NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|737122454|ref|WP_035110142|]
View 

HAD-IB family hydrolase [Clostridium tetani]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 5-207 2.97e-61

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member TIGR01490:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 202  Bit Score: 191.01  E-value: 2.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    5 AAFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRtgdYDDYLLKMAKIYIEAIKGLHKYQVEFIAK 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   85 NVVEQK-GDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIYTGEV-KPMWDSRNKK 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIdGNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 737122454  163 MAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPTREL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-207 2.97e-61

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: 191.01  E-value: 2.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    5 AAFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRtgdYDDYLLKMAKIYIEAIKGLHKYQVEFIAK 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   85 NVVEQK-GDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIYTGEV-KPMWDSRNKK 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIdGNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 737122454  163 MAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPTREL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-207 1.29e-53

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: 172.33  E-value: 1.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   1 MKRVAAFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRTGDYDDYLlkmaKIYIEAIKGLHKYQVE 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESL----RFRVALLAGLPEEELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  81 FIAKNVVEQKgDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEV-KPMWDSR 159
Cdd:COG0560   77 ELAERLFEEV-PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDG-RLTGEVvGPIVDGE 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 737122454 160 NKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPTREL 207
Cdd:COG0560  155 GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPAL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-204 5.13e-47

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: 154.39  E-value: 5.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   5 AAFFDIDGTLYReGLITEVFkkmIKYEIIHPKRWYNEVRPEYLkwdnrtgDYDDYLL-KMAKIYIEA-IKGL---HKYQV 79
Cdd:cd02612    1 LAFFDLDGTLIA-GDSFFAF---LRFKGIAERRAPLEELLLLR-------LMALYALgRLDGAGMEAlLGFAtagLAGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  80 EFIAKNVVEQKGDRV-YTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEV-KPMWD 157
Cdd:cd02612   70 AALVEEFVEEYILRVlYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDG-RYTGRIiGPPCY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 737122454 158 SRNKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPT 204
Cdd:cd02612  149 GEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD pfam12710
haloacid dehalogenase-like hydrolase;
6-193 2.08e-19

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 82.58  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    6 AFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRTGDYDDYLLKMAKIYieaiKGLHKYQVEFIAKN 85
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALL----AGLPEEDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   86 VVEQKGDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEVKPMWDS---RNKK 162
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDG-RFTGELRLIGPPcagEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 737122454  163 MAIAELI--EKYNVDINKSYAYGDTTGDLSMFQ 193
Cdd:pfam12710 156 RRLRAWLaaRGLGLDLADSVAYGDSPSDLPMLR 188
 
Name Accession Description Interval E-value
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 5-207 2.97e-61

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: 191.01  E-value: 2.97e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    5 AAFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRtgdYDDYLLKMAKIYIEAIKGLHKYQVEFIAK 84
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLASKNILFEELRLPKVLARFEFFLNR---GLDYMAYYRAFALDALAGLLEEDVRAIVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   85 NVVEQK-GDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIYTGEV-KPMWDSRNKK 162
Cdd:TIGR01490  78 EFVNQKiESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGNIdGNNCKGEGKV 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 737122454  163 MAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPTREL 207
Cdd:TIGR01490 158 HALAELLAEEQIDLKDSYAYGDSISDLPLLSLVGHPYVVNPDKKL 202
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-207 1.29e-53

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: 172.33  E-value: 1.29e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   1 MKRVAAFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRTGDYDDYLlkmaKIYIEAIKGLHKYQVE 80
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVLEEVAAITERAMAGELDFEESL----RFRVALLAGLPEEELE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  81 FIAKNVVEQKgDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEV-KPMWDSR 159
Cdd:COG0560   77 ELAERLFEEV-PRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDG-RLTGEVvGPIVDGE 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 737122454 160 NKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPTREL 207
Cdd:COG0560  155 GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPAL 202
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 5-204 5.13e-47

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: 154.39  E-value: 5.13e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   5 AAFFDIDGTLYReGLITEVFkkmIKYEIIHPKRWYNEVRPEYLkwdnrtgDYDDYLL-KMAKIYIEA-IKGL---HKYQV 79
Cdd:cd02612    1 LAFFDLDGTLIA-GDSFFAF---LRFKGIAERRAPLEELLLLR-------LMALYALgRLDGAGMEAlLGFAtagLAGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  80 EFIAKNVVEQKGDRV-YTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEV-KPMWD 157
Cdd:cd02612   70 AALVEEFVEEYILRVlYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDG-RYTGRIiGPPCY 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 737122454 158 SRNKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNPT 204
Cdd:cd02612  149 GEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVNPD 195
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 5-194 7.80e-32

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: 114.76  E-value: 7.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    5 AAFFDIDGTLYREGLITEVFKKMIKY--EIIHPKRWYNEVRPEYLKWDNRTGDYDDYLLKmakiyieaikglHKYQVEFI 82
Cdd:TIGR01488   1 LAIFDFDGTLTRQDSLIDLLAKLLGTndEVIELTRLAPSGRISFEDALGRRLALLHRSRS------------EEVAKEFL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   83 AKNVVEQkgdrvyTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIYTG----EVKPMWDS 158
Cdd:TIGR01488  69 ARQVALR------PGARELISWLKERGIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGpiegQVNPEGEC 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 737122454  159 RNKKMaiAELIEKYNVDINKSYAYGDTTGDLSMFQM 194
Cdd:TIGR01488 143 KGKVL--KELLEESKITLKKIIAVGDSVNDLPMLKL 176
HAD pfam12710
haloacid dehalogenase-like hydrolase;
6-193 2.08e-19

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 82.58  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    6 AFFDIDGTLYREGLITEVFKKMIKYEIIHPKRWYNEVRPEYLKWDNRTGDYDDYLLKMAKIYieaiKGLHKYQVEFIAKN 85
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALLRRGGPDLWRALLVLLLLALLRLLGRLSRAGARELLRALL----AGLPEEDAAELERF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   86 VVEQKGDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNeIYTGEVKPMWDS---RNKK 162
Cdd:pfam12710  77 VAEVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDG-RFTGELRLIGPPcagEGKV 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 737122454  163 MAIAELI--EKYNVDINKSYAYGDTTGDLSMFQ 193
Cdd:pfam12710 156 RRLRAWLaaRGLGLDLADSVAYGDSPSDLPMLR 188
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-193 1.89e-06

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: 46.81  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    5 AAFFDIDGTLYR-EGLITEVFKKM--IKYEIIHPKRWYNEVRPEYLKWDNRTGDYDDYLLKMAKIYIEAI-----KGLHK 76
Cdd:pfam00702   3 AVVFDLDGTLTDgEPVVTEAIAELasEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVetleaEGLTV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   77 YQVEFIAKNVVEQKgDRVYTYTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIYtgevKPMW 156
Cdd:pfam00702  83 VLVELLGVIALADE-LKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVG----KPKP 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 737122454  157 DsrnkkmAIAELIEKYNVDINKSYAYGDTTGDLSMFQ 193
Cdd:pfam00702 158 E------IYLAALERLGVKPEEVLMVGDGVNDIPAAK 188
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 7-199 1.04e-04

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong 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: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 42.21  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   7 FFDIDGTLYREGL-----ITEVFKKMIKYEI---IHPKRWYNEVRPEylkwDNRTGdYDDYLlkmakiyieAIKGLH-KY 77
Cdd:cd07517    4 FFDIDGTLLDEDTtipesTKEAIAALKEKGIlvvIATGRAPFEIQPI----VKALG-IDSYV---------SYNGQYvFF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  78 QVEFIAKNVVEQKGDRVYtytrnrIKWHKEQGHlivtvsgsPIELVKEMSL---KHGFDDFRGSIYEL---DNNEIYTgE 151
Cdd:cd07517   70 EGEVIYKNPLPQELVERL------TEFAKEQGH--------PVSFYGQLLLfedEEEEQKYEELRPELrfvRWHPLST-D 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 737122454 152 VKPMWDSrnKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPI 199
Cdd:cd07517  135 VIPKGGS--KAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGI 180
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 106-193 2.54e-04

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: 40.61  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454 106 KEQGHLIVTVSGSPIELVKEMSLKHGFDDFRGSIYELDNNEIyTGEVK-PMWDSRNKKMAIAELIEKYNVDINKSYAYGD 184
Cdd:cd07500   83 KAKGYKTAVVSGGFTYFTDRLAEELGLDYAFANELEIKDGKL-TGKVLgPIVDAQRKAETLQELAARLGIPLEQTVAVGD 161


                 ....*....
gi 737122454 185 TTGDLSMFQ 193
Cdd:cd07500  162 GANDLPMLK 170
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 97-201 3.12e-04

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: 40.50  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  97 YTRNRIKWHKEQGHLIVTVSGSPIELVKEMSLKHGFDDFR-----GSIYELDNNEIYTGEVKP----------------- 154
Cdd:COG0561   23 RTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLitsngALIYDPDGEVLYERPLDPedvreilellrehglhl 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454 155 --MWDSR-----------NKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICV 201
Cdd:COG0561  103 qvVVRSGpgfleilpkgvSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-213 3.62e-03

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 37.60  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454    7 FFDIDGTLYRE-GLITEVFKKMIKYeiIHPK---------RWYNEVRPEYLKWDNRTG----------DYDDYLLKMAKI 66
Cdd:pfam08282   2 ASDLDGTLLNSdKKISEKTKEAIKK--LKEKgikfviatgRPYRAILPVIKELGLDDPvicyngaliyDENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454   67 YIEAIKGLHKYQVEFIAKNVVEQkGDRVYTYTRNR---IKWHKEQGH--------------------LIVTVSGSPIELV 123
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYT-DDGVYILNDNElekILKELNYTKsfvpeiddfellededinkiLILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122454  124 KEMsLKHGFDDFRGSIYELDNNEIYTGEVkpmwdsrNKKMAIAELIEKYNVDINKSYAYGDTTGDLSMFQMMKYPICVNP 203
Cdd:pfam08282 159 KEL-KELFGSLITITSSGPGYLEIMPKGV-------SKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGN 230

                         250
                  ....*....|
gi 737122454  204 TRELLTKISK 213
Cdd:pfam08282 231 ASPEVKAAAD 240
 
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