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Conserved domains on  [gi|1907082715|ref|XP_036012792|]
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lysophospholipase D GDPD1 isoform X1 [Mus musculus]

Protein Classification

glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171264)

glycerophosphodiester phosphodiesterase (GDPD) family protein similar to Homo sapiens lysophospholipase D GDPD1/GDE4 and GDPD3/GDE7, which hydrolyze lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines glycerophosphodiester phosphodiesterase 1

CATH:  3.20.20.190
EC:  3.1.4.-
Gene Ontology:  GO:0008081|GO:0006629|GO:0046872|GO:0004622
SCOP:  4000418

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-242 1.38e-145

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: 408.53  E-value: 1.38e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKC--EGKDTRIPLLKEVFEAFPETP 78
Cdd:cd08612    57 MLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvpKGSDRRIPLLEEVFEAFPDTP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  79 INIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFF 158
Cdd:cd08612   137 INIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 159 EIPMPSIILKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKD 238
Cdd:cd08612   217 EIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLRE 296


                  ....
gi 1907082715 239 FLNN 242
Cdd:cd08612   297 FLDK 300
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-242 1.38e-145

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: 408.53  E-value: 1.38e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKC--EGKDTRIPLLKEVFEAFPETP 78
Cdd:cd08612    57 MLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvpKGSDRRIPLLEEVFEAFPDTP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  79 INIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFF 158
Cdd:cd08612   137 INIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 159 EIPMPSIILKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKD 238
Cdd:cd08612   217 EIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLRE 296


                  ....
gi 1907082715 239 FLNN 242
Cdd:cd08612   297 FLDK 300
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-241 3.62e-38

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 133.07  E-value: 3.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVPFQRackcEGKDTRIPLLKEVFEAFP-ETPI 79
Cdd:COG0584    33 GIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAE----LRQLDAGSGP----DFAGERIPTLEEVLELVPgDVGL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 NIDIKVNNNV---LIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPilfslqRVLLILGLfftgllpfvpireq 156
Cdd:COG0584   105 NIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVP------LGLLVEEL-------------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 157 ffeipmpsiilkLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKL 236
Cdd:COG0584   165 ------------PADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232


                  ....*
gi 1907082715 237 KDFLN 241
Cdd:COG0584   233 RAVLR 237
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 1-233 2.88e-21

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: 89.00  E-value: 2.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPIN 80
Cdd:pfam03009  26 YIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELK----RLDIGAGNSGPLSGERVPFPTLEEVLEFDWDVGFN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  81 IDIKVnnnvlikkvsELVKQYKREHLTVWGNANSEIVDKCYKENSD-IPILFSLQRVLLILGLffTGLLPFVPIREQFFE 159
Cdd:pfam03009 102 IEIKI----------KPYVEAIAPEEGLIVKDLLLSVDEILAKKADpRRVIFSSFNPDELKRL--RELAPKLPLVFLSSG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 160 IPMpsiilklKEPHTISKGHKFL--------IWLSDTLLMRkaLFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTD 231
Cdd:pfam03009 170 RAY-------AEADLLERAAAFAgapallgeVALVDEALPD--LVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 1907082715 232 YP 233
Cdd:pfam03009 241 RP 242
 
Name Accession Description Interval E-value
GDPD_GDE4 cd08612
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-242 1.38e-145

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: 408.53  E-value: 1.38e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKC--EGKDTRIPLLKEVFEAFPETP 78
Cdd:cd08612    57 MLELDVHLTKDGQVVVSHDENLLRSCGVDKLVSDLNYADLPPYLEKLEVTFSPGDYCvpKGSDRRIPLLEEVFEAFPDTP 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  79 INIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFF 158
Cdd:cd08612   137 INIDIKVENDELIKKVSDLVRKYKREDITVWGSFNDEIVKKCHKENPNIPLFFSLKRVLLLLLLYYTGLLPFIPIKESFL 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 159 EIPMPSIILKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKLKD 238
Cdd:cd08612   217 EIPMPSIFLKTYFPKSMSRLNRFVLFLIDWLLMRPSLFRHLQKRGIQVYGWVLNDEEEFERAFELGADGVMTDYPTKLRE 296


                  ....
gi 1907082715 239 FLNN 242
Cdd:cd08612   297 FLDK 300
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-236 3.13e-116

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: 333.03  E-value: 3.13e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRA---CKCEGKDTRIPLLKEVFEAFPET 77
Cdd:cd08575    31 MLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSDLTYAELPPLDAGYGYTFDGGktgYPRGGGDGRIPTLEEVFKAFPDT 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  78 PINIDIKVNN-NVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLL-ILGLFFTGLLPFVPIRE 155
Cdd:cd08575   111 PINIDIKSPDaEELIAAVLDLLEKYKREDRTVWGSTNPEYLRALHPENPNLFESFSMTRCLLlYLALGYTGLLPFVPIKE 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 156 QFFEIPMPSIILKLKEPhtiskghKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTK 235
Cdd:cd08575   191 SFFEIPRPVIVLETFTL-------GEGASIVAALLWWPNLFDHLRKRGIQVYLWVLNDEEDFEEAFDLGADGVMTDSPTK 263


                  .
gi 1907082715 236 L 236
Cdd:cd08575   264 L 264
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 1-240 1.61e-39

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: 137.00  E-value: 1.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPF------QRACKCEGKDTRIPLLKEVFEAF 74
Cdd:cd08561    29 VLETDVHATKDGVLVVIHDETLDRTTDGTGPVADLTLAELR----RLDAGYhftddgGRTYPYRGQGIRIPTLEELFEAF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  75 PETPINIDIKVNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIR 154
Cdd:cd08561   105 PDVRLNIEIKDDGPAAAAALADLIERYGAQDRVLVASFSDRVLRRFRRLCPRVATSAGEGEVAAFVLASRLGLGSLYSPP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 155 EQFFEIPMPSIILKLKEPHTISKGHkfliwlsdtllmrkalfdhltARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPT 234
Cdd:cd08561   185 YDALQIPVRYGGVPLVTPRFVRAAH---------------------AAGLEVHVWTVNDPAEMRRLLDLGVDGIITDRPD 243


                  ....*.
gi 1907082715 235 KLKDFL 240
Cdd:cd08561   244 LLLEVL 249
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
1-241 3.62e-38

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 133.07  E-value: 3.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVPFQRackcEGKDTRIPLLKEVFEAFP-ETPI 79
Cdd:COG0584    33 GIELDVQLTKDGVLVVFHDPTLDRTTNGTGRVADLTLAE----LRQLDAGSGP----DFAGERIPTLEEVLELVPgDVGL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 NIDIKVNNNV---LIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPilfslqRVLLILGLfftgllpfvpireq 156
Cdd:COG0584   105 NIEIKSPPAAepdLAEAVAALLKRYGLEDRVIVSSFDPEALRRLRELAPDVP------LGLLVEEL-------------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 157 ffeipmpsiilkLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPTKL 236
Cdd:COG0584   165 ------------PADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRRLLDLGVDGIITDRPDLL 232


                  ....*
gi 1907082715 237 KDFLN 241
Cdd:COG0584   233 RAVLR 237
GDPD_memb_like cd08579
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 1-233 2.64e-24

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: 96.46  E-value: 2.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVpfqracKCEGKDTRIPLLKEVFEAF--PETP 78
Cdd:cd08579    29 YVEIDVQETKDGQFVVMHDANLKRLAGVNKKVWDLTLEELK----KLTI------GENGHGAKIPSLDEYLALAkgLKQK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  79 INIDIKVNNNV---LIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPilfslqrVLLILGLFFTGlLPFVPIre 155
Cdd:cd08579    99 LLIELKPHGHDspdLVEKFVKLYKQNLIENQHQVHSLDYRVIEKVKKLDPKIK-------TGYILPFNIGN-LPKTNV-- 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082715 156 QFFEIpmpsiilklkEPHTISKGhkfliwlsdtlLMRKAlfdhlTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYP 233
Cdd:cd08579   169 DFYSI----------EYSTLNKE-----------FIRQA-----HQNGKKVYVWTVNDPDDMQRYLAMGVDGIITDYP 220
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 3-233 2.96e-23

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: 93.78  E-value: 2.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLD--VPFQRACKCEgkdtRIPLLKEVFEAFPETPIN 80
Cdd:cd08563    33 ELDVHLTKDGQLVVIHDETVDRTTNGKGYVKDLTLEE----LKKLDagSWFDEKFTGE----KIPTLEEVLDLLKDKDLL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  81 IDIKVNNNV-----LIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPIlfslqrvllilglfftGLLpfvpire 155
Cdd:cd08563   105 LNIEIKTDVihypgIEKKVLELVKEYNLEDRVIFSSFNHESLKRLKKLDPKIKL----------------ALL------- 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082715 156 qfFEIpmpsiilKLKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYP 233
Cdd:cd08563   162 --YET-------GLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNEEEDMKRLKDLGVDGIITNYP 230
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 3-236 8.74e-22

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: 90.05  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVpfqrackcegKDTRIPLLKEVFEAFPETPI-NI 81
Cdd:cd08568    32 ELDVWLTKDGKLVVLHDENLKRVGGVDLKVKELTYKELK----KLHP----------GGELIPTLEEVFRALPNDAIiNV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  82 DIKVNNNVliKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDipilfslqrvlLILGLFFTGLLPFVPIREQFFEIP 161
Cdd:cd08568    98 EIKDIDAV--EPVLEIVEKFNALDRVIFSSFNHDALRELRKLDPD-----------AKVGLLIGEEEEGFSIPELHEKLK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082715 162 MPSIILKLKEPHTIS--KGHKFLIWLsdtllmRKalfdhltaRGIQVYVWVLNEEYEYKRAFDLgATGVMTDYPTKL 236
Cdd:cd08568   165 LYSLHVPIDAIGYIGfeKFVELLRLL------RK--------LGLKIVLWTVNDPELVPKLKGL-VDGVITDDVEKI 226
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 1-233 2.88e-21

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: 89.00  E-value: 2.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQRACKCEGKDTRIPLLKEVFEAFPETPIN 80
Cdd:pfam03009  26 YIEFDVQLTKDGVPVVLHDFNLDRTTDGAGYVRDLTLEELK----RLDIGAGNSGPLSGERVPFPTLEEVLEFDWDVGFN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  81 IDIKVnnnvlikkvsELVKQYKREHLTVWGNANSEIVDKCYKENSD-IPILFSLQRVLLILGLffTGLLPFVPIREQFFE 159
Cdd:pfam03009 102 IEIKI----------KPYVEAIAPEEGLIVKDLLLSVDEILAKKADpRRVIFSSFNPDELKRL--RELAPKLPLVFLSSG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 160 IPMpsiilklKEPHTISKGHKFL--------IWLSDTLLMRkaLFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTD 231
Cdd:pfam03009 170 RAY-------AEADLLERAAAFAgapallgeVALVDEALPD--LVKRAHARGLVVHVWTVNNEDEMKRLLELGVDGVITD 240


                  ..
gi 1907082715 232 YP 233
Cdd:pfam03009 241 RP 242
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 1-232 4.24e-21

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: 87.32  E-value: 4.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDanlkrstgvnvnvsdlkycelppylckldvpfqrackcegkdtrIPLLKEVFEAFPE-TPI 79
Cdd:cd08556    29 GVELDVQLTKDGVLVVIHD--------------------------------------------IPTLEEVLELVKGgVGL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 NIDIKVNN--NVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDIPIlfslqrvllilGLFFTGLLPFVPIREQF 157
Cdd:cd08556    65 NIELKEPTryPGLEAKVAELLREYGLEERVVVSSFDHEALRALKELDPEVPT-----------GLLVDKPPLDPLLAELA 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082715 158 FEIPMPSIILKLKephtiskghkfliwlsdtlLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDY 232
Cdd:cd08556   134 RALGADAVNPHYK-------------------LLTPELVRAAHAAGLKVYVWTVNDPEDARRLLALGVDGIITDD 189
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 1-233 4.52e-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: 82.65  E-value: 4.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYcelPPYLCKLdvpfqracKC-EGKDTRIPLLKEVFEAF----- 74
Cdd:cd08570    29 AIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDST---WDELSHL--------RTiEEPHQPMPTLKDVLEWLvehel 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  75 PETPINIDIKVNNN--VLIKKVSELVKQYK-----REHLtVWGNANSEIVDKCYKENSDIP---ILFSLqrvllilglff 144
Cdd:cd08570    98 PDVKLMLDIKRDNDpeILFKLIAEMLAVKPdldfwRERI-ILGLWHLDFLKYGKEVLPGFPvfhIGFSL----------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 145 tgllpfvPIREQFFEIPmpsiiLKLkepHTISKGHKfLIWLSDtllmRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLG 224
Cdd:cd08570   166 -------DYARHFLNYS-----EKL---VGISMHFV-SLWGPF----GQAFLPELKKNGKKVFVWTVNTEEDMRYAIRLG 225


                  ....*....
gi 1907082715 225 ATGVMTDYP 233
Cdd:cd08570   226 VDGVITDDP 234
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 2-234 6.05e-16

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: 74.27  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   2 LELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQRACKceGKDTRIPLLKEVFEAFPETP--I 79
Cdd:cd08582    30 IETDVRLTKDGELVCVHDPTLKRTSGGDGAVSDLTLAELR----KLDIGSWKGES--YKGEKVPTLEEYLAIVPKYGkkL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 NIDIKVNNNVliKKVSELVKQykrehltvwgnanseIVDKCYKENSDIPILfSLQRVLLILglfftgllpfvpIREQFFE 159
Cdd:cd08582   104 FIEIKHPRRG--PEAEEELLK---------------LLKESGLLPEQIVII-SFDAEALKR------------VRELAPT 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082715 160 IP---MPSIILKLKEPHTISKGHKFL-IWLSDTLLMRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYPT 234
Cdd:cd08582   154 LEtlwLRNYKSPKEDPRPLAKSGGAAgLDLSYEKKLNPAFIKALRDAGLKLNVWTVDDAEDAKRLIELGVDSITTNRPG 232
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 3-102 1.34e-15

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: 73.51  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELppylckldvpfqRACKCEGKDTRIPLLKEVFEAFP-ETPINI 81
Cdd:cd08585    38 ELDVQLTADGEVVVFHDDNLKRLTGVEGRVEELTAAEL------------RALRLLGTDEHIPTLDEVLELVAgRVPLLI 105

                          90       100
                  ....*....|....*....|....
gi 1907082715  82 DIKV---NNNVLIKKVSELVKQYK 102
Cdd:cd08585   106 ELKScggGDGGLERRVLAALKDYK 129
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 2-233 4.42e-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: 72.34  E-value: 4.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   2 LELDCHITKDEQVVVSHD----------ANLKRSTGVNVNVSDLKYCEL---------PPYLCKLDVPFQRACkcegKDT 62
Cdd:cd08567    32 LELDLVLTKDGVIVVSHDpklnpditrdPDGAWLPYEGPALYELTLAEIkqldvgekrPGSDYAKLFPEQIPV----PGT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  63 RIPLLKEVFEAFP-----ETPINIDIKVN--NNVLIKKVSELVKqykrehltvwgNANSEIvdkcykENSDIPILFSLQ- 134
Cdd:cd08567   108 RIPTLEEVFALVEkygnqKVRFNIETKSDpdRDILHPPPEEFVD-----------AVLAVI------RKAGLEDRVVLQs 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 135 ---RVLLIlglfftgllpfvpIREQFFEIPMPSIILK--LKEPHTISKGHKFLIWLSDTLLMRKALFDHLTARGIQVYVW 209
Cdd:cd08567   171 fdwRTLQE-------------VRRLAPDIPTVALTEEttLGNLPRAAKKLGADIWSPYFTLVTKELVDEAHALGLKVVPW 237

                         250       260
                  ....*....|....*....|....
gi 1907082715 210 VLNEEYEYKRAFDLGATGVMTDYP 233
Cdd:cd08567   238 TVNDPEDMARLIDLGVDGIITDYP 261
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 1-233 8.92e-12

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: 62.70  E-value: 8.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELppYLCKLDVPFQRackceGKDTRIPLLKEVFEAFPE-TPI 79
Cdd:cd08566    31 IVEIDVRRTKDGVLVLMHDDTLDRTTNGKGKVSDLTLAEI--RKLRLKDGDGE-----VTDEKVPTLEEALAWAKGkILL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 NIDIKvnnNVLIKKVSELVKQYK-REHLTVWGNANSEivdkcYKENSDIpilfsLQRVLLILGLFFTGLLPFVPIREQFF 158
Cdd:cd08566   104 NLDLK---DADLDEVIALVKKHGaLDQVIFKSYSEEQ-----AKELRAL-----APEVMLMPIVRDAEDLDEEEARAIDA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 159 EIPMPSIILKLKEPH-----TISKGHKFLIWlsdtllmrkalFDHLTARGIQVYVWVLNEEYE-YKRAFDLGATGVMTDY 232
Cdd:cd08566   171 LNLLAFEITFDDLDLpplfdELLRALGIRVW-----------VNTLGDDDTAGLDRALSDPREvWGELVDAGVDVIQTDR 239


                  .
gi 1907082715 233 P 233
Cdd:cd08566   240 P 240
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 2-240 3.71e-11

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: 61.18  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   2 LELDCHITKDEQVVVSHDANLKRSTGVNVN--VSDLKYCELPpylcKLDV--------PfQRAcKCEGKDTRIPLLKEVF 71
Cdd:cd08601    32 IELDLQMTKDGVLVAMHDETLDRTTNIERPgpVKDYTLAEIK----QLDAgswfnkayP-EYA-RESYSGLKVPTLEEVI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  72 EAF-PETPINIDIKVNNNV--LIKKVSELVKQYkreHLTVWGNANSEIV---------DKCYKENSDIPILfslqrvlli 139
Cdd:cd08601   106 ERYgGRANYYIETKSPDLYpgMEEKLLATLDKY---GLLTDNLKNGQVIiqsfskeslKKLHQLNPNIPLV--------- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 140 lglfftgllpfvpireQFFEIPMPSIILKLKephtISKGHKFLIWLSDTL-LMRKALFDHLTARGIQVYVWVLNEEYEYK 218
Cdd:cd08601   174 ----------------QLLWYGEGAETYDKW----LDEIKEYAIGIGPSIaDADPWMVHLIHKKGLLVHPYTVNEKADMI 233

                         250       260
                  ....*....|....*....|..
gi 1907082715 219 RAFDLGATGVMTDYPTKLKDFL 240
Cdd:cd08601   234 RLINWGVDGMFTNYPDRLKEVL 255
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 3-233 4.24e-10

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: 58.42  E-value: 4.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCElppyLCKLDVPFQRACKCEGKDTRIPLLKEVFEAFPE--TPIN 80
Cdd:cd08573    31 EFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAELTWEE----LRKLNAAAKHRLSSRFPGEKIPTLEEAVKECLEnnLRMI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  81 IDIKVNNNVLIKKVSELVKQYKRehltVWGNA-----NSEIVDKCYKENSDIpilfslqrvllILGL-----FFTGLLPF 150
Cdd:cd08573   107 FDVKSNSSKLVDALKNLFKKYPG----LYDKAivcsfNPIVIYKVRKADPKI-----------LTGLtwrpwFLSYTDDE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 151 VPIR-EQFFEIPMPSIILKLKEPHTiskgHKFLIWL--SDTLLMRK-----ALFDHLTARGIQVYVWVLNEEYEyKRAF- 221
Cdd:cd08573   172 GGPRrKSGWKHFLYSMLDVILEWSL----HSWLPYFlgVSALLIHKddissAYVRYWRARGIRVIAWTVNTPTE-KQYFa 246

                         250
                  ....*....|...
gi 1907082715 222 -DLGATgVMTDYP 233
Cdd:cd08573   247 kTLNVP-YITDSL 258
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 1-234 5.72e-10

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: 57.80  E-value: 5.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPfqrackcEGKDTRIPLLKEVFEAFPETPI- 79
Cdd:cd08565    29 AVEFDVHLTADGEVVVIHDPTLDRTTHGTGAVRDLTLAERK----ALRLR-------DSFGEKIPTLEEVLALFAPSGLe 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  80 -NIDIKVNNNV-----LIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSdIPILFSL-QRVLLILGlfftGLLPFVP 152
Cdd:cd08565    98 lHVEIKTDADGtpypgAAALAAATLRRHGLLERSVLTSFDPAVLTEVRKHPG-VRTLGSVdEDMLERLG----GELPFLT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 153 IReqffeipmpsiilklKEP-HTISKGHKFLIwlsDTLLMRKAlfdhlTARGIQVYVWVLNEEYEYKRAFDLGATGVMTD 231
Cdd:cd08565   173 AT---------------ALKaHIVAVEQSLLA---ATWELVRA-----AVPGLRLGVWTVNDDSLIRYWLACGVRQLTTD 229


                  ...
gi 1907082715 232 YPT 234
Cdd:cd08565   230 RPD 232
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 1-233 2.20e-09

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: 56.08  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDV--PFQRackcEGKDTRIPLLKEVFEAFPETP 78
Cdd:cd08562    29 WVEFDVKLSGDGTLVLIHDDTLDRTTNGSGAVTELTWAELA----QLDAgsWFSP----EFAGEPIPTLADVLELARELG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  79 I--NIDIKVNNNVLiKKVSELVKQYKREHltvWgNANSEIVDKCYkensDIPILFSLQRVL--LILGLFFTGLLPfvPIR 154
Cdd:cd08562   101 LglNLEIKPDPGDE-ALTARVVAAALREL---W-PHASKLLLSSF----SLEALRAARRAApeLPLGLLFDTLPA--DWL 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082715 155 EQFFEIPMPSIILKlkephtiskgHKFLiwlsdtllmRKALFDHLTARGIQVYVWVLNEEYEYKRAFDLGATGVMTDYP 233
Cdd:cd08562   170 ELLAALGAVSIHLN----------YRGL---------TEEQVKALKDAGYKLLVYTVNDPARAAELLEWGVDAIFTDRP 229
GDPD_GDE4_like_1 cd08613
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial homologs of ...
 2-110 3.31e-07

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: 50.05  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   2 LELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDV------------PFQrackceGKDT-RIPLLK 68
Cdd:cd08613    77 VELDVHPTKDGEFAVFHDWTLDCRTDGSGVTRDHTMAELK----TLDIgygytadggktfPFR------GKGVgMMPTLD 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907082715  69 EVFEAFPETPINIDIKVNNNVLIKKVSELVK---QYKREHLTVWG 110
Cdd:cd08613   147 EVFAAFPDRRFLINFKSDDAAEGELLAEKLAtlpRKRLQVLTVYG 191
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 1-235 9.42e-07

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: 48.48  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKYCELPpylcKLDVPFQRACKCE----GKDTRIPLLKEVFEAFPE 76
Cdd:cd08580    31 AIWLTVQLSKDGVPVLYRPSDLKSLTNGSGAVSAYTAAQLA----TLNAGYNFKPEGGypyrGKPVGIPTLEQVLRAFPD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  77 TPINIDIK-VNNNVLIKKVSELVKQYKREHLTVWGNANSEIVDKCYKENSDipILF----SLQRVLLILGLFFTGLLPFV 151
Cdd:cd08580   107 TPFILDMKsLPADPQAKAVARVLERENAWSRVRIYSTNADYQDALAPYPQA--RLFesrdVTRTRLANVAMAHQCDLPPD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 152 PIREQFFEIPMPsiiLKLKEPHTISKGH---KFLIWLSDTL-LMRKALFDHLTARGIqvyvwvlNEEYEYKRAFDLGATG 227
Cdd:cd08580   185 SGAWAGFELRRK---VTVVETFTLGEGRspvQATLWTPAAVdCFRRNSKVKIVLFGI-------NTADDYRLAKCLGADA 254


                  ....*...
gi 1907082715 228 VMTDYPTK 235
Cdd:cd08580   255 VMVDSPAA 262
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 3-241 1.10e-06

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: 48.24  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSH--------DANLKRSTGVNVNVSDLKYCELPPYLCKLDVPFQRACKCEGKDTRIPLLKEVFEAF 74
Cdd:cd08564    38 ELDVFLTKDNEIVVFHgteddtnpDTSIQLDDSGFKNINDLSLDEITRLHFKQLFDEKPCGADEIKGEKIPTLEDVLVTF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715  75 -PETPINIDIKVNNNVLIKKVSELVKQYKrehltvwgnanseivdkcYKENSDIPILFSLQRVLLILGLFFTGLLpfVPI 153
Cdd:cd08564   118 kDKLKYNIELKGREVGLGERVLNLVEKYG------------------MILQVHFSSFLHYDRLDLLKALRPNKLN--VPI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715 154 REQFFEIPMPSIILKLKephTISKGHKFLIWLSDTLLMRKALFdHLTARGIQVYVW----VLNEEYEYKRAFDLGATGVM 229
Cdd:cd08564   178 ALLFNEVKSPSPLDFLE---QAKYYNATWVNFSYDFWTEEFVK-KAHENGLKVMTYfdepVNDNEEDYKVYLELGVDCIC 253

                         250
                  ....*....|..
gi 1907082715 230 TDYPTKLKDFLN 241
Cdd:cd08564   254 PNDPVLLVNFLK 265
GDPD_GDE5 cd08607
Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester ...
 1-84 1.01e-05

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: 45.75  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHD----ANLKRSTGVN------VNVSDLKYCELppylcKLDVPFQRA-----------CKCEG 59
Cdd:cd08607    37 MVEFDVQLTKDLVPVVYHDftlrVSLKSKGDSDrddlleVPVKDLTYEQL-----KLLKLFHISalkvkeyksveEDEDP 111

                          90       100
                  ....*....|....*....|....*..
gi 1907082715  60 KDTRI-PLLKEVFEAFPE-TPINIDIK 84
Cdd:cd08607   112 PEHQPfPTLSDVLESVPEdVGFNIEIK 138
GDPD_GDE5_like cd08572
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 1-84 7.02e-05

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: 43.04  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   1 MLELDCHITKDEQVVVSHD----------ANLKRSTGVNVNVSDLKYCEL-------------PPYLCKLDVPFQRACKC 57
Cdd:cd08572    38 MVEFDVQLTKDGVPVIYHDftisvsekskTGSDEGELIEVPIHDLTLEQLkelglqhisalkrKALTRKAKGPKPNPWGM 117

                          90       100
                  ....*....|....*....|....*...
gi 1907082715  58 EgKDTRIPLLKEVFEAFPE-TPINIDIK 84
Cdd:cd08572   118 D-EHDPFPTLQEVLEQVPKdLGFNIEIK 144
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 3-87 1.53e-04

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: 41.55  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   3 ELDCHITKDEQVVVSHDANLKRSTGVNVNVSDLKycelppylcklDVPFQRACKCEGK-------DTRIPLLKEVFEA-- 73
Cdd:cd08581    31 EFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELE-----------DAELDSLRVAEPArfgsrfaGEPLPSLAAVVQWla 99

                          90
                  ....*....|....*
gi 1907082715  74 -FPETPINIDIKVNN 87
Cdd:cd08581   100 qHPQVTLFVEIKTES 114
GDPD_2 pfam13653
Glycerophosphoryl diester phosphodiesterase family; This family also includes ...
 205-234 6.13e-04

Glycerophosphoryl diester phosphodiesterase family; This family also includes glycerophosphoryl diester phosphodiesterases as well as 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: 433380 [Multi-domain]  Cd Length: 30  Bit Score: 36.32  E-value: 6.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907082715 205 QVYVWVLNEEYEYKRAFDLGATGVMTDYPT 234
Cdd:pfam13653   1 KVRFWTIDNKAAWKELMRLGVDGLNTDDPE 30
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 2-103 3.67e-03

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: 37.03  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082715   2 LELDCHITKDEQVVVSHDANLKRSTGvnvnvsdlkyCELPPYLCKLdvpfqrackcegkdtrIPLLKEVFEAFPETPI-N 80
Cdd:cd08555    30 LELDVRLTKDGELVVYHGPTLDRTTA----------GILPPTLEEV----------------LELIADYLKNPDYTIIlS 83

                          90       100
                  ....*....|....*....|...
gi 1907082715  81 IDIKVNNNVLIKKVSELVKQYKR 103
Cdd:cd08555    84 LEIKQDSPEYDEFLAKVLKELRV 106
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 2-28 9.30e-03

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: 36.48  E-value: 9.30e-03
                          10        20
                  ....*....|....*....|....*..
gi 1907082715   2 LELDCHITKDEQVVVSHDANLKRSTGV 28
Cdd:cd08559    32 IEQDLVMTKDGVLVARHDPTLDRTTNV 58
 
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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