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Conserved domains on  [gi|81884045|sp|Q640M6|]
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RecName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 5; AltName: Full=Glycerophosphocholine phosphodiesterase GDPD5; AltName: Full=Glycerophosphodiester phosphodiesterase 2; AltName: Full=Phosphoinositide phospholipase C GDPD5

Protein Classification

PI-PLC domain-containing protein( domain architecture ID 49489)

PI-PLC (phosphoinositide-specific phospholipase C) domain-containing protein may hydrolyze the membrane lipid phosphatidylinositol to produce phosphorylated myo-inositol and diacylglycerol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI-PLCc_GDPD_SF super family cl14615
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 227-576 0e+00

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.


The actual alignment was detected with superfamily member cd08608:

Pssm-ID: 472694  Cd Length: 351  Bit Score: 666.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 227 KPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQ 306
Cdd:cd08608   1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 307 RLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAK-GNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGF 385
Cdd:cd08608  81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608 161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 466 WCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608 241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                       330       340       350
                ....*....|....*....|....*....|.
gi 81884045 546 VSIMKEKLIFSEISDGVEVSDELSVCSDSSY 576
Cdd:cd08608 321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
 
Name Accession Description Interval E-value
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-576 0e+00

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: 666.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 227 KPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQ 306
Cdd:cd08608   1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 307 RLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAK-GNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGF 385
Cdd:cd08608  81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608 161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 466 WCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608 241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                       330       340       350
                ....*....|....*....|....*....|.
gi 81884045 546 VSIMKEKLIFSEISDGVEVSDELSVCSDSSY 576
Cdd:cd08608 321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
226-484 2.27e-33

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 127.68  E-value: 2.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 226 PKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVL 305
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVADLTLAEL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 306 QRLNAGqwflktdpfwtasslspsDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPyrgSFLNVTLEAVLRSGF 385
Cdd:COG0584  73 RQLDAG------------------SGPDFAGERIPTLEEVLELVPGDVGLNIEIKSPPAAEP---DLAEAVAALLKRYGL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFN-RQRPLVRKMAPGFQ----QTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPW 460
Cdd:COG0584 132 EDRVIVSSFDpEALRRLRELAPDVPlgllVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPE 211

                       250       260
                ....*....|....*....|....
gi 81884045 461 LFSLLWCAGVPSVTSDNSHTLSRV 484
Cdd:COG0584 212 EMRRLLDLGVDGIITDRPDLLRAV 235
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 226-314 1.43e-14

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 73.82  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045  226 PKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNvehlfpelARRPAAMLNWTVL 305
Cdd:PRK09454   6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN--------GWGVAGELTWQDL 77


                 ....*....
gi 81884045  306 QRLNAGQWF 314
Cdd:PRK09454  78 AQLDAGSWF 86
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 233-316 3.70e-13

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: 69.35  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045   233 HRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVLQRLNAGQ 312
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDG--------AGYVRDLTLEELKRLDIGA 72


                  ....
gi 81884045   313 WFLK 316
Cdd:pfam03009  73 GNSG 76
 
Name Accession Description Interval E-value
GDPD_GDE2 cd08608
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-576 0e+00

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: 666.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 227 KPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQ 306
Cdd:cd08608   1 KPAIIGHRGAPMLAPENTLMSFQKALEQKVYGLQADVTISLDGVPFLMHDRTLRRTTNVDRVFPERQYEDASMFNWTDLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 307 RLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAK-GNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGF 385
Cdd:cd08608  81 RLNAGQWFLKDDPFWTAQSLSPSDRKEAGNQSVCSLAELLELAKrYNASVLLNLRRPPPNHPYHQSWINLTLKTILASGI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08608 161 PQEQVMWTPDWQRKLVRKVAPGFQQTSGEKLPVASLRERGITRLNLRYTQASAQEIRDYSASNLSVNLYTVNEPWLYSLL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 466 WCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRD 545
Cdd:cd08608 241 WCSGVPSVTSDASHVLRKVPFPLWLMPPDEYCLIWITSDLISFAVIVGIFIFQKWRLGGIRSYNPEQIMLSAAVRRSSRD 320

                       330       340       350
                ....*....|....*....|....*....|.
gi 81884045 546 VSIMKEKLIFSEISDGVEVSDELSVCSDSSY 576
Cdd:cd08608 321 VNIMKEKLIFSEINNGVETTDELSLCSDNGY 351
GDPD_GDE_2_3_6 cd08574
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 227-477 8.01e-157

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: 449.84  E-value: 8.01e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 227 KPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLNWTVLQ 306
Cdd:cd08574   1 KPALIGHRGAPMLAPENTLMSFEKALEHGVYGLETDVTISYDGVPFLMHDRTLRRTTNVADVFPERAHERASMFTWTDLQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 307 RLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAK-GNASLLLNLRDPPRDHPYRGSFLNVTLEAVLRSGF 385
Cdd:cd08574  81 QLNAGQWFLKDDPFWTASSLSESDREEAGNQSIPSLAELLRLAKkHNKSVIFDLRRPPPNHPYYQSYVNITLDTILASGI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLFSLL 465
Cdd:cd08574 161 PQHQVFWLPDEYRALVRKVAPGFQQVSGRKLPVESLRENGISRLNLEYSQLSAQEIREYSKANISVNLYVVNEPWLYSLL 240

                       250
                ....*....|..
gi 81884045 466 WCAGVPSVTSDN 477
Cdd:cd08574 241 WCSGVQSVTTNA 252
GDPD_GDE6 cd08610
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 207-517 1.09e-123

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: 367.66  E-value: 1.09e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 207 YLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVE 286
Cdd:cd08610   2 YLIPLGIYSPCIREKETLGPKPTIIGHRGAPMLAPENTMMSFEKAIEHGAHGLETDVTLSYDGVPFLMHDFTLKRTTNIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 287 HLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELA-KGNASLLLNLRDPPRD 365
Cdd:cd08610  82 EVQPESACENPAFFNWDFLSTLNAGKWFVKPRPFYNMKPLSEADKERARNQSIPKLSNFLRLAeKENKLVIFDLYRPPPK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 366 HPYRGSFLNVTLEAVL-RSGFPQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDY 444
Cdd:cd08610 162 HPYRHTWIRRVLEVILnEVGIEQHLVLWLPAHDRQYVQSVAPGFKQHVGRKVPIETLLKNNISILNLAYKKLFSNDIRDY 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81884045 445 ASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVL 517
Cdd:cd08610 242 KAANIHTNVYVINEPWLFSLAWCSGIHSVTTNNIHLLKQLDHPHFFMTPKFYVFMWLLADIISVLFIVLIFCF 314
GDPD_GDE3 cd08609
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 202-518 1.65e-116

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: 349.22  E-value: 1.65e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 202 VVFTFYLIPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRR 281
Cdd:cd08609   1 VSAAVYLAPLAICSPCIMEENNLPPKPALVGHRGAPMLAPENTLMSLRKSLECGVVVFETDVMVSKDGVPFLMHDEGLLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 282 TTNVEHLFPELARRPAAMLNWTVLQRLNAGQWFLKTDPFWTASSLSPSDHREVQNQSICSLAELLELAKG-NASLLLNLR 360
Cdd:cd08609  81 TTNVKDVFPGRDAAGSNNFTWTELKTLNAGSWFLERRPFWTLSSLSEEDRREADNQTVPSLSELLDLAKKhNVSIMFDLR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 361 DPPRDHPYRGSFLNVTLEAVLRSGFPQHQVMWLFNRQRPLVRKMAPGFQQTSGSKEaiANLRKGhIQKLNLRYTQVSHQE 440
Cdd:cd08609 161 NENNSHVFYSSFVFYTLETILKLGIPPDKVWWLPDEYRHDVMKMEPGFKQVYGRQK--EMLMDG-GNFMNLPYQDLSALE 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81884045 441 LRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHTLSRVPSPLWIMPPDEYCLMWVTADLISFSLIIGIFVLQ 518
Cdd:cd08609 238 IKELRKDNVSVNLWVVNEPWLFSLLWCSGVSSVTTNACQLLKDMSKPIWLLEPNTYLGIWIATDCVSLLLMLWLFLLQ 315
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
226-484 2.27e-33

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 127.68  E-value: 2.27e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 226 PKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVL 305
Cdd:COG0584   1 PRPLIIAHRGASGLAPENTLAAFRAALELGADGIELDVQLTKDGVLVVFHDPTLDRTTNG--------TGRVADLTLAEL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 306 QRLNAGqwflktdpfwtasslspsDHREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPyrgSFLNVTLEAVLRSGF 385
Cdd:COG0584  73 RQLDAG------------------SGPDFAGERIPTLEEVLELVPGDVGLNIEIKSPPAAEP---DLAEAVAALLKRYGL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 386 PQHQVMWLFN-RQRPLVRKMAPGFQ----QTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPW 460
Cdd:COG0584 132 EDRVIVSSFDpEALRRLRELAPDVPlgllVEELPADPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPE 211

                       250       260
                ....*....|....*....|....
gi 81884045 461 LFSLLWCAGVPSVTSDNSHTLSRV 484
Cdd:COG0584 212 EMRRLLDLGVDGIITDRPDLLRAV 235
GDPD_EcUgpQ_like cd08562
Glycerophosphodiester phosphodiesterase domain in Escherichia coli cytosolic ...
 230-477 8.59e-25

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: 103.07  E-value: 8.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNvehlfpelARRPAAMLNWTVLQRLN 309
Cdd:cd08562   1 IIAHRGASSLAPENTLAAFRAAAELGVRWVEFDVKLSGDGTLVLIHDDTLDRTTN--------GSGAVTELTWAELAQLD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 310 AGQWFlktdpfwtasslSPsdhrEVQNQSICSLAELLELAKGNAsLLLNLRDPPrdHPYRGSFLNVTLEAVLRSGFPQHQ 389
Cdd:cd08562  73 AGSWF------------SP----EFAGEPIPTLADVLELARELG-LGLNLEIKP--DPGDEALTARVVAAALRELWPHAS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 390 ----------VMWLFNRQRP------LVRKMAPGFQQTSGSKEAIAnlrkghiqkLNLRYTQVSHQELRDYASWNLSVNL 453
Cdd:cd08562 134 klllssfsleALRAARRAAPelplglLFDTLPADWLELLAALGAVS---------IHLNYRGLTEEQVKALKDAGYKLLV 204

                       250       260
                ....*....|....*....|....
gi 81884045 454 YTVNAPWLFSLLWCAGVPSVTSDN 477
Cdd:cd08562 205 YTVNDPARAAELLEWGVDAIFTDR 228
GDPD cd08556
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and ...
 230-477 5.03e-22

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: 93.87  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDttlrrttnvehlfpelarrpaamlnwtvlqrln 309
Cdd:cd08556   1 IIAHRGASGEAPENTLAAFRKALEAGADGVELDVQLTKDGVLVVIHD--------------------------------- 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 310 agqwflktdpfwtasslspsdhrevqnqsICSLAELLELAKGNASLLLNLRDPPRDHPyrgsFLNVTLEAVLRSGFPQHQ 389
Cdd:cd08556  48 -----------------------------IPTLEEVLELVKGGVGLNIELKEPTRYPG----LEAKVAELLREYGLEERV 94

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 390 VMWLFN-RQRPLVRKMAPG------FQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNAPWLF 462
Cdd:cd08556  95 VVSSFDhEALRALKELDPEvptgllVDKPPLDPLLAELARALGADAVNPHYKLLTPELVRAAHAAGLKVYVWTVNDPEDA 174

                       250
                ....*....|....*
gi 81884045 463 SLLWCAGVPSVTSDN 477
Cdd:cd08556 175 RRLLALGVDGIITDD 189
GDPD_periplasmic_GlpQ_like cd08559
Periplasmic glycerophosphodiester phosphodiesterase domain (GlpQ) and similar proteins; This ...
 228-351 4.75e-19

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: 88.10  E-value: 4.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARrpaAMLNWTV--- 304
Cdd:cd08559   1 PLVIAHRGASGYAPEHTLAAYALAIEMGADYIEQDLVMTKDGVLVARHDPTLDRTTNVAEHFPFRGR---KDTGYFVidf 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 81884045 305 ----LQRLNAGQWFLKTDPFwtasslspSDHREVQNQSICSLAELLELAKG 351
Cdd:cd08559  78 tlaeLKTLRAGSWFNQRYPE--------RAPSYYGGFKIPTLEEVIELAQG 120
GDPD_SaGlpQ_like cd08601
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins; ...
 228-362 4.09e-18

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: 84.29  E-value: 4.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEhlfpelARRPAAMLNWTVLQR 307
Cdd:cd08601   1 NAVIAHRGASGYAPEHTFAAYDLAREMGADYIELDLQMTKDGVLVAMHDETLDRTTNIE------RPGPVKDYTLAEIKQ 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 81884045 308 LNAGQWFLKTDPFWTASSLSpsdhrevqNQSICSLAELLELAKGNASLLLNLRDP 362
Cdd:cd08601  75 LDAGSWFNKAYPEYARESYS--------GLKVPTLEEVIERYGGRANYYIETKSP 121
GDPD_like_2 cd08582
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 230-476 1.83e-17

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: 81.98  E-value: 1.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVLQRLN 309
Cdd:cd08582   1 VIAHRGASAEAPENTLAAFELAWEQGADGIETDVRLTKDGELVCVHDPTLKRTSGG--------DGAVSDLTLAELRKLD 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 310 AGQWflktdpfwtasslspsDHREVQNQSICSLAELLELA-KGNASLLLNLRDPPRDHPyrgsFLNVTLEAVLRSGFPQH 388
Cdd:cd08582  73 IGSW----------------KGESYKGEKVPTLEEYLAIVpKYGKKLFIEIKHPRRGPE----AEEELLKLLKESGLLPE 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 389 QVMWL-FNR---QRplVRKMAPGFQ-----QTSGSKEAIANLRKGH-IQKLNLRYTQVSHQE----LRDYAswnLSVNLY 454
Cdd:cd08582 133 QIVIIsFDAealKR--VRELAPTLEtlwlrNYKSPKEDPRPLAKSGgAAGLDLSYEKKLNPAfikaLRDAG---LKLNVW 207

                       250       260
                ....*....|....*....|....*.
gi 81884045 455 TVN----APWLFSLlwcaGVPSVTSD 476
Cdd:cd08582 208 TVDdaedAKRLIEL----GVDSITTN 229
GDPD_TtGDE_like cd08563
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar ...
 230-476 9.04e-17

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


Pssm-ID: 176506 [Multi-domain]  Cd Length: 230  Bit Score: 79.91  E-value: 9.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNV-----EHLFPElarrpaamlnwtv 304
Cdd:cd08563   3 IFAHRGYSGTAPENTLLAFKKAIEAGADGIELDVHLTKDGQLVVIHDETVDRTTNGkgyvkDLTLEE------------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 305 LQRLNAGQWFlktdpfwtasslspsdHREVQNQSICSLAELLELAKGNaSLLLNLRDPPRDHPYRGSFLNVtLEAVLRSG 384
Cdd:cd08563  70 LKKLDAGSWF----------------DEKFTGEKIPTLEEVLDLLKDK-DLLLNIEIKTDVIHYPGIEKKV-LELVKEYN 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 385 FPqHQVMW-LFNRQR-PLVRKMAP----GFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRDYASWNLSVNLYTVNA 458
Cdd:cd08563 132 LE-DRVIFsSFNHESlKRLKKLDPkiklALLYETGLQDPKDYAKKIGADSLHPDFKLLTEEVVEELKKRGIPVRLWTVNE 210

                       250
                ....*....|....*...
gi 81884045 459 PWLFSLLWCAGVPSVTSD 476
Cdd:cd08563 211 EEDMKRLKDLGVDGIITN 228
GDPD_SpGDE_like cd08567
Glycerophosphodiester phosphodiesterase domain of putative Silicibacter pomeroyi ...
 228-476 1.18e-14

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: 1.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTT--NVEHLFPELARRPAAMLNWTVL 305
Cdd:cd08567   1 FDLQGHRGARGLLPENTLPAFAKALDLGVDTLELDLVLTKDGVIVVSHDPKLNPDItrDPDGAWLPYEGPALYELTLAEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 306 QRLNAGQwflkTDPFWTASSLSPsDHREVQNQSICSLAELLELAK--GNASLLLNLR-----DPPRDHPYRGSFLNVTLE 378
Cdd:cd08567  81 KQLDVGE----KRPGSDYAKLFP-EQIPVPGTRIPTLEEVFALVEkyGNQKVRFNIEtksdpDRDILHPPPEEFVDAVLA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 379 AVLRSGFPQHQVMWLFN-RQRPLVRKMAPGF-------QQTSGS-KEAIANLrKGHIqkLNLRYTQVSHQELRDYASWNL 449
Cdd:cd08567 156 VIRKAGLEDRVVLQSFDwRTLQEVRRLAPDIptvalteETTLGNlPRAAKKL-GADI--WSPYFTLVTKELVDEAHALGL 232

                       250       260
                ....*....|....*....|....*..
gi 81884045 450 SVNLYTVNAPWLFSLLWCAGVPSVTSD 476
Cdd:cd08567 233 KVVPWTVNDPEDMARLIDLGVDGIITD 259
ugpQ PRK09454
cytoplasmic glycerophosphodiester phosphodiesterase; Provisional
 226-314 1.43e-14

cytoplasmic glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236524 [Multi-domain]  Cd Length: 249  Bit Score: 73.82  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045  226 PKPALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNvehlfpelARRPAAMLNWTVL 305
Cdd:PRK09454   6 PYPRIVAHRGGGKLAPENTLAAIDVGARYGHRMIEFDAKLSADGEIFLLHDDTLERTSN--------GWGVAGELTWQDL 77


                 ....*....
gi 81884045  306 QRLNAGQWF 314
Cdd:PRK09454  78 AQLDAGSWF 86
GDPD_cytoplasmic_ScUgpQ2_like cd08561
Glycerophosphodiester phosphodiesterase domain of Streptomyces coelicolor cytoplasmic ...
 231-459 2.36e-14

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: 73.06  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNvehlfpelARRPAAMLNWTVLQRLNA 310
Cdd:cd08561   2 IAHRGGAGLAPENTLLAFEDAVELGADVLETDVHATKDGVLVVIHDETLDRTTD--------GTGPVADLTLAELRRLDA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 311 GQWFlKTDPFWTASslspsdhREVQNQSICSLAELLElAKGNASLLLNLRDPPRDHPyrgsflnVTLEAVLRSGFPQHQV 390
Cdd:cd08561  74 GYHF-TDDGGRTYP-------YRGQGIRIPTLEELFE-AFPDVRLNIEIKDDGPAAA-------AALADLIERYGAQDRV 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 391 MWLFNRQRPL--VRKMAPGFqQTSGSKEAIANLRKGHIQKLNLRY----------------TQVSHQELRDYASWNLSVN 452
Cdd:cd08561 138 LVASFSDRVLrrFRRLCPRV-ATSAGEGEVAAFVLASRLGLGSLYsppydalqipvryggvPLVTPRFVRAAHAAGLEVH 216


                ....*..
gi 81884045 453 LYTVNAP 459
Cdd:cd08561 217 VWTVNDP 223
GDPD_AtGDE_like cd08566
Glycerophosphodiester phosphodiesterase domain of Agrobacterium tumefaciens and similar ...
 230-369 3.68e-14

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: 72.33  E-value: 3.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPM-LAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVLQRL 308
Cdd:cd08566   2 VVAHRGGWGaGAPENSLAAIEAAIDLGADIVEIDVRRTKDGVLVLMHDDTLDRTTNG--------KGKVSDLTLAEIRKL 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81884045 309 NAGQWFlktdpfwtasslspsdhREVQNQSICSLAELLELAKGNASLLLNLRDPPRDHPYR 369
Cdd:cd08566  74 RLKDGD-----------------GEVTDEKVPTLEEALAWAKGKILLNLDLKDADLDEVIA 117
GDPD_GDE1 cd08573
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 230-311 1.47e-13

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: 71.14  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPElarrpaamLNWTVLQRLN 309
Cdd:cd08573   1 IIGHRGAGHDAPENTLAAFRQAKKNGADGVEFDLEFTKDGVPVLMHDDTVDRTTDGTGLVAE--------LTWEELRKLN 72


                ..
gi 81884045 310 AG 311
Cdd:cd08573  73 AA 74
GDPD_like_1 cd08581
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 230-477 2.67e-13

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: 69.67  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARRPAAMLnwtvlqRLN 309
Cdd:cd08581   1 LVAHRGYPARYPENTLVGFRAAVDAGARFVEFDVQLSADGVPVVFHDDTLLRLTGVEGLLHELEDAELDSL------RVA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 310 AGQWFLKTDPfwtasslspsdhrevqNQSICSLAELLELAKGNAS--LLLNLRDPPRDHPyrGsfLNVTLEAVLRSGFPQ 387
Cdd:cd08581  75 EPARFGSRFA----------------GEPLPSLAAVVQWLAQHPQvtLFVEIKTESLDRF--G--LERVVDKVLRALPAV 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 388 HQVMWLFNRQRPLVRKM-APGFQQTSGSKEAIANLRKGHIQKLNLRYTQVSHQELRD-----YASWNLSVnlYTVNAPWL 461
Cdd:cd08581 135 AAQRVLISFDYDLLALAkQQGGPRTGWVLPDWDDASLAEADELQPDYLFCDKNLLPDtgdlwAGTWKWVI--YEVNEPAE 212

                       250
                ....*....|....*.
gi 81884045 462 FSLLWCAGVPSVTSDN 477
Cdd:cd08581 213 ALALAARGVALIETDN 228
GDPD pfam03009
Glycerophosphoryl diester phosphodiesterase family; E. coli has two sequence related isozymes ...
 233-316 3.70e-13

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: 69.35  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045   233 HRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVehlfpelaRRPAAMLNWTVLQRLNAGQ 312
Cdd:pfam03009   1 HRGASGSYPENTLASFRKAAEAGADYIEFDVQLTKDGVPVVLHDFNLDRTTDG--------AGYVRDLTLEELKRLDIGA 72


                  ....
gi 81884045   313 WFLK 316
Cdd:pfam03009  73 GNSG 76
GDPD_EcGlpQ_like cd08600
Glycerophosphodiester phosphodiesterase domain of Escherichia coli (GlpQ) and similar proteins; ...
 231-295 1.15e-10

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: 63.18  E-value: 1.15e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELARR 295
Cdd:cd08600   4 IAHRGASGYLPEHTLEAKALAYAQGADYLEQDVVLTKDDKLVVIHDHYLDNVTNVAEKFPDRKRK 68
GDPD_GDE4_like cd08575
Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester ...
 228-347 2.35e-10

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: 61.46  E-value: 2.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPElarrpaamLNWTVLQR 307
Cdd:cd08575   1 PLHIAHRGGAAEFPENTIAAFRHAVKNGADMLELDVQLTKDGQVVVFHDWDLDRLTGGSGLVSD--------LTYAELPP 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 81884045 308 LNAGqWFLKTDPFWTASSLSPSDhrevqnQSICSLAELLE 347
Cdd:cd08575  73 LDAG-YGYTFDGGKTGYPRGGGD------GRIPTLEEVFK 105
GDPD_TmGDE_like cd08568
Glycerophosphodiester phosphodiesterase domain of Thermotoga maritime and similar proteins; ...
 230-286 7.63e-10

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: 59.23  E-value: 7.63e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81884045 230 LIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVE 286
Cdd:cd08568   2 ILGHRGYRAKYPENTLEAFKKAIEYGADGVELDVWLTKDGKLVVLHDENLKRVGGVD 58
GDPD_ScGlpQ1_like cd08602
Glycerophosphodiester phosphodiesterase domain of Streptomycin coelicolor (GlpQ1) and similar ...
 228-295 1.03e-09

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: 60.00  E-value: 1.03e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNV-EHlfPELARR 295
Cdd:cd08602   1 PLVIAHRGASGYRPEHTLAAYQLAIEQGADFIEPDLVSTKDGVLICRHEPELSGTTDVaDH--PEFADR 67
GDPD_Rv2277c_like cd08580
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c ...
 228-318 8.06e-09

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: 56.95  E-value: 8.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 228 PALIGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHlfpelarrPAAMLNWTVLQR 307
Cdd:cd08580   1 PLIVAHRGGTADAPENTLLAISKALANGADAIWLTVQLSKDGVPVLYRPSDLKSLTNGSG--------AVSAYTAAQLAT 72

                        90
                ....*....|.
gi 81884045 308 LNAGqWFLKTD 318
Cdd:cd08580  73 LNAG-YNFKPE 82
GDPD_pAtGDE_like cd08565
Glycerophosphodiester phosphodiesterase domain of putative Agrobacterium tumefaciens ...
 231-284 1.09e-08

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: 56.26  E-value: 1.09e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTN 284
Cdd:cd08565   2 AGHRGGRNLWPENTLEGFRKALELGVDAVEFDVHLTADGEVVVIHDPTLDRTTH 55
glpQ PRK11143
glycerophosphodiester phosphodiesterase; Provisional
 211-294 9.89e-08

glycerophosphodiester phosphodiesterase; Provisional


Pssm-ID: 236859 [Multi-domain]  Cd Length: 355  Bit Score: 54.29  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045  211 LTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTVMSfrKALEqrlYGLQAD-----ITISLDGVPFLMHDTTLRRTTNV 285
Cdd:PRK11143  10 LAALLAGSAAAAADSAEKIVIAHRGASGYLPEHTLPA--KAMA---YAQGADyleqdLVMTKDDQLVVLHDHYLDRVTDV 84


                 ....*....
gi 81884045  286 EHLFPELAR 294
Cdd:PRK11143  85 AERFPDRAR 93
GDPD_YPL206cp_fungi cd08570
Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and ...
 231-308 1.07e-06

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: 49.91  E-value: 1.07e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELArrpaamlNWTVLQRL 308
Cdd:cd08570   2 IGHRGYKAKYPENTLLAFEKAVEAGADAIETDVHLTKDGVVVISHDPNLKRCFGKDGLIIDDS-------TWDELSHL 72
PI-PLCc_GDPD_SF cd08555
Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases ...
 231-287 1.33e-06

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: 48.97  E-value: 1.33e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTTLRRTTNVEH 287
Cdd:cd08555   2 LSHRGYSQNGQENTLEAFYRALDAGARGLELDVRLTKDGELVVYHGPTLDRTTAGIL 58
GDPD_like_3 cd08585
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial ...
 231-415 1.10e-05

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: 46.93  E-value: 1.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 231 IGHRG---APMLAPEHTVMSFRKALEqRLYGLQADITISLDGVPFLMHDTTLRRTTNVEHLFPELarrPAAMLnwtvlqr 307
Cdd:cd08585   7 IAHRGlhdRDAGIPENSLSAFRAAAE-AGYGIELDVQLTADGEVVVFHDDNLKRLTGVEGRVEEL---TAAEL------- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81884045 308 lnagqwflktdpfwTASSLSPSDHRevqnqsICSLAELLELAKGNASLLLNLRDPPRD------------HPYRGsflnv 375
Cdd:cd08585  76 --------------RALRLLGTDEH------IPTLDEVLELVAGRVPLLIELKSCGGGdgglerrvlaalKDYKG----- 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 81884045 376 tleAVLRSGFPQHQVMWLfnrqrplvRKMAPGFQ--QTSGSK 415
Cdd:cd08585 131 ---PAAIMSFDPRVVRWF--------RKLAPGIPrgQLSEGS 161
GDPD_EcGlpQ_like_1 cd08560
Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic ...
 231-293 5.32e-05

Glycerophosphodiester phosphodiesterase domain similar to Escherichia coli periplasmic phosphodiesterase (GlpQ) include uncharacterized proteins; This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46) and their hypothetical homologs. Members in this subfamily show 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: 176503  Cd Length: 356  Bit Score: 45.88  E-value: 5.32e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81884045 231 IGHRGAPMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDTT-LRRTTNVEhLFPELA 293
Cdd:cd08560  20 IGHRGAPLQFPEHTRESYEAAARMGAGILECDVTFTKDRELVCRHSQCdLHTTTNIL-AIPELA 82
GDPD_GsGDE_like cd08564
Glycerophosphodiester phosphodiesterase domain of putative Galdieria sulphuraria ...
 226-277 6.25e-04

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: 42.07  E-value: 6.25e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 81884045 226 PKPALIGHRGA--PMLAPEHTVMSFRKALEQRLYGLQADITISLDGVPFLMHDT 277
Cdd:cd08564   2 VRPIIVGHRGAgcSTLYPENTLPSFRRALEIGVDGVELDVFLTKDNEIVVFHGT 55
 
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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