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Conserved domains on  [gi|2648343523|ref|WP_324488457.1|]
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HAD family hydrolase

Protein Classification

HAD family hydrolase( domain architecture ID 11425524)

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

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|7966317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
19-234 4.56e-48

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


:

Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 157.78  E-value: 4.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAvepgLARQLEEEYMDQYM 98
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDE----ELEELLARFRELYE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:COG0546    77 EELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2648343523 179 AAAALLVGDSYMDASCARLSQVGFAAHLGGYAvHPGDLLPHMTS--FSDYNEFTNWVL 234
Cdd:COG0546   157 PEEVLMVGDSPHDIEAARAAGVPFIGVTWGYG-SAEELEAAGADyvIDSLAELLALLA 213
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
19-234 4.56e-48

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 157.78  E-value: 4.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAvepgLARQLEEEYMDQYM 98
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDE----ELEELLARFRELYE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:COG0546    77 EELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2648343523 179 AAAALLVGDSYMDASCARLSQVGFAAHLGGYAvHPGDLLPHMTS--FSDYNEFTNWVL 234
Cdd:COG0546   157 PEEVLMVGDSPHDIEAARAAGVPFIGVTWGYG-SAEELEAAGADyvIDSLAELLALLA 213
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 21-233 3.41e-40

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 137.83  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMQR 100
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGHGAPALIRRAFAAAGEDLDGPLHDALLARFLDHYEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAA 180
Cdd:cd07512    81 PPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2648343523 181 AALLVGDSYMDASCARLSQVGFAAHLGGYAVHPGDLLPHMTSFSDYNEFTNWV 233
Cdd:cd07512   161 RALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAELPHDAVFSDFDALPDLL 213
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
14-239 3.54e-35

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 124.92  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  14 NKNAQFRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEY 93
Cdd:PRK13222    1 MKFMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGNGADVLVERALTWAGREPDEELLEKLRELF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  94 MDQYmQRWLPA-APLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGmGDA-PRPKPAADPLLMV 171
Cdd:PRK13222   81 DRHY-AENVAGgSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIG-GDSlPNKKPDPAPLLLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 172 IERMGIPAAAALLVGDSYMDASCARLSQVGFAAHLGGY--AVHPGDLLPHMTsFSDYNEFTnWVLGRQSA 239
Cdd:PRK13222  159 CEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYnyGEPIALSEPDVV-IDHFAELL-PLLGLALS 226
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
22-204 8.73e-34

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 120.00  E-value: 8.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  22 IIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMqrw 101
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 102 lpaAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAAA 181
Cdd:pfam13419  78 ---VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154

                         170       180
                  ....*....|....*....|...
gi 2648343523 182 ALLVGDSYMDASCARLSQVGFAA 204
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKVIA 177
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 21-188 5.57e-15

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: 70.53  E-value: 5.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTlPSLSAAANSVLGQAGLHEVstplLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMqR 100
Cdd:TIGR01509   1 AILFDLDGVLVDT-EFAIAKLINREELGLVPDE----LGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQI-E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPAAPLFDHVHEALLALKALDMRLGICTNRDRAsTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAA 180
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPS 153


                  ....*...
gi 2648343523 181 AALLVGDS 188
Cdd:TIGR01509 154 ECVFVDDS 161
 
Name Accession Description Interval E-value
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
19-234 4.56e-48

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 157.78  E-value: 4.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAvepgLARQLEEEYMDQYM 98
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPDE----ELEELLARFRELYE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:COG0546    77 EELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2648343523 179 AAAALLVGDSYMDASCARLSQVGFAAHLGGYAvHPGDLLPHMTS--FSDYNEFTNWVL 234
Cdd:COG0546   157 PEEVLMVGDSPHDIEAARAAGVPFIGVTWGYG-SAEELEAAGADyvIDSLAELLALLA 213
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 21-233 3.41e-40

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 137.83  E-value: 3.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMQR 100
Cdd:cd07512     1 AVIFDLDGTLIDSAPDLHAALNAVLAAEGLAPLSLAEVRSFVGHGAPALIRRAFAAAGEDLDGPLHDALLARFLDHYEAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAA 180
Cdd:cd07512    81 PPGLTRPYPGVIEALERLRAAGWRLAICTNKPEAPARALLSALGLADLFAAVVGGDTLPQRKPDPAPLRAAIRRLGGDVS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2648343523 181 AALLVGDSYMDASCARLSQVGFAAHLGGYAVHPGDLLPHMTSFSDYNEFTNWV 233
Cdd:cd07512   161 RALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAELPHDAVFSDFDALPDLL 213
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
14-239 3.54e-35

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 124.92  E-value: 3.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  14 NKNAQFRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEY 93
Cdd:PRK13222    1 MKFMDIRAVAFDLDGTLVDSAPDLAAAVNAALAALGLPPAGEERVRTWVGNGADVLVERALTWAGREPDEELLEKLRELF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  94 MDQYmQRWLPA-APLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGmGDA-PRPKPAADPLLMV 171
Cdd:PRK13222   81 DRHY-AENVAGgSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFSVVIG-GDSlPNKKPDPAPLLLA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 172 IERMGIPAAAALLVGDSYMDASCARLSQVGFAAHLGGY--AVHPGDLLPHMTsFSDYNEFTnWVLGRQSA 239
Cdd:PRK13222  159 CEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGVTYGYnyGEPIALSEPDVV-IDHFAELL-PLLGLALS 226
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
22-204 8.73e-34

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 120.00  E-value: 8.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  22 IIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMqrw 101
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLRKYNEELHDKL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 102 lpaAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAAA 181
Cdd:pfam13419  78 ---VKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKPDPDPILKALEQLGLKPEE 154

                         170       180
                  ....*....|....*....|...
gi 2648343523 182 ALLVGDSYMDASCARLSQVGFAA 204
Cdd:pfam13419 155 VIYVGDSPRDIEAAKNAGIKVIA 177
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 21-196 2.23e-31

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: 114.64  E-value: 2.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSI--ALQASAVEPgLARQLEEEYMDQYM 98
Cdd:cd16417     1 LVAFDLDGTLVDSAPDLAEAANAMLAALGLPPLPEETVRTWIGNGADVLVERALtgAREAEPDEE-LFKEARALFDRHYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:cd16417    80 ETLSVHSHLYPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFSLVLGGDSLPEKKPDPAPLLHACEKLGIA 159

                         170
                  ....*....|....*...
gi 2648343523 179 AAAALLVGDSYMDASCAR 196
Cdd:cd16417   160 PAQMLMVGDSRNDILAAR 177
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 19-217 3.57e-28

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: 106.21  E-value: 3.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVStpllraalNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYM 98
Cdd:cd02616     1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYT--------REEVLPFIGPPLRETFEKIDPDKLEDMVEEFRKYYR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:cd02616    73 EHNDDLTKEYPGVYETLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAE 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2648343523 179 AAAALLVGDSYMDASCARLSQVGFAAhlGGYAVHPGDLL 217
Cdd:cd02616   153 PEEALMVGDSPHDILAGKNAGVKTVG--VTWGYKGREYL 189
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
18-188 5.07e-28

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 106.06  E-value: 5.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  18 QFRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLhEVSTPLLRA----ALNEGLRpMFRQSIALQASAVEpgLARQLEEEY 93
Cdd:COG0637     1 MIKAVIFDMDGTLVDSEPLHARAWREAFAELGI-DLTEEEYRRlmgrSREDILR-YLLEEYGLDLPEEE--LAARKEELY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  94 MDQYMQRwlpAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIE 173
Cdd:COG0637    77 RELLAEE---GLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVIVTGDDVARGKPDPDIYLLAAE 153

                         170
                  ....*....|....*
gi 2648343523 174 RMGIPAAAALLVGDS 188
Cdd:COG0637   154 RLGVDPEECVVFEDS 168
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 19-233 1.18e-27

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: 105.11  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLL---RAALNEGLRPMFRQSI----ALQASAVEPGLArqLEE 91
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAeayRAIEYALWRRYERGEItfaeLLRRLLEELGLD--LAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  92 EYMDQYMQRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMV 171
Cdd:COG1011    79 ELAEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVGVRKPDPEIFELA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648343523 172 IERMGIPAAAALLVGDSY-MDASCARlsQVGFAAHL--GGYAVHPGDLLPHMTsFSDYNEFTNWV 233
Cdd:COG1011   159 LERLGVPPEEALFVGDSPeTDVAGAR--AAGMRTVWvnRSGEPAPAEPRPDYV-ISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 19-192 6.61e-23

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: 92.26  E-value: 6.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAA----------ANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLARQ 88
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAiaelasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  89 LEEEYMDQYMQRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPL 168
Cdd:pfam00702  81 TVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY 160

                         170       180
                  ....*....|....*....|....
gi 2648343523 169 LMVIERMGIPAAAALLVGDSYMDA 192
Cdd:pfam00702 161 LAALERLGVKPEEVLMVGDGVNDI 184
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 20-209 1.94e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 79.14  E-value: 1.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIA--LQASAVEPGLARQLEEEYMDQY 97
Cdd:PRK13223   14 RLVMFDLDGTLVDSVPDLAAAVDRMLLELGRPPAGLEAVRHWVGNGAPVLVRRALAgsIDHDGVDDELAEQALALFMEAY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  98 MQRWlPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGI 177
Cdd:PRK13223   94 ADSH-ELTVVYPGVRDTLKWLKKQGVEMALITNKPERFVAPLLDQMKIGRYFRWIIGGDTLPQKKPDPAALLFVMKMAGV 172

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2648343523 178 PAAAALLVGDSYMDASCARLSQVGFAAHLGGY 209
Cdd:PRK13223  173 PPSQSLFVGDSRSDVLAAKAAGVQCVALSYGY 204
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 20-217 2.86e-17

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 77.97  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSIALQASAVEPGLArqleEEYMDQYMQ 99
Cdd:PRK13226   13 RAVLFDLDGTLLDSAPDMLATVNAMLAARGRAPITLAQLRPVVSKGARAMLAVAFPELDAAARDALI----PEFLQRYEA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 100 RWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPA 179
Cdd:PRK13226   89 LIGTQSQLFDGVEGMLQRLECAGCVWGIVTNKPEYLARLILPQLGWEQRCAVLIGGDTLAERKPHPLPLLVAAERIGVAP 168

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2648343523 180 AAALLVGDSYMDASCARLSQVGFAAHLGGYAVHPGDLL 217
Cdd:PRK13226  169 TDCVYVGDDERDILAARAAGMPSVAALWGYRLHDDDPL 206
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 22-196 3.38e-17

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: 77.05  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  22 IIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRA----ALNEGLRPMFRQsialqasaVEPGLARQLE--EEYMD 95
Cdd:cd07533     2 VIFDWDGTLADSQHNIVAAMTAAFADLGLPVPSAAEVRSiiglSLDEAIARLLPM--------ATPALVAVAEryKEAFD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  96 QYMQRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAP-RPKPAadpllMVIER 174
Cdd:cd07533    74 ILRLLPEHAEPLFPGVREALDALAAQGVLLAVATGKSRRGLDRVLEQHGLGGYFDATRTADDTPsKPHPE-----MLREI 148

                         170       180
                  ....*....|....*....|....*
gi 2648343523 175 M---GIPAAAALLVGDSYMDASCAR 196
Cdd:cd07533   149 LaelGVDPSRAVMVGDTAYDMQMAA 173
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 20-191 3.85e-17

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 77.38  E-value: 3.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDTlpslsaaaNSVLGQAGLHEVSTPLLRAALNEGLRPMFRQSI-----ALQASAVEPGLA--RQLEEE 92
Cdd:PRK13288    4 NTVLFDLDGTLINT--------NELIISSFLHTLKTYYPNQYKREDVLPFIGPSLhdtfsKIDESKVEEMITtyREFNHE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  93 YMDQYMQrwlpaapLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVI 172
Cdd:PRK13288   76 HHDELVT-------EYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDVVITLDDVEHAKPDPEPVLKAL 148

                         170
                  ....*....|....*....
gi 2648343523 173 ERMGIPAAAALLVGDSYMD 191
Cdd:PRK13288  149 ELLGAKPEEALMVGDNHHD 167
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 107-204 1.08e-16

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: 73.20  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 107 LFD-----HVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAAA 181
Cdd:cd01427     3 LFDldgtlLAVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEE 82

                          90       100
                  ....*....|....*....|...
gi 2648343523 182 ALLVGDSYMDASCARLSQVGFAA 204
Cdd:cd01427    83 VLFVGDSENDIEAARAAGGRTVA 105
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 21-188 5.57e-15

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: 70.53  E-value: 5.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTlPSLSAAANSVLGQAGLHEVstplLRAALNEGLRPMFRQSIALQASAVEPGLARQLEEEYMDQYMqR 100
Cdd:TIGR01509   1 AILFDLDGVLVDT-EFAIAKLINREELGLVPDE----LGVSAVGRLELALRRFKAQYGRTISPEDAQLLYKQLFYEQI-E 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPAAPLFDHVHEALLALKALDMRLGICTNRDRAsTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAA 180
Cdd:TIGR01509  75 EEAKLKPLPGVRALLEALRARGKKLALLTNSPRA-HKLVLALLGLRDLFDVVIDSSDVGLGKPDPDIYLQALKALGLEPS 153


                  ....*...
gi 2648343523 181 AALLVGDS 188
Cdd:TIGR01509 154 ECVFVDDS 161
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 21-188 1.50e-14

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: 68.41  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPslsaaansvlgqagLHEVstpllraalneglrpmfrqsialqasavepglARQLEEEYMDQYMQR 100
Cdd:cd07505     1 AVIFDMDGVLIDTEP--------------LHRQ--------------------------------AWQLLERKNALLLEL 34

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPA-APLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGI-AGLFDTVVGMGDAPRPKPAADPLLMVIERMGIP 178
Cdd:cd07505    35 IASEgLKLKPGVVELLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFDVIVSGDDVERGKPAPDIYLLAAERLGVD 114

                         170
                  ....*....|
gi 2648343523 179 AAAALLVGDS 188
Cdd:cd07505   115 PERCLVFEDS 124
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 20-196 2.48e-14

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: 69.60  E-value: 2.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDTLPSLSAAANSVLGqaGLHEVStPLLRAALNE--GLRPMFRQSI--------ALQASAVEPGLArqL 89
Cdd:cd02588     1 KALVFDVYGTLIDWHSGLAAAERAFPG--RGEELS-RLWRQKQLEytWLVTLMGPYVdfdeltrdALRATAAELGLE--L 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  90 EEEYMDQYMQRWLPAAPlFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLL 169
Cdd:cd02588    76 DESDLDELGDAYLRLPP-FPDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFDAVLSAEDVRAYKPAPAVYE 154

                         170       180
                  ....*....|....*....|....*..
gi 2648343523 170 MVIERMGIPAAAALLVGDSYMDASCAR 196
Cdd:cd02588   155 LAAERLGVPPDEILHVASHAWDLAGAR 181
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 21-188 3.42e-12

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: 62.66  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLsaaansvlgqaglHEVSTPLLRAALNEGLrpmfrqsialqasavepglARQLEEeymdqymqr 100
Cdd:cd16423     1 AVIFDFDGVIVDTEPLW-------------YEAWQELLNERRNELI-------------------KRQFSE--------- 39

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 wLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAA 180
Cdd:cd16423    40 -KTDLPPIEGVKELLEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPE 118


                  ....*...
gi 2648343523 181 AALLVGDS 188
Cdd:cd16423   119 ECVVIEDS 126
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 21-196 4.40e-12

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: 62.41  E-value: 4.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAansvlgqaglhevstplLRAALNE--GLRPMFRQSIALQASAVEpGLARQLE---EEYMD 95
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRA-----------------FPQTFEEfgLDPASFKALKQAGGLAEE-EWYRIATsalEELQG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  96 QYMQRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIaGLFDTVVGMGDAPRPKPAADPLLMVIERM 175
Cdd:TIGR01549  63 RFWSEYDAEEAYIRGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGL-GDYFELILVSDEPGSKPEPEIFLAALESL 141

                         170       180
                  ....*....|....*....|.
gi 2648343523 176 GIPaAAALLVGDSYMDASCAR 196
Cdd:TIGR01549 142 GVP-PEVLHVGDNLNDIEGAR 161
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 19-188 7.88e-12

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: 61.97  E-value: 7.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHevstplLRAALNEGLRPMFRQSIA---LQASAVEPGLAR--QLEEEY 93
Cdd:TIGR02009   1 YKAVIFDMDGVITDTAPLHAQAWKHIAAKYGIS------FDKQYNESLKGLSREDILraiLKLRGDGLSLEEihQLAERK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  94 MDQYmQRWLPAAP--LFDHVHEALLALKALDMRLGICTNrdRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMV 171
Cdd:TIGR02009  75 NELY-RELLRLTGvaVLPGIRNLLKRLKAKGIAVGLGSS--SKNAPRILAKLGLRDYFDAIVDASEVKNGKPHPETFLLA 151

                         170
                  ....*....|....*..
gi 2648343523 172 IERMGIPAAAALLVGDS 188
Cdd:TIGR02009 152 AELLGVPPNECIVFEDA 168
PRK13225 PRK13225
phosphoglycolate phosphatase; Provisional
 19-204 1.53e-11

phosphoglycolate phosphatase; Provisional


Pssm-ID: 106187 [Multi-domain]  Cd Length: 273  Bit Score: 62.81  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAalnegLRPMFRQSIALQASAVEPGLARQLEEeyMDQYM 98
Cdd:PRK13225   62 LQAIIFDFDGTLVDSLPTVVAIANAHAPDFGYDPIDERDYAQ-----LRQWSSRTIVRRAGLSPWQQARLLQR--VQRQL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  99 QRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFdTVVGMGDAPRPKPAAdpLLMVIERMGIP 178
Cdd:PRK13225  135 GDCLPALQLFPGVADLLAQLRSRSLCLGILSSNSRQNIEAFLQRQGLRSLF-SVVQAGTPILSKRRA--LSQLVAREGWQ 211

                         170       180
                  ....*....|....*....|....*.
gi 2648343523 179 AAAALLVGDSYMDASCARlsQVGFAA 204
Cdd:PRK13225  212 PAAVMYVGDETRDVEAAR--QVGLIA 235
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 19-196 3.73e-11

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: 60.43  E-value: 3.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  19 FRAIIFDVDGTLFDtLPSLSAAANSVLGQAGlHEVSTpLLRAALNEG---LRPM-----FRQ--SIALQASAVEPGLArq 88
Cdd:TIGR01428   1 IKALVFDVYGTLFD-VHSVAERAAELYGGRG-EALSQ-LWRQKQLEYswlRTLMgpykdFWDltREALRYLLGRLGLE-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  89 LEEEYMDQYMQRWLPAAPlFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPL 168
Cdd:TIGR01428  76 DDESAADRLAEAYLRLPP-HPDVPAGLRALKERGYRLAILSNGSPAMLKSLVKHAGLDDPFDAVLSADAVRAYKPAPQVY 154

                         170       180
                  ....*....|....*....|....*...
gi 2648343523 169 LMVIERMGIPAAAALLVGDSYMDASCAR 196
Cdd:TIGR01428 155 QLALEALGVPPDEVLFVASNPWDLGGAK 182
PRK10725 PRK10725
fructose-1-phosphate/6-phosphogluconate phosphatase;
17-188 5.59e-11

fructose-1-phosphate/6-phosphogluconate phosphatase;


Pssm-ID: 182679 [Multi-domain]  Cd Length: 188  Bit Score: 59.70  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  17 AQFRAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLraALNEGlrPMFR--QSI-ALQASAVEPglaRQLEEEY 93
Cdd:PRK10725    3 DRYAGLIFDMDGTILDTEPTHRKAWREVLGRYGLQFDEQAMV--ALNGS--PTWRiaQAIiELNQADLDP---HALAREK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  94 MDqymqrwLPAAPLFDHVHEALLA--LKALDMR--LGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLL 169
Cdd:PRK10725   76 TE------AVKSMLLDSVEPLPLIevVKAWHGRrpMAVGTGSESAIAEALLAHLGLRRYFDAVVAADDVQHHKPAPDTFL 149

                         170
                  ....*....|....*....
gi 2648343523 170 MVIERMGIPAAAALLVGDS 188
Cdd:PRK10725  150 RCAQLMGVQPTQCVVFEDA 168
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 21-211 9.58e-10

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 56.60  E-value: 9.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAG-----LHEVSTpLLRAALNEGLR----PMFRQsialqasavePGLARQLEe 91
Cdd:cd04303     1 LIIFDFDGTLADSFPWFLSILNQLAARHGfktvdEEEIEQ-LRQLSSREILKqlgvPLWKL----------PLIAKDFR- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  92 eymdQYMQRWLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDtvVGMGDAPRPKPAAdpLLMV 171
Cdd:cd04303    69 ----RLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA--VIEGSSLFGKAKK--IRRV 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2648343523 172 IERMGIPAAAALLVGDSYMDASCARLSQVGFAAHLGGYAV 211
Cdd:cd04303   141 LRRTKITAAQVIYVGDETRDIEAARKVGLAFAAVSWGYAK 180
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 21-191 6.86e-09

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 53.54  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAalnegLRPMFRQSiALQASAVEPGLA---RQLEEEYMDQY 97
Cdd:cd07523     1 NFIWDLDGTLLDSYPAMTKALSETLADFGIPQDLETVYKI-----IKESSVQF-AIQYYAEVPDLEeeyKELEAEYLAKP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  98 MqrwlpaapLFDHVHEALLALKALDMRLGICTNRDRASTDvLLTQAGIAGLFDTVVGMGDA-PRpKPAADPLLMVIERMG 176
Cdd:cd07523    75 I--------LFPGAKAVLRWIKEQGGKNFLMTHRDHSALT-ILKKDGIASYFTEIVTSDNGfPR-KPNPEAINYLLNKYQ 144

                         170
                  ....*....|....*
gi 2648343523 177 IPAAAALLVGDSYMD 191
Cdd:cd07523   145 LNPEETVMIGDRELD 159
HAD_CbbY-like cd07528
subfamily of beta-phosphoglucomutase-like family, similar to Rhodobacter sphaeroides ...
 21-188 8.72e-08

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: 50.84  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPS-LSAAANSVLGQAGLH-----EVSTPLLRAAlnEGLRPMFRQSialqaSAVEPGLARQLEEEYM 94
Cdd:cd07528     1 ALIFDVDGTLAETEELhRRAFNNAFFAERGLDwywdrELYGELLRVG--GGKERIAAYF-----EKVGWPESAPKDLKEL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  95 DQYMQRW-------LPAA---PLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQA-GIAG--LFDTVVGMGDAPRP 161
Cdd:cd07528    74 IADLHKAkteryaeLIAAgllPLRPGVARLIDEAKAAGVRLAIATTTSPANVDALLSALlGPERraIFDAIAAGDDVAEK 153

                         170       180
                  ....*....|....*....|....*..
gi 2648343523 162 KPAADPLLMVIERMGIPAAAALLVGDS 188
Cdd:cd07528   154 KPDPDIYLLALERLGVSPSDCLAIEDS 180
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 20-196 1.29e-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: 47.66  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVStpllrAALNEGLRPMFRQS---------------------IALQA 78
Cdd:TIGR02252   1 KLITFDAVGTLLALKEPVGEVYCEIARKYGVEVSP-----DELEQAFRKAFKAMseafpnfgfssgltpqqwwqkLVRDT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  79 SAVEPGLARQLEEEYMDQYMQRWLPAAP--LFDHVHEALLALKALDMRLGICTNRDRaSTDVLLTQAGIAGLFDTVVGMG 156
Cdd:TIGR02252  76 FGRAGVPDPESFEKIFEELYSYFATPEPwqVYPDAIKLLKDLRERGLILGVISNFDS-RLRGLLEALGLLEYFDFVVTSY 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2648343523 157 DAPRPKPaaDPL--LMVIERMGIPAAAALLVGDSY-MDASCAR 196
Cdd:TIGR02252 155 EVGAEKP--DPKifQEALERAGISPEEALHIGDSLrNDYQGAR 195
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 113-225 2.28e-06

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: 45.75  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 113 EALLALKALDMRLGICTNRDRaSTDVLLTQAGIAGLFDTVVGMGDAPRPKPaaDPLLM--VIERMGIPAAAALLVGDSY- 189
Cdd:cd16415    14 ETLKDLKEKGLKLAVVSNFDR-RLRELLEALGLDDYFDFVVFSYEVGYEKP--DPRIFqkALERLGVSPEEALHVGDDLk 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2648343523 190 MDASCARlsQVGFAAHLggyaVHPGDLLPHMTSFSD 225
Cdd:cd16415    91 NDYLGAR--AVGWHALL----VDREGALHELPSLAN 120
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 107-189 2.53e-06

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: 45.23  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 107 LFDHVHEALLALKAlDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAAAALLVG 186
Cdd:cd04305    10 LLPGAKELLEELKK-GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVG 88


                  ...
gi 2648343523 187 DSY 189
Cdd:cd04305    89 DSL 91
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 111-200 4.17e-06

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; 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: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 44.37  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 111 VHEALLALKALDMRLGICTNRDRASTDVLLTQAGiAGLFDTVVGMGDAPRPKPAADPLLMVIERMGIPAAAALLVGDSYM 190
Cdd:cd16421    12 ILELLKALRQKGIKLAVLSNKPNEAVQVLVEELF-PGSFDFVLGEKEGIRRKPDPT*ALECAKVLGVPPDEVLYVGDSGV 90

                          90
                  ....*....|
gi 2648343523 191 DASCARLSQV 200
Cdd:cd16421    91 DMQTARNAGM 100
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 21-191 4.21e-06

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: 46.05  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLHEVSTPLLRAALNEGLRPMFRQsiALQASavePGLARQLEEEYMDQYMQR 100
Cdd:cd04302     1 TILFDLDGTLTDSAEGITASVQYALEELGIPVPDESELRRFIGPPLEDSFRE--LLPFD---EEEAQRAVDAYREYYKEK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 WLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVG--MGDAPRPKpaADPLLMVIERMGIP 178
Cdd:cd04302    76 GLFENEVYPGIPELLEKLKAAGYRLYVATSKPEVFARRILEHFGLDEYFDGIAGasLDGSRVHK--ADVIRYALDTLGIA 153

                         170
                  ....*....|...
gi 2648343523 179 AAAALLVGDSYMD 191
Cdd:cd04302   154 PEQAVMIGDRKHD 166
PLN03243 PLN03243
haloacid dehalogenase-like hydrolase; Provisional
 85-217 5.94e-06

haloacid dehalogenase-like hydrolase; Provisional


Pssm-ID: 215644 [Multi-domain]  Cd Length: 260  Bit Score: 46.18  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  85 LARQLEEEYmdQYMQ----RWLPAAplfdhvHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAPR 160
Cdd:PLN03243   92 LAIRKEDLY--EYMQgglyRLRPGS------REFVQALKKHEIPIAVASTRPRRYLERAIEAVGMEGFFSVVLAAEDVYR 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 161 PKPAADPLLMVIERMGIPAAAALLVGDSYMDASCA---RLSQVGFAAHLGGYAVHPGDLL 217
Cdd:PLN03243  164 GKPDPEMFMYAAERLGFIPERCIVFGNSNSSVEAAhdgCMKCVAVAGKHPVYELSAGDLV 223
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 107-212 1.68e-05

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; 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: 319817 [Multi-domain]  Cd Length: 131  Bit Score: 43.18  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 107 LFDHVHEALLALKAlDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDAprpkpAADPLLMVIERMGIPAAAALLVG 186
Cdd:cd07515    18 LLPGVREALAALKA-DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVVSEK-----DPDTYRRVLSRYGIGPERFVMVG 91

                          90       100
                  ....*....|....*....|....*.
gi 2648343523 187 DSYMdascarlSQVGFAAHLGGYAVH 212
Cdd:cd07515    92 NSLR-------SDILPVLAAGGWGVH 110
HAD pfam12710
haloacid dehalogenase-like hydrolase;
22-196 3.00e-05

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 43.29  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  22 IIFDVDGTLFDTlPSLSAAANSVLGQAGLHEVST--PLLRAALNEGL----RPMFRQSIALQASAVEPGLARQLEEEYMD 95
Cdd:pfam12710   1 ALFDLDGTLLDG-DSLFLLIRALLRRGGPDLWRAllVLLLLALLRLLgrlsRAGARELLRALLAGLPEEDAAELERFVAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  96 QYMQRWLPAAplfdhvHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGD--------------APRP 161
Cdd:pfam12710  80 VALPRLHPGA------LELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDgrftgelrligppcAGEG 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2648343523 162 KPAADPLLMVIERMGIPAAAALLVGDSYMDASCAR 196
Cdd:pfam12710 154 KVRRLRAWLAARGLGLDLADSVAYGDSPSDLPMLR 188
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 20-206 6.66e-05

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: 42.33  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  20 RAIIFDVDGTLFDT-----LPSLSAAANSVLGqAGLHEVSTPLLRAALNEGLRPM--FRQSIALQasavepgLARQLEEE 92
Cdd:cd02603     2 RAVLFDFGGVLIDPdpaaaVARFEALTGEPSE-FVLDTEGLAGAFLELERGRITEeeFWEELREE-------LGRPLSAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  93 YMDQYMQRWLpaaPLFDHVHEALLALKALDMRLGICTN-RDRASTDVLLTQAGIAGLFDTVVGMGDAPRPKPAADPLLMV 171
Cdd:cd02603    74 LFEELVLAAV---DPNPEMLDLLEALRAKGYKVYLLSNtWPDHFKFQLELLPRRGDLFDGVVESCRLGVRKPDPEIYQLA 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2648343523 172 IERMGIPAAAALLVGDsyMDASCARLSQVGFAAHL 206
Cdd:cd02603   151 LERLGVKPEEVLFIDD--REENVEAARALGIHAIL 183
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 21-188 1.15e-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: 41.15  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGLhevstpLLRAALNEGLRPMfrqsialqasavepglarqleeeymdqymqr 100
Cdd:cd07526     2 LVIFDCDGVLVDSEVIAARVLVEVLAELGA------RVLAAFEAELQPI------------------------------- 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 101 wlpaaplfDHVHEALLALkalDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMG-DAPRPKPAADPLLMVIERMGIPA 179
Cdd:cd07526    45 --------PGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEGRIFSAsDVGRGKPAPDLFLHAAAQMGVAP 113


                  ....*....
gi 2648343523 180 AAALLVGDS 188
Cdd:cd07526   114 ERCLVIEDS 122
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 21-188 1.88e-04

subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p); This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong 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), 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: 319829 [Multi-domain]  Cd Length: 205  Bit Score: 41.18  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  21 AIIFDVDGTLFDTLPSLSAAANSVLGQAGL--HEVstpllrAALNEGLRPmfRQSIA-LQASAVEPGLARQLEEEYMDQY 97
Cdd:cd07527     1 ALLFDMDGTLVDSTPAVERAWHKWAKEHGVdpEEV------LKVSHGRRA--IDVIRkLAPDDADIELVLALETEEPESY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523  98 mqrwLPAAPLFDHVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIaGLFDTVVGMGDAPRPKPAADPLLMVIERMGI 177
Cdd:cd07527    73 ----PEGVIAIPGAVDLLASLPAAGDRWAIVTSGTRALAEARLEAAGL-PHPEVLVTADDVKNGKPDPEPYLLGAKLLGL 147

                         170
                  ....*....|.
gi 2648343523 178 PAAAALLVGDS 188
Cdd:cd07527   148 DPSDCVVFEDA 158
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
 110-191 2.79e-04

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 41.13  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2648343523 110 HVHEALLALKALDMRLGICTNRDRASTDVLLTQAGIAGLF-DTVVGMGDAPRPKPAADPLLMVIERMGIPAAAALL-VGD 187
Cdd:cd02586   102 GVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRpDSLVTPDDVPAGRPYPWMCYKNAIELGVYDVAAVVkVGD 181


                  ....
gi 2648343523 188 SYMD 191
Cdd:cd02586   182 TVPD 185
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 117-190 7.24e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 39.15  E-value: 7.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2648343523 117 ALKALDMRLGICTNRDRASTDVLLTQAGIAGLFDTVVGMGDA-PRPKPAADPLLMVIERMGIPAAAALLVGDSYM 190
Cdd:cd02604    91 LLLALPGRKIIFTNASKNHAIRVLKRLGLADLFDGIFDIEYAgPDPKPHPAAFEKAIREAGLDPKRAAFFDDSIR 165
 
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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