaDGIELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEELKKLdags 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 111 --PVLGTAEHIPLFQDVLDLVDGKVPLL-VEIK---YKHVGssICRKAAELLDHY--SGSYCIESFHPVALMWFRKYRPY 182
Cdd:cd08563    78 wfDEKFTGEKIPTLEEVLDLLKDKDLLLnIEIKtdvIHYPG--IEKKVLELVKEYnlEDRVIFSSFNHESLKRLKKLDPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 183 TVRGQL---GMNFHKDDGRVHPVYYFprHLLTNFLtkpdfiaYDHHARSALSlticrvvFGIPCFAWTVKSPREYyacEH 259
Cdd:cd08563   156 IKLALLyetGLQDPKDYAKKIGADSL--HPDFKLL-------TEEVVEELKK-------RGIPVRLWTVNEEEDM---KR 216


                  ....
gi 1472785098 260 VFDY 263
Cdd:cd08563   217 LKDL 220
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 40-254 1.05e-32

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: 118.52  E-value: 1.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDfdlkricgvekdvdeltyeelkalpvlgtaeh 118
Cdd:cd08556     3 AHRGASGEA---PENTLAAFRKALEAGaDGVELDVQLTKDGVLVVIHD-------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 119 IPLFQDVLDLVDGKVPLLVEIKYKHVGSSICRKAAELLDHYS--GSYCIESFHPVALMWFRKYRPYTVRGQLGMNFHKDD 196
Cdd:cd08556    48 IPTLEEVLELVKGGVGLNIELKEPTRYPGLEAKVAELLREYGleERVVVSSFDHEALRALKELDPEVPTGLLVDKPPLDP 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472785098 197 G------RVHPVYYFPRHLLTNfltkPDFIAYDHHArsalslticrvvfGIPCFAWTVKSPREY 254
Cdd:cd08556   128 LlaelarALGADAVNPHYKLLT----PELVRAAHAA-------------GLKVYVWTVNDPEDA 174
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 40-181 8.72e-32

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: 116.88  E-value: 8.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHG--YgIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVL--GT 115
Cdd:cd08579     3 AHRGVSSNG---VENTLEALEAAIKAKpdY-VEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELKKLTIGenGH 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 116 AEHIPLFQDVLDLVDG-KVPLLVEIK-YKHVGSSICRKAAELLDHY--SGSYCIESFHPVALMWFRKYRP 181
Cdd:cd08579    79 GAKIPSLDEYLALAKGlKQKLLIELKpHGHDSPDLVEKFVKLYKQNliENQHQVHSLDYRVIEKVKKLDP 148
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 40-145 5.29e-30

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: 112.78  E-value: 5.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLHDLslGIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVL----- 113
Cdd:cd08566     4 AHRGGWGA--GAPENSLAAIEAAIDLGAdIVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEIRKLRLKdgdge 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1472785098 114 GTAEHIPLFQDVLDLVDGKVPLLVEIKYKHVG 145
Cdd:cd08566    82 VTDEKVPTLEEALAWAKGKILLNLDLKDADLD 113
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 41-265 1.17e-28

Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermotoga maritime glycerophosphodiester phosphodiesterase (TmGDE, 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. TmGDE exists as a monomer that might be the biologically relevant form.


Pssm-ID: 176511 [Multi-domain]  Cd Length: 226  Bit Score: 108.92  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  41 HRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGtaEHI 119
Cdd:cd08568     5 HRGY---RAKYPENTLEAFKKAIEYGaDGVELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELKKLHPGG--ELI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 120 PLFQDVLDLVDGKVPLLVEIKYKhvgssicrKAAELLDHYSGSYCIE------SFHPVALMWFRKYRPYTVRGQL----- 188
Cdd:cd08568    80 PTLEEVFRALPNDAIINVEIKDI--------DAVEPVLEIVEKFNALdrvifsSFNHDALRELRKLDPDAKVGLLigeee 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 189 -GMNFHKDDGRVHPVYYFPRHLLTNFLTKPDFIAYDHHARSalslticrvvFGIPCFAWTVKSPREYYACEHVFDYFI 265
Cdd:cd08568   152 eGFSIPELHEKLKLYSLHVPIDAIGYIGFEKFVELLRLLRK----------LGLKIVLWTVNDPELVPKLKGLVDGVI 219
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 40-183 4.79e-28

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: 107.79  E-value: 4.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPV------ 112
Cdd:cd08582     3 AHRGA---SAEAPENTLAAFELAWEQGaDGIETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELRKLDIgswkge 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472785098 113 LGTAEHIPLFQDVLDLV-DGKVPLLVEIKYKHVGSSICRKAAELLDHYSGS---YCIESFHPVALMWFRKYRPYT 183
Cdd:cd08582    80 SYKGEKVPTLEEYLAIVpKYGKKLFIEIKHPRRGPEAEEELLKLLKESGLLpeqIVIISFDAEALKRVRELAPTL 154
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-158 2.98e-26

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function is not elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests mammalian GDE4 may play some distinct role from other members of mammalian GDEs family. Also included in this subfamily are uncharacterized mammalian glycerophosphodiester phosphodiesterase domain-containing protein 3 (GDPD3) and similar proteins which display very high sequence homology to mammalian GDE4.


Pssm-ID: 176517 [Multi-domain]  Cd Length: 264  Bit Score: 103.45  E-value: 2.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLH-DLslgiPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL------- 110
Cdd:cd08575     5 AHRGGAaEF----PENTIAAFRHAVKNGAdMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLdagygyt 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1472785098 111 --------PVLGTAEHIPLFQDVLDlVDGKVPLLVEIKYKHVGSSICRKAAELLDH 158
Cdd:cd08575    81 fdggktgyPRGGGDGRIPTLEEVFK-AFPDTPINIDIKSPDAEELIAAVLDLLEKY 135
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 41-255 8.83e-25

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: 99.40  E-value: 8.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  41 HRGLHDLslgIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL--------P 111
Cdd:pfam03009   1 HRGASGS---YPENTLASFRKAAEAGAdYIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELKRLdigagnsgP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 112 VLGTAEHIPLFQDVLDLVDGkVPLLVEIKYKHVGSSICRK--------AAELLDHYSGSYC-----IESFHPVALMWFRK 178
Cdd:pfam03009  78 LSGERVPFPTLEEVLEFDWD-VGFNIEIKIKPYVEAIAPEeglivkdlLLSVDEILAKKADprrviFSSFNPDELKRLRE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 179 YRPytvRGQLGMNFHKDDgrvhPVYYFPRHLLTNFLTKPDFIAYDHHARSALSLTICRV-VFGIPCFAWTVKSPREYY 255
Cdd:pfam03009 157 LAP---KLPLVFLSSGRA----YAEADLLERAAAFAGAPALLGEVALVDEALPDLVKRAhARGLVVHVWTVNNEDEMK 227
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 17-159 2.44e-22

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE4 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE4 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 1 (GDPD1)) and similar proteins. Mammalian GDE4 is a transmembrane protein whose cellular function has not yet been elucidated. It is expressed widely, including in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocytes. It is also expressed in the growth cones in neuroblastoma Neuro2a cells, which suggests GDE4 may play some distinct role from other members of the GDE family.


Pssm-ID: 176553 [Multi-domain]  Cd Length: 300  Bit Score: 93.82  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  17 LFYLLSIAPRLIGRPKRMPgkFY----AHRGLhdlSLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDLKR 91
Cdd:cd08612     6 TSYFLLRNPTLLHKKKKSP--FPcrhiSHRGG---SGENLENTMEAFEHAVKVGTDmLELDVHLTKDGQVVVSHDENLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  92 ICGVEKDVDELTYEEL----KALPVLGTAEH----------IPLFQDVLDLVDGkVPLLVEIKYKhvGSSICRKAAELLD 157
Cdd:cd08612    81 SCGVDKLVSDLNYADLppylEKLEVTFSPGDycvpkgsdrrIPLLEEVFEAFPD-TPINIDIKVE--NDELIKKVSDLVR 157


                  ..
gi 1472785098 158 HY 159
Cdd:cd08612   158 KY 159
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 40-254 4.49e-22

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: 91.94  E-value: 4.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL-------- 110
Cdd:cd08561     3 AHRGGAGLA---PENTLLAFEDAVELGADvLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELRRLdagyhftd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 111 ------PVLGTAEHIPLFQDVLDLVDGkVPLLVEIKYKHVGSS--ICR--KAAELLDHysgsYCIESFHPVALMWFRKYR 180
Cdd:cd08561    80 dggrtyPYRGQGIRIPTLEELFEAFPD-VRLNIEIKDDGPAAAaaLADliERYGAQDR----VLVASFSDRVLRRFRRLC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 181 P--------YTVRGQLGMNFHKDDGRVHPVYYF----PRHLLTNFLTkPDFIAyDHHARsalslticrvvfGIPCFAWTV 248
Cdd:cd08561   155 PrvatsageGEVAAFVLASRLGLGSLYSPPYDAlqipVRYGGVPLVT-PRFVR-AAHAA------------GLEVHVWTV 220


                  ....*.
gi 1472785098 249 KSPREY 254
Cdd:cd08561   221 NDPAEM 226
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 40-256 6.85e-22

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: 91.94  E-value: 6.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGT--- 115
Cdd:cd08573     3 GHRGA---GHDAPENTLAAFRQAKKNGaDGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEELRKLNAAAKhrl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 116 -----AEHIPLFQDVLD-LVDGKVPLLVEIkyKHVGSSICRKAAELLDHYSGSY---CIESFHPVALMWFRK-------- 178
Cdd:cd08573    80 ssrfpGEKIPTLEEAVKeCLENNLRMIFDV--KSNSSKLVDALKNLFKKYPGLYdkaIVCSFNPIVIYKVRKadpkiltg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 179 --YRPYTVRgqlgmnfHKDDGRVHPVYYFPRHLLTNFLtkpDFIAYDHHARSALSLTICRVVF----------------- 239
Cdd:cd08573   158 ltWRPWFLS-------YTDDEGGPRRKSGWKHFLYSML---DVILEWSLHSWLPYFLGVSALLihkddissayvrywrar 227

                         250
                  ....*....|....*....
gi 1472785098 240 GIPCFAWTVKSPRE--YYA 256
Cdd:cd08573   228 GIRVIAWTVNTPTEkqYFA 246
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 39-188 2.64e-21

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: 89.59  E-value: 2.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLhdlSLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVlG--- 114
Cdd:cd08562     2 IAHRGA---SSLAPENTLAAFRAAAELGVRwVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELAQLDA-Gswf 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 115 ----TAEHIPLFQDVLDLV-DGKVPLLVEIK-YKHVGSSICRKAAELLDHYSGSYC---IESFHPVALMWFRKYRPYTVR 185
Cdd:cd08562    78 spefAGEPIPTLADVLELArELGLGLNLEIKpDPGDEALTARVVAAALRELWPHASkllLSSFSLEALRAARRAAPELPL 157


                  ...
gi 1472785098 186 GQL 188
Cdd:cd08562   158 GLL 160
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 38-140 2.27e-19

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: 84.31  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  38 FYAHRGLHDlslGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGTA 116
Cdd:cd08581     1 LVAHRGYPA---RYPENTLVGFRAAVDAGaRFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSLRVAEPA 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1472785098 117 --------EHIPLFQDVLDLVDGK--VPLLVEIK 140
Cdd:cd08581    78 rfgsrfagEPLPSLAAVVQWLAQHpqVTLFVEIK 111
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 41-141 2.47e-19

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.


Pssm-ID: 176514 [Multi-domain]  Cd Length: 293  Bit Score: 85.41  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  41 HRGL------HDLsLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDL-----KRICGVEKD-----VDELT 103
Cdd:cd08572     5 HRGLgknyasGSL-AGIRENTIASFLAAAKHGADmVEFDVQLTKDGVPVIYHDFTIsvsekSKTGSDEGElievpIHDLT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098 104 YEELKALPV----------------------LGTAEH--IPLFQDVLDLVDGKVPLLVEIKY 141
Cdd:cd08572    84 LEQLKELGLqhisalkrkaltrkakgpkpnpWGMDEHdpFPTLQEVLEQVPKDLGFNIEIKY 145
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 40-265 7.93e-19

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase.


Pssm-ID: 176512 [Multi-domain]  Cd Length: 234  Bit Score: 83.04  E-value: 7.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDV-DELTYEELKALPVL-GTA 116
Cdd:cd08570     3 GHRGY---KAKYPENTLLAFEKAVEAGaDAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIiDDSTWDELSHLRTIeEPH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 117 EHIPLFQDVLD-LVDGKVP---LLVEIKYKHVGSSICRKAAELLDHYSgsyCIESFHP-VAL-MWFRKYRPYTVRGQLGM 190
Cdd:cd08570    80 QPMPTLKDVLEwLVEHELPdvkLMLDIKRDNDPEILFKLIAEMLAVKP---DLDFWRErIILgLWHLDFLKYGKEVLPGF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 191 N-------------FHKDDGRVHPVYYFPRHLLTNFLTKpdFIAYdhhARSAlslticrvvfGIPCFAWTVKSPRE-YYA 256
Cdd:cd08570   157 PvfhigfsldyarhFLNYSEKLVGISMHFVSLWGPFGQA--FLPE---LKKN----------GKKVFVWTVNTEEDmRYA 221


                  ....*....
gi 1472785098 257 CEHVFDYFI 265
Cdd:cd08570   222 IRLGVDGVI 230
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 41-141 3.14e-18

Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism.


Pssm-ID: 176549 [Multi-domain]  Cd Length: 290  Bit Score: 82.34  E-value: 3.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  41 HRGLHD----LSLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDL----KRICGVEKD------VDELTYE 105
Cdd:cd08607     5 HRGAGNsytaASAVVRENTIASFLQAAEHGADmVEFDVQLTKDLVPVVYHDFTLrvslKSKGDSDRDdllevpVKDLTYE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1472785098 106 ELKALPVLGTA-----------------EH--IPLFQDVLDLVDGKVPLLVEIKY 141
Cdd:cd08607    85 QLKLLKLFHISalkvkeyksveededppEHqpFPTLSDVLESVPEDVGFNIEIKW 139
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 39-141 1.59e-15

Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and similar proteins. The prototype of this CD is a putative GP-GDE from Silicibacter pomeroyi (SpGDE). It 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.


Pssm-ID: 176510 [Multi-domain]  Cd Length: 263  Bit Score: 74.27  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  39 YAHRGLHDLslgIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKriCGVEKDVD------------ELTYE 105
Cdd:cd08567     4 QGHRGARGL---LPENTLPAFAKALDLGVdTLELDLVLTKDGVIVVSHDPKLN--PDITRDPDgawlpyegpalyELTLA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1472785098 106 ELKAL-------------------PVLGTaeHIPLFQDVLDLVDG----KVPLLVEIKY 141
Cdd:cd08567    79 EIKQLdvgekrpgsdyaklfpeqiPVPGT--RIPTLEEVFALVEKygnqKVRFNIETKS 135
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 35-169 8.31e-15

Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative Galdieria sulphuraria glycerophosphodiester phosphodiesterase (GsGDE, EC 3.1.4.46) and its uncharacterized eukaryotic 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: 176507 [Multi-domain]  Cd Length: 265  Bit Score: 72.51  E-value: 8.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  35 PGKFYAHRGLhDLSLGIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFD-----LKRIC---GVEKDVDELTYE 105
Cdd:cd08564     3 RPIIVGHRGA-GCSTLYPENTLPSFRRALEIGVdGVELDVFLTKDNEIVVFHGTEddtnpDTSIQlddSGFKNINDLSLD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 106 EL-----------KALPVLGTA-EHIPLFQDVLDLVDGKVPLLVEIKYKHVGssICRKAAELLDHYSGSY--CIESFH 169
Cdd:cd08564    82 EItrlhfkqlfdeKPCGADEIKgEKIPTLEDVLVTFKDKLKYNIELKGREVG--LGERVLNLVEKYGMILqvHFSSFL 157
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 40-188 1.63e-14

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: 70.90  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKALPVLGTA-E 117
Cdd:cd08565     3 GHRGGRNLW---PENTLEGFRKALELGVdAVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERKALRLRDSFgE 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472785098 118 HIPLFQDVLDL-VDGKVPLLVEIKYKHVGSS----ICRKAAELLDHYSGSYCI-ESFHPVALMWFRKYrpYTVRGQL 188
Cdd:cd08565    80 KIPTLEEVLALfAPSGLELHVEIKTDADGTPypgaAALAAATLRRHGLLERSVlTSFDPAVLTEVRKH--PGVRTLG 154
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 40-159 4.45e-14

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: 70.04  E-value: 4.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHG--YgIELDVQLTKDGQVVAAHDFDLKRICGVEKD--VDELTYEELKAL----- 110
Cdd:cd08601     5 AHRGA---SGYAPEHTFAAYDLAREMGadY-IELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEIKQLdagsw 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1472785098 111 -----PVLGTAEH----IPLFQDVLDLVDGKVPLLVEIKYKHVGSSICRKAAELLDHY 159
Cdd:cd08601    81 fnkayPEYARESYsglkVPTLEEVIERYGGRANYYIETKSPDLYPGMEEKLLATLDKY 138
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 40-159 6.75e-13

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: 67.30  E-value: 6.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHG--YgIELDVQLTKDGQVVAAHDFDLKRICGVEKD------------VDELTYE 105
Cdd:cd08559     5 AHRGA---SGYAPEHTLAAYALAIEMGadY-IEQDLVMTKDGVLVARHDPTLDRTTNVAEHfpfrgrkdtgyfVIDFTLA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472785098 106 ELKALPVLGTAEH--------------IPLFQDVLDLVDG-------KVPLLVEIK----YKHVGSSICRKAAELLDHY 159
Cdd:cd08559    81 ELKTLRAGSWFNQryperapsyyggfkIPTLEEVIELAQGlnkstgrNVGIYPETKhptfHKQEGPDIEEKLLEVLKKY 159
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 40-110 1.12e-11

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 63.42  E-value: 1.12e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472785098  40 AHRGLHDLSlgiPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL 110
Cdd:PRK09454   12 AHRGGGKLA---PENTLAAIDVGARYGHrMIEFDAKLSADGEIFLLHDDTLERTSNGWGVAGELTWQDLAQL 80
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 40-140 3.70e-10

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.


Pssm-ID: 176522 [Multi-domain]  Cd Length: 263  Bit Score: 58.88  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHR-GLHDLslgiPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL------- 110
Cdd:cd08580     5 AHRgGTADA----PENTLLAISKALANGAdAIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLATLnagynfk 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1472785098 111 -----PVLGTAEHIPLFQDVLDLVDgKVPLLVEIK 140
Cdd:cd08580    81 peggyPYRGKPVGIPTLEQVLRAFP-DTPFILDMK 114
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 24-96 8.48e-10

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2, GDE3, GDE6-like proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase domain-containing protein subtype 5 (GDE2), subtype 2 (GDE3), subtype 1 (GDE6), and their eukaryotic homologs. Mammalian GDE2, GDE3, and GDE6 show very high sequence similarity to each other and have been classified into the same family. Although they are all transmembrane proteins, based on different pattern of tissue distribution, these enzymes might display diverse cellular functions. Mammalian GDE2 is primarily expressed in mature neurons. It selectively hydrolyzes glycerophosphocholine (GPC) and mainly functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE3 is specifically expressed in bone tissues and spleen. It selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol and functions as an inducer of osteoblast differentiation. Mammalian GDE6 is predominantly expressed in the spermatocytes of testis, and its specific physiological function has not been elucidated yet.


Pssm-ID: 176516 [Multi-domain]  Cd Length: 252  Bit Score: 57.70  E-value: 8.48e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472785098  24 APRLIGrpkrmpgkfyaHRGLHDLSlgiPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVE 96
Cdd:cd08574     1 KPALIG-----------HRGAPMLA---PENTLMSFEKALEHGvYGLETDVTISYDGVPFLMHDRTLRRTTNVA 60
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 40-141 4.17e-09

Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases superfamily; The PI-PLC-like phosphodiesterases superfamily represents the catalytic domains of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11), glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), 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, as well as their uncharacterized homologs found in organisms ranging from bacteria and archaea to metazoans, plants, and fungi. PI-PLCs are ubiquitous enzymes hydrolyzing the membrane lipid phosphoinositides to yield two important second messengers, inositol phosphates and diacylglycerol (DAG). GP-GDEs play essential roles in glycerol metabolism and catalyze the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols that are major sources of carbon and phosphate. Both, PI-PLCs and GP-GDEs, can hydrolyze the 3'-5' phosphodiester bonds in different substrates, and utilize a similar mechanism of general base and acid catalysis with conserved histidine residues, which consists of two steps, a phosphotransfer and a phosphodiesterase reaction. This superfamily also includes Neurospora crassa ankyrin repeat protein NUC-2 and its Saccharomyces cerevisiae counterpart, Phosphate system positive regulatory protein PHO81, glycerophosphodiester phosphodiesterase (GP-GDE)-like protein SHV3 and SHV3-like proteins (SVLs). The residues essential for enzyme activities and metal binding are not conserved in these sequence homologs, which might suggest that the function of catalytic domains in these proteins might be distinct from those in typical PLC-like phosphodiesterases.


Pssm-ID: 176498 [Multi-domain]  Cd Length: 179  Bit Score: 54.75  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHGY-GIELDVQLTKDGQVVAAHDFDLKRICGVEKDVdelTYEELkalpvlgtaeh 118
Cdd:cd08555     3 SHRGY---SQNGQENTLEAFYRALDAGArGLELDVRLTKDGELVVYHGPTLDRTTAGILPP---TLEEV----------- 65

                          90       100
                  ....*....|....*....|...
gi 1472785098 119 IPLFQDVLDLVDGKVPLLVEIKY 141
Cdd:cd08555    66 LELIADYLKNPDYTIILSLEIKQ 88
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 13-110 1.56e-08

Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of mammalian glycerophosphodiester phosphodiesterase GDE4; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial homologs of mammalian GDE4, a transmembrane protein whose cellular function has not been elucidated yet.


Pssm-ID: 176554 [Multi-domain]  Cd Length: 309  Bit Score: 54.67  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  13 LTAGLFYLLS---IAPRLIGRPKrmpgkFYAHRGLH---DLSlGI------------P-----ENTMAAFRRAVEHGYG- 68
Cdd:cd08613     3 LAAAGVWLNNtslLAPPPGGKPK-----LLAHRGLAqtfDRE-GVendtctaeridpPthdylENTIASMQAAFDAGADv 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1472785098  69 IELDVQLTKDGQVVAAHDFDLKRICGVEKDVDELTYEELKAL 110
Cdd:cd08613    77 VELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELKTL 118
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 38-91 2.47e-08

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE6 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE6 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 4 (GDPD4)) and their metazoan homologs. Mammalian GDE6 is a transmembrane protein predominantly expressed in the spermatocytes of testis. Although the specific physiological function of mammalian GDE6 has not been elucidated, its different pattern of tissue distribution suggests it might play a critical role in the completion of meiosis during male germ cell differentiation.


Pssm-ID: 176552 [Multi-domain]  Cd Length: 316  Bit Score: 54.11  E-value: 2.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1472785098  38 FYAHRGLHDLSlgiPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKR 91
Cdd:cd08610    25 IIGHRGAPMLA---PENTMMSFEKAIEHGaHGLETDVTLSYDGVPFLMHDFTLKR 76
GDPD_GDE5_like_1_plant cd08605
Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester ...
 40-110 4.47e-08

Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs.


Pssm-ID: 176547 [Multi-domain]  Cd Length: 282  Bit Score: 53.18  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGL------HDLS--LGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFD--LKRICGVEKD-VDELTYEEL 107
Cdd:cd08605     4 GHRGLgmnrasHQPSvgPGIRENTIASFIAASKFGADfVEFDVQVTRDGVPVIWHDDFivVERGGEVESSrIRDLTLAEL 83


                  ...
gi 1472785098 108 KAL 110
Cdd:cd08605    84 KAL 86
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 40-160 5.06e-08

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.


Pssm-ID: 176542 [Multi-domain]  Cd Length: 318  Bit Score: 53.16  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFrrAVEHGYG---IELDVQLTKDGQVVAAHDFDLKRICGV--------EKD----VDELTY 104
Cdd:cd08600     5 AHRGA---SGYLPEHTLEAK--ALAYAQGadyLEQDVVLTKDDKLVVIHDHYLDNVTNVaekfpdrkRKDgryyVIDFTL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 105 EELKALPV-------LGTAEH--------------IPLFQDVLDLVDG-------KVPLLVEIK----YKHVGSSICRKA 152
Cdd:cd08600    80 DELKSLSVterfdieNGKKVQvypnrfplwksdfkIHTLEEEIELIQGlnkstgkNVGIYPEIKapwfHHQEGKDIAAAT 159


                  ....*...
gi 1472785098 153 AELLDHYS 160
Cdd:cd08600   160 LEVLKKYG 167
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 40-129 8.98e-08

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.


Pssm-ID: 176544 [Multi-domain]  Cd Length: 309  Bit Score: 52.30  E-value: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDL------------------KRICGVEKD-- 98
Cdd:cd08602     5 AHRGA---SGYRPEHTLAAYQLAIEQGADfIEPDLVSTKDGVLICRHEPELsgttdvadhpefadrkttKTVDGVNVTgw 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1472785098  99 -VDELTYEELKAL------PVL-----GTAEhIPLFQDVLDLV 129
Cdd:cd08602    82 fTEDFTLAELKTLrarqrlPYRdqsydGQFP-IPTFEEIIALA 123
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 24-105 5.18e-07

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE2 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE2 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 5 (GDPD5)) and their metazoan homologs. Mammalian GDE2 is transmembrane protein primarily expressed in mature neurons. It is a mammalian homolog of bacterial glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), which catalyze the hydrolysis of various glycerophosphodiesters, and produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Mammalian GDE2 selectively hydrolyzes glycerophosphocholine (GPC) and has been characterized as GPC-GDE (EC 3.1.4.2) that contributes to osmotic regulation of cellular GPC. Mammalian GDE2 functions in a complex with an antioxidant scavenger peroxiredoxin1 (Prdx1) to control motor neuron differentiation in the spinal cord. Mammalian GDE2 also plays a critical role for retinoid-induced neuronal outgrowth. The catalytic activity of GDPD domain is essential for mammalian GDE2 cellular function.


Pssm-ID: 176550  Cd Length: 351  Bit Score: 50.23  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  24 APRLIGrpkrmpgkfyaHRGLHDLSlgiPENTMAAFRRAVEHG-YGIELDVQLTKDGQVVAAHDFDLKRICGVEKDVDEL 102
Cdd:cd08608     1 KPAIIG-----------HRGAPMLA---PENTLMSFQKALEQKvYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPER 66


                  ...
gi 1472785098 103 TYE 105
Cdd:cd08608    67 QYE 69
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 40-160 1.66e-06

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 48.52  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  40 AHRGLhdlSLGIPENTMAAfrRAVEHGYG---IELDVQLTKDGQVVAAHDFDLKRICGV--------EKD----VDELTY 104
Cdd:PRK11143   31 AHRGA---SGYLPEHTLPA--KAMAYAQGadyLEQDLVMTKDDQLVVLHDHYLDRVTDVaerfpdraRKDgryyAIDFTL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098 105 EELKALPV--------------------LGTAE-HIPLFQDVLDLVDG-------KVPLLVEIK----YKHVGSSICRKA 152
Cdd:PRK11143  106 DEIKSLKFtegfdiengkkvqvypgrfpMGKSDfRVHTFEEEIEFIQGlnhstgkNIGIYPEIKapwfHHQEGKDIAAKV 185


                  ....*...
gi 1472785098 153 AELLDHYS 160
Cdd:PRK11143  186 LEVLKKYG 193
PI-PLCc_GDPD_SF_unchar1 cd08583
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
 54-130 1.73e-06

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176525 [Multi-domain]  Cd Length: 237  Bit Score: 48.07  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  54 NTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFD---LKR-ICGVEKDVDELTYEELKALPVLGTAEhiPL-FQDVLD 127
Cdd:cd08583    16 NSLDAFEHNYKKGYRvFEVDLSLTSDGVLVARHSWDeslLKQlGLPTSKNTKPLSYEEFKSKKIYGKYT--PMdFKDVID 93


                  ...
gi 1472785098 128 LVD 130
Cdd:cd08583    94 LLK 96
GDPD_YPL110cp_fungi cd08606
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and ...
 24-106 2.64e-06

Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C.


Pssm-ID: 176548 [Multi-domain]  Cd Length: 286  Bit Score: 47.83  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  24 APRLIGrpkrmpgkfyaHRGL-----HDLSLGIPENTMAAFRRAVEHGYG-IELDVQLTKDGQVVAAHDFDLKRiCGVEK 97
Cdd:cd08606     1 SVQVIG-----------HRGLgkntaERKSLQLGENTVESFILAASLGASyVEVDVQLTKDLVPVIYHDFLVSE-TGTDV 68


                  ....*....
gi 1472785098  98 DVDELTYEE 106
Cdd:cd08606    69 PIHDLTLEQ 77
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 21-110 1.00e-05

Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE3 and similar proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian GDE3 (also known as glycerophosphodiester phosphodiesterase domain-containing protein 2 (GDPD2), Osteoblast differentiation promoting factor) and their metazoan homologs. Mammalian GDE3 is a transmembrane protein specifically expressed in bone tissues and spleen. It is a mammalian homolog of 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. Mammalian GDE3 has been characterized as glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) that selectively hydrolyzes extracellular glycerophosphoinositol (GPI) to generate inositol 1-phosphate (Ins1P) and glycerol. Mammalian GDE3 functions as an inducer of osteoblast differentiation. It also plays a critical role for actin cytoskeletal modulation. The catalytic activity of GDPD domain is essential for mammalian GDE3 cellular function.


Pssm-ID: 176551 [Multi-domain]  Cd Length: 315  Bit Score: 46.07  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472785098  21 LSIAPRLIGRPKRMPGK--FYAHRGLHDLSlgiPENTMAAFRRAVEHGYGI-ELDVQLTKDGQVVAAHDFDLKRICGVeK 97
Cdd:cd08609    10 LAICSPCIMEENNLPPKpaLVGHRGAPMLA---PENTLMSLRKSLECGVVVfETDVMVSKDGVPFLMHDEGLLRTTNV-K 85

                          90       100
                  ....*....|....*....|..
gi 1472785098  98 DV---------DELTYEELKAL 110
Cdd:cd08609    86 DVfpgrdaagsNNFTWTELKTL 107
 
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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