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Conserved domains on  [gi|90111459|ref|NP_417055|]
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phosphatidylglycerophosphatase C [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

phosphatidylglycerolphosphatase C family protein( domain architecture ID 10019288)

phosphatidylglycerolphosphatase C family protein similar to Escherichia coli phosphatidylglycerophosphatase C, which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YfhB_g-proteo TIGR01545
haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade ...
 2-211 1.22e-142

haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.


:

Pssm-ID: 130608  Cd Length: 210  Bit Score: 396.23  E-value: 1.22e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     2 ATHERRVVFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPLLPIIAIALLIKGRAARWPMSLLLWGCTFGHSEARLQT 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    82 LQADFVRWFRDNVTAFPLVQERLTTYLLSSDADIWLITGSPQPLVEAVYFDTPWLPRVNLIASQIQRGYGGWVLTMRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111459   162 HEKVAQLERKIGTPLRLYSGYSDSNQDNPLLYFCQHRWRVTPRGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
 
Name Accession Description Interval E-value
YfhB_g-proteo TIGR01545
haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade ...
 2-211 1.22e-142

haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.


Pssm-ID: 130608  Cd Length: 210  Bit Score: 396.23  E-value: 1.22e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     2 ATHERRVVFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPLLPIIAIALLIKGRAARWPMSLLLWGCTFGHSEARLQT 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    82 LQADFVRWFRDNVTAFPLVQERLTTYLLSSDADIWLITGSPQPLVEAVYFDTPWLPRVNLIASQIQRGYGGWVLTMRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111459   162 HEKVAQLERKIGTPLRLYSGYSDSNQDNPLLYFCQHRWRVTPRGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-204 2.99e-43

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 143.60  E-value: 2.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459   9 VFFDLDGTLHQQDMFGSFLRYLLRRQplNALLVLPLLPIIAIALLIKGRAARWPMSLLLWGCTFGHSEaRLQTLQADFVR 88
Cdd:cd02612   2 AFFDLDGTLIAGDSFFAFLRFKGIAE--RRAPLEELLLLRLMALYALGRLDGAGMEALLGFATAGLAG-ELAALVEEFVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459  89 WFRDNVtAFPLVQERLTTYLLSSDaDIWLITGSPQPLVEAVyFDTPWLPrvNLIASQIQ--RGYGGWVLTMR-CLGHEKV 165
Cdd:cd02612  79 EYILRV-LYPEARELIAWHKAAGH-DVVLISASPEELVAPI-ARKLGID--NVLGTQLEteDGRYTGRIIGPpCYGEGKV 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 90111459 166 AQLERKI---GTPLRLYSGYSDSNQDNPLLYFCQHRWRVTPR 204
Cdd:cd02612 154 KRLREWLaeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
9-192 4.84e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 56.77  E-value: 4.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     9 VFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPLLPIIAIALLIkGRAARWPMSLLLWGCTFGHSEArlqtLQADFVR 88
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLL-GRLSRAGARELLRALLAGLPEE----DAAELER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    89 WFRDNVTA--FPLVQERLtTYLLSSDADIWLITGSPQPLVEavyfdtPWLPRV---NLIASQIQRGY----GGWVLTMR- 158
Cdd:pfam12710  76 FVAEVALPrlHPGALELL-AAHRAAGDRVVVVTGGLRPLVE------PVLAELgfdEVLATELEVDDgrftGELRLIGPp 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 90111459   159 CLGHEKVAQLERKIG------TPLRLYsGYSDSNQDNPLL 192
Cdd:pfam12710 149 CAGEGKVRRLRAWLAarglglDLADSV-AYGDSPSDLPML 187
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-192 5.35e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 45.60  E-value: 5.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459   5 ERRVVFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPllpiIAIALLIKGRAARWPMSLLLwgctfghsEARLQTL-- 82
Cdd:COG0560   2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLE----EVAAITERAMAGELDFEESL--------RFRVALLag 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459  83 --QADFVRWFRDNVTAFPLVQ---ERLTTYLLSSDADIWLITGSP----QPLVEAVYFDtpwlprvNLIASQ--IQRG-Y 150
Cdd:COG0560  70 lpEEELEELAERLFEEVPRLYpgaRELIAEHRAAGHKVAIVSGGFtffvEPIAERLGID-------HVIANEleVEDGrL 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 90111459 151 GGWVLTMRCLGHEKVAQLER---KIGTPLRLYSGYSDSNQDNPLL 192
Cdd:COG0560 143 TGEVVGPIVDGEGKAEALRElaaELGIDLEQSYAYGDSANDLPML 187
 
Name Accession Description Interval E-value
YfhB_g-proteo TIGR01545
haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade ...
 2-211 1.22e-142

haloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB; This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.


Pssm-ID: 130608  Cd Length: 210  Bit Score: 396.23  E-value: 1.22e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     2 ATHERRVVFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPLLPIIAIALLIKGRAARWPMSLLLWGCTFGHSEARLQT 81
Cdd:TIGR01545   1 AAGAKRIIFFDLDGTLHQQDMFGSFLRFLLRHLPLNALLVIPLLPIIAIALLIGGRAARWPMSLLLWACTFGHREAHLQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    82 LQADFVRWFRDNVTAFPLVQERLTTYLLSSDADIWLITGSPQPLVEAVYFDTPWLPRVNLIASQIQRGYGGWVLTMRCLG 161
Cdd:TIGR01545  81 LEADFVAAFRDKVTAFPLVAERLRQYLESSDADIWLITGSPQPLVEAVYFDSNFIHRLNLIASQIERGNGGWVLPLRCLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 90111459   162 HEKVAQLERKIGTPLRLYSGYSDSNQDNPLLYFCQHRWRVTPRGELQQLE 211
Cdd:TIGR01545 161 HEKVAQLEQKIGSPLKLYSGYSDSKQDNPLLAFCEHRWRVSKRGELQQLE 210
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 9-204 2.99e-43

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 143.60  E-value: 2.99e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459   9 VFFDLDGTLHQQDMFGSFLRYLLRRQplNALLVLPLLPIIAIALLIKGRAARWPMSLLLWGCTFGHSEaRLQTLQADFVR 88
Cdd:cd02612   2 AFFDLDGTLIAGDSFFAFLRFKGIAE--RRAPLEELLLLRLMALYALGRLDGAGMEALLGFATAGLAG-ELAALVEEFVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459  89 WFRDNVtAFPLVQERLTTYLLSSDaDIWLITGSPQPLVEAVyFDTPWLPrvNLIASQIQ--RGYGGWVLTMR-CLGHEKV 165
Cdd:cd02612  79 EYILRV-LYPEARELIAWHKAAGH-DVVLISASPEELVAPI-ARKLGID--NVLGTQLEteDGRYTGRIIGPpCYGEGKV 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 90111459 166 AQLERKI---GTPLRLYSGYSDSNQDNPLLYFCQHRWRVTPR 204
Cdd:cd02612 154 KRLREWLaeeGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
9-192 4.84e-10

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 56.77  E-value: 4.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     9 VFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPLLPIIAIALLIkGRAARWPMSLLLWGCTFGHSEArlqtLQADFVR 88
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLL-GRLSRAGARELLRALLAGLPEE----DAAELER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    89 WFRDNVTA--FPLVQERLtTYLLSSDADIWLITGSPQPLVEavyfdtPWLPRV---NLIASQIQRGY----GGWVLTMR- 158
Cdd:pfam12710  76 FVAEVALPrlHPGALELL-AAHRAAGDRVVVVTGGLRPLVE------PVLAELgfdEVLATELEVDDgrftGELRLIGPp 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 90111459   159 CLGHEKVAQLERKIG------TPLRLYsGYSDSNQDNPLL 192
Cdd:pfam12710 149 CAGEGKVRRLRAWLAarglglDLADSV-AYGDSPSDLPML 187
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 9-207 1.38e-08

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 52.73  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459     9 VFFDLDGTLHQQDMFGSFLRYLLRRQplnallvlpllpiiaiallIKGRAARWPMSLLLWGCTFGH-----SEARLQTLQ 83
Cdd:TIGR01490   2 AFFDFDGTLTAKDTLFIFLKFLASKN-------------------ILFEELRLPKVLARFEFFLNRgldymAYYRAFALD 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459    84 ADF------VRWFRDnVTAFPLVQERLTTY-------LLSSDADIWLITGSPQPLVEAVY----FDtpwlprvNLIASQ- 145
Cdd:TIGR01490  63 ALAglleedVRAIVE-EFVNQKIESILYPEardlirwHKAEGHTIVLVSASLTILVKPLArilgID-------NAIGTRl 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111459   146 --IQRG-YGGWVLTMRCLGHEKVAQLERKIGT---PLRLYSGYSDSNQDNPLLYFCQHRWRVTPRGEL 207
Cdd:TIGR01490 135 eeSEDGiYTGNIDGNNCKGEGKVHALAELLAEeqiDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-192 5.35e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 45.60  E-value: 5.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459   5 ERRVVFFDLDGTLHQQDMFGSFLRYLLRRQPLNALLVLPllpiIAIALLIKGRAARWPMSLLLwgctfghsEARLQTL-- 82
Cdd:COG0560   2 KMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLE----EVAAITERAMAGELDFEESL--------RFRVALLag 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111459  83 --QADFVRWFRDNVTAFPLVQ---ERLTTYLLSSDADIWLITGSP----QPLVEAVYFDtpwlprvNLIASQ--IQRG-Y 150
Cdd:COG0560  70 lpEEELEELAERLFEEVPRLYpgaRELIAEHRAAGHKVAIVSGGFtffvEPIAERLGID-------HVIANEleVEDGrL 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 90111459 151 GGWVLTMRCLGHEKVAQLER---KIGTPLRLYSGYSDSNQDNPLL 192
Cdd:COG0560 143 TGEVVGPIVDGEGKAEALRElaaELGIDLEQSYAYGDSANDLPML 187
 
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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