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Conserved domains on  [gi|1763957597|gb|KAB5253402|]
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HAD family hydrolase [Bacteroides thetaiotaomicron]

Protein Classification

HAD family hydrolase( domain architecture ID 12008672)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 100-218 9.93e-69

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: 207.27  E-value: 9.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 100 PIELLPGVKETLKTLKEtgKYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKEYLRLLSILQIAPSELLMVGN 179
Cdd:cd07515    15 PIELLPGVREALAALKA--DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVVSEKDPDTYRRVLSRYGIGPERFVMVGN 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1763957597 180 SFKSDIQPVLSLGGYGVHIPFEVMWKHEVTETFAHERLK 218
Cdd:cd07515    93 SLRSDILPVLAAGGWGVHIPYELTWKEEADEPDAHPRAA 131
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-186 9.12e-16

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: 72.62  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPffqEVEKQYTDLLKPYGTSKEISAALFQTEM---NNLQILGYGAKAFTISMVETALQISNGKI 81
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEP---VVTEAIAELASEHPLAKAIVAAAEDLPIpveDFTARLLLGKRDWLEELDILRGLVETLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  82 AADIIRQIVDLGKSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE-- 159
Cdd:pfam00702  78 EGLTVVLVELLGVIALADELKLYPGAAEALKALKERG-IKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpk 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1763957597 160 ---YLRLLSILQIAPSELLMVGNSFKsDIQ 186
Cdd:pfam00702 157 peiYLAALERLGVKPEEVLMVGDGVN-DIP 185
 
Name Accession Description Interval E-value
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 100-218 9.93e-69

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: 207.27  E-value: 9.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 100 PIELLPGVKETLKTLKEtgKYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKEYLRLLSILQIAPSELLMVGN 179
Cdd:cd07515    15 PIELLPGVREALAALKA--DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVVSEKDPDTYRRVLSRYGIGPERFVMVGN 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1763957597 180 SFKSDIQPVLSLGGYGVHIPFEVMWKHEVTETFAHERLK 218
Cdd:cd07515    93 SLRSDILPVLAAGGWGVHIPYELTWKEEADEPDAHPRAA 131
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-230 8.51e-30

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: 110.50  E-value: 8.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVEKQYTDLLKPYGTSKEISAALFQTEMNNLQILGYGAKAFTiSMVETALQISNGKIAAD 84
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFA-ELLRRLLEELGLDLAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  85 IIRQIVDlgksLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMSD-----KTEKE 159
Cdd:COG1011    80 LAEAFLA----ALPELVEPYPDALELLEALKARG-YRLALLTNGSAELQEAKLRRLGLDDLFDAV-VSSEevgvrKPDPE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1763957597 160 -YLRLLSILQIAPSELLMVGNSFKSDIQPVLSLGGYGVHI-PFEVMWKHEVTETFaherlkQVKRLDDLLSLL 230
Cdd:COG1011   154 iFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVnRSGEPAPAEPRPDY------VISDLAELLELL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-186 9.12e-16

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: 72.62  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPffqEVEKQYTDLLKPYGTSKEISAALFQTEM---NNLQILGYGAKAFTISMVETALQISNGKI 81
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEP---VVTEAIAELASEHPLAKAIVAAAEDLPIpveDFTARLLLGKRDWLEELDILRGLVETLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  82 AADIIRQIVDLGKSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE-- 159
Cdd:pfam00702  78 EGLTVVLVELLGVIALADELKLYPGAAEALKALKERG-IKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpk 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1763957597 160 ---YLRLLSILQIAPSELLMVGNSFKsDIQ 186
Cdd:pfam00702 157 peiYLAALERLGVKPEEVLMVGDGVN-DIP 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
94-186 5.35e-11

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 59.52  E-value: 5.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  94 KSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE-----YLRLLSILQ 168
Cdd:pfam13419  71 EELHDKLVKPYPGIKELLEELKEQG-YKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKpdpdpILKALEQLG 149

                          90
                  ....*....|....*...
gi 1763957597 169 IAPSELLMVGNSfKSDIQ 186
Cdd:pfam13419 150 LKPEEVIYVGDS-PRDIE 166
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-180 1.09e-09

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 56.37  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVEKQytdLLKPYGtsKEISAALFQtemnnlQILGYGakafTISMVETALQISNGKI-AA 83
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWRE---AFAELG--IDLTEEEYR------RLMGRS----REDILRYLLEEYGLDLpEE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  84 DIIRQIVDLGKSLLKM-PIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMSDKTEKE--- 159
Cdd:COG0637    67 ELAARKEELYRELLAEeGLPLIPGVVELLEALKEAG-IKIAVATSSPRENAEAVLEAAGLLDYFDVI-VTGDDVARGkpd 144

                         170       180
                  ....*....|....*....|....
gi 1763957597 160 ---YLRLLSILQIAPSELLMVGNS 180
Cdd:COG0637   145 pdiYLLAAERLGVDPEECVVFEDS 168
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 103-192 8.72e-09

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: 54.03  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 103 LLPGVKETLKTLKetGKYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSD----KTEKEY--LRLLSILQIAPSELLM 176
Cdd:TIGR02254  98 LLPGAFELMENLQ--QKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDagiqKPDKEIfnYALERMPKFSKEEVLM 175

                          90
                  ....*....|....*.
gi 1763957597 177 VGNSFKSDIQPVLSLG 192
Cdd:TIGR02254 176 IGDSLTADIKGGQNAG 191
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
102-231 6.79e-08

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 51.35  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 102 ELLPGVKETLKTLKETGkYKLVVATkgdlldqeNK--------LERSGLSPYF------DHIEVMsdKTEKEYLRLL-SI 166
Cdd:PRK13222   93 RLYPGVKETLAALKAAG-YPLAVVT--------NKptpfvaplLEALGIADYFsvviggDSLPNK--KPDPAPLLLAcEK 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1763957597 167 LQIAPSELLMVGNSfKSDIQ-------PVLSLG-GY--GVHIPfevMWKHEVTetfaherlkqVKRLDDLLSLLG 231
Cdd:PRK13222  162 LGLDPEEMLFVGDS-RNDIQaaraagcPSVGVTyGYnyGEPIA---LSEPDVV----------IDHFAELLPLLG 222
 
Name Accession Description Interval E-value
HAD-like cd07515
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 100-218 9.93e-69

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: 207.27  E-value: 9.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 100 PIELLPGVKETLKTLKEtgKYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKEYLRLLSILQIAPSELLMVGN 179
Cdd:cd07515    15 PIELLPGVREALAALKA--DYRLVLITKGDLLDQEQKLARSGLSDYFDAVEVVSEKDPDTYRRVLSRYGIGPERFVMVGN 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1763957597 180 SFKSDIQPVLSLGGYGVHIPFEVMWKHEVTETFAHERLK 218
Cdd:cd07515    93 SLRSDILPVLAAGGWGVHIPYELTWKEEADEPDAHPRAA 131
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 5-230 8.51e-30

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: 110.50  E-value: 8.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVEKQYTDLLKPYGTSKEISAALFQTEMNNLQILGYGAKAFTiSMVETALQISNGKIAAD 84
Cdd:COG1011     1 IKAVLFDLDGTLLDFDPVIAEALRALAERLGLLDEAEELAEAYRAIEYALWRRYERGEITFA-ELLRRLLEELGLDLAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  85 IIRQIVDlgksLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMSD-----KTEKE 159
Cdd:COG1011    80 LAEAFLA----ALPELVEPYPDALELLEALKARG-YRLALLTNGSAELQEAKLRRLGLDDLFDAV-VSSEevgvrKPDPE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1763957597 160 -YLRLLSILQIAPSELLMVGNSFKSDIQPVLSLGGYGVHI-PFEVMWKHEVTETFaherlkQVKRLDDLLSLL 230
Cdd:COG1011   154 iFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVnRSGEPAPAEPRPDY------VISDLAELLELL 220
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 103-192 7.06e-16

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: 70.65  E-value: 7.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 103 LLPGVKETLKTLKEtgKYKLVVATKGDLLDQENKLERSGLSPYFDHI----EVMSDKTEKEYLRL-LSILQIAPSELLMV 177
Cdd:cd04305    10 LLPGAKELLEELKK--GYKLGIITNGPTEVQWEKLEQLGIHKYFDHIviseEVGVQKPNPEIFDYaLNQLGVKPEETLMV 87

                          90
                  ....*....|....*
gi 1763957597 178 GNSFKSDIQPVLSLG 192
Cdd:cd04305    88 GDSLESDILGAKNAG 102
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
5-231 9.04e-16

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 73.04  E-value: 9.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVekqYTDLLKPYGTSKEISAALfqtemnnLQILGYGAKAftisMVETALQISNGKIAAD 84
Cdd:COG0546     1 IKLVLFDLDGTLVDSAPDIAAA---LNEALAELGLPPLDLEEL-------RALIGLGLRE----LLRRLLGEDPDEELEE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  85 IIRQIVDLGKSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE----- 159
Cdd:COG0546    67 LLARFRELYEEELLDETRLFPGVRELLEALKARG-IKLAVVTNKPREFAERLLEALGLDDYFDAIVGGDDVPPAKpkpep 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1763957597 160 YLRLLSILQIAPSELLMVGNSfKSDIQPVLSLGGYGVHIPFEVMWKHEVTETFAHERlkqVKRLDDLLSLLG 231
Cdd:COG0546   146 LLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTWGYGSAEELEAAGADYV---IDSLAELLALLA 213
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 5-186 9.12e-16

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: 72.62  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPffqEVEKQYTDLLKPYGTSKEISAALFQTEM---NNLQILGYGAKAFTISMVETALQISNGKI 81
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEP---VVTEAIAELASEHPLAKAIVAAAEDLPIpveDFTARLLLGKRDWLEELDILRGLVETLEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  82 AADIIRQIVDLGKSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE-- 159
Cdd:pfam00702  78 EGLTVVLVELLGVIALADELKLYPGAAEALKALKERG-IKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKpk 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 1763957597 160 ---YLRLLSILQIAPSELLMVGNSFKsDIQ 186
Cdd:pfam00702 157 peiYLAALERLGVKPEEVLMVGDGVN-DIP 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
94-186 5.35e-11

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 59.52  E-value: 5.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  94 KSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSDKTEKE-----YLRLLSILQ 168
Cdd:pfam13419  71 EELHDKLVKPYPGIKELLEELKEQG-YKLGIVTSKSRENVEEFLKQLGLEDYFDVIVGGDDVEGKKpdpdpILKALEQLG 149

                          90
                  ....*....|....*...
gi 1763957597 169 IAPSELLMVGNSfKSDIQ 186
Cdd:pfam13419 150 LKPEEVIYVGDS-PRDIE 166
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 107-198 7.19e-10

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: 54.71  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 107 VKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHI----EVMSDKTE-KEYLRLLSILQIAPSELLMVGNSf 181
Cdd:cd01427    12 AVELLKRLRAAG-IKLAIVTNRSREALRALLEKLGLGDLFDGIigsdGGGTPKPKpKPLLLLLLKLGVDPEEVLFVGDS- 89

                          90
                  ....*....|....*..
gi 1763957597 182 KSDIQPVLSLGGYGVHI 198
Cdd:cd01427    90 ENDIEAARAAGGRTVAV 106
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
5-180 1.09e-09

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 56.37  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVEKQytdLLKPYGtsKEISAALFQtemnnlQILGYGakafTISMVETALQISNGKI-AA 83
Cdd:COG0637     2 IKAVIFDMDGTLVDSEPLHARAWRE---AFAELG--IDLTEEEYR------RLMGRS----REDILRYLLEEYGLDLpEE 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  84 DIIRQIVDLGKSLLKM-PIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMSDKTEKE--- 159
Cdd:COG0637    67 ELAARKEELYRELLAEeGLPLIPGVVELLEALKEAG-IKIAVATSSPRENAEAVLEAAGLLDYFDVI-VTGDDVARGkpd 144

                         170       180
                  ....*....|....*....|....
gi 1763957597 160 ---YLRLLSILQIAPSELLMVGNS 180
Cdd:COG0637   145 pdiYLLAAERLGVDPEECVVFEDS 168
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 103-192 8.72e-09

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: 54.03  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 103 LLPGVKETLKTLKetGKYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSD----KTEKEY--LRLLSILQIAPSELLM 176
Cdd:TIGR02254  98 LLPGAFELMENLQ--QKFRLYIVTNGVRETQYKRLRKSGLFPFFDDIFVSEDagiqKPDKEIfnYALERMPKFSKEEVLM 175

                          90
                  ....*....|....*.
gi 1763957597 177 VGNSFKSDIQPVLSLG 192
Cdd:TIGR02254 176 IGDSLTADIKGGQNAG 191
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 103-186 2.74e-08

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: 52.24  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 103 LLPGVKETLKTLKETGkYKLVVATkgdlldqeNK--------LERSGLSPYFDhiEVMSDKTEKE-------YLRLLSIL 167
Cdd:cd16417    88 LYPGVKEGLAALKAQG-YPLACVT--------NKperfvaplLEALGISDYFS--LVLGGDSLPEkkpdpapLLHACEKL 156

                          90
                  ....*....|....*....
gi 1763957597 168 QIAPSELLMVGNSfKSDIQ 186
Cdd:cd16417   157 GIAPAQMLMVGDS-RNDIL 174
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
102-231 6.79e-08

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 51.35  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 102 ELLPGVKETLKTLKETGkYKLVVATkgdlldqeNK--------LERSGLSPYF------DHIEVMsdKTEKEYLRLL-SI 166
Cdd:PRK13222   93 RLYPGVKETLAALKAAG-YPLAVVT--------NKptpfvaplLEALGIADYFsvviggDSLPNK--KPDPAPLLLAcEK 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1763957597 167 LQIAPSELLMVGNSfKSDIQ-------PVLSLG-GY--GVHIPfevMWKHEVTetfaherlkqVKRLDDLLSLLG 231
Cdd:PRK13222  162 LGLDPEEMLFVGDS-RNDIQaaraagcPSVGVTyGYnyGEPIA---LSEPDVV----------IDHFAELLPLLG 222
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 101-180 7.54e-08

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 51.18  E-value: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 101 IELLPGVKETLKTLKETGkYKL-VVATKgdLLDQENK-LERSGLSPYFDHIEVMSD----KTEKEYLRL-LSILQIAPSE 173
Cdd:PRK13288   81 VTEYETVYETLKTLKKQG-YKLgIVTTK--MRDTVEMgLKLTGLDEFFDVVITLDDvehaKPDPEPVLKaLELLGAKPEE 157


                  ....*..
gi 1763957597 174 LLMVGNS 180
Cdd:PRK13288  158 ALMVGDN 164
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 7-192 2.92e-07

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 48.55  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   7 VIAFDADDTLWSnepffqevekqytdllkpygtSKEISAALFQTEMNNLQILGYGAKAFTISMVETALQISNgkIAADII 86
Cdd:TIGR01549   1 AILFDIDGTLVD---------------------IKFAIRRAFPQTFEEFGLDPASFKALKQAGGLAEEEWYR--IATSAL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  87 RQIVDLGKSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSD---KTEKEYLRL 163
Cdd:TIGR01549  58 EELQGRFWSEYDAEEAYIRGAADLLARLKSAG-IKLGIISNGSLRAQKLLLRLFGLGDYFELILVSDEpgsKPEPEIFLA 136

                         170       180       190
                  ....*....|....*....|....*....|
gi 1763957597 164 LsILQI-APSELLMVGNSfKSDIQPVLSLG 192
Cdd:TIGR01549 137 A-LESLgVPPEVLHVGDN-LNDIEGARNAG 164
PRK09449 PRK09449
dUMP phosphatase; Provisional
 102-230 6.78e-07

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 48.36  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 102 ELLPGVKETLKTLKetGKYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMS--------DKTEKEY-LRLLSilQIAPS 172
Cdd:PRK09449   95 TPLPGAVELLNALR--GKVKMGIITNGFTELQQVRLERTGLRDYFDLL-VISeqvgvakpDVAIFDYaLEQMG--NPDRS 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1763957597 173 ELLMVGNSFKSDIqpvlsLGgyGVHIPFEVMWKHeVTETFAHERLK---QVKRLDDLLSLL 230
Cdd:PRK09449  170 RVLMVGDNLHSDI-----LG--GINAGIDTCWLN-AHGREQPEGIAptyQVSSLSELEQLL 222
HAD_BPGM-like cd16423
uncharacterized subfamily of beta-phosphoglucomutase-like family, similar to uncharacterized ...
 96-181 2.81e-06

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: 46.09  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  96 LLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHI----EVMSDKTEKE-YLRLLSILQIA 170
Cdd:cd16423    38 SEKTDLPPIEGVKELLEFLKEKG-IKLAVASSSPRRWIEPHLERLGLLDYFEVIvtgdDVEKSKPDPDlYLEAAERLGVN 116

                          90
                  ....*....|.
gi 1763957597 171 PSELLMVGNSF 181
Cdd:cd16423   117 PEECVVIEDSR 127
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 102-178 8.42e-06

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 45.27  E-value: 8.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 102 ELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIEVMSD---KTEKEYL--RLLSILQIAPSELLM 176
Cdd:cd04302    81 EVYPGIPELLEKLKAAG-YRLYVATSKPEVFARRILEHFGLDEYFDGIAGASLdgsRVHKADVirYALDTLGIAPEQAVM 159


                  ..
gi 1763957597 177 VG 178
Cdd:cd04302   160 IG 161
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
5-185 1.48e-05

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 44.73  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597   5 IKVIAFDADDTLWSNEPFFQEVEKQYTDLLKPYGTS-KEISAALFQTEMNNLQ---------ILGYGAKAFTISMVETAL 74
Cdd:PRK10748   10 ISALTFDLDDTLYDNRPVILRTEQEALAFVQNYHPAlRSFQNEDLQRLRQALReaepeiyhdVTRWRWRAIEQAMLDAGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  75 QISNGKIAADIIRQIVDLGKSLLKMPIEllpgVKETLKTLKEtgKYKLVVATKGDLldqenKLERSGLSPYFDHI----- 149
Cdd:PRK10748   90 SAEEASAGADAAMINFAKWRSRIDVPQA----THDTLKQLAK--KWPLVAITNGNA-----QPELFGLGDYFEFVlragp 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1763957597 150 EVMSDKTEKEYLRLLSILQIAPSELLMVGNSFKSDI 185
Cdd:PRK10748  159 HGRSKPFSDMYHLAAEKLNVPIGEILHVGDDLTTDV 194
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 105-180 2.24e-05

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: 43.81  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 105 PGVKETLKTLKETGKYKLVVATKgdLLDQENK-LERSGLSPYFDHIeVMSDKTEKE------YLRLLSILQIAPSELLMV 177
Cdd:cd02616    83 PGVYETLARLKSQGIKLGVVTTK--LRETALKgLKLLGLDKYFDVI-VGGDDVTHHkpdpepVLKALELLGAEPEEALMV 159


                  ...
gi 1763957597 178 GNS 180
Cdd:cd02616   160 GDS 162
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 107-192 1.52e-04

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: 40.35  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597 107 VKETLKTLKETGkYKLVVATKGDLLdQENKLERSGLSPYFDHI----EVMSDKTEKEYLRL-LSILQIAPSELLMVGNSF 181
Cdd:cd16415    12 AVETLKDLKEKG-LKLAVVSNFDRR-LRELLEALGLDDYFDFVvfsyEVGYEKPDPRIFQKaLERLGVSPEEALHVGDDL 89

                          90
                  ....*....|.
gi 1763957597 182 KSDIQPVLSLG 192
Cdd:cd16415    90 KNDYLGARAVG 100
PRK10826 PRK10826
hexitol phosphatase HxpB;
77-150 3.87e-04

hexitol phosphatase HxpB;


Pssm-ID: 236770 [Multi-domain]  Cd Length: 222  Bit Score: 40.32  E-value: 3.87e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1763957597  77 SNGKIAADIIRQIVdlgkSLLKMPIELLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIE 150
Cdd:PRK10826   71 SRQEVVQRIIARVI----SLIEETRPLLPGVREALALCKAQG-LKIGLASASPLHMLEAVLTMFDLRDYFDALA 139
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 91-177 5.43e-04

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: 39.94  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1763957597  91 DLGKSLLKMPieLLPGVKETLKTLKETGkYKLVVATKGDLLDQENKLERSGLSPYFDHIeVMSDKTEKE------YLRLL 164
Cdd:cd02588    82 ELGDAYLRLP--PFPDVVAGLRRLREAG-YRLAILSNGSPDLIEDVVANAGLRDLFDAV-LSAEDVRAYkpapavYELAA 157

                          90
                  ....*....|...
gi 1763957597 165 SILQIAPSELLMV 177
Cdd:cd02588   158 ERLGVPPDEILHV 170
HAD_MDP-1_like cd07501
eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to ...
 100-151 8.82e-03

eukaryotic hypothetical phosphotyrosine phosphatase MDP-1 and related phosphatases, similar to Bacillus cereus phosphonoacetaldehyde hydrolase and Streptomyces FkbH; This family includes eukaryotic magnesium-dependent phosphatase-1 (MDP-1) which is most likely a phosphotyrosine phosphatase catalyzing the dephosphorylation of tyrosine-phosphorylated proteins, Bacillus cereus phosphonoacetaldehyde hydrolase (phosphonatase)which catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor, and sequences annotated as FkbH including BafAIV an FkbH-like protein from Streptomyces griseus encoded in ORF12 of the bafilomycin synthesis gene cluster. 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: 319804 [Multi-domain]  Cd Length: 129  Bit Score: 35.40  E-value: 8.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1763957597 100 PIELLPGVKETLKTLKETGkYKLVVATKGDLLDQEN-KLERSGLSPYFDHIEV 151
Cdd:cd07501    32 EVSLYPDAQEILKELKERG-ILLAVASRNNEFDHANeVLEKLDLKELFDAFEI 83
 
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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