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Conserved domains on  [gi|767996527|ref|XP_011523789|]
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CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase( domain architecture ID 10173612)

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase catalyzes the committed step in the biosynthesis of acidic phospholipids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 186-359 7.00e-101

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


:

Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 304.86  E-value: 7.00e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 186 HVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 265
Cdd:cd09135    1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 266 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 343
Cdd:cd09135   75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154

                        170
                 ....*....|....*.
gi 767996527 344 DCAEIADFFTELVDAV 359
Cdd:cd09135  155 NCPELADFYHDLIKAV 170
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 439-598 6.38e-91

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


:

Pssm-ID: 197235  Cd Length: 186  Bit Score: 279.46  E-value: 6.38e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 439 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 518
Cdd:cd09137    1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 519 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 598
Cdd:cd09137   81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 186-359 7.00e-101

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 304.86  E-value: 7.00e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 186 HVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 265
Cdd:cd09135    1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 266 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 343
Cdd:cd09135   75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154

                        170
                 ....*....|....*.
gi 767996527 344 DCAEIADFFTELVDAV 359
Cdd:cd09135  155 NCPELADFYHDLIKAV 170
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 439-598 6.38e-91

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197235  Cd Length: 186  Bit Score: 279.46  E-value: 6.38e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 439 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 518
Cdd:cd09137    1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 519 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 598
Cdd:cd09137   81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
178-357 2.63e-15

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 78.70  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 178 PEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLestleksLQAK--FPsNLKVSILLDF 255
Cdd:PRK09428  18 PKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDAL-------YQAKqqNP-ELDIKVLVDW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 256 TRGSRGR---KNSRT---MLLPLLRRFPEqVRVSLFhtphlrGllrllIPERFNETIGLQHIKVYLFDNSVILSGANLSD 329
Cdd:PRK09428  90 HRAQRGLigaAASNTnadWYCEMAQEYPG-VDIPVY------G-----VPVNTREALGVLHLKGFIIDDTVLYSGASLNN 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767996527 330 SYFtNRQDRYVF----LQDCAEIADFFTELVD 357
Cdd:PRK09428 158 VYL-HQHDKYRYdryhLIRNAELADSMVNFIQ 188
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 181-594 3.30e-14

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 74.59  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 181 GVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLEstlekslqAKFPSNLKVSILLDFTrGSR 260
Cdd:COG1502   11 LVGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALI--------AAARRGVKVRVLLDGI-GSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 261 GRKNSrtmLLPLLRRfpEQVRVSLFHTPHLRgllrlliPERFNetiGLQHIKVYLFDNSV-ILSGANLSDSYFTN----- 334
Cdd:COG1502   82 ALNRD---FLRRLRA--AGVEVRLFNPVRLL-------FRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfg 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 335 -RQDRYVFLQD--CAEIADFFTELVDAVGDVSL---QLQGDDTVQVVdgMVHPYKGDRaeyckAANKRVMDVINSARTRq 408
Cdd:COG1502  147 pWRDTHVRIEGpaVADLQAVFAEDWNFATGEALpfpEPAGDVRVQVV--PSGPDSPRE-----TIERALLAAIASARRR- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 409 qmlhaqtfhsnslltqedaaaagdrrpapdtwIYplIQMkpFEIQIDEIVTETLLTEAERGAKVYLttgyfnLTQAYMDL 488
Cdd:COG1502  219 --------------------------------IY--IET--PYFVPDRSLLRALIAAARRGVDVRI------LLPAKSDH 256

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 489 VL---GTRAEYQILLAspevngffgakgvAGaipaayVHIerqffsevcslgqqervqlqeYWRRGWTFHAKGLWL--YL 563
Cdd:COG1502  257 PLvhwASRSYYEELLE-------------AG------VRI---------------------YEYEPGFLHAKVMVVddEW 296

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767996527 564 AgsslpcltLIGSPNFGYRSVHRDLEAQIAI 594
Cdd:COG1502  297 A--------LVGSANLDPRSLRLNFEVNLVI 319
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
 186-359 7.00e-101

Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic domain, repeat 1, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197233 [Multi-domain]  Cd Length: 170  Bit Score: 304.86  E-value: 7.00e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 186 HVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 265
Cdd:cd09135    1 QIRILRTPSEFYNTLLDKIRNAKRRIVLSSLYIGTGPLEQELVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 266 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 343
Cdd:cd09135   75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154

                        170
                 ....*....|....*.
gi 767996527 344 DCAEIADFFTELVDAV 359
Cdd:cd09135  155 NCPELADFYHDLIKAV 170
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
 439-598 6.38e-91

Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate (PGP) synthases, also called CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5). Eukaryotic PGP synthases are different and unrelated to prokaryotic PGP synthases and yeast phosphatidylserine synthase. They catalyze the synthesis of PGP from CDP-diacylglycerol and sn-glycerol 3-phosphate, the committed and rate-limiting step in the biosynthesis of cardiolipin (CL), which is an essential component of many mitochondrial functions in eukaryotes. Members in this subfamily all have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism involving a substrate-enzyme intermediate to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involved in the phosphatidyl group transfer.


Pssm-ID: 197235  Cd Length: 186  Bit Score: 279.46  E-value: 6.38e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 439 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 518
Cdd:cd09137    1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 519 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 598
Cdd:cd09137   81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
PLDc_CDP-OH_P_transf_II_1 cd09102
Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 186-359 4.81e-90

Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197201 [Multi-domain]  Cd Length: 168  Bit Score: 276.78  E-value: 4.81e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 186 HVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 265
Cdd:cd09102    1 HIRFLGSPAEFKTQIIELIRNAKRRVYVASLYWGKDEAGQEILDEIYSVKQEN------PNLDVSVLIDWHRAQRNLLGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 266 RTMLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQDC 345
Cdd:cd09102   75 ETKSATNADWYCEQRQTSQLHLLPDDGN*FFGVPINTNEVFGVLHVKGYVFDDTVLLSGANLSNVYFHYRYDRYVKITHG 154

                        170
                 ....*....|....
gi 767996527 346 AEIADFFTELVDAV 359
Cdd:cd09102  155 AELADS*VNLINAY 168
PLDc_CDP-OH_P_transf_II_2 cd09103
Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; ...
 439-624 2.88e-53

Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members; Catalytic domain, repeat 2, of CDP-alcohol phosphatidyltransferase class-II family members, which mainly include gram-negative bacterial phosphatidylserine synthases (PSS; CDP-diacylglycerol--serine O-phosphatidyltransferase, EC 2.7.8.8), yeast phosphatidylglycerophosphate synthase (PGP synthase; CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, EC 2.7.8.5), and metazoan PGP synthase 1. All members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterize the phospholipase D (PLD) superfamily. They may utilize a common two-step ping-pong catalytic mechanism, involving a substrate-enzyme intermediate, to cleave phosphodiester bonds. The two motifs are suggested to constitute the active site involving phosphatidyl group transfer. Phosphatidylserine synthases from gram-positive bacteria and eukaryotes, and prokaryotic phosphatidylglycerophosphate synthases are not members of this subfamily.


Pssm-ID: 197202 [Multi-domain]  Cd Length: 184  Bit Score: 180.50  E-value: 2.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 439 TWIYPLIQMKPFeIQIDEIVTETLLTEAERgaKVYLTTGYFNLTQAYMDLVLG---TRAEYQILLASPEVNGFFGAK--- 512
Cdd:cd09103    1 LSITPLVGLGKR-GNILNRTIEQLITSAES--KIILCTPYFNLPQALMRDILRllkRGVKVEIIVGDKTANDFYIPPeep 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 513 -GVAGAIPAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLagsslpCLTLIGSPNFGYRSVHRDLEAQ 591
Cdd:cd09103   78 fKVIGALPYLYEINLRRFAKRLQKYIDQGQLNVRLWKDGDNSFHLKGIWVDD------RYTLLTGNNLNPRAWRLDLENG 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767996527 592 IAIVTENQALQQQLHQEQEQLYLRSGVVSSATF 624
Cdd:cd09103  152 LLIHDPQKQLQQQLEKELEQILLHTTRISHYTQ 184
PLDc_PSS_G_neg_1 cd09134
Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; ...
 178-357 1.87e-21

Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; Catalytic domain, repeat 1, of phosphatidylserine synthases (PSSs) from gram-negative bacteria. There are two subclasses of PSS enzymes in bacteria: subclass I of gram-negative bacteria and subclass II of gram-positive bacteria. It is common that PSSs in gram-positive bacteria and yeast are tight membrane-associated enzymes. By contrast, the gram-negative bacterial PSSs, such as Escherichia coli PSS, are commonly bound to the ribosomes. They are peripheral membrane proteins that can interact with the surface of the inner membrane by binding to the lipid substrate (CDP-diacylglycerol) and the lipid product (phosphatidylserine). The prototypical member of this subfamily is Escherichia coli PSS (also called CDP-diacylglycerol-L-serine O-phosphatidyltransferase, EC 2.7.8.8), which catalyzes the exchange reactions between CMP and CDP-diacylglycerol, and between serine and phosphatidylserine. The phosphatidylserine is then decarboxylated by phosphatidylserine decarboxylase to yield phosphatidylethanolamine, the major phospholipid in Escherichia coli. It also catalyzes the hydrolysis of CDP-diacylglycerol to form phosphatidic acid with the release of CMP. PSS may utilize a ping-pong mechanism involving a phosphatidyl-enzyme intermediate, which is distinct from those of gram-positive bacterial phosphatidylserine synthases. Moreover, all members in this subfamily have two HKD motifs (H-x-K-x(4)-D, where x represents any amino acid residue) that characterizes the phospholipase D (PLD) superfamily. The two motifs constitute an active site for the formation of a covalent substrate-enzyme intermediate.


Pssm-ID: 197232 [Multi-domain]  Cd Length: 173  Bit Score: 91.93  E-value: 1.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 178 PEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLestleksLQAK--FPsNLKVSILLDF 255
Cdd:cd09134    2 PKIPQQPEDIDVLYSPKDFRARLLELISNAKKRIYIVALYLEDDEAGREILDAL-------YEAKanNP-GLDIKVLVDW 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 256 TRGSRGR---KNSRT---MLLPLLRRFPEQVRVslfhtphlrgllrLLIPERFNETIGLQHIKVYLFDNSVILSGANLSD 329
Cdd:cd09134   74 HRAQRGLigaKKSLGnadWYRKIAQRYGHDVPI-------------YGVPVKTRELFGVLHLKGFIIDDTVLYSGASLNN 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767996527 330 SYFTN----RQDRYVFLQDcAEIADFFTELVD 357
Cdd:cd09134  141 VYLHQfdkyRYDRYHLIYN-PELADSMVNFIQ 171
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
178-357 2.63e-15

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 78.70  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 178 PEFGVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLestleksLQAK--FPsNLKVSILLDF 255
Cdd:PRK09428  18 PKIPQSPDDVETLYSPADFRETLLEKIASAKKRIYIVALYLEDDEAGREILDAL-------YQAKqqNP-ELDIKVLVDW 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 256 TRGSRGR---KNSRT---MLLPLLRRFPEqVRVSLFhtphlrGllrllIPERFNETIGLQHIKVYLFDNSVILSGANLSD 329
Cdd:PRK09428  90 HRAQRGLigaAASNTnadWYCEMAQEYPG-VDIPVY------G-----VPVNTREALGVLHLKGFIIDDTVLYSGASLNN 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767996527 330 SYFtNRQDRYVF----LQDCAEIADFFTELVD 357
Cdd:PRK09428 158 VYL-HQHDKYRYdryhLIRNAELADSMVNFIQ 188
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
 181-594 3.30e-14

Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and metabolism]; Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 441111 [Multi-domain]  Cd Length: 367  Bit Score: 74.59  E-value: 3.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 181 GVSSSHVRVLSSPAEFFELMKGQIRVAKRRVVMASLYLGTGPLEQELVDCLEstlekslqAKFPSNLKVSILLDFTrGSR 260
Cdd:COG1502   11 LVGGNRVTLLVDGDEAFAALLEAIEAARRSIDLEYYIFDDDEVGRRLADALI--------AAARRGVKVRVLLDGI-GSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 261 GRKNSrtmLLPLLRRfpEQVRVSLFHTPHLRgllrlliPERFNetiGLQHIKVYLFDNSV-ILSGANLSDSYFTN----- 334
Cdd:COG1502   82 ALNRD---FLRRLRA--AGVEVRLFNPVRLL-------FRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfg 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 335 -RQDRYVFLQD--CAEIADFFTELVDAVGDVSL---QLQGDDTVQVVdgMVHPYKGDRaeyckAANKRVMDVINSARTRq 408
Cdd:COG1502  147 pWRDTHVRIEGpaVADLQAVFAEDWNFATGEALpfpEPAGDVRVQVV--PSGPDSPRE-----TIERALLAAIASARRR- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 409 qmlhaqtfhsnslltqedaaaagdrrpapdtwIYplIQMkpFEIQIDEIVTETLLTEAERGAKVYLttgyfnLTQAYMDL 488
Cdd:COG1502  219 --------------------------------IY--IET--PYFVPDRSLLRALIAAARRGVDVRI------LLPAKSDH 256

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 489 VL---GTRAEYQILLAspevngffgakgvAGaipaayVHIerqffsevcslgqqervqlqeYWRRGWTFHAKGLWL--YL 563
Cdd:COG1502  257 PLvhwASRSYYEELLE-------------AG------VRI---------------------YEYEPGFLHAKVMVVddEW 296

                        410       420       430
                 ....*....|....*....|....*....|.
gi 767996527 564 AgsslpcltLIGSPNFGYRSVHRDLEAQIAI 594
Cdd:COG1502  297 A--------LVGSANLDPRSLRLNFEVNLVI 319
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
 204-340 5.53e-06

Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D (PLD) superfamily proteins. The PLD superfamily is composed of a large and diverse group of proteins including plant, mammalian and bacterial PLDs, bacterial cardiolipin (CL) synthases, bacterial phosphatidylserine synthases (PSS), eukaryotic phosphatidylglycerophosphate (PGP) synthase, eukaryotic tyrosyl-DNA phosphodiesterase 1 (Tdp1), and some bacterial endonucleases (Nuc and BfiI), among others. PLD enzymes hydrolyze phospholipid phosphodiester bonds to yield phosphatidic acid and a free polar head group. They can also catalyze the transphosphatidylation of phospholipids to acceptor alcohols. The majority of members in this superfamily contain a short conserved sequence motif (H-x-K-x(4)-D, where x represents any amino acid residue), called the HKD signature motif. There are varying expanded forms of this motif in different family members. Some members contain variant HKD motifs. Most PLD enzymes are monomeric proteins with two HKD motif-containing domains. Two HKD motifs from two domains form a single active site. Some PLD enzymes have only one copy of the HKD motif per subunit but form a functionally active dimer, which has a single active site at the dimer interface containing the two HKD motifs from both subunits. Different PLD enzymes may have evolved through domain fusion of a common catalytic core with separate substrate recognition domains. Despite their various catalytic functions and a very broad range of substrate specificities, the diverse group of PLD enzymes can bind to a phosphodiester moiety. Most of them are active as bi-lobed monomers or dimers, and may possess similar core structures for catalytic activity. They are generally thought to utilize a common two-step ping-pong catalytic mechanism, involving an enzyme-substrate intermediate, to cleave phosphodiester bonds. The two histidine residues from the two HKD motifs play key roles in the catalysis. Upon substrate binding, a histidine from one HKD motif could function as the nucleophile, attacking the phosphodiester bond to create a covalent phosphohistidine intermediate, while the other histidine residue from the second HKD motif could serve as a general acid, stabilizing the leaving group.


Pssm-ID: 197200 [Multi-domain]  Cd Length: 119  Bit Score: 45.97  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996527 204 IRVAKRRVVMASLYLGTGpleqelvdcLESTLEKSLQAKFPSNLKVSILLDftRGSRGRKNSRTMLLPLLRRFPEQVRVS 283
Cdd:cd00138    7 LKNAKESIFIATPNFSFN---------SADRLLKALLAAAERGVDVRLIID--KPPNAAGSLSAALLEALLRAGVNVRSY 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996527 284 LFHTPHLRGLlrlliperfnetiglqHIKVYLFDNS-VILSGANLSDSYFTNRQDRYV 340
Cdd:cd00138   76 VTPPHFFERL----------------HAKVVVIDGEvAYVGSANLSTASAAQNREAGV 117
 
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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