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Conserved domains on  [gi|1981167282|ref|WP_203162692|]
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haloacid dehalogenase type II [Legionella bononiensis]

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

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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 ...
 51-278 3.23e-51

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 cd02588:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 216  Bit Score: 167.83  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  51 KFIAFDVFGTLVDWRgTMIREFAVLFEekeitnVSCEEFIGLWVNAYSENMTkISEGTRPFATVDELNKIALNKTLEHYQ 130
Cdd:cd02588     1 KALVFDVYGTLIDWH-SGLAAAERAFP------GRGEELSRLWRQKQLEYTW-LVTLMGPYVDFDELTRDALRATAAELG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 131 IlnKFTEPEREQMWMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG--FEWDIILSGELVQCYKPNP 207
Cdd:cd02588    73 L--ELDESDLDELGDAYLRLPPFPDVVAGLRRLREAgYRLAILSNGSPDLIEDVVANAGlrDLFDAVLSAEDVRAYKPAP 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981167282 208 LVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLEFGTvkeeqiPGDDGFDFVTEGMDDLA 278
Cdd:cd02588   151 AVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPD------PLGPAPDFVVPDLGELA 215
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 51-278 3.23e-51

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 167.83  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  51 KFIAFDVFGTLVDWRgTMIREFAVLFEekeitnVSCEEFIGLWVNAYSENMTkISEGTRPFATVDELNKIALNKTLEHYQ 130
Cdd:cd02588     1 KALVFDVYGTLIDWH-SGLAAAERAFP------GRGEELSRLWRQKQLEYTW-LVTLMGPYVDFDELTRDALRATAAELG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 131 IlnKFTEPEREQMWMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG--FEWDIILSGELVQCYKPNP 207
Cdd:cd02588    73 L--ELDESDLDELGDAYLRLPPFPDVVAGLRRLREAgYRLAILSNGSPDLIEDVVANAGlrDLFDAVLSAEDVRAYKPAP 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981167282 208 LVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLEFGTvkeeqiPGDDGFDFVTEGMDDLA 278
Cdd:cd02588   151 AVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPD------PLGPAPDFVVPDLGELA 215
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 50-252 1.12e-50

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 165.97  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIReFAVLFEEKEitnvscEEFIGLWVNAYSENMTKISEGtRPFATVDELNKIALNKTLEHY 129
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAER-AAELYGGRG------EALSQLWRQKQLEYSWLRTLM-GPYKDFWDLTREALRYLLGRL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QIlnKFTEPEREQMWMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKPN 206
Cdd:TIGR01428  73 GL--EDDESAADRLAEAYLRLPPHPDVPAGLRALKERgYRLAILSNGSPAMLKSLVKHAGLDdpFDAVLSADAVRAYKPA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1981167282 207 PLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLE 252
Cdd:TIGR01428 151 PQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGE 196
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 50-281 5.24e-34

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 123.21  E-value: 5.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITnVSCEEFIGLWVNAYSENMTKISEGTRPFATVdelnkiaLNKTLEHY 129
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLL-DEAEELAEAYRAIEYALWRRYERGEITFAEL-------LRRLLEEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QIlnKFTEPEREQMWMVWHRL-EPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKP 205
Cdd:COG1011    73 GL--DLAEELAEAFLAALPELvEPYPDALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDdlFDAVVSSEEVGVRKP 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981167282 206 NPLVYQSAAKVLKLKASEILLVASH-KYDLEAARQCGFKTAYIFRPlefgtvkEEQIPGDDGFDFVTEGMDDLAKQV 281
Cdd:COG1011   151 DPEIFELALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVNRS-------GEPAPAEPRPDYVISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 50-241 6.16e-17

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: 77.24  E-value: 6.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITNVSCEEFIGLWVnAYSENMTKISEGTRPFATvDELNKIALNKTLEHY 129
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPI-PVEDFTARLLLGKRDWLE-ELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QILNKFTEPEREQMwmVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG--FEWDIILSGELVQCYKPN 206
Cdd:pfam00702  79 GLTVVLVELLGVIA--LADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGldDYFDVVISGDDVGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1981167282 207 PLVYQSAAKVLKLKASEILLVASHKYDLEAARQCG 241
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
49-245 1.40e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 39.41  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  49 SIKFIAFDVFGTLVDwrgT----------MIREF--AVLfEEKEITNvsceeFIG-----LWVNAYSENMTKISEgtrpf 111
Cdd:PRK13222    5 DIRAVAFDLDGTLVD---SapdlaaavnaALAALglPPA-GEERVRT-----WVGngadvLVERALTWAGREPDE----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 112 atvdELNKIALNKTLEHY-QILNKFTEPereqmwmvwhrlepWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG- 188
Cdd:PRK13222   71 ----ELLEKLRELFDRHYaENVAGGSRL--------------YPGVKETLAALKAAgYPLAVVTNKPTPFVAPLLEALGi 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 189 ---FEwdIILSGELVQCYKPNPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTA 245
Cdd:PRK13222  133 adyFS--VVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSV 190
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 51-278 3.23e-51

L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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: 319787 [Multi-domain]  Cd Length: 216  Bit Score: 167.83  E-value: 3.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  51 KFIAFDVFGTLVDWRgTMIREFAVLFEekeitnVSCEEFIGLWVNAYSENMTkISEGTRPFATVDELNKIALNKTLEHYQ 130
Cdd:cd02588     1 KALVFDVYGTLIDWH-SGLAAAERAFP------GRGEELSRLWRQKQLEYTW-LVTLMGPYVDFDELTRDALRATAAELG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 131 IlnKFTEPEREQMWMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG--FEWDIILSGELVQCYKPNP 207
Cdd:cd02588    73 L--ELDESDLDELGDAYLRLPPFPDVVAGLRRLREAgYRLAILSNGSPDLIEDVVANAGlrDLFDAVLSAEDVRAYKPAP 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981167282 208 LVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLEFGTvkeeqiPGDDGFDFVTEGMDDLA 278
Cdd:cd02588   151 AVYELAAERLGVPPDEILHVASHAWDLAGARALGLRTAWINRPGEVPD------PLGPAPDFVVPDLGELA 215
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 50-252 1.12e-50

2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Belongs to the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), class (subfamily) I. Note that the Type I HAD enzymes have not yet been fully characterized, but clearly utilize a substantially different catalytic mechanism and are thus unlikely to be related.


Pssm-ID: 130495 [Multi-domain]  Cd Length: 198  Bit Score: 165.97  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIReFAVLFEEKEitnvscEEFIGLWVNAYSENMTKISEGtRPFATVDELNKIALNKTLEHY 129
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAER-AAELYGGRG------EALSQLWRQKQLEYSWLRTLM-GPYKDFWDLTREALRYLLGRL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QIlnKFTEPEREQMWMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKPN 206
Cdd:TIGR01428  73 GL--EDDESAADRLAEAYLRLPPHPDVPAGLRALKERgYRLAILSNGSPAMLKSLVKHAGLDdpFDAVLSADAVRAYKPA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1981167282 207 PLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLE 252
Cdd:TIGR01428 151 PQVYQLALEALGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGE 196
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 50-281 5.24e-34

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 123.21  E-value: 5.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITnVSCEEFIGLWVNAYSENMTKISEGTRPFATVdelnkiaLNKTLEHY 129
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLL-DEAEELAEAYRAIEYALWRRYERGEITFAEL-------LRRLLEEL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QIlnKFTEPEREQMWMVWHRL-EPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKP 205
Cdd:COG1011    73 GL--DLAEELAEAFLAALPELvEPYPDALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDdlFDAVVSSEEVGVRKP 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981167282 206 NPLVYQSAAKVLKLKASEILLVASH-KYDLEAARQCGFKTAYIFRPlefgtvkEEQIPGDDGFDFVTEGMDDLAKQV 281
Cdd:COG1011   151 DPEIFELALERLGVPPEEALFVGDSpETDVAGARAAGMRTVWVNRS-------GEPAPAEPRPDYVISDLAELLELL 220
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 53-238 1.03e-22

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 92.20  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  53 IAFDVFGTLVDWRGTMIREFAVLFEEKEitnVSCEEFIGLWVnAYSEnMTKISEGTRPFAtvdELNKIALNKTLEHYQIL 132
Cdd:TIGR01493   2 MVFDVYGTLVDVHGGVRACLAAIAPEGG---AFSDLWRAKQQ-EYSW-RRSLMGDRRAFP---EDTVRALRYIADRLGLD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 133 NKftEPEREQMWMVWHRLEPWPDVPSGINKlkerfsIGVLSNGNIRLLEDLSKNAGFEW--DIILSGELVQCYKPNPLVY 210
Cdd:TIGR01493  74 AE--PKYGERLRDAYKNLPPWPDSAAALAR------VAILSNASHWAFDQFAQQAGLPWyfDRAFSVDTVRAYKPDPVVY 145

                         170       180
                  ....*....|....*....|....*...
gi 1981167282 211 QSAAKVLKLKASEILLVASHKYDLEAAR 238
Cdd:TIGR01493 146 ELVFDTVGLPPDRVLMVAAHQWDLIGAR 173
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 50-241 6.16e-17

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: 77.24  E-value: 6.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITNVSCEEFIGLWVnAYSENMTKISEGTRPFATvDELNKIALNKTLEHY 129
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPI-PVEDFTARLLLGKRDWLE-ELDILRGLVETLEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QILNKFTEPEREQMwmVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG--FEWDIILSGELVQCYKPN 206
Cdd:pfam00702  79 GLTVVLVELLGVIA--LADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGldDYFDVVISGDDVGVGKPK 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1981167282 207 PLVYQSAAKVLKLKASEILLVASHKYDLEAARQCG 241
Cdd:pfam00702 157 PEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
50-278 3.43e-15

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 72.65  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITNVSCEEFIGlWVNAYSENMTKISEGTRPFATVDELNKIAlnktLEHY 129
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRA-LIGLGLRELLRRLLGEDPDEELEELLARF----RELY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 QILNkftepereqmwmvWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFEW--DIILSGELVQCYKPN 206
Cdd:COG0546    76 EEEL-------------LDETRLFPGVRELLEALKARgIKLAVVTNKPREFAERLLEALGLDDyfDAIVGGDDVPPAKPK 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981167282 207 PLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIfrplEFGTVKEEQIPgDDGFDFVTEGMDDLA 278
Cdd:COG0546   143 PEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGV----TWGYGSAEELE-AAGADYVIDSLAELL 209
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
53-245 3.35e-11

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 60.68  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  53 IAFDVFGTLVDWRGTMIREFAVLFEEKEITNVSCEE---FIGLwvnaysenmtkISEGTRPFATVDELNKIALNKTLEHY 129
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEilkFIGL-----------PLREIFRYLGVSEDEEEKIEFYLRKY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 130 -QILNKFTepereqmwmvwhrLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKP 205
Cdd:pfam13419  70 nEELHDKL-------------VKPYPGIKELLEELKEQgYKLGIVTSKSRENVEEFLKQLGLEdyFDVIVGGDDVEGKKP 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1981167282 206 NPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTA 245
Cdd:pfam13419 137 DPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVI 176
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 50-277 7.45e-10

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. 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: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 57.67  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDWRGTMIREFAVLFEEKEITNVSCEE---FIGLWVNAYSENMTKISEGTRpfatVDELnkialnktL 126
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEvlpFIGPPLRETFEKIDPDKLEDM----VEEF--------R 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 127 EHY-QILNKFTepereqmwmvwhrlEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG-FEW-DIILSGELVQC 202
Cdd:cd02616    69 KYYrEHNDDLT--------------KEYPGVYETLARLKSQgIKLGVVTTKLRETALKGLKLLGlDKYfDVIVGGDDVTH 134

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981167282 203 YKPNPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTA---YIFRPLEFgtvKEEQIPgddgfDFVTEGMDDL 277
Cdd:cd02616   135 HKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVgvtWGYKGREY---LKAFNP-----DFIIDKMSDL 204
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 50-244 4.16e-08

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 52.35  E-value: 4.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVDW-RGTMIREFAVLFEEKEITNVSCEEFIGLWVnaysenmtKISEGTRPFATVDELNKIALNKTLEH 128
Cdd:cd02603     1 IRAVLFDFGGVLIDPdPAAAVARFEALTGEPSEFVLDTEGLAGAFL--------ELERGRITEEEFWEELREELGRPLSA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 129 YQIlnkfteperEQMWMVWHRLEPwpDVPSGINKLKER-FSIGVLSNGNI----RLLEDLSKNAGFEWDIILSGElVQCY 203
Cdd:cd02603    73 ELF---------EELVLAAVDPNP--EMLDLLEALRAKgYKVYLLSNTWPdhfkFQLELLPRRGDLFDGVVESCR-LGVR 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1981167282 204 KPNPLVYQSAAKVLKLKASEILLVashkyD-----LEAARQCGFKT 244
Cdd:cd02603   141 KPDPEIYQLALERLGVKPEEVLFI-----DdreenVEAARALGIHA 181
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 53-244 8.91e-08

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 51.27  E-value: 8.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  53 IAFDVFGTLVDwrGTMIREFAVLFEEKeitnvsceEFIGLW-VNAYSENMTKisegtrpFATVDELNKIALNKTLEHYQI 131
Cdd:TIGR01509   2 ILFDLDGVLVD--TEFAIAKLINREEL--------GLVPDElGVSAVGRLEL-------ALRRFKAQYGRTISPEDAQLL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 132 LNKFTEPEREQMWMvwhrLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKN---AGFEwDIILSGELVQCyKPNP 207
Cdd:TIGR01509  65 YKQLFYEQIEEEAK----LKPLPGVRALLEALRARgKKLALLTNSPRAHKLVLALLglrDLFD-VVIDSSDVGLG-KPDP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1981167282 208 LVYQSAAKVLKLKASEILLV---ASHkydLEAARQCGFKT 244
Cdd:TIGR01509 139 DIYLQALKALGLEPSECVFVddsPAG---IEAAKAAGMHT 175
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 53-241 2.24e-07

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 49.70  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  53 IAFDVFGTLVDwRGTMIRE-FAVLFEEKEITNVSCEEFiglwvnaysenmtkisegtrpfatvdelnKIALNKTLEHYQ- 130
Cdd:TIGR01549   2 ILFDIDGTLVD-IKFAIRRaFPQTFEEFGLDPASFKAL-----------------------------KQAGGLAEEEWYr 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 131 ILNKFTEPEREQMWMVWHRLEPW-PDVPSGINKLKER-FSIGVLSNGN---IRLLEDLSKNAGFEWDIILSGELvqCYKP 205
Cdd:TIGR01549  52 IATSALEELQGRFWSEYDAEEAYiRGAADLLARLKSAgIKLGIISNGSlraQKLLLRLFGLGDYFELILVSDEP--GSKP 129

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1981167282 206 NPLVYQSAAKVLKLkASEILLVASHKYDLEAARQCG 241
Cdd:TIGR01549 130 EPEIFLAALESLGV-PPEVLHVGDNLNDIEGARNAG 164
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 52-242 5.64e-07

Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGP; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. 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 (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) 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: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 49.16  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  52 FIAFDVFGTLVDWRGTMIREFAVLFEEKEITNVScEEFIGLWVNAYSENMTKIS-EGTRPFATVDELNKIALNKTLEHYQ 130
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLP-EETVRTWIGNGADVLVERAlTGAREAEPDEELFKEARALFDRHYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 131 IlnkftepereqmwMVWHRLEPWPDVPSGINKLKER-FSIGVLSNGNIR----LLEDLSKNAGFEWdiILSGELVQCYKP 205
Cdd:cd16417    80 E-------------TLSVHSHLYPGVKEGLAALKAQgYPLACVTNKPERfvapLLEALGISDYFSL--VLGGDSLPEKKP 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1981167282 206 NPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGF 242
Cdd:cd16417   145 DPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGC 181
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
50-277 1.11e-06

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 48.28  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  50 IKFIAFDVFGTLVD--------WRgTMIREFAVLFEEKEItnvscEEFIGLwvnAYSENMTKISEgtrpfatvdelnkiA 121
Cdd:COG0637     2 IKAVIFDMDGTLVDseplharaWR-EAFAELGIDLTEEEY-----RRLMGR---SREDILRYLLE--------------E 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 122 LNKTLEHYQILNKFTEPEREQMWMvwHRLEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGF-EW-DIILSGE 198
Cdd:COG0637    59 YGLDLPEEELAARKEELYRELLAE--EGLPLIPGVVELLEALKEAgIKIAVATSSPRENAEAVLEAAGLlDYfDVIVTGD 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981167282 199 LVQCYKPNPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTAYIFRPLEfgtvKEEQIPgddGFDFVTEGMDDL 277
Cdd:COG0637   137 DVARGKPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDGGT----AEEELA---GADLVVDDLAEL 208
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 160-247 1.66e-06

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: 45.85  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 160 INKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKPNPLVYQSAAKVLKLKASEILLVASHKYDLEA 236
Cdd:cd01427    16 LKRLRAAgIKLAIVTNRSREALRALLEKLGLGdlFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEA 95

                          90
                  ....*....|.
gi 1981167282 237 ARQCGFKTAYI 247
Cdd:cd01427    96 ARAAGGRTVAV 106
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 51-241 7.89e-06

REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes uncharacterized sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster which has been identified as a rhythmically (diurnally) regulated gene. This family is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. This family is a member of subfamily 1A in which the cap domain consists of a predicted alpha helical bundle found in between the first and second catalytic motifs. A distinctive feature of this family is a conserved tandem pair of tryptophan residues in the cap domain. The most divergent sequences included within the scope of this model are from plants and have "FW" at this position instead. Most likely, these sequences, like the vast majority of HAD sequences, represent phosphatase enzymes.


Pssm-ID: 274056 [Multi-domain]  Cd Length: 203  Bit Score: 45.74  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  51 KFIAFDVFGTLVDWRGTM-------IREFAVLFEEKEITNVSCEEFIGLWVN----AYSENMT------KISEGTrpFAT 113
Cdd:TIGR02252   1 KLITFDAVGTLLALKEPVgevyceiARKYGVEVSPDELEQAFRKAFKAMSEAfpnfGFSSGLTpqqwwqKLVRDT--FGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 114 VDELNKIALNKTLEHyqILNKFTEPereqmwmvwhrlEPW---PDVPSGINKLKER-FSIGVLSNGNIRlLEDLSKNAGF 189
Cdd:TIGR02252  79 AGVPDPESFEKIFEE--LYSYFATP------------EPWqvyPDAIKLLKDLRERgLILGVISNFDSR-LRGLLEALGL 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1981167282 190 E--WDIILSGELVQCYKPNPLVYQSAAKVLKLKASEILLVA-SHKYDLEAARQCG 241
Cdd:TIGR02252 144 LeyFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALHIGdSLRNDYQGARAAG 198
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 153-247 3.77e-05

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 42.14  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 153 WPDVPSGINKLKERFSIGVLSNGNIRL----LEDLSKNAGFEwDIILSGEL-VQcyKPNPLVYQSAAKVLKLKASEILLV 227
Cdd:cd04305    11 LPGAKELLEELKKGYKLGIITNGPTEVqwekLEQLGIHKYFD-HIVISEEVgVQ--KPNPEIFDYALNQLGVKPEETLMV 87

                          90       100
                  ....*....|....*....|.
gi 1981167282 228 A-SHKYDLEAARQCGFKTAYI 247
Cdd:cd04305    88 GdSLESDILGAKNAGIKTVWF 108
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 169-244 9.39e-05

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It 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: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 41.83  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 169 IGVLSNGNIRLLEDLSKNAGFEW---DIILSGELVQCYKPNPLVYQSAAKVLKLKASEILLVAshkyD----LEAARQCG 241
Cdd:cd07505    60 VAVATSSSRRNVELLLLELGLLRgyfDVIVSGDDVERGKPAPDIYLLAAERLGVDPERCLVFE----DslagIEAAKAAG 135


                  ...
gi 1981167282 242 FKT 244
Cdd:cd07505   136 MTV 138
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 150-243 5.01e-04

uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized Bacillus subtilis YhcW; This subfamily includes the uncharacterized Bacillus subtilis YhcW. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319859 [Multi-domain]  Cd Length: 169  Bit Score: 39.93  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 150 LEPWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAGFE--WDIILSGELVQCYKPNPLVYQSAAKVLKLKASEILL 226
Cdd:cd16423    43 LPPIEGVKELLEFLKEKgIKLAVASSSPRRWIEPHLERLGLLdyFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVV 122

                          90
                  ....*....|....*..
gi 1981167282 227 VASHKYDLEAARQCGFK 243
Cdd:cd16423   123 IEDSRNGVLAAKAAGMK 139
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 149-244 1.17e-03

subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides xylulose-1,5-bisphosphate phosphatase CbbY; This family includes Rhodobacter sphaeroides and Arabidopsis thaliana xylulose-1,5-bisphosphate phosphatase CbbY which convert xylulose-1,5-bisphosphate (a potent inhibitor of Ribulose-1,5-bisphosphate carboxylase/oxygenase, Rubisco), to the non-inhibitory compound xylulose-5-phosphate. It belongs to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. 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: 319830 [Multi-domain]  Cd Length: 199  Bit Score: 39.29  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 149 RLEPWPDVPSGINKLKE---RFSIGVLSN-GNIR-LLEDLSKNAGFEW-DIILSGELVQCYKPNPLVYQSAAKVLKLKAS 222
Cdd:cd07528    93 LLPLRPGVARLIDEAKAagvRLAIATTTSpANVDaLLSALLGPERRAIfDAIAAGDDVAEKKPDPDIYLLALERLGVSPS 172

                          90       100
                  ....*....|....*....|..
gi 1981167282 223 EILLVASHKYDLEAARQCGFKT 244
Cdd:cd07528   173 DCLAIEDSAIGLQAAKAAGLPC 194
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
49-245 1.40e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 39.41  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282  49 SIKFIAFDVFGTLVDwrgT----------MIREF--AVLfEEKEITNvsceeFIG-----LWVNAYSENMTKISEgtrpf 111
Cdd:PRK13222    5 DIRAVAFDLDGTLVD---SapdlaaavnaALAALglPPA-GEERVRT-----WVGngadvLVERALTWAGREPDE----- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 112 atvdELNKIALNKTLEHY-QILNKFTEPereqmwmvwhrlepWPDVPSGINKLKER-FSIGVLSNGNIRLLEDLSKNAG- 188
Cdd:PRK13222   71 ----ELLEKLRELFDRHYaENVAGGSRL--------------YPGVKETLAALKAAgYPLAVVTNKPTPFVAPLLEALGi 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981167282 189 ---FEwdIILSGELVQCYKPNPLVYQSAAKVLKLKASEILLVASHKYDLEAARQCGFKTA 245
Cdd:PRK13222  133 adyFS--VVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSV 190
 
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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