NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462558904|ref|XP_054173834|]
View 

CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial isoform X2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
413-572 3.33e-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: 3.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 413 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 492
Cdd:cd09137     1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 493 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 572
Cdd:cd09137    81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
186-333 3.13e-76

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: 240.14  E-value: 3.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 186 HVRVLSSPAEFFELMK--------------------------VDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 239
Cdd:cd09135     1 QIRILRTPSEFYNTLLdkirnakrrivlsslyigtgpleqelVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 240 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 317
Cdd:cd09135    75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154
                         170
                  ....*....|....*.
gi 2462558904 318 DCAEIADFFTELVDAV 333
Cdd:cd09135   155 NCPELADFYHDLIKAV 170
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
413-572 3.33e-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: 3.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 413 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 492
Cdd:cd09137     1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 493 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 572
Cdd:cd09137    81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
186-333 3.13e-76

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: 240.14  E-value: 3.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 186 HVRVLSSPAEFFELMK--------------------------VDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 239
Cdd:cd09135     1 QIRILRTPSEFYNTLLdkirnakrrivlsslyigtgpleqelVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 240 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 317
Cdd:cd09135    75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154
                         170
                  ....*....|....*.
gi 2462558904 318 DCAEIADFFTELVDAV 333
Cdd:cd09135   155 NCPELADFYHDLIKAV 170
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
178-331 3.41e-08

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 56.36  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 178 PEFGVSSSHVRVLSSPAEFFElmkvdCLestLEKSLQAK-----------------------------FPsNLKVSILLD 228
Cdd:PRK09428   18 PKIPQSPDDVETLYSPADFRE-----TL---LEKIASAKkriyivalyleddeagreildalyqakqqNP-ELDIKVLVD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 229 FTRGSRGR---KNSRT---MLLPLLRRFPEqVRVSLFhtphlrGllrllIPERFNETIGLQHIKVYLFDNSVILSGANLS 302
Cdd:PRK09428   89 WHRAQRGLigaAASNTnadWYCEMAQEYPG-VDIPVY------G-----VPVNTREALGVLHLKGFIIDDTVLYSGASLN 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462558904 303 DSYFtNRQDRYVF----LQDCAEIADFFTELVD 331
Cdd:PRK09428  157 NVYL-HQHDKYRYdryhLIRNAELADSMVNFIQ 188
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
181-568 2.05e-07

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: 53.41  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 181 GVSSSHVRVLSSPAEFFELMkVDCLES-------------------TLEKSLQAKFPSNLKVSILLDFTrGSRGRKNSrt 241
Cdd:COG1502    11 LVGGNRVTLLVDGDEAFAAL-LEAIEAarrsidleyyifdddevgrRLADALIAAARRGVKVRVLLDGI-GSRALNRD-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 242 mLLPLLRRfpEQVRVSLFHTPHLRgllrlliPERFNetiGLQHIKVYLFDNSV-ILSGANLSDSYFTN------RQDRYV 314
Cdd:COG1502    87 -FLRRLRA--AGVEVRLFNPVRLL-------FRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfgpWRDTHV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 315 FLQD--CAEIADFFTELVDAVGDVSL---QLQGDDTVQVVdgMVHPYKGDRaeyckAANKRVMDVINSARTRqqmlhaqt 389
Cdd:COG1502   154 RIEGpaVADLQAVFAEDWNFATGEALpfpEPAGDVRVQVV--PSGPDSPRE-----TIERALLAAIASARRR-------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 390 fhsnslltqedaaaagdrrpapdtwIYplIQMkpFEIQIDEIVTETLLTEAERGAKVYLttgyfnLTQAYMDLVL---GT 466
Cdd:COG1502   219 -------------------------IY--IET--PYFVPDRSLLRALIAAARRGVDVRI------LLPAKSDHPLvhwAS 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 467 RAEYQILLAspevngffgakgvAGaipaayVHIerqffsevcslgqqervqlqeYWRRGWTFHAKGLWL--YLAgsslpc 544
Cdd:COG1502   264 RSYYEELLE-------------AG------VRI---------------------YEYEPGFLHAKVMVVddEWA------ 297
                         410       420
                  ....*....|....*....|....
gi 2462558904 545 ltLIGSPNFGYRSVHRDLEAQIAI 568
Cdd:COG1502   298 --LVGSANLDPRSLRLNFEVNLVI 319
 
Name Accession Description Interval E-value
PLDc_PGS1_euk_2 cd09137
Catalytic domain, repeat 2, of eukaryotic phosphatidylglycerophosphate synthases; Catalytic ...
413-572 3.33e-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: 3.33e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 413 TWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVYLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAI 492
Cdd:cd09137     1 TWVYPLLQMGPLNISQEEQVTSRLLQLLPRGSSLTLASGYFNLTPEYLNLLLNSSANLDVLTASPEANGFYGSKGVSGYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 493 PAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTEN 572
Cdd:cd09137    81 PPAYTYIARQFLKRVRKNGKQPRIKLFEYKRPGWTFHAKGLWIYLPGTDLPSLTLIGSSNYGYRSVHRDLEAQFLIVTNN 160
PLDc_PGS1_euk_1 cd09135
Catalytic domain, repeat 1, of eukaryotic PhosphatidylGlycerophosphate Synthases; Catalytic ...
186-333 3.13e-76

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: 240.14  E-value: 3.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 186 HVRVLSSPAEFFELMK--------------------------VDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 239
Cdd:cd09135     1 QIRILRTPSEFYNTLLdkirnakrrivlsslyigtgpleqelVDALQEALERN------PNLKVSILLDYLRGTRGEPNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 240 RT--MLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQ 317
Cdd:cd09135    75 RTasLLLPLLKLFPDRVRVSLYHTPNLRGLLKKLLPERFNEIIGLQHMKLYIFDDDVILSGANLSDDYFTNRQDRYMLIE 154
                         170
                  ....*....|....*.
gi 2462558904 318 DCAEIADFFTELVDAV 333
Cdd:cd09135   155 NCPELADFYHDLIKAV 170
PLDc_CDP-OH_P_transf_II_1 cd09102
Catalytic domain, repeat 1, of CDP-alcohol phosphatidyltransferase class-II family members; ...
186-333 1.71e-67

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: 217.46  E-value: 1.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 186 HVRVLSSPAEFFELMK--------------------------VDCLESTLEKSlqakfpSNLKVSILLDFTRGSRGRKNS 239
Cdd:cd09102     1 HIRFLGSPAEFKTQIIelirnakrrvyvaslywgkdeagqeiLDEIYSVKQEN------PNLDVSVLIDWHRAQRNLLGS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 240 RTMLLPLLRRFPEQVRVSLFHTPHLRGLLRLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTNRQDRYVFLQDC 319
Cdd:cd09102    75 ETKSATNADWYCEQRQTSQLHLLPDDGN*FFGVPINTNEVFGVLHVKGYVFDDTVLLSGANLSNVYFHYRYDRYVKITHG 154
                         170
                  ....*....|....
gi 2462558904 320 AEIADFFTELVDAV 333
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; ...
413-598 2.11e-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: 2.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 413 TWIYPLIQMKPFeIQIDEIVTETLLTEAERgaKVYLTTGYFNLTQAYMDLVLG---TRAEYQILLASPEVNGFFGAK--- 486
Cdd:cd09103     1 LSITPLVGLGKR-GNILNRTIEQLITSAES--KIILCTPYFNLPQALMRDILRllkRGVKVEIIVGDKTANDFYIPPeep 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 487 -GVAGAIPAAYVHIERQFFSEVCSLGQQERVQLQEYWRRGWTFHAKGLWLYLagsslpCLTLIGSPNFGYRSVHRDLEAQ 565
Cdd:cd09103    78 fKVIGALPYLYEINLRRFAKRLQKYIDQGQLNVRLWKDGDNSFHLKGIWVDD------RYTLLTGNNLNPRAWRLDLENG 151
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462558904 566 IAIVTENQALQQQLHQEQEQLYLRSGVVSSATF 598
Cdd:cd09103   152 LLIHDPQKQLQQQLEKELEQILLHTTRISHYTQ 184
PLDc_PSS_G_neg_1 cd09134
Catalytic domain, repeat 1, of phosphatidylserine synthases from gram-negative bacteria; ...
178-331 4.82e-13

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: 67.66  E-value: 4.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 178 PEFGVSSSHVRVLSSPAEFFE-------------------LMKVDCLESTLEKSLQAK--FPsNLKVSILLDFTRGSRGR 236
Cdd:cd09134     2 PKIPQQPEDIDVLYSPKDFRArllelisnakkriyivalyLEDDEAGREILDALYEAKanNP-GLDIKVLVDWHRAQRGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 237 ---KNSRT---MLLPLLRRFPEQVRVslfhtphlrgllrLLIPERFNETIGLQHIKVYLFDNSVILSGANLSDSYFTN-- 308
Cdd:cd09134    81 igaKKSLGnadWYRKIAQRYGHDVPI-------------YGVPVKTRELFGVLHLKGFIIDDTVLYSGASLNNVYLHQfd 147
                         170       180
                  ....*....|....*....|....*
gi 2462558904 309 --RQDRYVFLQDcAEIADFFTELVD 331
Cdd:cd09134   148 kyRYDRYHLIYN-PELADSMVNFIQ 171
pssA PRK09428
CDP-diacylglycerol--serine O-phosphatidyltransferase;
178-331 3.41e-08

CDP-diacylglycerol--serine O-phosphatidyltransferase;


Pssm-ID: 236510 [Multi-domain]  Cd Length: 451  Bit Score: 56.36  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 178 PEFGVSSSHVRVLSSPAEFFElmkvdCLestLEKSLQAK-----------------------------FPsNLKVSILLD 228
Cdd:PRK09428   18 PKIPQSPDDVETLYSPADFRE-----TL---LEKIASAKkriyivalyleddeagreildalyqakqqNP-ELDIKVLVD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 229 FTRGSRGR---KNSRT---MLLPLLRRFPEqVRVSLFhtphlrGllrllIPERFNETIGLQHIKVYLFDNSVILSGANLS 302
Cdd:PRK09428   89 WHRAQRGLigaAASNTnadWYCEMAQEYPG-VDIPVY------G-----VPVNTREALGVLHLKGFIIDDTVLYSGASLN 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462558904 303 DSYFtNRQDRYVF----LQDCAEIADFFTELVD 331
Cdd:PRK09428  157 NVYL-HQHDKYRYdryhLIRNAELADSMVNFIQ 188
Cls COG1502
Phosphatidylserine/phosphatidylglycerophosphate/cardiolipin synthase [Lipid transport and ...
181-568 2.05e-07

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: 53.41  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 181 GVSSSHVRVLSSPAEFFELMkVDCLES-------------------TLEKSLQAKFPSNLKVSILLDFTrGSRGRKNSrt 241
Cdd:COG1502    11 LVGGNRVTLLVDGDEAFAAL-LEAIEAarrsidleyyifdddevgrRLADALIAAARRGVKVRVLLDGI-GSRALNRD-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 242 mLLPLLRRfpEQVRVSLFHTPHLRgllrlliPERFNetiGLQHIKVYLFDNSV-ILSGANLSDSYFTN------RQDRYV 314
Cdd:COG1502    87 -FLRRLRA--AGVEVRLFNPVRLL-------FRRLN---GRNHRKIVVIDGRVaFVGGANITDEYLGRdpgfgpWRDTHV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 315 FLQD--CAEIADFFTELVDAVGDVSL---QLQGDDTVQVVdgMVHPYKGDRaeyckAANKRVMDVINSARTRqqmlhaqt 389
Cdd:COG1502   154 RIEGpaVADLQAVFAEDWNFATGEALpfpEPAGDVRVQVV--PSGPDSPRE-----TIERALLAAIASARRR-------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 390 fhsnslltqedaaaagdrrpapdtwIYplIQMkpFEIQIDEIVTETLLTEAERGAKVYLttgyfnLTQAYMDLVL---GT 466
Cdd:COG1502   219 -------------------------IY--IET--PYFVPDRSLLRALIAAARRGVDVRI------LLPAKSDHPLvhwAS 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 467 RAEYQILLAspevngffgakgvAGaipaayVHIerqffsevcslgqqervqlqeYWRRGWTFHAKGLWL--YLAgsslpc 544
Cdd:COG1502   264 RSYYEELLE-------------AG------VRI---------------------YEYEPGFLHAKVMVVddEWA------ 297
                         410       420
                  ....*....|....*....|....
gi 2462558904 545 ltLIGSPNFGYRSVHRDLEAQIAI 568
Cdd:COG1502   298 --LVGSANLDPRSLRLNFEVNLVI 319
PLDc_SF cd00138
Catalytic domain of phospholipase D superfamily proteins; Catalytic domain of phospholipase D ...
207-314 3.41e-04

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: 40.58  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558904 207 STLEKSLQAKFPSNLKVSILLDftRGSRGRKNSRTMLLPLLRRFPEQVRVSLFHTPHLRGLlrlliperfnetiglqHIK 286
Cdd:cd00138    27 DRLLKALLAAAERGVDVRLIID--KPPNAAGSLSAALLEALLRAGVNVRSYVTPPHFFERL----------------HAK 88
                          90       100
                  ....*....|....*....|....*....
gi 2462558904 287 VYLFDNS-VILSGANLSDSYFTNRQDRYV 314
Cdd:cd00138    89 VVVIDGEvAYVGSANLSTASAAQNREAGV 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH