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Conserved domains on  [gi|756975698|ref|WP_042663907|]
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haloacid dehalogenase type II [Haloferax sp. ATB1]

Protein Classification

HAD family hydrolase( domain architecture ID 11552332)

HAD (haloacid dehalogenase) family hydrolase, similar to Pseudomonas putida (S)-2-haloacid dehalogenase (HadL), which catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids, and Moraxella sp. B haloacetate dehalogenase DehH2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 11-223 2.07e-57

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: 181.31  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  11 VTFDSYSTLVDVDAAEK-ALADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSERDE 89
Cdd:cd02588    3 LVFDVYGTLIDWHSGLAaAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAELGLELDESDLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  90 ILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGT 169
Cdd:cd02588   83 LGDAYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 756975698 170 PIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTPWEPFGPDPDLTIETFYELAE 223
Cdd:cd02588  163 PPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPDLGELAD 216
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 11-223 2.07e-57

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: 181.31  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  11 VTFDSYSTLVDVDAAEK-ALADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSERDE 89
Cdd:cd02588    3 LVFDVYGTLIDWHSGLAaAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAELGLELDESDLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  90 ILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGT 169
Cdd:cd02588   83 LGDAYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 756975698 170 PIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTPWEPFGPDPDLTIETFYELAE 223
Cdd:cd02588  163 PPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPDLGELAD 216
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 11-203 1.02e-47

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: 155.96  E-value: 1.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   11 VTFDSYSTLVDV----DAAEKALADRVEDPqpvSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSE 86
Cdd:TIGR01428   4 LVFDVYGTLFDVhsvaERAAELYGGRGEAL---SQLWRQKQLEYSWLRTLMGPYKDFWDLTREALRYLLGRLGLEDDESA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   87 RDEILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAAR 166
Cdd:TIGR01428  81 ADRLAEAYLRLPPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 756975698  167 TGTPIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTP 203
Cdd:TIGR01428 161 LGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGEP 197
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-225 5.45e-43

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: 144.40  E-value: 5.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   8 VSTVTFDSYSTLVDVD----AAEKALADRVEDPQPVSKLWRA-RSLEYTFVANAIDAYQPFYEMnrdaLQYALDASGVDI 82
Cdd:COG1011    1 IKAVLFDLDGTLLDFDpviaEALRALAERLGLLDEAEELAEAyRAIEYALWRRYERGEITFAEL----LRRLLEELGLDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  83 STSERDEILAVYHEL-DVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYR 161
Cdd:COG1011   77 AEELAEAFLAALPELvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756975698 162 HAAARTGTPIDEIVHVTA-GWFDVMGAQHAGMQAAWVDRKSTPWePFGPDPDLTIETFYELAETL 225
Cdd:COG1011  157 LALERLGVPPEEALFVGDsPETDVAGARAAGMRTVWVNRSGEPA-PAEPRPDYVISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-191 3.53e-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: 76.47  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698    8 VSTVTFDSYSTLVD-----VDAAEKALADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRD--ALQYALDASGV 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDgepvvTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDIlrGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   81 DISTSERDEILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIY 160
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 756975698  161 RHAAARTGTPIDEIVHVTAGWFDVMGAQHAG 191
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
154-197 7.62e-04

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 39.33  E-value: 7.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 756975698 154 KPAAEIYRHAAARTGTPIDEIVHV----TAgwfDVMGAQHAGMQAAWV 197
Cdd:PRK10748 163 KPFSDMYHLAAEKLNVPIGEILHVgddlTT---DVAGAIRCGMQACWI 207
 
Name Accession Description Interval E-value
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 11-223 2.07e-57

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: 181.31  E-value: 2.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  11 VTFDSYSTLVDVDAAEK-ALADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSERDE 89
Cdd:cd02588    3 LVFDVYGTLIDWHSGLAaAERAFPGRGEELSRLWRQKQLEYTWLVTLMGPYVDFDELTRDALRATAAELGLELDESDLDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  90 ILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGT 169
Cdd:cd02588   83 LGDAYLRLPPFPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYELAAERLGV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 756975698 170 PIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTPWEPFGPDPDLTIETFYELAE 223
Cdd:cd02588  163 PPDEILHVASHAWDLAGARALGLRTAWINRPGEVPDPLGPAPDFVVPDLGELAD 216
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 11-203 1.02e-47

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: 155.96  E-value: 1.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   11 VTFDSYSTLVDV----DAAEKALADRVEDPqpvSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSE 86
Cdd:TIGR01428   4 LVFDVYGTLFDVhsvaERAAELYGGRGEAL---SQLWRQKQLEYSWLRTLMGPYKDFWDLTREALRYLLGRLGLEDDESA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   87 RDEILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAAR 166
Cdd:TIGR01428  81 ADRLAEAYLRLPPHPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVYQLALEA 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 756975698  167 TGTPIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTP 203
Cdd:TIGR01428 161 LGVPPDEVLFVASNPWDLGGAKKFGFKTAWINRPGEP 197
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 8-225 5.45e-43

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: 144.40  E-value: 5.45e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   8 VSTVTFDSYSTLVDVD----AAEKALADRVEDPQPVSKLWRA-RSLEYTFVANAIDAYQPFYEMnrdaLQYALDASGVDI 82
Cdd:COG1011    1 IKAVLFDLDGTLLDFDpviaEALRALAERLGLLDEAEELAEAyRAIEYALWRRYERGEITFAEL----LRRLLEELGLDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  83 STSERDEILAVYHEL-DVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYR 161
Cdd:COG1011   77 AEELAEAFLAALPELvEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFE 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 756975698 162 HAAARTGTPIDEIVHVTA-GWFDVMGAQHAGMQAAWVDRKSTPWePFGPDPDLTIETFYELAETL 225
Cdd:COG1011  157 LALERLGVPPEEALFVGDsPETDVAGARAAGMRTVWVNRSGEPA-PAEPRPDYVISDLAELLELL 220
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 11-189 4.57e-25

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: 96.83  E-value: 4.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   11 VTFDSYSTLVDVDAAEKA-LADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDASGVDISTSERDE 89
Cdd:TIGR01493   2 MVFDVYGTLVDVHGGVRAcLAAIAPEGGAFSDLWRAKQQEYSWRRSLMGDRRAFPEDTVRALRYIADRLGLDAEPKYGER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   90 ILAVYHELDVFDDVRDGIERLRdggydcyVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGT 169
Cdd:TIGR01493  82 LRDAYKNLPPWPDSAAALARVA-------ILSNASHWAFDQFAQQAGLPWYFDRAFSVDTVRAYKPDPVVYELVFDTVGL 154

                         170       180
                  ....*....|....*....|
gi 756975698  170 PIDEIVHVTAGWFDVMGAQH 189
Cdd:TIGR01493 155 PPDRVLMVAAHQWDLIGARK 174
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
18-226 3.56e-18

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 79.59  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  18 TLVD-----VDAAEKALADRVEDPQPVSKLWRARSLeytfvanaidayqPFYEMNRDALQYALDAsgvdistsERDEILA 92
Cdd:COG0546   11 TLVDsapdiAAALNEALAELGLPPLDLEELRALIGL-------------GLRELLRRLLGEDPDE--------ELEELLA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  93 VYHEL---------DVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHA 163
Cdd:COG0546   70 RFRELyeeelldetRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEA 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975698 164 AARTGTPIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTPWEPFGP-DPDLTIETFYELAETLG 226
Cdd:COG0546  150 LERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAaGADYVIDSLAELLALLA 213
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 8-191 3.53e-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: 76.47  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698    8 VSTVTFDSYSTLVD-----VDAAEKALADRVEDPQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRD--ALQYALDASGV 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDgepvvTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDIlrGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   81 DISTSERDEILAVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIY 160
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 756975698  161 RHAAARTGTPIDEIVHVTAGWFDVMGAQHAG 191
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
67-221 1.16e-16

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 75.25  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  67 NRDALQYALDASGVDISTSE-RDEILAVYHEL------DVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGD 139
Cdd:COG0637   48 REDILRYLLEEYGLDLPEEElAARKEELYRELlaeeglPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLD 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698 140 ILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIVHV---TAGwfdVMGAQHAGMQAAWVDRKSTPWEPFgPDPDLTIE 216
Cdd:COG0637  128 YFDVIVTGDDVARGKPDPDIYLLAAERLGVDPEECVVFedsPAG---IRAAKAAGMRVVGVPDGGTAEEEL-AGADLVVD 203


                 ....*
gi 756975698 217 TFYEL 221
Cdd:COG0637  204 DLAEL 208
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
96-197 3.25e-13

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 65.30  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   96 ELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIV 175
Cdd:pfam13419  77 LVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVI 156

                          90       100
                  ....*....|....*....|..
gi 756975698  176 HVTAGWFDVMGAQHAGMQAAWV 197
Cdd:pfam13419 157 YVGDSPRDIEAAKNAGIKVIAV 178
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 103-197 1.61e-12

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: 61.64  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698 103 VRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIVHVTAGWF 182
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSEN 91

                         90
                 ....*....|....*
gi 756975698 183 DVMGAQHAGMQAAWV 197
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 92-197 8.74e-11

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: 57.17  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  92 AVYHELD--VFDDVRDGIERLRdGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGT 169
Cdd:cd04305    1 AIIFDLDdtLLPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGV 79

                         90       100
                 ....*....|....*....|....*....
gi 756975698 170 PIDEIVHVTAGW-FDVMGAQHAGMQAAWV 197
Cdd:cd04305   80 KPEETLMVGDSLeSDILGAKNAGIKTVWF 108
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 10-191 1.69e-10

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: 57.79  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   10 TVTFDSYSTLVDVDAA-EKALADRVEdpqpvsklwrarslEYTFVANAIDAYQPFYEMNRDALQyaldasgvDISTSERD 88
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAiRRAFPQTFE--------------EFGLDPASFKALKQAGGLAEEEWY--------RIATSALE 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   89 EILAVY-HELDV----FDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTfKPAAEIYRHA 163
Cdd:TIGR01549  59 ELQGRFwSEYDAeeayIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEPGS-KPEPEIFLAA 137

                         170       180
                  ....*....|....*....|....*...
gi 756975698  164 AARTGTPiDEIVHVTAGWFDVMGAQHAG 191
Cdd:TIGR01549 138 LESLGVP-PEVLHVGDNLNDIEGARNAG 164
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 10-197 8.12e-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: 50.50  E-value: 8.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   10 TVTFDSYSTLVDVDAAEKALADRVEdpQPVSKLWRARSLEYTFVANAIDAYQPFYEMNRDALQYALDasgvdistsERDE 89
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREE--LGLVPDELGVSAVGRLELALRRFKAQYGRTISPEDAQLLY---------KQLF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   90 ILAVYHELDVF--DDVRDGIERLRDGGYDCYVVSNGNPEMLDSMvEHADIGDILKDTISADEVKTFKPAAEIYRHAAART 167
Cdd:TIGR01509  70 YEQIEEEAKLKplPGVRALLEALRARGKKLALLTNSPRAHKLVL-ALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKAL 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 756975698  168 GTPIDEIVhvtagWFD-----VMGAQHAGMQAAWV 197
Cdd:TIGR01509 149 GLEPSECV-----FVDdspagIEAAKAAGMHTVGV 178
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 86-175 8.83e-08

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: 49.54  E-value: 8.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  86 ERDEILAVYHELDV---FDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTI-SADEVKTFKPAAEIYR 161
Cdd:cd07505   26 RKNALLLELIASEGlklKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLLRGYFDVIvSGDDVERGKPAPDIYL 105

                         90
                 ....*....|....
gi 756975698 162 HAAARTGTPIDEIV 175
Cdd:cd07505  106 LAAERLGVDPERCL 119
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 97-205 1.74e-07

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to uncharacterized Drosophila melanogaster rhythmically expressed gene 2 protein and human haloacid dehalogenase-like hydrolase domain-containing protein 3; The haloacid dehalogenase-like (HAD) hydrolases are 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 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. Members 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: 319852 [Multi-domain]  Cd Length: 128  Bit Score: 48.44  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  97 LDVFDD--VRDGIERLRDGGYDCYVVSNGNPeMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEI 174
Cdd:cd16415    4 FDVTGTllAVETLKDLKEKGLKLAVVSNFDR-RLRELLEALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEA 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 756975698 175 VHVTAGWF-DVMGAQHAGMQAAWVDRKSTPWE 205
Cdd:cd16415   83 LHVGDDLKnDYLGARAVGWHALLVDREGALHE 114
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 92-194 1.74e-07

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: 49.65  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  92 AVYHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEM-LDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTP 170
Cdd:cd02603   78 LVLAAVDPNPEMLDLLEALRAKGYKVYLLSNTWPDHfKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLALERLGVK 157

                         90       100
                 ....*....|....*....|....*....
gi 756975698 171 IDEIVhvtagWFD-----VMGAQHAGMQA 194
Cdd:cd02603  158 PEEVL-----FIDdreenVEAARALGIHA 181
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 99-221 9.24e-06

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: 44.96  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  99 VFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIVHVT 178
Cdd:cd02616   81 EYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEALMVG 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 756975698 179 AGWFDVMGAQHAGMQAAWVDRKSTPWEPFGP-DPDLTIETFYEL 221
Cdd:cd02616  161 DSPHDILAGKNAGVKTVGVTWGYKGREYLKAfNPDFIIDKMSDL 204
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 57-194 1.16e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. 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: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 41.81  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  57 IDAYQPFYEMNRDALQYALDAsgvdisTSERDEILAVYhELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHAD 136
Cdd:cd04302   47 EDSFRELLPFDEEEAQRAVDA------YREYYKEKGLF-ENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFG 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698 137 IGDILKDTISA--DEVKTFKpaAEIYRHAAARTGTPIDEIVHVTAGWFDVMGAQHAGMQA 194
Cdd:cd04302  120 LDEYFDGIAGAslDGSRVHK--ADVIRYALDTLGIAPEQAVMIGDRKHDIIGARANGIDS 177
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 68-194 7.62e-04

beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).


Pssm-ID: 213673 [Multi-domain]  Cd Length: 185  Bit Score: 39.25  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698   68 RDALQYALDASGVDISTSERDEILA----VYHEL------DVFDDVRDGIERLRDGGYDCYVVSNG-NPEMLdsmVEHAD 136
Cdd:TIGR02009  48 EDILRAILKLRGDGLSLEEIHQLAErkneLYRELlrltgvAVLPGIRNLLKRLKAKGIAVGLGSSSkNAPRI---LAKLG 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 756975698  137 IGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIVHVTAGWFDVMGAQHAGMQA 194
Cdd:TIGR02009 125 LRDYFDAIVDASEVKNGKPHPETFLLAAELLGVPPNECIVFEDALAGVQAARAAGMFA 182
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
154-197 7.62e-04

5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 39.33  E-value: 7.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 756975698 154 KPAAEIYRHAAARTGTPIDEIVHV----TAgwfDVMGAQHAGMQAAWV 197
Cdd:PRK10748 163 KPFSDMYHLAAEKLNVPIGEILHVgddlTT---DVAGAIRCGMQACWI 207
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 119-193 8.23e-04

subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli 6-phosphogluconate phosphatase YieH; This subfamily includes Escherichia coli YieH/HAD3 an 6-phosphogluconate phosphatase, which can hydrolyzed purines and pyrimidines as secondary substrates. 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. 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: 319828 [Multi-domain]  Cd Length: 141  Bit Score: 38.45  E-value: 8.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 756975698 119 VVSNGNPEMLDSMVEHADIGDILKDTI-SADEVKTFKPAAEIYRHAAARTGTPIDEIVHVTAGWFDVMGAQHAGMQ 193
Cdd:cd07526   60 VASNSSRERLTHSLGLAGLLAYFEGRIfSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDSPTGVRAALAAGMT 135
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 86-220 1.07e-03

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: 38.39  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  86 ERDEILAVYHELDVFDDVRDGIERL----RDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYR 161
Cdd:cd16423   28 RRNELIKRQFSEKTDLPPIEGVKELleflKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 756975698 162 HAAARTGTPIDEIVHVTAGWFDVMGAQHAGMQAAWVDRKSTPWEPFgPDPDLTIETFYE 220
Cdd:cd16423  108 EAAERLGVNPEECVVIEDSRNGVLAAKAAGMKCVGVPNPVTGSQDF-SKADLVLSSFAE 165
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 100-227 1.33e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 38.47  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698 100 FDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTFKPAAEIYRHAAARTGTPIDEIVHVTA 179
Cdd:PRK13288  84 YETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALMVGD 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 756975698 180 GWFDVMGAQHAGMQAAWVdrkstPWEPFGPD------PDLTIETFYELAETLGV 227
Cdd:PRK13288 164 NHHDILAGKNAGTKTAGV-----AWTIKGREyleqykPDFMLDKMSDLLAIVGD 212
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 11-198 1.75e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 38.15  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  11 VTFDSYSTLVD-----VDAAEKALADRVEDPQPVSKLWR--ARSLEYTFVANAIDAYQPfyeMNRDALQYALDASgvdiS 83
Cdd:cd07533    2 VIFDWDGTLADsqhniVAAMTAAFADLGLPVPSAAEVRSiiGLSLDEAIARLLPMATPA---LVAVAERYKEAFD----I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975698  84 TSERDEilavyHELDVFDDVRDGIERLRDGGYDCYVVSNGNPEMLDSMVEHADIGDILKDTISADEVKTfKPAAEIYRHA 163
Cdd:cd07533   75 LRLLPE-----HAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPS-KPHPEMLREI 148

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 756975698 164 AARTGTPIDEIVHVTAGWFDVMGAQHAGMQAAWVD 198
Cdd:cd07533  149 LAELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVA 183
Hydrolase_like pfam13242
HAD-hyrolase-like;
154-221 3.84e-03

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 35.28  E-value: 3.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975698  154 KPAAEIYRHAAARTGTPIDEIVHVtaG---WFDVMGAQHAGMQAAWVDR---KSTPWEPFGPDPDLTIETFYEL 221
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMI--GdrlDTDILGAREAGARTILVLTgvtRPADLEKAPIRPDYVVDDLAEA 75
 
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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