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HAD family hydrolase [Streptococcus equi]

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

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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 ...
 2-232 3.16e-50

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: 165.59  E-value: 3.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDF-DMSLINRAYIRFRHYSDVGFPRVMSGEWTTEYFRfwrcRETLLEFGYRD 80
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLgLLDEAEELAEAYRAIEYALWRRYERGEITFAELL----RRLLEELGLDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  81 IDQAtgvhFQEVYEHELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKP 160
Cdd:COG1011   77 AEEL----AEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFD--AVVSSEEVGVRKP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501964610 161 EKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPiyDVAIDNFEQLFGAV 232
Cdd:COG1011  151 DPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRP--DYVISDLAELLELL 220
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 2-232 3.16e-50

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: 165.59  E-value: 3.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDF-DMSLINRAYIRFRHYSDVGFPRVMSGEWTTEYFRfwrcRETLLEFGYRD 80
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLgLLDEAEELAEAYRAIEYALWRRYERGEITFAELL----RRLLEELGLDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  81 IDQAtgvhFQEVYEHELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKP 160
Cdd:COG1011   77 AEEL----AEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFD--AVVSSEEVGVRKP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501964610 161 EKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPiyDVAIDNFEQLFGAV 232
Cdd:COG1011  151 DPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRP--DYVISDLAELLELL 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 101-204 8.34e-38

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: 129.58  E-value: 8.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 101 TMLDEMRMTLDFLKsKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKPEKEIFNLAAEQFDMNPATTL 180
Cdd:cd04305    9 TLLPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFD--HIVISEEVGVQKPNPEIFDYALNQLGVKPEETL 85

                         90       100
                 ....*....|....*....|....
gi 501964610 181 YVGDSYDNDVMGAKNGGWHAMWFN 204
Cdd:cd04305   86 MVGDSLESDILGAKNAGIKTVWFN 109
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-197 5.08e-30

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: 111.33  E-value: 5.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    4 AIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINrayirFRHYSDVGFprvMSGEWTTEYFRFWRcrETLLEfgyrdidq 83
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPAS-----FKALKQAGG---LAEEEWYRIATSAL--EELQG-------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   84 atgvHFQEVYEHELQHITMLDEMrmtLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYvdPKRVIVSQATGfQKPEKE 163
Cdd:TIGR01549  63 ----RFWSEYDAEEAYIRGAADL---LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDY--FELILVSDEPG-SKPEPE 132

                         170       180       190
                  ....*....|....*....|....*....|....
gi 501964610  164 IFNLAAEQFDMNPaTTLYVGDSyDNDVMGAKNGG 197
Cdd:TIGR01549 133 IFLAALESLGVPP-EVLHVGDN-LNDIEGARNAG 164
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-197 2.36e-23

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 94.58  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIRFRHYSDVGFP-RVMSGEWtteyfRFWRCRETLLEFGYRD 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTaRLLLGKR-----DWLEELDILRGLVETL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   81 IDQATGVHFQEVYEHEL--QHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQ 158
Cdd:pfam00702  76 EAEGLTVVLVELLGVIAlaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFD--VVISGDDVGVG 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 501964610  159 KPEKEIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGG 197
Cdd:pfam00702 154 KPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
PRK09449 PRK09449
dUMP phosphatase; Provisional
 101-221 4.63e-21

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 89.19  E-value: 4.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 101 TMLDEMRMTLDFLKSKnVPMGIITNGPTEHQLRKVRKLGLYDYVDPkrVIVSQATGFQKPEKEIFNLAAEQFDmNPATT- 179
Cdd:PRK09449  95 TPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDL--LVISEQVGVAKPDVAIFDYALEQMG-NPDRSr 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501964610 180 -LYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPIYDVA 221
Cdd:PRK09449 171 vLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVS 213
 
Name Accession Description Interval E-value
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 2-232 3.16e-50

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: 165.59  E-value: 3.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDF-DMSLINRAYIRFRHYSDVGFPRVMSGEWTTEYFRfwrcRETLLEFGYRD 80
Cdd:COG1011    1 IKAVLFDLDGTLLDFDPVIAEALRALAERLgLLDEAEELAEAYRAIEYALWRRYERGEITFAELL----RRLLEELGLDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  81 IDQAtgvhFQEVYEHELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKP 160
Cdd:COG1011   77 AEEL----AEAFLAALPELVEPYPDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDDLFD--AVVSSEEVGVRKP 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501964610 161 EKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPiyDVAIDNFEQLFGAV 232
Cdd:COG1011  151 DPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNRSGEPAPAEPRP--DYVISDLAELLELL 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 101-204 8.34e-38

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: 129.58  E-value: 8.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 101 TMLDEMRMTLDFLKsKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKPEKEIFNLAAEQFDMNPATTL 180
Cdd:cd04305    9 TLLPGAKELLEELK-KGYKLGIITNGPTEVQWEKLEQLGIHKYFD--HIVISEEVGVQKPNPEIFDYALNQLGVKPEETL 85

                         90       100
                 ....*....|....*....|....
gi 501964610 181 YVGDSYDNDVMGAKNGGWHAMWFN 204
Cdd:cd04305   86 MVGDSLESDILGAKNAGIKTVWFN 109
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 4-197 5.08e-30

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: 111.33  E-value: 5.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    4 AIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINrayirFRHYSDVGFprvMSGEWTTEYFRFWRcrETLLEfgyrdidq 83
Cdd:TIGR01549   1 AILFDIDGTLVDIKFAIRRAFPQTFEEFGLDPAS-----FKALKQAGG---LAEEEWYRIATSAL--EELQG-------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   84 atgvHFQEVYEHELQHITMLDEMrmtLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYvdPKRVIVSQATGfQKPEKE 163
Cdd:TIGR01549  63 ----RFWSEYDAEEAYIRGAADL---LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGDY--FELILVSDEPG-SKPEPE 132

                         170       180       190
                  ....*....|....*....|....*....|....
gi 501964610  164 IFNLAAEQFDMNPaTTLYVGDSyDNDVMGAKNGG 197
Cdd:TIGR01549 133 IFLAALESLGVPP-EVLHVGDN-LNDIEGARNAG 164
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 5-220 2.96e-27

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: 106.04  E-value: 2.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    5 IVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIRFRHYSDVGFPRVMSGEWTTEYFRFWRCRETLLEFGYRDIDQA 84
Cdd:TIGR02254   4 LLFDLDDTILDFQAAEALALRLLFEDQGIPLTEDMFAQYKEINQGLWRAYEEGKITKDEVVNTRFSALLKEYNTEADEAL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   85 TGVHFQEVYEHELQHITMLDEMrmtLDFLKSKnVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKPEKEI 164
Cdd:TIGR02254  84 LNQKYLRFLEEGHQLLPGAFEL---MENLQQK-FRLYIVTNGVRETQYKRLRKSGLFPFFD--DIFVSEDAGIQKPDKEI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 501964610  165 FNLAAEQFDMNPAT-TLYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPIYDV 220
Cdd:TIGR02254 158 FNYALERMPKFSKEeVLMIGDSLTADIKGGQNAGLDTCWMNPDMHPNPDDIIPTYEI 214
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
2-233 1.22e-25

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 101.16  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIR-FRHYSDVGFPRVMSGEWTTEYFrfwrcrETLLEfgyrd 80
Cdd:COG0546    1 IKLVLFDLDGTLVDSAPDIAAALNEALAELGLPPLDLEELRaLIGLGLRELLRRLLGEDPDEEL------EELLA----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  81 idqatgvHFQEVY-EHELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQK 159
Cdd:COG0546   70 -------RFRELYeEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDYFD--AIVGGDDVPPAK 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501964610 160 PEKEIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGGWHAM---WFNHRGRSLKPgTRPiyDVAIDNFEQLFGAVK 233
Cdd:COG0546  141 PKPEPLLEALERLGLDPEEVLMVGDSP-HDIEAARAAGVPFIgvtWGYGSAEELEA-AGA--DYVIDSLAELLALLA 213
DREG-2 TIGR02252
REG-2-like, HAD superfamily (subfamily IA) hydrolase; This family of proteins includes ...
 4-202 5.00e-24

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: 96.58  E-value: 5.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    4 AIVFDVDDTIYDQQAP----YRIAMEK----CFPDFDMSLINRAYIRFRHYSDvGFPRVMSGEWtteyFRFWR--CRETL 73
Cdd:TIGR02252   2 LITFDAVGTLLALKEPvgevYCEIARKygveVSPDELEQAFRKAFKAMSEAFP-NFGFSSGLTP----QQWWQklVRDTF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   74 LEFGYRDiDQATGVHFQEVYEH--ELQHITMLDEMRMTLDFLKSKNVPMGIITNgpTEHQLRKV-RKLGLYDYVDPkrVI 150
Cdd:TIGR02252  77 GRAGVPD-PESFEKIFEELYSYfaTPEPWQVYPDAIKLLKDLRERGLILGVISN--FDSRLRGLlEALGLLEYFDF--VV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 501964610  151 VSQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMW 202
Cdd:TIGR02252 152 TSYEVGAEKPDPKIFQEALERAGISPEEALHIGDSLRNDYQGARAAGWRALL 203
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-197 2.36e-23

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 94.58  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIRFRHYSDVGFP-RVMSGEWtteyfRFWRCRETLLEFGYRD 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTaRLLLGKR-----DWLEELDILRGLVETL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   81 IDQATGVHFQEVYEHEL--QHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQ 158
Cdd:pfam00702  76 EAEGLTVVLVELLGVIAlaDELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFD--VVISGDDVGVG 153

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 501964610  159 KPEKEIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGG 197
Cdd:pfam00702 154 KPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 109-204 1.59e-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: 90.43  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 109 TLDFLKSKNVPMGIITNgpTEHQLRKV-RKLGLYDYVDpkRVIVSQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSYD 187
Cdd:cd16415   15 TLKDLKEKGLKLAVVSN--FDRRLRELlEALGLDDYFD--FVVFSYEVGYEKPDPRIFQKALERLGVSPEEALHVGDDLK 90

                         90
                 ....*....|....*..
gi 501964610 188 NDVMGAKNGGWHAMWFN 204
Cdd:cd16415   91 NDYLGARAVGWHALLVD 107
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 1-228 5.77e-22

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. 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: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 91.70  E-value: 5.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    1 MISAIVFDVDDTIYDQQAPYRIAMEkcfpdfdmsliNRAYIRFRHYSDVGFPRVMS--GEWTTEYF-----RFWRCRETL 73
Cdd:TIGR02253   1 MIKAIFFDLDDTLIDTSGLAEKARR-----------NAIEVLIEAGLNVDFEEAYEelLKLIKEYGsnyptHFDYLIRRL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   74 LEFgYRDIDQATGVhfqEVYeHELQHITM--LDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIV 151
Cdd:TIGR02253  70 WEE-YNPKLVAAFV---YAY-HKLKFAYLrvYPGVRDTLMELRESGYRLGIITDGLPVKQWEKLERLGVRDFFD--AVIT 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501964610  152 SQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMWFNHRGRS-LKPGTRPIYDVAIDNFEQL 228
Cdd:TIGR02253 143 SEEEGVEKPHPKIFYAALKRLGVKPEEAVMVGDRLDKDIKGAKNAGMKTVWINQGKSSkMEDDVYPYPDYEISSLREL 220
PRK09449 PRK09449
dUMP phosphatase; Provisional
 101-221 4.63e-21

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 89.19  E-value: 4.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 101 TMLDEMRMTLDFLKSKnVPMGIITNGPTEHQLRKVRKLGLYDYVDPkrVIVSQATGFQKPEKEIFNLAAEQFDmNPATT- 179
Cdd:PRK09449  95 TPLPGAVELLNALRGK-VKMGIITNGFTELQQVRLERTGLRDYFDL--LVISEQVGVAKPDVAIFDYALEQMG-NPDRSr 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 501964610 180 -LYVGDSYDNDVMGAKNGGWHAMWFNHRGRSLKPGTRPIYDVA 221
Cdd:PRK09449 171 vLMVGDNLHSDILGGINAGIDTCWLNAHGREQPEGIAPTYQVS 213
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
5-197 7.85e-21

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 87.25  E-value: 7.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    5 IVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIRFRhysdVGFPRVMSGEWTTEYFRFWRCRETLLefgyrdidqa 84
Cdd:pfam13419   1 IIFDFDGTLLDTEELIIKSFNYLLEEFGYGELSEEEILKF----IGLPLREIFRYLGVSEDEEEKIEFYL---------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   85 tgvhfQEVYEHELQ-HITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIVSQATGFQ-KPEK 162
Cdd:pfam13419  67 -----RKYNEELHDkLVKPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFD---VIVGGDDVEGkKPDP 138

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 501964610  163 EIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGG 197
Cdd:pfam13419 139 DPILKALEQLGLKPEEVIYVGDSP-RDIEAAKNAG 172
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 2-211 7.16e-18

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: 79.70  E-value: 7.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDqqapyrIAMEKCFPDFDMSLINRAYIRFRHYSDVG-FPRVMSGEWTTEyfRFWR-CRETLLEFGYR 79
Cdd:cd02603    1 IRAVLFDFGGVLID------PDPAAAVARFEALTGEPSEFVLDTEGLAGaFLELERGRITEE--EFWEeLREELGRPLSA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  80 DIDQATGVHFQEVYEHelqhitMLDEMRMtldfLKSKNVPMGIITNGPTEHQLRKVRKL-GLYDYVDpkRVIVSQATGFQ 158
Cdd:cd02603   73 ELFEELVLAAVDPNPE------MLDLLEA----LRAKGYKVYLLSNTWPDHFKFQLELLpRRGDLFD--GVVESCRLGVR 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501964610 159 KPEKEIFNLAAEQFDMNPATTLYVGDSYDNdVMGAKNGGWHAMWFNHRGRSLK 211
Cdd:cd02603  141 KPDPEIYQLALERLGVKPEEVLFIDDREEN-VEAARALGIHAILVTDAEDALR 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-197 2.32e-17

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 78.71  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   1 MISAIVFDVDDTIYDqqapyriamekcfpdfDMSLINRAYIR-FRHYsdvGFPrvmsgeWTTEYFR------FWRCRETL 73
Cdd:COG0637    1 MIKAVIFDMDGTLVD----------------SEPLHARAWREaFAEL---GID------LTEEEYRrlmgrsREDILRYL 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  74 LEFGYRDIDQATGV-----HFQEVYEHElqHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkr 148
Cdd:COG0637   56 LEEYGLDLPEEELAarkeeLYRELLAEE--GLPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFD--- 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501964610 149 VIVsqaTGFQ----KPEKEIFNLAAEQFDMNPATTLYVGDSyDNDVMGAKNGG 197
Cdd:COG0637  131 VIV---TGDDvargKPDPDIYLLAAERLGVDPEECVVFEDS-PAGIRAAKAAG 179
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 4-202 8.39e-16

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: 73.61  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610    4 AIVFDVDDTIYDQQAPYRIAMEKC-FPDFDMSLINRAYIRFR---HYSDVGFPRVMSGEWTTEYFrfwrcretllefgyr 79
Cdd:TIGR01509   1 AILFDLDGVLVDTEFAIAKLINREeLGLVPDELGVSAVGRLElalRRFKAQYGRTISPEDAQLLY--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   80 didqatgvhFQEVYEH--ELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLrKVRKLGLYDYvdPKRVIVSQATGF 157
Cdd:TIGR01509  66 ---------KQLFYEQieEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDL--FDVVIDSSDVGL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 501964610  158 QKPEKEIFNLAAEQFDMNPATTLYVGDSYDNdVMGAKNGGWHAMW 202
Cdd:TIGR01509 134 GKPDPDIYLQALKALGLEPSECVFVDDSPAG-IEAAKAAGMHTVG 177
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 109-203 3.37e-15

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: 70.12  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 109 TLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDPkrVIVSQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSyDN 188
Cdd:cd01427   15 LLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDG--IIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-EN 91

                         90
                 ....*....|....*
gi 501964610 189 DVMGAKNGGWHAMWF 203
Cdd:cd01427   92 DIEAARAAGGRTVAV 106
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 89-228 1.03e-13

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: 68.80  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  89 FQEVYEHELQHITML-DEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIVSQATGFQ-KPEKEIFN 166
Cdd:cd16417   74 FDRHYAETLSVHSHLyPGVKEGLAALKAQGYPLACVTNKPERFVAPLLEALGISDYFS---LVLGGDSLPEkKPDPAPLL 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 167 LAAEQFDMNPATTLYVGDSyDNDVMGAKNGGWHAMW----FNHrgrslkpgTRPIY----DVAIDNFEQL 228
Cdd:cd16417  151 HACEKLGIAPAQMLMVGDS-RNDILAARAAGCPSVGltygYNY--------GEDIAasgpDAVIDSLAEL 211
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
89-232 4.37e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 67.14  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  89 FQEVYEHEL-QHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIVSQAT-GFQKPEKEIFN 166
Cdd:PRK13222  80 FDRHYAENVaGGSRLYPGVKETLAALKAAGYPLAVVTNKPTPFVAPLLEALGIADYFS---VVIGGDSlPNKKPDPAPLL 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501964610 167 LAAEQFDMNPATTLYVGDSyDNDVMGAKNGGWH--AMWFNHRG----RSLKPgtrpiyDVAIDNFEQLFGAV 232
Cdd:PRK13222 157 LACEKLGLDPEEMLFVGDS-RNDIQAARAAGCPsvGVTYGYNYgepiALSEP------DVVIDHFAELLPLL 221
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
2-210 5.81e-12

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 64.37  E-value: 5.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYD---------QQApyrIA-MEKCFPDFDmSLINRAYIRFRH---------YSDVGfprvmsgEWTte 62
Cdd:PRK10748  10 ISALTFDLDDTLYDnrpvilrteQEA---LAfVQNYHPALR-SFQNEDLQRLRQalreaepeiYHDVT-------RWR-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  63 yfrfWRCRE-TLLEFGYRDIDQATGVHF-QEVYEHELQHITMLDEMRMTLDFLkSKNVPMGIITNGPTEHQLrkvrkLGL 140
Cdd:PRK10748  77 ----WRAIEqAMLDAGLSAEEASAGADAaMINFAKWRSRIDVPQATHDTLKQL-AKKWPLVAITNGNAQPEL-----FGL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 141 YDYVdpKRVIVSQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMWFNHRGRSL 210
Cdd:PRK10748 147 GDYF--EFVLRAGPHGRSKPFSDMYHLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQACWINPENGDL 214
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 4-216 1.38e-11

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: 62.67  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   4 AIVFDVDDTIYDQQAPYRIAMEKcFPDFDMSLINRAYIRFRHYSDV---GFPRVMSGEWTTEYFRFwrcreTLLEFGyRD 80
Cdd:cd02588    2 ALVFDVYGTLIDWHSGLAAAERA-FPGRGEELSRLWRQKQLEYTWLvtlMGPYVDFDELTRDALRA-----TAAELG-LE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  81 IDQATGVHFQEVYEHELQHitmlDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQKP 160
Cdd:cd02588   75 LDESDLDELGDAYLRLPPF----PDVVAGLRRLREAGYRLAILSNGSPDLIEDVVANAGLRDLFD--AVLSAEDVRAYKP 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 501964610 161 EKEIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGGWHAMWFNHRGRSLKPGTRP 216
Cdd:cd02588  149 APAVYELAAERLGVPPDEILHVASHA-WDLAGARALGLRTAWINRPGEVPDPLGPA 203
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 2-197 1.13e-09

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 57.29  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   2 ISAIVFDVDDTIYDQQAPYRIAMEKCFPDFDMSLINRAYIRfrHYSDVGFPRVMSGEWTTEYFRFWrcrETLLEFgYRDI 81
Cdd:cd02616    1 ITTILFDLDGTLIDTNELIIKSFNHTLKEYGLEGYTREEVL--PFIGPPLRETFEKIDPDKLEDMV---EEFRKY-YREH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  82 DQATGVHFQEVYEhelqhitmldemrmTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIV-SQATGFQKP 160
Cdd:cd02616   75 NDDLTKEYPGVYE--------------TLARLKSQGIKLGVVTTKLRETALKGLKLLGLDKYFD---VIVgGDDVTHHKP 137

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 501964610 161 EKEIFNLAAEQFDMNPATTLYVGDSYdNDVMGAKNGG 197
Cdd:cd02616  138 DPEPVLKALELLGAEPEEALMVGDSP-HDILAGKNAG 173
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 110-197 1.30e-08

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: 53.41  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 110 LDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIVsqaTGFQ----KPEKEIFNLAAEQFDMNPATTLYVGDS 185
Cdd:cd16423   53 LEFLKEKGIKLAVASSSPRRWIEPHLERLGLLDYFE---VIV---TGDDveksKPDPDLYLEAAERLGVNPEECVVIEDS 126

                         90
                 ....*....|..
gi 501964610 186 yDNDVMGAKNGG 197
Cdd:cd16423  127 -RNGVLAAKAAG 137
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 109-197 2.35e-08

beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; This family represents the beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. Family members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. It belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319808 [Multi-domain]  Cd Length: 143  Bit Score: 52.23  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 109 TLDFLKSKNVPMGIITNGPTEHQLRKVRKLGL-YDYVDpkrVIVSQATGFQ-KPEKEIFNLAAEQFDMNPATTLYVGDSY 186
Cdd:cd07505   49 LLDALKAAGIPVAVATSSSRRNVELLLLELGLlRGYFD---VIVSGDDVERgKPAPDIYLLAAERLGVDPERCLVFEDSL 125

                         90
                 ....*....|.
gi 501964610 187 dNDVMGAKNGG 197
Cdd:cd07505  126 -AGIEAAKAAG 135
HAD_BPGM_like cd07526
subfamily of beta-phosphoglucomutase-like family, similar to Escherichia coli ...
 70-185 3.63e-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: 51.55  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  70 RETLLEFGYRDIdqatgvhfqEVYEHELQHItmlDEMRMTLDFLkskNVPMGIITNGPTEHQLRKVRKLGLYDYVDPkRV 149
Cdd:cd07526   23 VEVLAELGARVL---------AAFEAELQPI---PGAAAALSAL---TLPFCVASNSSRERLTHSLGLAGLLAYFEG-RI 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 501964610 150 IVSQATGFQKPEKEIFNLAAEQFDMNPATTLYVGDS 185
Cdd:cd07526   87 FSASDVGRGKPAPDLFLHAAAQMGVAPERCLVIEDS 122
Hydrolase_like pfam13242
HAD-hyrolase-like;
159-202 6.14e-08

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 49.15  E-value: 6.14e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 501964610  159 KPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMW 202
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTIL 47
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
151-202 1.88e-07

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 51.26  E-value: 1.88e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501964610 151 VSQATGFQ-----KPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGGWHAMW 202
Cdd:COG0647  173 LEAATGGEplvvgKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLL 229
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 93-197 1.36e-06

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 48.10  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  93 YEHElQH---ITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDPkrVIVSQATGFQKPEKEIFNLAA 169
Cdd:PRK13288  72 FNHE-HHdelVTEYETVYETLKTLKKQGYKLGIVTTKMRDTVEMGLKLTGLDEFFDV--VITLDDVEHAKPDPEPVLKAL 148

                         90       100
                 ....*....|....*....|....*...
gi 501964610 170 EQFDMNPATTLYVGDSYdNDVMGAKNGG 197
Cdd:PRK13288 149 ELLGAKPEEALMVGDNH-HDILAGKNAG 175
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 109-197 5.11e-06

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: 46.54  E-value: 5.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 109 TLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrVIVSQAT-GFQKPEKEIFNLAAEQFDMNPATTLYVGDSyD 187
Cdd:cd07512   94 ALERLRAAGWRLAICTNKPEAPARALLSALGLADLFA---AVVGGDTlPQRKPDPAPLRAAIRRLGGDVSRALMVGDS-E 169

                         90
                 ....*....|
gi 501964610 188 NDVMGAKNGG 197
Cdd:cd07512  170 TDAATARAAG 179
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 151-197 1.22e-05

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: 45.66  E-value: 1.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501964610 151 VSQATGFQ-----KPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGG 197
Cdd:cd07530  164 LEAATGVKplfigKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAG 215
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 78-202 2.07e-05

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: 45.01  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   78 YRDIDQATGVHFQEV----YEHELQHitmldEMRMTLDFLKSKNVPMGIITNGPT-----EHQLRkvrkLGLYDYVDP-K 147
Cdd:TIGR01460 106 FDDIDHLAIEKIPAAvivgEPSDFSY-----DELAKAAYLLAEGDVPFIAANRDDlvrlgDGRFR----PGAGAIAAGiK 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 501964610  148 RVIVSQATGFQKPEKEIFNLAAEQFDMNPATTLY-VGDSYDNDVMGAKNGGWHAMW 202
Cdd:TIGR01460 177 ELSGREPTVVGKPSPAIYRAALNLLQARPERRDVmVGDNLRTDILGAKNAGFDTLL 232
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 122-202 5.98e-05

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: 43.01  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 122 IITNGPTEHQLRKVRKLGLYDYVDpkRVIVSQATGFQ-KPEKEIFNLAAEQFDMNPATTLYVGDSYDNdVMGAKNGGWHA 200
Cdd:cd02604  101 IFTNASKNHAIRVLKRLGLADLFD--GIFDIEYAGPDpKPHPAAFEKAIREAGLDPKRAAFFDDSIRN-LLAAKALGMKT 177


                 ..
gi 501964610 201 MW 202
Cdd:cd02604  178 VL 179
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 153-197 1.55e-04

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: 42.27  E-value: 1.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 501964610 153 QATGFQKPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGG 197
Cdd:cd07509  166 KATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACG 210
HAD_BPGM cd02598
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM); ...
 60-238 3.56e-04

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: 40.35  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  60 TTEY-FRFWRCRETLLEFGYRDIDqatgvhfqeVYEHELQHIT---MLDEMRMTLDFLKSKNVPMGIIT---NGPTehql 132
Cdd:cd02598   13 TAEYhYRAWKKLADKEELAARKNR---------IYVELIEELTpvdVLPGIASLLVDLKAKGIKIALASaskNAPK---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 133 rKVRKLGLYDYVDpkrVIVSQAT-GFQKPEKEIFNLAAEQFDMNPATTLYVGDSyDNDVMGAKNGGwhamwfnhrgrslk 211
Cdd:cd02598   80 -ILEKLGLAEYFD---AIVDGAVlAKGKPDPDIFLAAAEGLGLNPKDCIGVEDA-QAGIRAIKAAG-------------- 140

                        170       180
                 ....*....|....*....|....*..
gi 501964610 212 pgtrpIYDVAIDNFEQLFGAVKVLFDL 238
Cdd:cd02598  141 -----FLVVGVGREEDLLGADIVVPDT 162
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 159-197 8.96e-04

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It 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: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 40.06  E-value: 8.96e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501964610 159 KPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGG 197
Cdd:cd07510  204 KPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQNCG 242
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 104-199 3.64e-03

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: 36.48  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610 104 DEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLyDYVDPKRvivsqatgfqKPEKEIFNLAAEQFDMNPATTLYVG 183
Cdd:cd16416   20 PEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDL-PFVARAG----------KPRPRAFRRALKEMDLPPEQVAMVG 88

                         90
                 ....*....|....*.
gi 501964610 184 DSYDNDVMGAKNGGWH 199
Cdd:cd16416   89 DQLFTDILGGNRAGLY 104
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 150-197 3.99e-03

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. 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: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 38.11  E-value: 3.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501964610 150 IVSQATGFQ-----KPEKEIFNLAAEQFDMNPATTLYVGDSYDNDVMGAKNGG 197
Cdd:cd07508  183 AVEAATGRQplvlgKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACG 235
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-190 6.45e-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: 37.12  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   1 MISAIVFDVDDTIYDQQAPYRIAMEkcfpdfdmsLINRAYIRFRHYSDV---GFPRVMSGEWT-TEYFRFwrcRETLLEf 76
Cdd:COG0560    2 KMRLAVFDLDGTLIAGESIDELARF---------LGRRGLVDRREVLEEvaaITERAMAGELDfEESLRF---RVALLA- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  77 GyRDIDQATGVHfQEVYEhelQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEhQLRKV-RKLGL-------YDYVDPK- 147
Cdd:COG0560   69 G-LPEEELEELA-ERLFE---EVPRLYPGARELIAEHRAAGHKVAIVSGGFTF-FVEPIaERLGIdhvianeLEVEDGRl 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501964610 148 --RVIVSQATGFQKPekEIFNLAAEQFDMNPATTLYVGDSYdNDV 190
Cdd:COG0560  143 tgEVVGPIVDGEGKA--EALRELAAELGIDLEQSYAYGDSA-NDL 184
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 4-184 7.14e-03

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: 36.95  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610   4 AIVFDVDDTIYDQQApyriamekcfpdFDMSLINRAYIRFrhysdvGFPRVMSGEwtTEYFRFWRCRETLLEFGYRDIDQ 83
Cdd:cd04303    1 LIIFDFDGTLADSFP------------WFLSILNQLAARH------GFKTVDEEE--IEQLRQLSSREILKQLGVPLWKL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501964610  84 ATGV-HFQEVYEHELQHITMLDEMRMTLDFLKSKNVPMGIITNGPTEHQLRKVRKLGLYDYVDpkrvIVSQATGFQKPEK 162
Cdd:cd04303   61 PLIAkDFRRLMAEAAPELALFPGVEDMLRALHARGVRLAVVSSNSEENIRRVLGPEELISLFA----VIEGSSLFGKAKK 136

                        170       180
                 ....*....|....*....|..
gi 501964610 163 EIFNLAAEQfdMNPATTLYVGD 184
Cdd:cd04303  137 IRRVLRRTK--ITAAQVIYVGD 156
 
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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