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Conserved domains on  [gi|15600474|ref|NP_253968|]
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hydrolase [Pseudomonas aeruginosa PAO1]

Protein Classification

HAD family hydrolase( domain architecture ID 11436852)

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-228 4.40e-54

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: 172.91  E-value: 4.40e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   5 RLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLGPvpIEHLWAIRTRLLDREPMLRHRLSELRRRILFHALLDagyp 84
Cdd:COG1011   2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEEL--AEAYRAIEYALWRRYERGEITFAELLRRLLEELGLD---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  85 qaeaesLAEAGFQVFLEARHR-VTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGVGK 157
Cdd:COG1011  76 ------LAEELAEAFLAALPElVEPYPDALELLEALKARgYRLALLTNGSAElqeakLRRLGLDDLFDAVVSSEEVGVRK 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600474 158 PDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAELPALL 228
Cdd:COG1011 150 PDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-228 4.40e-54

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: 172.91  E-value: 4.40e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   5 RLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLGPvpIEHLWAIRTRLLDREPMLRHRLSELRRRILFHALLDagyp 84
Cdd:COG1011   2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEEL--AEAYRAIEYALWRRYERGEITFAELLRRLLEELGLD---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  85 qaeaesLAEAGFQVFLEARHR-VTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGVGK 157
Cdd:COG1011  76 ------LAEELAEAFLAALPElVEPYPDALELLEALKARgYRLALLTNGSAElqeakLRRLGLDDLFDAVVSSEEVGVRK 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600474 158 PDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAELPALL 228
Cdd:COG1011 150 PDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
4-228 5.68e-38

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 132.17  E-value: 5.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    4 LRLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLGPVPIEHLWAIRTRLLDREPMLRHRLSELRRRILFHALLDAGY 83
Cdd:PRK10748  10 ISALTFDLDDTLYDNRPVILRTEQEALAFVQNYHPALRSFQNEDLQRLRQALREAEPEIYHDVTRWRWRAIEQAMLDAGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   84 PQAEAESLAEAGFQVFLEARHRVTLFPEVHPTLEILADRFTLGVLTNGNADVRRLGLADYFRFALCAEELGVGKPDPTPF 163
Cdd:PRK10748  90 SAEEASAGADAAMINFAKWRSRIDVPQATHDTLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMY 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600474  164 REALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSG----KPWAGEEEPSAEIRSLAELPALL 228
Cdd:PRK10748 170 HLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQACWINPENgdlmQTWDSRLLPHIEISRLASLTSLI 238
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 107-202 6.75e-28

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: 102.24  E-value: 6.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 107 TLFPEVHPTLEILADRFTLGVLTNGNADV-----RRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIG 181
Cdd:cd04305   9 TLLPGAKELLEELKKGYKLGIITNGPTEVqweklEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVG 88

                        90       100
                ....*....|....*....|.
gi 15600474 182 DHPSDDIAGARRAGMRAIWFN 202
Cdd:cd04305  89 DSLESDILGAKNAGIKTVWFN 109
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 5-224 6.93e-28

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 105.65  E-value: 6.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     5 RLVTFDLDDTLWDVAPvmNNAEALLREWLASNaarlgpVPI------------EHLWairtRLLDREPMLRHRLSELRRR 72
Cdd:TIGR02254   2 KTLLFDLDDTILDFQA--AEALALRLLFEDQG------IPLtedmfaqykeinQGLW----RAYEEGKITKDEVVNTRFS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    73 ILFHALldaGYPQAEAesLAEAGFQVFLEARHRvtLFPEVHPTLEILADRFTLGVLTNG-----NADVRRLGLADYFRFA 147
Cdd:TIGR02254  70 ALLKEY---NTEADEA--LLNQKYLRFLEEGHQ--LLPGAFELMENLQQKFRLYIVTNGvretqYKRLRKSGLFPFFDDI 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600474   148 LCAEELGVGKPDPTPFREALKRAG-VEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAEL 224
Cdd:TIGR02254 143 FVSEDAGIQKPDKEIFNYALERMPkFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
9-200 3.05e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.57  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     9 FDLDDTLWDVAPVMnnaEALLREWLASNAarLGPVPIEHLwaIRTRLLDREPMLRHRLSELRRRILFHALLDAgYPQAEA 88
Cdd:pfam13419   3 FDFDGTLLDTEELI---IKSFNYLLEEFG--YGELSEEEI--LKFIGLPLREIFRYLGVSEDEEEKIEFYLRK-YNEELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    89 ESLaeagfqvflearhrVTLFPEVHPTLEILADR-FTLGVLTNGNADV-----RRLGLADYFRFALCAEELGVGKPDPTP 162
Cdd:pfam13419  75 DKL--------------VKPYPGIKELLEELKEQgYKLGIVTSKSRENveeflKQLGLEDYFDVIVGGDDVEGKKPDPDP 140

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15600474   163 FREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIW 200
Cdd:pfam13419 141 ILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVIA 177
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-228 4.40e-54

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: 172.91  E-value: 4.40e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   5 RLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLGPvpIEHLWAIRTRLLDREPMLRHRLSELRRRILFHALLDagyp 84
Cdd:COG1011   2 KAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEEL--AEAYRAIEYALWRRYERGEITFAELLRRLLEELGLD---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  85 qaeaesLAEAGFQVFLEARHR-VTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGVGK 157
Cdd:COG1011  76 ------LAEELAEAFLAALPElVEPYPDALELLEALKARgYRLALLTNGSAElqeakLRRLGLDDLFDAVVSSEEVGVRK 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600474 158 PDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAELPALL 228
Cdd:COG1011 150 PDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRPDYVISDLAELLELL 220
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
4-228 5.68e-38

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 132.17  E-value: 5.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    4 LRLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLGPVPIEHLWAIRTRLLDREPMLRHRLSELRRRILFHALLDAGY 83
Cdd:PRK10748  10 ISALTFDLDDTLYDNRPVILRTEQEALAFVQNYHPALRSFQNEDLQRLRQALREAEPEIYHDVTRWRWRAIEQAMLDAGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   84 PQAEAESLAEAGFQVFLEARHRVTLFPEVHPTLEILADRFTLGVLTNGNADVRRLGLADYFRFALCAEELGVGKPDPTPF 163
Cdd:PRK10748  90 SAEEASAGADAAMINFAKWRSRIDVPQATHDTLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMY 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600474  164 REALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSG----KPWAGEEEPSAEIRSLAELPALL 228
Cdd:PRK10748 170 HLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQACWINPENgdlmQTWDSRLLPHIEISRLASLTSLI 238
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
4-230 3.24e-30

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 111.17  E-value: 3.24e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   4 LRLVTFDLDDTLWDVAPVMNNA--EALLREWLAsnaarlgPVPIEHLWAIRTRLLDRepmlrhrlselrrriLFHALLDA 81
Cdd:COG0546   1 IKLVLFDLDGTLVDSAPDIAAAlnEALAELGLP-------PLDLEELRALIGLGLRE---------------LLRRLLGE 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  82 gYPQAEAESLAEAgFQVFLEARH--RVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEEL 153
Cdd:COG0546  59 -DPDEELEELLAR-FRELYEEELldETRLFPGVRELLEALKARgIKLAVVTNKPREfaerlLEALGLDDYFDAIVGGDDV 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 154 GVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAI---WFNPSGKPWAgEEEPSAEIRSLAELPALLAR 230
Cdd:COG0546 137 PPAKPKPEPLLEALERLGLDPEEVLMVGDSPH-DIEAARAAGVPFIgvtWGYGSAEELE-AAGADYVIDSLAELLALLAE 214
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 107-202 6.75e-28

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: 102.24  E-value: 6.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 107 TLFPEVHPTLEILADRFTLGVLTNGNADV-----RRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIG 181
Cdd:cd04305   9 TLLPGAKELLEELKKGYKLGIITNGPTEVqweklEQLGIHKYFDHIVISEEVGVQKPNPEIFDYALNQLGVKPEETLMVG 88

                        90       100
                ....*....|....*....|.
gi 15600474 182 DHPSDDIAGARRAGMRAIWFN 202
Cdd:cd04305  89 DSLESDILGAKNAGIKTVWFN 109
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 5-224 6.93e-28

noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 162788 [Multi-domain]  Cd Length: 224  Bit Score: 105.65  E-value: 6.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     5 RLVTFDLDDTLWDVAPvmNNAEALLREWLASNaarlgpVPI------------EHLWairtRLLDREPMLRHRLSELRRR 72
Cdd:TIGR02254   2 KTLLFDLDDTILDFQA--AEALALRLLFEDQG------IPLtedmfaqykeinQGLW----RAYEEGKITKDEVVNTRFS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    73 ILFHALldaGYPQAEAesLAEAGFQVFLEARHRvtLFPEVHPTLEILADRFTLGVLTNG-----NADVRRLGLADYFRFA 147
Cdd:TIGR02254  70 ALLKEY---NTEADEA--LLNQKYLRFLEEGHQ--LLPGAFELMENLQQKFRLYIVTNGvretqYKRLRKSGLFPFFDDI 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600474   148 LCAEELGVGKPDPTPFREALKRAG-VEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAEL 224
Cdd:TIGR02254 143 FVSEDAGIQKPDKEIFNYALERMPkFSKEEVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEIRSLEEL 220
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 5-226 4.11e-27

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: 103.50  E-value: 4.11e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   5 RLVTFDLDDTLWDVAPVM--------NNAEALLREWLASNaarlgpvpIEHLWAirtrlldREPMLR-HRLSELRRRILF 75
Cdd:cd02588   1 KALVFDVYGTLIDWHSGLaaaerafpGRGEELSRLWRQKQ--------LEYTWL-------VTLMGPyVDFDELTRDALR 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  76 HALLDAGypqaeaESLAEAGFQVFLEARHRVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALC 149
Cdd:cd02588  66 ATAAELG------LELDESDLDELGDAYLRLPPFPDVVAGLRRLREAgYRLAILSNGSPDliedvVANAGLRDLFDAVLS 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600474 150 AEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIWFN-PSGKPWAGEEEPSAEIRSLAELPA 226
Cdd:cd02588 140 AEDVRAYKPAPAVYELAAERLGVPPDEILHVASHAW-DLAGARALGLRTAWINrPGEVPDPLGPAPDFVVPDLGELAD 216
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
9-200 3.05e-22

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 89.57  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     9 FDLDDTLWDVAPVMnnaEALLREWLASNAarLGPVPIEHLwaIRTRLLDREPMLRHRLSELRRRILFHALLDAgYPQAEA 88
Cdd:pfam13419   3 FDFDGTLLDTEELI---IKSFNYLLEEFG--YGELSEEEI--LKFIGLPLREIFRYLGVSEDEEEKIEFYLRK-YNEELH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    89 ESLaeagfqvflearhrVTLFPEVHPTLEILADR-FTLGVLTNGNADV-----RRLGLADYFRFALCAEELGVGKPDPTP 162
Cdd:pfam13419  75 DKL--------------VKPYPGIKELLEELKEQgYKLGIVTSKSRENveeflKQLGLEDYFDVIVGGDDVEGKKPDPDP 140

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15600474   163 FREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIW 200
Cdd:pfam13419 141 ILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVIA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-195 3.16e-22

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: 89.95  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     4 LRLVTFDLDDTLWDVAPVMNNAEALL---REWLASNAARLGPVPI------EHLWAIRTRLLDREPMLRHRLSELRRRIL 74
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELaseHPLAKAIVAAAEDLPIpvedftARLLLGKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    75 FHALLDAGYpqaeaeslaeagfqvFLEARHRVTLFPEVHPTLEILADR-FTLGVLTNGN-----ADVRRLGLADYFRFAL 148
Cdd:pfam00702  81 TVVLVELLG---------------VIALADELKLYPGAAEALKALKERgIKVAILTGDNpeaaeALLRLLGLDDYFDVVI 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15600474   149 CAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPsDDIAGARRAG 195
Cdd:pfam00702 146 SGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 136-228 9.33e-22

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: 86.96  E-value: 9.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 136 RRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNPSGKPwageeeps 215
Cdd:cd16415  41 EALGLDDYFDFVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLVDREGAL-------- 112

                        90
                ....*....|...
gi 15600474 216 AEIRSLAELPALL 228
Cdd:cd16415 113 HELPSLANLLERL 125
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 9-200 4.09e-20

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: 84.01  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     9 FDLDDTLWDVAPVMnnaeallreWLASNAARLGPVPIEhlwairtrlLDREPMLRHRLSELRRRILFHAlldagypQAEA 88
Cdd:TIGR01509   4 FDLDGVLVDTEFAI---------AKLINREELGLVPDE---------LGVSAVGRLELALRRFKAQYGR-------TISP 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    89 ESLAEAGFQVFLEARHR---VTLFPEVHPTLEIL-ADRFTLGVLTNGNAD----VRRLGLADYFRFALCAEELGVGKPDP 160
Cdd:TIGR01509  59 EDAQLLYKQLFYEQIEEeakLKPLPGVRALLEALrARGKKLALLTNSPRAhklvLALLGLRDLFDVVIDSSDVGLGKPDP 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15600474   161 TPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIW 200
Cdd:TIGR01509 139 DIYLQALKALGLEPSECVFVDDSPA-GIEAAKAAGMHTVG 177
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 7-229 2.49e-19

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: 82.75  E-value: 2.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   7 VTFDLDDTLWDVAPVMNNA-EALLREW---------LASNAARLGPVPIEHLWAIRTRLLDrepmlrhrlsELRRRILFH 76
Cdd:cd07512   2 VIFDLDGTLIDSAPDLHAAlNAVLAAEglaplslaeVRSFVGHGAPALIRRAFAAAGEDLD----------GPLHDALLA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  77 ALLDAGYPQAEAESlaeagfqvflearhrvTLFPEVHPTLEILADR-FTLGVLTN---GNAD--VRRLGLADYFRFALCA 150
Cdd:cd07512  72 RFLDHYEADPPGLT----------------RPYPGVIEALERLRAAgWRLAICTNkpeAPARalLSALGLADLFAAVVGG 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 151 EELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMR--AIWFNPSGKPWAgEEEPSAEIRSLAELPALL 228
Cdd:cd07512 136 DTLPQRKPDPAPLRAAIRRLGGDVSRALMVGDSET-DAATARAAGVPfvLVTFGYRHAPVA-ELPHDAVFSDFDALPDLL 213


                .
gi 15600474 229 A 229
Cdd:cd07512 214 A 214
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
4-224 9.78e-19

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 81.02  E-value: 9.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   4 LRLVTFDLDDTLWDVAPVMNNAealLREWLAsnaaRLGpvpiehlwairtrlLDREPMLRHRLSELRRRILFHALLDAGY 83
Cdd:COG0637   2 IKAVIFDMDGTLVDSEPLHARA---WREAFA----ELG--------------IDLTEEEYRRLMGRSREDILRYLLEEYG 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  84 PQAEAESLAEAGFQVFLE--ARHRVTLFPEVHPTLEILADR-FTLGVLTNG---NADV--RRLGLADYFRFALCAEELGV 155
Cdd:COG0637  61 LDLPEEELAARKEELYREllAEEGLPLIPGVVELLEALKEAgIKIAVATSSpreNAEAvlEAAGLLDYFDVIVTGDDVAR 140

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600474 156 GKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAEL 224
Cdd:COG0637 141 GKPDPDIYLLAAERLGVDPEECVVFEDSPA-GIRAAKAAGMRVVGVPDGGTAEEELAGADLVVDDLAEL 208
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 107-200 1.55e-18

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: 80.41  E-value: 1.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   107 TLFPEVHPTLEILADR-FTLGVLTNgnADVR------RLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIH 179
Cdd:TIGR02252 105 QVYPDAIKLLKDLRERgLILGVISN--FDSRlrglleALGLLEYFDFVVTSYEVGAEKPDPKIFQEALERAGISPEEALH 182

                          90       100
                  ....*....|....*....|.
gi 15600474   180 IGDHPSDDIAGARRAGMRAIW 200
Cdd:TIGR02252 183 IGDSLRNDYQGARAAGWRALL 203
PRK09449 PRK09449
dUMP phosphatase; Provisional
 107-228 1.79e-17

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 78.02  E-value: 1.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  107 TLFPEVHPTLEILADRFTLGVLTNGNAD---VR--RLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAI-HI 180
Cdd:PRK09449  95 TPLPGAVELLNALRGKVKMGIITNGFTElqqVRleRTGLRDYFDLLVISEQVGVAKPDVAIFDYALEQMGNPDRSRVlMV 174

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15600474  181 GDHPSDDIAGARRAGMRAIWFNPSGKPWAGEEEPSAEIRSLAELPALL 228
Cdd:PRK09449 175 GDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVSSLSELEQLL 222
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
1-230 4.41e-17

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 76.77  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    1 MSSLRLVTFDLDDTLWDVAPvmnnaeALLrewLASNAAR----LGPVPIEHlwaIRTRLLDREPMLRHRLSELRRRILFH 76
Cdd:PRK13222   3 FMDIRAVAFDLDGTLVDSAP------DLA---AAVNAALaalgLPPAGEER---VRTWVGNGADVLVERALTWAGREPDE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   77 ALLDAGYPqaeaeslaeagfqVFLE--ARH---RVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFR 145
Cdd:PRK13222  71 ELLEKLRE-------------LFDRhyAENvagGSRLYPGVKETLAALKAAgYPLAVVTNKPTPfvaplLEALGIADYFS 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  146 FALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIWFNP---SGKPWAgEEEPSAEIRSLA 222
Cdd:PRK13222 138 VVIGGDSLPNKKPDPAPLLLACEKLGLDPEEMLFVGDSRN-DIQAARAAGCPSVGVTYgynYGEPIA-LSEPDVVIDHFA 215


                 ....*...
gi 15600474  223 ELPALLAR 230
Cdd:PRK13222 216 ELLPLLGL 223
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 107-201 4.60e-17

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: 73.97  E-value: 4.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 107 TLFpeVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHI 180
Cdd:cd01427   9 TLL--AVELLKRLRAAgIKLAIVTNRSREalralLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFV 86

                        90       100
                ....*....|....*....|.
gi 15600474 181 GDHPsDDIAGARRAGMRAIWF 201
Cdd:cd01427  87 GDSE-NDIEAARAAGGRTVAV 106
HAD_type_II TIGR01428
2-haloalkanoic acid dehalogenase, type II; Catalyzes the hydrolytic dehalogenation of small ...
 4-207 5.23e-17

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: 76.22  E-value: 5.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     4 LRLVTFDLDDTLWDVAPVMNNAEALLREWLASnaarlgpvpIEHLWaiRTRLLD----REPMLRHR-LSELRRRILFHAL 78
Cdd:TIGR01428   1 IKALVFDVYGTLFDVHSVAERAAELYGGRGEA---------LSQLW--RQKQLEyswlRTLMGPYKdFWDLTREALRYLL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    79 ldAGYPQAEAESLAEAgfqvFLEARHRVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEE 152
Cdd:TIGR01428  70 --GRLGLEDDESAADR----LAEAYLRLPPHPDVPAGLRALKERgYRLAILSNGSPAmlkslVKHAGLDDPFDAVLSADA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15600474   153 LGVGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIaGARRAGMRAIWFNPSGKP 207
Cdd:TIGR01428 144 VRAYKPAPQVYQLALEALGVPPDEVLFVASNPWDLG-GAKKFGFKTAWINRPGEP 197
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 6-199 1.48e-16

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: 75.35  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   6 LVTFDLDDTLWDVAPVMNNA-EALLREwlasnaarLG--PVPIEhlwAIRTRLLDREPMLRHRlselrrrilfhALLDAG 82
Cdd:cd16417   1 LVAFDLDGTLVDSAPDLAEAaNAMLAA--------LGlpPLPEE---TVRTWIGNGADVLVER-----------ALTGAR 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  83 YpQAEAESLAEAGFQVFLEA-----RHRVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAE 151
Cdd:cd16417  59 E-AEPDEELFKEARALFDRHyaetlSVHSHLYPGVKEGLAALKAQgYPLACVTNKPERfvaplLEALGISDYFSLVLGGD 137

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15600474 152 ELGVGKPDPTPFREALKRAGVEASAAIHIGDhPSDDIAGARRAGMRAI 199
Cdd:cd16417 138 SLPEKKPDPAPLLHACEKLGIAPAQMLMVGD-SRNDILAARAAGCPSV 184
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 6-195 1.56e-16

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: 73.97  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     6 LVTFDLDDTLWDVAPVmnnAEALLREWLAsnAARLGPVPIEHLwaIRTRLLDREPMLRHRLSELRRRilfhalldagypQ 85
Cdd:TIGR01549   1 AILFDIDGTLVDIKFA---IRRAFPQTFE--EFGLDPASFKAL--KQAGGLAEEEWYRIATSALEEL------------Q 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    86 AEAESLAEAGFQvflearhrvtLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGvGKPD 159
Cdd:TIGR01549  62 GRFWSEYDAEEA----------YIRGAADLLARLKSAgIKLGIISNGSLRaqkllLRLFGLGDYFELILVSDEPG-SKPE 130

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 15600474   160 PTPFREALKRAGVEaSAAIHIGDHPSdDIAGARRAG 195
Cdd:TIGR01549 131 PEIFLAALESLGVP-PEVLHVGDNLN-DIEGARNAG 164
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 105-195 1.88e-13

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: 66.53  E-value: 1.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 105 RVTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAI 178
Cdd:cd02616  78 LTKEYPGVYETLARLKSQgIKLGVVTTKLREtalkgLKLLGLDKYFDVIVGGDDVTHHKPDPEPVLKALELLGAEPEEAL 157

                        90
                ....*....|....*..
gi 15600474 179 HIGDHPSdDIAGARRAG 195
Cdd:cd02616 158 MVGDSPH-DILAGKNAG 173
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 4-204 1.61e-12

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: 63.90  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   4 LRLVTFDLDDTLWDVAPvmnnaEALLREWLASNAARLGPVPIEHLWAIRTRLLDR----EPMLRHRLSELRRRILFHALL 79
Cdd:cd02603   1 IRAVLFDFGGVLIDPDP-----AAAVARFEALTGEPSEFVLDTEGLAGAFLELERgritEEEFWEELREELGRPLSAELF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  80 DAGYpqaeaeslaeagfqvfleaRHRVTLFPEVHPTLEILADR-FTLGVLTNGNADVRRLGLA------DYFRFALCAEE 152
Cdd:cd02603  76 EELV-------------------LAAVDPNPEMLDLLEALRAKgYKVYLLSNTWPDHFKFQLEllprrgDLFDGVVESCR 136

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600474 153 LGVGKPDPTPFREALKRAGVEASAAIHIGDHPsDDIAGARRAGMRAIWFNPS 204
Cdd:cd02603 137 LGVRKPDPEIYQLALERLGVKPEEVLFIDDRE-ENVEAARALGIHAILVTDA 187
PRK13223 PRK13223
phosphoglycolate phosphatase; Provisional
 5-224 3.97e-10

phosphoglycolate phosphatase; Provisional


Pssm-ID: 171912 [Multi-domain]  Cd Length: 272  Bit Score: 58.34  E-value: 3.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    5 RLVTFDLDDTLWDVAPVMNNAeallrewLASNAARLGPvPIEHLWAIRTRLLDREPMLRHRlselrrrilfhALLDAGYP 84
Cdd:PRK13223  14 RLVMFDLDGTLVDSVPDLAAA-------VDRMLLELGR-PPAGLEAVRHWVGNGAPVLVRR-----------ALAGSIDH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   85 QAEAESLAEAGFQVFLEA---RHRVT-LFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELG 154
Cdd:PRK13223  75 DGVDDELAEQALALFMEAyadSHELTvVYPGVRDTLKWLKKQgVEMALITNKPERfvaplLDQMKIGRYFRWIIGGDTLP 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600474  155 VGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAgARRAGMRAIWFN---PSGKPWAgEEEPSAEIRSLAEL 224
Cdd:PRK13223 155 QKKPDPAALLFVMKMAGVPPSQSLFVGDSRSDVLA-AKAAGVQCVALSygyNHGRPIA-EESPALVIDDLRAL 225
Hydrolase_like pfam13242
HAD-hyrolase-like;
156-224 4.37e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.16  E-value: 4.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600474   156 GKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFnPSGKPWAGEEE-----PSAEIRSLAEL 224
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILV-LTGVTRPADLEkapirPDYVVDDLAEA 75
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 98-199 1.97e-09

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: 54.16  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  98 VFLEARHRVTLFPEVHPTLEIL-ADRFTLGVLTNGNAD------VRRLGLADYFRFALCAEELGVGKPDPTPFREALKRA 170
Cdd:cd07505  32 LELIASEGLKLKPGVVELLDALkAAGIPVAVATSSSRRnvelllLELGLLRGYFDVIVSGDDVERGKPAPDIYLLAAERL 111

                        90       100
                ....*....|....*....|....*....
gi 15600474 171 GVEASAAIHIGDHPSdDIAGARRAGMRAI 199
Cdd:cd07505 112 GVDPERCLVFEDSLA-GIEAAKAAGMTVV 139
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 155-199 2.23e-09

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 55.75  E-value: 2.23e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15600474 155 VGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAI 199
Cdd:cd07509 170 VGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGI 214
bPGM TIGR01990
beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which ...
 7-199 3.87e-09

beta-phosphoglucomutase; This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 213672 [Multi-domain]  Cd Length: 185  Bit Score: 54.24  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     7 VTFDLDDTLWDVApvmnnaEALLREWLASnAARLGpVPIEHLWAIRTRLLDREPMLRhrlselrrRILFHAllDAGYPQA 86
Cdd:TIGR01990   2 VIFDLDGVITDTA------EYHYLAWKHL-ADELG-IPFDEEFNESLKGVSREESLE--------RILDLG--GKKYSEE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    87 EAESLAEAGFQVFLEARHRVT---LFPEVHPTLEILADR---FTLG-VLTNGNADVRRLGLADYFRFALCAEELGVGKPD 159
Cdd:TIGR01990  64 EKEELAERKNDYYVELLKELTpadVLPGIKSLLADLKKNnikIALAsASKNAPTILEKLELIDYFDAIVDPAELKKGKPD 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15600474   160 PTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAI 199
Cdd:TIGR01990 144 PEIFLAAAEGLGVSPSECIGIEDAQA-GIEAIKAAGMFAV 182
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 145-213 4.56e-09

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 55.25  E-value: 4.56e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600474   145 RFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNpSGKPWAGEEE 213
Cdd:TIGR01458 167 EYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRGIQVR-TGKYRPSDEE 234
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 136-202 4.80e-09

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: 53.80  E-value: 4.80e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600474 136 RRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAgARRAGMRAIWFN 202
Cdd:cd16423  79 ERLGLLDYFEVIVTGDDVEKSKPDPDLYLEAAERLGVNPEECVVIEDSRNGVLA-AKAAGMKCVGVP 144
PGMB-YQAB-SF TIGR02009
beta-phosphoglucomutase family hydrolase; This subfamily model groups together three clades: ...
 7-199 1.69e-08

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: 52.73  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     7 VTFDLDDTLWDVAPVmnNAEAllreWLASnAARLGpVPIEHLWAIRTRLLDREPMLR---------------HRLSElRR 71
Cdd:TIGR02009   4 VIFDMDGVITDTAPL--HAQA----WKHI-AAKYG-ISFDKQYNESLKGLSREDILRailklrgdglsleeiHQLAE-RK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    72 RILFHALLDagypqaEAESLAEAGFQVFLEaRHR-----VTLFPEVHPTLEILAdrftlgvltngnadvrRLGLADYFRF 146
Cdd:TIGR02009  75 NELYRELLR------LTGVAVLPGIRNLLK-RLKakgiaVGLGSSSKNAPRILA----------------KLGLRDYFDA 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15600474   147 ALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDhPSDDIAGARRAGMRAI 199
Cdd:TIGR02009 132 IVDASEVKNGKPHPETFLLAAELLGVPPNECIVFED-ALAGVQAARAAGMFAV 183
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
155-224 3.03e-08

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 52.80  E-value: 3.03e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600474 155 VGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNpSGKPWAGEEE-----PSAEIRSLAEL 224
Cdd:COG0647 184 VGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVL-TGVTTAEDLEaapirPDYVLDSLAEL 257
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
100-203 3.82e-08

Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];


Pssm-ID: 441782  Cd Length: 164  Bit Score: 51.28  E-value: 3.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 100 LEARHRVTLFPEVHPTLEILADR-FTLGVLTNGNADvrrlgladyfRFALCAEELGV------GKPDPTPFREALKRAGV 172
Cdd:COG2179  37 LVPWDEPEATPEVIEWLEELKEAgFKVCIVSNNSEK----------RVKRFAEKLGIpyiaraKKPLPRGFRKALKLMGL 106

                        90       100       110
                ....*....|....*....|....*....|.
gi 15600474 173 EASAAIHIGDHPSDDIAGARRAGMRAIWFNP 203
Cdd:COG2179 107 PPEETAVVGDQLFTDVLGGNRAGLYTILVKP 137
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 106-195 3.88e-08

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 51.95  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  106 VTLFPEVHPTLEILADR-FTLGVLTNGNADVRRLGL-----ADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIH 179
Cdd:PRK13288  81 VTEYETVYETLKTLKKQgYKLGIVTTKMRDTVEMGLkltglDEFFDVVITLDDVEHAKPDPEPVLKALELLGAKPEEALM 160

                         90
                 ....*....|....*.
gi 15600474  180 IGDHPSDDIAGaRRAG 195
Cdd:PRK13288 161 VGDNHHDILAG-KNAG 175
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 6-200 6.35e-08

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: 51.20  E-value: 6.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   6 LVTFDLDDTLWDVAPVMnnaEALLREwlasNAARLGPVPIEHlwairtrlldrepmlrHRLSELRRRILFHALLDAGYPQ 85
Cdd:cd04303   1 LIIFDFDGTLADSFPWF---LSILNQ----LAARHGFKTVDE----------------EEIEQLRQLSSREILKQLGVPL 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  86 AEAESLAEAGFQVFLEARHRVTLFPEVHPTLEILADR-FTLGVLT-NGNADVRR-LGLADYFRFALCAEELGV-GKPdpT 161
Cdd:cd04303  58 WKLPLIAKDFRRLMAEAAPELALFPGVEDMLRALHARgVRLAVVSsNSEENIRRvLGPEELISLFAVIEGSSLfGKA--K 135

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15600474 162 PFREALKRAGVEASAAIHIGDHpSDDIAGARRAGMRAIW 200
Cdd:cd04303 136 KIRRVLRRTKITAAQVIYVGDE-TRDIEAARKVGLAFAA 173
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 85-203 6.81e-08

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: 50.01  E-value: 6.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  85 QAEAESLAEAGFQVFLEARHRVTLFPEVHPTLEILADRFTlgVLTNG-----NADVRRLGLADYFRFAL-CAEELGVGKP 158
Cdd:cd07526  20 RVLVEVLAELGARVLAAFEAELQPIPGAAAALSALTLPFC--VASNSsrerlTHSLGLAGLLAYFEGRIfSASDVGRGKP 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15600474 159 DPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIWFNP 203
Cdd:cd07526  98 APDLFLHAAAQMGVAPERCLVIEDSPT-GVRAALAAGMTVFGFTG 141
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 6-199 1.02e-07

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: 50.47  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   6 LVTFDLDDTLWDVApvmNNAEALLREwlASNAARLGPVPIEHLWAIRTRLLDrepmlrhrlsELRRRILFHAlldAGYPQ 85
Cdd:cd07533   1 LVIFDWDGTLADSQ---HNIVAAMTA--AFADLGLPVPSAAEVRSIIGLSLD----------EAIARLLPMA---TPALV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  86 AEAESLAEAGFQVFLEARHRVTLFPEVHPTLEIL-ADRFTLGVLT-NGNADVRRL----GLADYFRFALCAEElGVGKPD 159
Cdd:cd07533  63 AVAERYKEAFDILRLLPEHAEPLFPGVREALDALaAQGVLLAVATgKSRRGLDRVleqhGLGGYFDATRTADD-TPSKPH 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15600474 160 PTPFREALKRAGVEASAAIHIGDhPSDDIAGARRAGMRAI 199
Cdd:cd07533 142 PEMLREILAELGVDPSRAVMVGD-TAYDMQMAANAGAHAV 180
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 108-203 1.50e-07

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 48.94  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   108 LFPEVHPTLEILADR-FTLGVLTNGNADVRR-LGLADYFRFALCAEELGVG-----------KPDPTPFREALKRA-GVE 173
Cdd:TIGR01662  26 LYPEVPDALAELKEAgYKVVIVTNQSGIGRGyFSRSFSGRVARRLEELGVPidilyacpgcrKPKPGMFLEALKRFnEID 105

                          90       100       110
                  ....*....|....*....|....*....|
gi 15600474   174 ASAAIHIGDHPSDDIAGARRAGMRAIWFNP 203
Cdd:TIGR01662 106 PEESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 155-199 1.73e-06

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and 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: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 47.59  E-value: 1.73e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15600474 155 VGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAI 199
Cdd:cd07530 175 IGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTL 219
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 136-199 3.74e-06

beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include 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: 319788 [Multi-domain]  Cd Length: 174  Bit Score: 45.75  E-value: 3.74e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600474 136 RRLGLADYFRFALCAEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAI 199
Cdd:cd02598  82 EKLGLAEYFDAIVDGAVLAKGKPDPDIFLAAAEGLGLNPKDCIGVEDAQA-GIRAIKAAGFLVV 144
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 127-200 5.69e-06

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: 45.32  E-value: 5.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 127 VLTNG-----NADVRRLGLADYFRFALCAEELG-VGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIW 200
Cdd:cd02604 101 IFTNAsknhaIRVLKRLGLADLFDGIFDIEYAGpDPKPHPAAFEKAIREAGLDPKRAAFFDDSIR-NLLAAKALGMKTVL 179
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 106-199 1.60e-05

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: 44.12  E-value: 1.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 106 VTLFPEVHPTLEILADR-FTLGVLTNGNAD-----VRRLGLADYFRFALCAEELG--VGKPDPtpFREALKRAGVEASAA 177
Cdd:cd04302  80 NEVYPGIPELLEKLKAAgYRLYVATSKPEVfarriLEHFGLDEYFDGIAGASLDGsrVHKADV--IRYALDTLGIAPEQA 157

                        90       100
                ....*....|....*....|..
gi 15600474 178 IHIGDHpSDDIAGARRAGMRAI 199
Cdd:cd04302 158 VMIGDR-KHDIIGARANGIDSI 178
HAD_ScGPP-like cd07527
subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae ...
 9-204 4.79e-05

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: 42.72  E-value: 4.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   9 FDLDDTLWDVAPVmnnAEALLREWlasnAARLGPVPIEHLWAI---RTRLLDREPMLRHRLSELRRRILfhalldagypQ 85
Cdd:cd07527   4 FDMDGTLVDSTPA---VERAWHKW----AKEHGVDPEEVLKVShgrRAIDVIRKLAPDDADIELVLALE----------T 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  86 AEAESLAEAgfqvflearhrVTLFPEVHPTLEIL-ADRFTLGVLTNGNADV--RRLGLA-----DYFrfaLCAEELGVGK 157
Cdd:cd07527  67 EEPESYPEG-----------VIAIPGAVDLLASLpAAGDRWAIVTSGTRALaeARLEAAglphpEVL---VTADDVKNGK 132

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15600474 158 PDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGMRAIWFNPS 204
Cdd:cd07527 133 PDPEPYLLGAKLLGLDPSDCVVFEDAPA-GIKAGKAAGARVVAVNTS 178
COG5610 COG5610
Predicted sugar hydrolase, contains GT1 and HAD domains [General function prediction only];
152-203 3.14e-04

Predicted sugar hydrolase, contains GT1 and HAD domains [General function prediction only];


Pssm-ID: 444341 [Multi-domain]  Cd Length: 501  Bit Score: 41.34  E-value: 3.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15600474 152 ELGVGKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAIWFNP 203
Cdd:COG5610 168 DYGLSKASGELFDYVLEEEGVDPKQILHIGDNPRSDVQRPRKLGIQALHYPR 219
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 145-199 4.11e-04

Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the uncharacterized protein Bacillus subtilis YqeG; 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: 319853 [Multi-domain]  Cd Length: 108  Bit Score: 38.79  E-value: 4.11e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600474 145 RFALCAEELGV------GKPDPTPFREALKRAGVEASAAIHIGDHPSDDIAGARRAGMRAI 199
Cdd:cd16416  46 RVAKVIEKLDLpfvaraGKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTI 106
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 114-199 4.13e-04

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: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 40.39  E-value: 4.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 114 PTLEILADRFTLGVLTNGNADVRRLGladyfRFALCA-------EELG-----VGKPDPTPFREALKRAGVEASAAI-HI 180
Cdd:cd07525 133 KLLKAAAARGLPLICANPDLVVPRGG-----KLIYCAgalaelyEELGgeviyFGKPHPPIYDLALARLGRPAKARIlAV 207

                        90
                ....*....|....*....
gi 15600474 181 GDHPSDDIAGARRAGMRAI 199
Cdd:cd07525 208 GDGLHTDILGANAAGLDSL 226
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 118-200 6.85e-04

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes 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. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 39.62  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   118 ILADRFTLGVLTNGnadVRRLGLADYFrfALCAEELG-----VGKPDPTPFREALKRAGV-EASAAIHIGDHPSDDIAGA 191
Cdd:TIGR01460 149 IAANRDDLVRLGDG---RFRPGAGAIA--AGIKELSGreptvVGKPSPAIYRAALNLLQArPERRDVMVGDNLRTDILGA 223


                  ....*....
gi 15600474   192 RRAGMRAIW 200
Cdd:TIGR01460 224 KNAGFDTLL 232
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 106-214 1.65e-03

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: 37.40  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474 106 VTLFPEVHPTLEILADRFTLGVLTNGN-----ADVRRLGLADYFRfalcAEELgVGKPDPTPFREALKRAGVEASAAIHI 180
Cdd:cd07515  16 IELLPGVREALAALKADYRLVLITKGDlldqeQKLARSGLSDYFD----AVEV-VSEKDPDTYRRVLSRYGIGPERFVMV 90

                        90       100       110
                ....*....|....*....|....*....|....
gi 15600474 181 GDHPSDDIAGARRAGMRAIWFnPSGKPWAGEEEP 214
Cdd:cd07515  91 GNSLRSDILPVLAAGGWGVHI-PYELTWKEEADE 123
PRK13226 PRK13226
phosphoglycolate phosphatase; Provisional
 5-196 2.11e-03

phosphoglycolate phosphatase; Provisional


Pssm-ID: 237311 [Multi-domain]  Cd Length: 229  Bit Score: 38.29  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    5 RLVTFDLDDTLWDVAPVMnnaeallrewLASNAARLgpvpiehlwAIRTRLLDREPMLRHRLSELRRrilfhALLDAGYP 84
Cdd:PRK13226  13 RAVLFDLDGTLLDSAPDM----------LATVNAML---------AARGRAPITLAQLRPVVSKGAR-----AMLAVAFP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   85 QAEAESLaEAGFQVFLE------ARHRVtLFPEVHPTLEILADRFTL-GVLTNGNADVRRLGLADYFRFALCA-----EE 152
Cdd:PRK13226  69 ELDAAAR-DALIPEFLQryealiGTQSQ-LFDGVEGMLQRLECAGCVwGIVTNKPEYLARLILPQLGWEQRCAvliggDT 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15600474  153 LGVGKPDPTPFREALKRAGVEASAAIHIGDHPSdDIAGARRAGM 196
Cdd:PRK13226 147 LAERKPHPLPLLVAAERIGVAPTDCVYVGDDER-DILAARAAGM 189
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 5-186 3.54e-03

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 37.51  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474   5 RLVTFDLDDTLWDVAPVMNNAEALLREWLASNAARLgpvpiEHLWAI----RTRLLDREPMLRHRLselrrrilfhALLd 80
Cdd:COG0560   4 RLAVFDLDGTLIAGESIDELARFLGRRGLVDRREVL-----EEVAAIteraMAGELDFEESLRFRV----------ALL- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474  81 AGYPQAEAESLAEAgfqvFLEARHRVTlfPEVHPTLEILADR-FTLGVLTNGNADV-----RRLGLADYFrfalcAEELG 154
Cdd:COG0560  68 AGLPEEELEELAER----LFEEVPRLY--PGARELIAEHRAAgHKVAIVSGGFTFFvepiaERLGIDHVI-----ANELE 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15600474 155 V------GKPDPTP-FREA--------LKRAGVEASAAIHIGDHPSD 186
Cdd:COG0560 137 VedgrltGEVVGPIvDGEGkaealrelAAELGIDLEQSYAYGDSAND 183
PRK09456 PRK09456
?-D-glucose-1-phosphatase; Provisional
 150-199 5.71e-03

?-D-glucose-1-phosphatase; Provisional


Pssm-ID: 181872 [Multi-domain]  Cd Length: 199  Bit Score: 36.55  E-value: 5.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15600474  150 AEELGVGKPDPTPFREALKRAGVEASAAIHIGDHPsDDIAGARRAGMRAI 199
Cdd:PRK09456 134 SQDLGMRKPEARIYQHVLQAEGFSAADAVFFDDNA-DNIEAANALGITSI 182
HAD pfam12710
haloacid dehalogenase-like hydrolase;
7-186 9.35e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 35.97  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474     7 VTFDLDDTLWDVapvmNNAEALLREWLASNAARLGPVPIEHLWAIRTRLLdrepmlrHRLSELRRRILFHALLdAGYPQA 86
Cdd:pfam12710   1 ALFDLDGTLLDG----DSLFLLIRALLRRGGPDLWRALLVLLLLALLRLL-------GRLSRAGARELLRALL-AGLPEE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600474    87 EAESLAEAGFQVFLEARHrvtlfPEVHPTLEILADR-FTLGVLTNGNADVRRLGLADYFRFALCAEEL--------GVGK 157
Cdd:pfam12710  69 DAAELERFVAEVALPRLH-----PGALELLAAHRAAgDRVVVVTGGLRPLVEPVLAELGFDEVLATELevddgrftGELR 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 15600474   158 PDPTPFREALKRAGVEASAAIH-----------IGDHPSD 186
Cdd:pfam12710 144 LIGPPCAGEGKVRRLRAWLAARglgldladsvaYGDSPSD 183
 
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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