NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501565927|ref|WP_012570375|]
View 

HAD family acid phosphatase [Coxiella burnetii]

Protein Classification

HAD family acid phosphatase( domain architecture ID 10510170)

HAD (haloacid dehalogenase) family acid phosphatase catalyzes the dephosphorylation of a wide variety of substrates such as sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 40-224 4.08e-47

HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins.


:

Pssm-ID: 397712  Cd Length: 213  Bit Score: 154.45  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   40 YHESGEYDVDISKVTHLAKRYLADRIRENQhashpKKLAMVLDIDETSLSNYSDIKVLNFGGTFLQQ---DLAEADGDDP 116
Cdd:pfam03767  29 YMNGQQYSSDSKAVVDQAYNYAKERELHGD-----KKDAVVFDIDETVLSNSPYYAYHGYGGEPFDPekfDEWVNKGEAP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  117 AITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIVL 196
Cdd:pfam03767 104 ALPGALELYNYLVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEKLILRGKKDSNKSATSYKSERRKKLVKKGYNIVG 183

                         170       180       190
                  ....*....|....*....|....*....|
gi 501565927  197 NMGDQYSDLKGG--YSEHNYKLPNFMYYIP 224
Cdd:pfam03767 184 NIGDQWSDFLGNgaRGIRTFKLPNPMYYIW 213
 
Name Accession Description Interval E-value
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 40-224 4.08e-47

HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins.


Pssm-ID: 397712  Cd Length: 213  Bit Score: 154.45  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   40 YHESGEYDVDISKVTHLAKRYLADRIRENQhashpKKLAMVLDIDETSLSNYSDIKVLNFGGTFLQQ---DLAEADGDDP 116
Cdd:pfam03767  29 YMNGQQYSSDSKAVVDQAYNYAKERELHGD-----KKDAVVFDIDETVLSNSPYYAYHGYGGEPFDPekfDEWVNKGEAP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  117 AITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIVL 196
Cdd:pfam03767 104 ALPGALELYNYLVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEKLILRGKKDSNKSATSYKSERRKKLVKKGYNIVG 183

                         170       180       190
                  ....*....|....*....|....*....|
gi 501565927  197 NMGDQYSDLKGG--YSEHNYKLPNFMYYIP 224
Cdd:pfam03767 184 NIGDQWSDFLGNgaRGIRTFKLPNPMYYIW 213
HAD_VSP cd07535
vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the ...
 39-223 1.07e-41

vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319837  Cd Length: 186  Bit Score: 139.82  E-value: 1.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  39 HYHESGEYDVDISKVTHLAKRYLADRIRENQHashpkKLAMVLDIDETSLSNYSDIKVLNFGGTFLQQDLAEA---DGDD 115
Cdd:cd07535    3 DYMKGGQYLRDSSVKTVNALAYAYSKVLAGDG-----MDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDEwveKGKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 116 PAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIV 195
Cdd:cd07535   78 PALPESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVVYKSEQRKELEEKGYRIV 157

                        170       180
                 ....*....|....*....|....*....
gi 501565927 196 LNMGDQYSDLKGGYSE-HNYKLPNFMYYI 223
Cdd:cd07535  158 GNIGDQWSDLLGDPEGdRTFKLPNPMYYI 186
plant-AP TIGR01675
plant acid phosphatase; This model represents a family of acid phosphatase from plants which ...
 27-224 1.07e-37

plant acid phosphatase; This model represents a family of acid phosphatase from plants which are most closely related to the (so called) class B non-specific acid phosphatase OlpA (TIGR01533, which is believed to be a 5'-nucleotide phosphatase) and somewhat more distantly to another class B phosphatase, AphA (TIGR01672). Together these three clades define a subfamily (pfam03767) which corresponds to the IIIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. It has been reported that the best substrate for this enzyme that could be found was purine 5'-nucleoside phosphates. This is in concordance with the assignment of the H. influenzae hel protein (from TIGR01533) as a 5'-nucleotidase, however there is presently no other evidence to support this specific function for these plant phosphatases. Many genes from this family have been annotated as vegetative storage proteins due to their close homology with these earlier-characterized gene products, which are highly expressed in leaves. There are significant differences however, including expression levels and distribution. The most important difference is the lack in authentic VSPs of the nucleophilic aspartate residue, which is instead replaced by serine, glycine or asparagine. Thus these proteins can not be expected to be active phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP. This model explicitly excludes the VSPs which lack the nucleophilc aspartate. The possibility exists, however, that some members of this family may, while containing all of the conserved HAD-superfamily catalytic residues, lack activity and have a function related to the function of the VSPs rather than the acid phosphatases.


Pssm-ID: 273749  Cd Length: 228  Bit Score: 131.03  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   27 PLNLDSLKKEiihYHESGEYDVDISKVTHLAKRYLADRIRENQHAShpkklAMVLDIDETSLSNYSDIKVLNFGGTFLQ- 105
Cdd:TIGR01675  35 PAECKDYVED---YMTSKQYKRDSKRVVDEAYFYAKSLALSGDGMD-----AWIFDVDDTLLSNIPYYKKHGYGTEKTDp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  106 ---QDLAEAdGDDPAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKIS 182
Cdd:TIGR01675 107 tafWDWLEK-GEAPALPETLKLYQKLLELGIKIFLLSGRWEELRSATVENLINAGFTGWKHLILRGLEDSQKTVVTYKSE 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 501565927  183 ERKAIEKEGYDIVLNMGDQYSDLKGGY-SEHNYKLPNFMYYIP 224
Cdd:TIGR01675 186 VRKSLVEEGYRIVGNIGDQWSDLLGSPpGRRTFKLPNPMYYVP 228
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
40-204 2.64e-20

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 86.17  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  40 YHESGEYDVDISKVTHLAKRYLADRIRENqhaSHPKKLAMVLDIDETSLSN--YSDIKVLNfGGTFLQQDLAE--ADGDD 115
Cdd:COG2503   47 MQTSAEYRALAYQAYNLAKLRLDAALAQP---SGGKPPAVVLDLDETVLDNspYQAWLIKN-GKSFDPKTWDEwvKEAQA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 116 PAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQwarlyMKPNDYRLNSAAPYKISERKAIEKEgYDIV 195
Cdd:COG2503  123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFPV-----VDEDHLLLKTDGSDKEARRQAVAKR-YRIV 196


                 ....*....
gi 501565927 196 LNMGDQYSD 204
Cdd:COG2503  197 MLVGDNLGD 205
 
Name Accession Description Interval E-value
Acid_phosphat_B pfam03767
HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid ...
 40-224 4.08e-47

HAD superfamily, subfamily IIIB (Acid phosphatase); This family proteins includes acid phosphatases and a number of vegetative storage proteins.


Pssm-ID: 397712  Cd Length: 213  Bit Score: 154.45  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   40 YHESGEYDVDISKVTHLAKRYLADRIRENQhashpKKLAMVLDIDETSLSNYSDIKVLNFGGTFLQQ---DLAEADGDDP 116
Cdd:pfam03767  29 YMNGQQYSSDSKAVVDQAYNYAKERELHGD-----KKDAVVFDIDETVLSNSPYYAYHGYGGEPFDPekfDEWVNKGEAP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  117 AITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIVL 196
Cdd:pfam03767 104 ALPGALELYNYLVELGVKIFFVSGRSEDLRAATVENLKKAGFHGWEKLILRGKKDSNKSATSYKSERRKKLVKKGYNIVG 183

                         170       180       190
                  ....*....|....*....|....*....|
gi 501565927  197 NMGDQYSDLKGG--YSEHNYKLPNFMYYIP 224
Cdd:pfam03767 184 NIGDQWSDFLGNgaRGIRTFKLPNPMYYIW 213
HAD_VSP cd07535
vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the ...
 39-223 1.07e-41

vegetative storage proteins similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases, it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319837  Cd Length: 186  Bit Score: 139.82  E-value: 1.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  39 HYHESGEYDVDISKVTHLAKRYLADRIRENQHashpkKLAMVLDIDETSLSNYSDIKVLNFGGTFLQQDLAEA---DGDD 115
Cdd:cd07535    3 DYMKGGQYLRDSSVKTVNALAYAYSKVLAGDG-----MDVWIFDIDDTLLSNIPYYKKHGYGGEKFDSTAFDEwveKGKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 116 PAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIV 195
Cdd:cd07535   78 PALPESLKLYNKLLELGFKIFLLSGRDETLRNATVENLKKAGYHGWEHLILRGPDDQGKSAVVYKSEQRKELEEKGYRIV 157

                        170       180
                 ....*....|....*....|....*....
gi 501565927 196 LNMGDQYSDLKGGYSE-HNYKLPNFMYYI 223
Cdd:cd07535  158 GNIGDQWSDLLGDPEGdRTFKLPNPMYYI 186
HAD_VSP_like cd01624
vegetative storage proteins and related proteins, similar to soybean VSPalpha and VSPbeta ...
 62-221 2.09e-40

vegetative storage proteins and related proteins, similar to soybean VSPalpha and VSPbeta proteins; belongs to the haloacid dehalogenase-like superfamily; Soybean [Glycine max (L.) Merr.] vegetative storage protein VSPalpha and VSPbeta levels were identified as storage proteins due to their abundance and pattern of expression in plant tissues, they accumulate to almost one-half the amount of soluble leaf protein when soybean plants are continually depodded. They possess acid phosphatase activity which appears to be low compared to several other plant acid phosphatases; it increases in the leaves of depodded soybean plants, but to no more than 0.1% of the total acid phosphatase activity in these leaves. This acid phosphatase activity has maximal activity at pH 5.0 - 5.5, and can liberate Pi from different substrates such as napthyl acid phosphate, carboxyphenyl phosphate, sugar-phosphates, glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, ATP, ADP, PPi, and short chain polyphosphates; they cleave phosphoenolpyruvate, ATP, ADP, PPI, and polyphosphates most efficiently. 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. Soybean VSPalpha and VSPbeta lack this active site aspartate, other members of this family have this aspartate and may be more active. 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: 319765 [Multi-domain]  Cd Length: 160  Bit Score: 135.75  E-value: 2.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  62 ADRIRENQHAshPKKLAMVLDIDETSLSNYSDIKVLNFG-GTFLQQDLAEAD-GDDPAITPTLNLYRYAIQHGVAVFFIT 139
Cdd:cd01624    1 KEAIAYAAGL--DTVNAWVFDIDDTLLSSIDYLKKYGGTeGTAPGIWNSWLErGDSPPVPETLELAEYALEKGVEVFFIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 140 GRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKISERKAIEKEGYDIVLNMGDQYSDLKGGYSEHNYKLPNF 219
Cdd:cd01624   79 DRWEKLREPTVENLKAAGYTVWSHLFLKPNGNKSKTVVVYKAKVRASIESKGYTIVANIGDQWSDLVGGYAERTFKLPNY 158


                 ..
gi 501565927 220 MY 221
Cdd:cd01624  159 LY 160
plant-AP TIGR01675
plant acid phosphatase; This model represents a family of acid phosphatase from plants which ...
 27-224 1.07e-37

plant acid phosphatase; This model represents a family of acid phosphatase from plants which are most closely related to the (so called) class B non-specific acid phosphatase OlpA (TIGR01533, which is believed to be a 5'-nucleotide phosphatase) and somewhat more distantly to another class B phosphatase, AphA (TIGR01672). Together these three clades define a subfamily (pfam03767) which corresponds to the IIIB subfamily of the haloacid dehalogenase (HAD) superfamily of aspartate nucleophile hydrolases. It has been reported that the best substrate for this enzyme that could be found was purine 5'-nucleoside phosphates. This is in concordance with the assignment of the H. influenzae hel protein (from TIGR01533) as a 5'-nucleotidase, however there is presently no other evidence to support this specific function for these plant phosphatases. Many genes from this family have been annotated as vegetative storage proteins due to their close homology with these earlier-characterized gene products, which are highly expressed in leaves. There are significant differences however, including expression levels and distribution. The most important difference is the lack in authentic VSPs of the nucleophilic aspartate residue, which is instead replaced by serine, glycine or asparagine. Thus these proteins can not be expected to be active phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP. This model explicitly excludes the VSPs which lack the nucleophilc aspartate. The possibility exists, however, that some members of this family may, while containing all of the conserved HAD-superfamily catalytic residues, lack activity and have a function related to the function of the VSPs rather than the acid phosphatases.


Pssm-ID: 273749  Cd Length: 228  Bit Score: 131.03  E-value: 1.07e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   27 PLNLDSLKKEiihYHESGEYDVDISKVTHLAKRYLADRIRENQHAShpkklAMVLDIDETSLSNYSDIKVLNFGGTFLQ- 105
Cdd:TIGR01675  35 PAECKDYVED---YMTSKQYKRDSKRVVDEAYFYAKSLALSGDGMD-----AWIFDVDDTLLSNIPYYKKHGYGTEKTDp 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  106 ---QDLAEAdGDDPAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMKPNDYRLNSAAPYKIS 182
Cdd:TIGR01675 107 tafWDWLEK-GEAPALPETLKLYQKLLELGIKIFLLSGRWEELRSATVENLINAGFTGWKHLILRGLEDSQKTVVTYKSE 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 501565927  183 ERKAIEKEGYDIVLNMGDQYSDLKGGY-SEHNYKLPNFMYYIP 224
Cdd:TIGR01675 186 VRKSLVEEGYRIVGNIGDQWSDLLGSPpGRRTFKLPNPMYYVP 228
Veg_Stor_Prot TIGR01680
vegetative storage protein; The proteins represented by this model are close relatives of the ...
 39-218 2.02e-28

vegetative storage protein; The proteins represented by this model are close relatives of the plant acid phosphatases (TIGR01675), are limited to members of the Phaseoleae including Glycine max (soybean) and Phaseolus vulgaris (kidney bean). These proteins are highly expressed in the leaves of repeatedly depodded plants. VSP differs most strinkingly from the acid phosphatases in the lack of the conserved nucleophilic aspartate residue in the N-terminus, thus, they should be inactive as phosphatases. This issue was confused by the publication in 1992 of an article claiming activity for the Glycine max VSP. In 1994 this assertion was refuted by the separation of the activity from the VSP.


Pssm-ID: 130741  Cd Length: 275  Bit Score: 108.28  E-value: 2.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927   39 HYHESGEYDVDISKVTHLAKRYLADRirenqhASHPKKLaMVLDIDETSLSNYSDIKVLNFGGTFLQQDLAEAD----GD 114
Cdd:TIGR01680  71 EYIEGEQYRSDSKTVNQQAYFFARDL------EVHEKDT-FLFNIDGTALSNIPYYKKHGYGSEKFDSELYDEEfvnkGE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  115 DPAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQWARLYMK-PNDYRLNSAAPYKISERKAIEKEGYD 193
Cdd:TIGR01680 144 APALPETLKNYNKLVSLGFKIIFLSGRLKDKQAVTEANLKKAGYHTWEKLILKdPQDNSAENAVEYKTAARAKLIQEGYN 223

                         170       180
                  ....*....|....*....|....*..
gi 501565927  194 IVLNMGDQYSDLKGGY--SEHNYKLPN 218
Cdd:TIGR01680 224 IVGIIGDQWNDLKGEHrgAIRSFKLPN 250
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
40-204 2.64e-20

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 86.17  E-value: 2.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  40 YHESGEYDVDISKVTHLAKRYLADRIRENqhaSHPKKLAMVLDIDETSLSN--YSDIKVLNfGGTFLQQDLAE--ADGDD 115
Cdd:COG2503   47 MQTSAEYRALAYQAYNLAKLRLDAALAQP---SGGKPPAVVLDLDETVLDNspYQAWLIKN-GKSFDPKTWDEwvKEAQA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 116 PAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIKNLKTAGYSQwarlyMKPNDYRLNSAAPYKISERKAIEKEgYDIV 195
Cdd:COG2503  123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFPV-----VDEDHLLLKTDGSDKEARRQAVAKR-YRIV 196


                 ....*....
gi 501565927 196 LNMGDQYSD 204
Cdd:COG2503  197 MLVGDNLGD 205
HAD_CAP cd07534
molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; ...
 74-221 2.43e-14

molecular class C acid phosphatases, similar to Haemophilus influenzae e (P4) acid phosphatase; belongs to the haloacid dehalogenase-like hydrolase superfamily; Molecular class C acid phosphatases (CAPs) are nonspecific acid phosphatases with generally broad substrate specificity and optimum activity at neutral to acidic pH. Members include Haemophilus influenzae lipoprotein e (P4), Elizabethkingia meningosepticum OlpA, Helicobacter pylori HppA, Enterobacter sp. 4 acid phosphatase PhoI, and Streptococcus pyogenes M1 GAS LppC. Lipoprotein e (P4) exhibits phosphomonoesterase activity with aryl phosphate substrates including nicotinamide mononucleotide (NMN), tyrosine phosphate, phenyl phosphate, p-nitrophenyl phosphate, and 4-methylumbelliferyl phosphate. The role of P4 in NAD+ uptake appears to be the dephosphorylation of NMN to nicotinamide riboside, which is then taken up by the organism. Elizabethkingia meningosepticum OlpA is a broad-spectrum nucleotidase with preference for 5'-nucleotides, it efficiently hydrolyzes nucleotide monophosphates, with a strong preference for 5'-nucleotides and for 3'-AMP; OlpA can also hydrolyze sugar phosphates and beta-glycerol phosphate, although with a lower efficiency. Helicobacter pylori HppA is also a 5' nucleotidase. 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: 319836 [Multi-domain]  Cd Length: 196  Bit Score: 68.90  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  74 PKKLAMVLDIDETSLSN--YSDIKVLNFGGTFLQQ-DLAEADGDDPAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATI 150
Cdd:cd07534   29 DKKPAVVLDLDETVLDNspYQARQVKNGKPFSPETwDKWVQEAQAKPIPGAVDFLNYANAKGVTIFYVSNRDQKLKAATL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927 151 KNLKTAGYSQwarlyMKPNDYRLNSAAPYKISERKAIeKEGYDIVLNMGDQYSD-------------------LKGGYSE 211
Cdd:cd07534  109 KNLKRLGFPQ-----ASDDHLLLKTDKSSKESRRQLV-KEKYNIVLLFGDNLGDfgdftykkenedrralvekNAEEFGE 182

                        170
                 ....*....|
gi 501565927 212 HNYKLPNFMY 221
Cdd:cd07534  183 KFIILPNPMY 192
HAD_PNKP-C cd07502
C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related ...
 78-200 5.44e-03

C-terminal phosphatase domain of T4 polynucleotide kinase/phosphatase (PNKP) and related phosphatases; This family includes the C-terminal domain of the bifunctional enzyme T4 polynucleotide kinase/phosphatase, PNKP. The PNKP phosphatase domain can catalyze the hydrolytic removal of the 3'-phosphoryl of DNA, RNA and deoxynucleoside 3'-monophosphates. 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: 319805  Cd Length: 145  Bit Score: 35.97  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501565927  78 AMVLDIDETsLSNysdikvLNFGGTFLQQ-----DLAEADGD-DPAITPTLNLYRYAIQHGVAVFFITGRQEKYRTATIK 151
Cdd:cd07502    3 AVIFDLDGT-LAD------TNGRQPYLERrprdwDAFFEAADhDPPNAPVIELVKESALTGYEIVYLSGRPERYRRDTLR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 501565927 152 NLKTAGYsQWARLYMKPN-DYRLNSAAPYKISERKAieKEGYDIVLNMGD 200
Cdd:cd07502   76 WLAKHGI-PDDALHMRGNaDRRKDRRVKLEILRRLI--RTRFEVRLLVDD 122
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH