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HAD-superfamily hydrolase, subfamily IB (PSPase-like) [Ignisphaera aggregans DSM 17230]

Protein Classification

HAD family hydrolase( domain architecture ID 10001729)

haloacid dehalogenase (HAD) family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-183 3.89e-29

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: 108.39  E-value: 3.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   1 MFIVAFDIDGTLTPIkSSWSYVHKVL---------NTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFNKILSS 71
Cdd:COG0560    3 MRLAVFDLDGTLIAG-ESIDELARFLgrrglvdrrEVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  72 IP------WRSGIESIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGK-AKFYPEYNDKGR 144
Cdd:COG0560   82 LFeevprlYPGARELIAEHR---AAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEvVGPIVDGEGKAE 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 304378358 145 LLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISISFC 183
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN 197
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-183 3.89e-29

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: 108.39  E-value: 3.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   1 MFIVAFDIDGTLTPIkSSWSYVHKVL---------NTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFNKILSS 71
Cdd:COG0560    3 MRLAVFDLDGTLIAG-ESIDELARFLgrrglvdrrEVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  72 IP------WRSGIESIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGK-AKFYPEYNDKGR 144
Cdd:COG0560   82 LFeevprlYPGARELIAEHR---AAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEvVGPIVDGEGKAE 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 304378358 145 LLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISISFC 183
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN 197
HAD-SF-IB-PSPlk TIGR01491
HAD-superfamily, subfamily-IB PSPase-like hydrolase, archaeal; This hypothetical equivalog is ...
 1-182 1.38e-27

HAD-superfamily, subfamily-IB PSPase-like hydrolase, archaeal; 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 from archaeal species. The phylogenetically closest group of sequences to these are phosphoserine phosphatases (TIGR00338). There are no known archaeal phosphoserine phosphatases, and no archaea fall within TIGR00338. It is likely, then, that this model represents the archaeal branch of the PSPase equivalog.


Pssm-ID: 273655 [Multi-domain]  Cd Length: 201  Bit Score: 103.81  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    1 MFIVAFDIDGTLTPIKSSWSYVHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSL----DTFNKILSSIPWRS 76
Cdd:TIGR01491   4 IKLIIFDLDGTLTDVMSSWEYLHRRLETCGLAKKNAELFFSGRISYEEWARLDASLWKRRSGrlrrEEVEEIFKEISLRD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   77 G-IESIRKLKNKYANNVLfiaVSGGFAQLGKRAVEELGFDAYIGVEIDYESN-RLNGKAKFYPEYNDKGRLLEEFLRQKH 154
Cdd:TIGR01491  84 YaEELVRWLKEKGLKTAI---VSGGIMCLAKKVAEKLNPDYVYSNELVFDEKgFIQPDGIVRVTFDNKGEAVERLKRELN 160

                         170       180
                  ....*....|....*....|....*...
gi 304378358  155 INVEKTICVGDNINDIGLFRYCDISISF 182
Cdd:TIGR01491 161 PSLTETVAVGDSKNDLPMFEVADISISL 188
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 41-183 1.99e-13

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 65.65  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  41 EGFISYDEWIVHDLSLWKGLSLDTFNKILSSIPWRSGIES-IRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIG 119
Cdd:cd07500   38 RGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEElIQTLK---AKGYKTAVVSGGFTYFTDRLAEELGLDYAFA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304378358 120 VEIDYESNRLNGKAKFYP-EYNDKGRLLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISISFC 183
Cdd:cd07500  115 NELEIKDGKLTGKVLGPIvDAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIAFH 179
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-174 1.31e-09

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 55.62  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    4 VAFDIDGTLTPIKSSWSY--------VHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFN----KILSS 71
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLirallrrgGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAelerFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   72 IPWRSGIESIRKLKNKYANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGKAKFYPEYN---DKGRLLEE 148
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGPPCageGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*...
gi 304378358  149 FL--RQKHINVEKTICVGDNINDIGLFR 174
Cdd:pfam12710 161 WLaaRGLGLDLADSVAYGDSPSDLPMLR 188
 
Name Accession Description Interval E-value
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-183 3.89e-29

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: 108.39  E-value: 3.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   1 MFIVAFDIDGTLTPIkSSWSYVHKVL---------NTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFNKILSS 71
Cdd:COG0560    3 MRLAVFDLDGTLIAG-ESIDELARFLgrrglvdrrEVLEEVAAITERAMAGELDFEESLRFRVALLAGLPEEELEELAER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  72 IP------WRSGIESIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGK-AKFYPEYNDKGR 144
Cdd:COG0560   82 LFeevprlYPGARELIAEHR---AAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDGRLTGEvVGPIVDGEGKAE 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 304378358 145 LLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISISFC 183
Cdd:COG0560  159 ALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN 197
HAD-SF-IB-PSPlk TIGR01491
HAD-superfamily, subfamily-IB PSPase-like hydrolase, archaeal; This hypothetical equivalog is ...
 1-182 1.38e-27

HAD-superfamily, subfamily-IB PSPase-like hydrolase, archaeal; 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 from archaeal species. The phylogenetically closest group of sequences to these are phosphoserine phosphatases (TIGR00338). There are no known archaeal phosphoserine phosphatases, and no archaea fall within TIGR00338. It is likely, then, that this model represents the archaeal branch of the PSPase equivalog.


Pssm-ID: 273655 [Multi-domain]  Cd Length: 201  Bit Score: 103.81  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    1 MFIVAFDIDGTLTPIKSSWSYVHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSL----DTFNKILSSIPWRS 76
Cdd:TIGR01491   4 IKLIIFDLDGTLTDVMSSWEYLHRRLETCGLAKKNAELFFSGRISYEEWARLDASLWKRRSGrlrrEEVEEIFKEISLRD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   77 G-IESIRKLKNKYANNVLfiaVSGGFAQLGKRAVEELGFDAYIGVEIDYESN-RLNGKAKFYPEYNDKGRLLEEFLRQKH 154
Cdd:TIGR01491  84 YaEELVRWLKEKGLKTAI---VSGGIMCLAKKVAEKLNPDYVYSNELVFDEKgFIQPDGIVRVTFDNKGEAVERLKRELN 160

                         170       180
                  ....*....|....*....|....*...
gi 304378358  155 INVEKTICVGDNINDIGLFRYCDISISF 182
Cdd:TIGR01491 161 PSLTETVAVGDSKNDLPMFEVADISISL 188
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 3-207 2.20e-16

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 74.70  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    3 IVAFDIDGTLTPIKSSWSyVHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFNKILSSIPWRSGI-ESI 81
Cdd:TIGR00338  16 LVVFDMDSTLINAETIDE-IAKIAGVEEEVSEITERAMRGELDFKASLRERVALLKGLPVELLKEVRENLPLTEGAeELV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   82 RKLKNKyanNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGKAKFYP-EYNDKGRLLEEFLRQKHINVEKT 160
Cdd:TIGR00338  95 KTLKEK---GYKVAVISGGFDLFAEHVKDKLGLDAAFANRLEVEDGKLTGLVEGPIvDASYKGKTLLILLRKEGISPENT 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 304378358  161 ICVGDNINDIGLFRYCDISISFCST-CLDRYATYVIKTCNIRMLAGFL 207
Cdd:TIGR00338 172 VAVGDGANDLSMIKAAGLGIAFNAKpKLQQKADICINKKDLTDILPLL 219
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-173 3.84e-16

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 73.16  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    3 IVAFDIDGTLTPIKSSWSYVHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGL--SLDTFNKILSSIPWRSGI-E 79
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRSrsEEVAKEFLARQVALRPGArE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   80 SIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEID-YESNRLNGK--AKFYPEYNDKGRLLEEFLRQKHIN 156
Cdd:TIGR01488  81 LISWLK---ERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEfDDNGLLTGPieGQVNPEGECKGKVLKELLEESKIT 157

                         170
                  ....*....|....*..
gi 304378358  157 VEKTICVGDNINDIGLF 173
Cdd:TIGR01488 158 LKKIIAVGDSVNDLPML 174
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 41-183 1.99e-13

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 65.65  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  41 EGFISYDEWIVHDLSLWKGLSLDTFNKILSSIPWRSGIES-IRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIG 119
Cdd:cd07500   38 RGELDFEESLRERVALLKGLPESVLDEVYERLTLTPGAEElIQTLK---AKGYKTAVVSGGFTYFTDRLAEELGLDYAFA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304378358 120 VEIDYESNRLNGKAKFYP-EYNDKGRLLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISISFC 183
Cdd:cd07500  115 NELEIKDGKLTGKVLGPIvDAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIAFH 179
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-174 1.31e-09

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 55.62  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    4 VAFDIDGTLTPIKSSWSY--------VHKVLNTLKRAESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFN----KILSS 71
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLirallrrgGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALLAGLPEEDAAelerFVAEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   72 IPWRSGIESIRKLKNKYANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGKAKFYPEYN---DKGRLLEE 148
Cdd:pfam12710  81 ALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDGRFTGELRLIGPPCageGKVRRLRA 160

                         170       180
                  ....*....|....*....|....*...
gi 304378358  149 FL--RQKHINVEKTICVGDNINDIGLFR 174
Cdd:pfam12710 161 WLaaRGLGLDLADSVAYGDSPSDLPMLR 188
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-170 8.78e-09

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 53.36  E-value: 8.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    3 IVAFDIDGTLTPIKSSWSYV-------HKVLNTLKRA--------ESMAKQFFEGFISYDEWIVHDLSLWKGLSLDTFNK 67
Cdd:pfam00702   3 AVVFDLDGTLTDGEPVVTEAiaelaseHPLAKAIVAAaedlpipvEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   68 IL-----------SSIPWRSGIESIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLnGKAKfy 136
Cdd:pfam00702  83 VLvellgvialadELKLYPGAAEALKALK---ERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGV-GKPK-- 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 304378358  137 peyndkGRLLEEFLRQKHINVEKTICVGDNINDI 170
Cdd:pfam00702 157 ------PEIYLAALERLGVKPEEVLMVGDGVNDI 184
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 3-181 6.24e-07

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 48.15  E-value: 6.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358    3 IVAFDIDGTLTPIKSSW------SYVHKVLN-----------TLKRAESMAKQ--FFEGFISYDEWIVHDLSLWKGLSLD 63
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHElspetiEALERLREagvkvvivtgrSLAEIKELLKQlnLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   64 TFNKILSSIPWRSGIESIRKLKNKYAN------NVLFIAVSGG------FAQLGKRAVEELGFDAYiGVEIDYESNRLNG 131
Cdd:TIGR01484  81 DVFEEILGIKFEEIGAELKSLSEHYVGtfiedkAIAVAIHYVGaelgqeLDSKMRERLEKIGRNDL-ELEAIYSGKTDLE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 304378358  132 kakFYPEYNDKGRLLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISIS 181
Cdd:TIGR01484 160 ---VLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVA 206
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-180 1.86e-05

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 43.59  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   3 IVAFDIDGTLTPIKSSWS-YVHKVLNTLK-----------RAESMAKQFFEGFISYDEWI------VHDLSlwkglsldt 64
Cdd:COG0561    4 LIALDLDGTLLNDDGEISpRTKEALRRLRekgikvviatgRPLRSALPLLEELGLDDPLItsngalIYDPD--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  65 fNKILSSIPW-RSGIESIRKLKNKYANNVLFIAVSGGFAqlgkraveelgfdayigVEIdyesnrlngkakfYPEYNDKG 143
Cdd:COG0561   75 -GEVLYERPLdPEDVREILELLREHGLHLQVVVRSGPGF-----------------LEI-------------LPKGVSKG 123

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 304378358 144 RLLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISI 180
Cdd:COG0561  124 SALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGV 160
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 6-177 2.42e-05

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: 43.45  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   6 FDIDGTLTPiKSSWS--YVHKVLNTLKRAESMAKQF---------------FEGFIS-----YDEWIVHDLSLWkglsld 63
Cdd:cd02612    4 FDLDGTLIA-GDSFFafLRFKGIAERRAPLEELLLLrlmalyalgrldgagMEALLGfatagLAGELAALVEEF------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  64 tFNKILSSIPWRSGIESIRKLKNKYANNVLfiaVSGGFAQLGKRAVEELGFDAYIGVEIDYESNRLNGKAKFYPEYND-K 142
Cdd:cd02612   77 -VEEYILRVLYPEARELIAWHKAAGHDVVL---ISASPEELVAPIARKLGIDNVLGTQLETEDGRYTGRIIGPPCYGEgK 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 304378358 143 GRLLEEFLRQKHINVEKTICVGDNINDIGLFRYCD 177
Cdd:cd02612  153 VKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVG 187
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 79-182 9.84e-05

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 42.65  E-value: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  79 ESIRKLKNKYANNVLFIavSGGFAQLGKRAVEELGFDAYigveidyesnrlngKAKFYPEynDKGRLLEEFLRQKHinve 158
Cdd:cd07550  428 EVIARLRALGGKRIIML--TGDHEQRARALAEQLGIDRY--------------HAEALPE--DKAEIVEKLQAEGR---- 485

                         90       100
                 ....*....|....*....|....*
gi 304378358 159 kTIC-VGDNINDIGLFRYCDISISF 182
Cdd:cd07550  486 -TVAfVGDGINDSPALSYADVGISM 509
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 4-170 2.64e-04

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 40.42  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   4 VAFDIDGTLTpikSSWSYVHKVLNTlkraesMAKQFfeGFISYDEwivHDLSLWKGLSLDTFNKILSSIPWRSGI---ES 80
Cdd:cd04303    2 IIFDFDGTLA---DSFPWFLSILNQ------LAARH--GFKTVDE---EEIEQLRQLSSREILKQLGVPLWKLPLiakDF 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  81 IRKLKNKYANNVLFIAVSGGFAQLGKRAVE--------------ELGFDAYIGVEIDYESNRLNGKAkfypeyndkgRLL 146
Cdd:cd04303   68 RRLMAEAAPELALFPGVEDMLRALHARGVRlavvssnseenirrVLGPEELISLFAVIEGSSLFGKA----------KKI 137

                        170       180
                 ....*....|....*....|....
gi 304378358 147 EEFLRQKHINVEKTICVGDNINDI 170
Cdd:cd04303  138 RRVLRRTKITAAQVIYVGDETRDI 161
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 78-180 7.51e-04

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 39.53  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358   78 IESIRKLKNKYANNVLFIAVSGGFAQLGKRaveelgFDAYIGVEIDYESNrLNGKAKFYPEYNDKGRLLEEFLRQKHINV 157
Cdd:pfam08282 131 IDDFELLEDEDINKILILLDEEDLDELEKE------LKELFGSLITITSS-GPGYLEIMPKGVSKGTALKALAKHLNISL 203

                          90       100
                  ....*....|....*....|...
gi 304378358  158 EKTICVGDNINDIGLFRYCDISI 180
Cdd:pfam08282 204 EEVIAFGDGENDIEMLEAAGLGV 226
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 78-178 3.89e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All 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. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 35.83  E-value: 3.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304378358  78 IESIRKLKnkyANNVLFIAVSGGFAQLGKRAVEELGFDAYIGVEIDYESnrlngkakfYPEYNDKGRLLEEFLRQKHINV 157
Cdd:cd01427   13 VELLKRLR---AAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDG---------GGTPKPKPKPLLLLLLKLGVDP 80

                         90       100
                 ....*....|....*....|.
gi 304378358 158 EKTICVGDNINDIGLFRYCDI 178
Cdd:cd01427   81 EEVLFVGDSENDIEAARAAGG 101
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 106-180 8.50e-03

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 35.80  E-value: 8.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304378358 106 KRAvEELGF-DAYIGVEidyesnrlngkakfypeynDKGRLLEEFLRQKHINVEKTICVGDNINDIGLFRYCDISI 180
Cdd:COG1778   67 RRA-EELGItHVYQGVK-------------------DKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSV 122
 
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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