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Conserved domains on  [gi|488219640|ref|WP_002290848|]
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MULTISPECIES: YqeG family HAD IIIA-type phosphatase [Enterococcus]

Protein Classification

YqeG family HAD IIIA-type phosphatase( domain architecture ID 11450658)

YqeG family HAD (haloacid dehalogenase) IIIA-type phosphatase similar to Bacillus subtilis YqeG, which may be involved in the hydrolysis of the phosphate group of 5'-nucleotides and is necessary for normal colony formation on solid medium

CATH:  3.30.1240.10
EC:  3.1.3.-
Gene Ontology:  GO:0042578
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
2-165 1.25e-80

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


:

Pssm-ID: 441782  Cd Length: 164  Bit Score: 236.18  E-value: 1.25e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   2 FSNYKPTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEK 81
Cdd:COG2179    1 LKLLKPDEYVKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNSEKRVKRFAEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  82 FDLLYVARAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKPIIATDSWKTQFNRFLEKRIMAYL 161
Cdd:COG2179   81 LGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFWFTRINRFLERRILKRL 160


                 ....
gi 488219640 162 LAKH 165
Cdd:COG2179  161 KKKG 164
 
Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
2-165 1.25e-80

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 236.18  E-value: 1.25e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   2 FSNYKPTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEK 81
Cdd:COG2179    1 LKLLKPDEYVKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNSEKRVKRFAEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  82 FDLLYVARAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKPIIATDSWKTQFNRFLEKRIMAYL 161
Cdd:COG2179   81 LGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFWFTRINRFLERRILKRL 160


                 ....
gi 488219640 162 LAKH 165
Cdd:COG2179  161 KKKG 164
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 29-136 5.35e-56

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: 171.68  E-value: 5.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEKFDLLYVARAMKPLARGINIAKKQLDLA 108
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDLP 80

                         90       100
                 ....*....|....*....|....*...
gi 488219640 109 DDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:cd16416   81 PEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 7-170 3.61e-37

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 125.98  E-value: 3.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640    7 PTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEK-FDLL 85
Cdd:TIGR01668   5 PHAIVKTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAGEQRAKAVEKaLGIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   86 YVARAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKPIIATD-SWKTQFNRFLEKRIMAYLLAK 164
Cdd:TIGR01668  85 VLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDqWFIKRIWRRVERTVLKFLVSR 164


                  ....*.
gi 488219640  165 HPDMGW 170
Cdd:TIGR01668 165 GGPAPE 170
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
45-136 6.26e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 60.68  E-value: 6.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEKFDLLY-----VARAM----KPLARGINIAKKQLDLADDEIVMV 115
Cdd:pfam13419  82 PGIKELLEEL---KEQGYKLGIVTSKSRENVEEFLKQLGLEDyfdviVGGDDvegkKPDPDPILKALEQLGLKPEEVIYV 158

                          90       100
                  ....*....|....*....|.
gi 488219640  116 GDQImTDIRGANRAGIRSILV 136
Cdd:pfam13419 159 GDSP-RDIEAAKNAGIKVIAV 178
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
45-136 2.53e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 42.87  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEKFDL-----LYVA----RAMKPLARGINIAKKQLDLADDEIVMV 115
Cdd:PRK13222  96 PGVKETLAAL---KAAGYPLAVVTNKPTPFVAPLLEALGIadyfsVVIGgdslPNKKPDPAPLLLACEKLGLDPEEMLFV 172

                         90       100
                 ....*....|....*....|.
gi 488219640 116 GDQImTDIRGANRAGIRSILV 136
Cdd:PRK13222 173 GDSR-NDIQAARAAGCPSVGV 192
 
Name Accession Description Interval E-value
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
2-165 1.25e-80

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 236.18  E-value: 1.25e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   2 FSNYKPTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEK 81
Cdd:COG2179    1 LKLLKPDEYVKSIYDIDPEKLKEKGIKGLILDLDNTLVPWDEPEATPEVIEWLEELKEAGFKVCIVSNNSEKRVKRFAEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  82 FDLLYVARAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKPIIATDSWKTQFNRFLEKRIMAYL 161
Cdd:COG2179   81 LGIPYIARAKKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTILVKPLVDKEFWFTRINRFLERRILKRL 160


                 ....
gi 488219640 162 LAKH 165
Cdd:COG2179  161 KKKG 164
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 29-136 5.35e-56

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: 171.68  E-value: 5.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEKFDLLYVARAMKPLARGINIAKKQLDLA 108
Cdd:cd16416    1 GVITDLDNTLLAWDNPDLTPEVKAWLADLKEAGIKVVLVSNNNERRVAKVIEKLDLPFVARAGKPRPRAFRRALKEMDLP 80

                         90       100
                 ....*....|....*....|....*...
gi 488219640 109 DDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:cd16416   81 PEQVAMVGDQLFTDILGGNRAGLYTILV 108
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 7-170 3.61e-37

HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. This family consists of sequences from fungi, plants, cyanobacteria, gram-positive bacteria and Deinococcus. There is presently no characterization of any sequence in this family.


Pssm-ID: 273744  Cd Length: 170  Bit Score: 125.98  E-value: 3.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640    7 PTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEK-FDLL 85
Cdd:TIGR01668   5 PHAIVKTLNDLTIDLLKKVGIKGVVLDKDNTLVYPDHNEAYPALRDWIEELKAAGRKLLIVSNNAGEQRAKAVEKaLGIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   86 YVARAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKPIIATD-SWKTQFNRFLEKRIMAYLLAK 164
Cdd:TIGR01668  85 VLPHAVKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDqWFIKRIWRRVERTVLKFLVSR 164


                  ....*.
gi 488219640  165 HPDMGW 170
Cdd:TIGR01668 165 GGPAPE 170
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 22-138 3.41e-17

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: 75.45  E-value: 3.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  22 LKNLGIKAVLTDLDNTLIAWNN----PDGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEK------FDLLYVA--- 88
Cdd:COG1011   69 LEELGLDLAEELAEAFLAALPElvepYPDALELLEAL---KARGYRLALLTNGSAELQEAKLRRlglddlFDAVVSSeev 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488219640  89 RAMKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKP 138
Cdd:COG1011  146 GVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVWVNR 195
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 28-138 4.58e-16

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


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 70.51  E-value: 4.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   28 KAVLTDLDNTLI-------AWNNPDGTEELLTWILEMKNAGIPVVVVSNNN-----------SKRVARAIEK----FDLL 85
Cdd:TIGR01662   1 KAVVLDLDGTLTddvpyvsDEDERILYPEVPDALAELKEAGYKVVIVTNQSgigrgyfsrsfSGRVARRLEElgvpIDIL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488219640   86 YVARAM-KPLARGINIAKKQLDLAD-DEIVMVGDQIMTDIRGANRAGIRSILVKP 138
Cdd:TIGR01662  81 YACPGCrKPKPGMFLEALKRFNEIDpEESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 29-136 1.75e-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: 68.19  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIAwnnpdgtEELLTwilEMKNAGIPVVVVSNNNSKRVARAIEKFDLLYV---------ARAMKPLARGIN 99
Cdd:cd01427    1 AVLFDLDGTLLA-------VELLK---RLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdgiigsdgGGTPKPKPKPLL 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488219640 100 IAKKQLDLADDEIVMVGDQImTDIRGANRAGIRSILV 136
Cdd:cd01427   71 LLLLKLGVDPEEVLFVGDSE-NDIEAARAAGGRTVAV 106
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
45-136 1.12e-12

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 63.41  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEKFDLL-YVAR--------AMKPLARGINIAKKQLDLADDEIVMV 115
Cdd:COG0546   87 PGVRELLEAL---KARGIKLAVVTNKPREFAERLLEALGLDdYFDAivggddvpPAKPKPEPLLEALERLGLDPEEVLMV 163

                         90       100
                 ....*....|....*....|.
gi 488219640 116 GDQImTDIRGANRAGIRSILV 136
Cdd:COG0546  164 GDSP-HDIEAARAAGVPFIGV 183
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 29-134 2.53e-12

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: 60.25  E-value: 2.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIawnnpDGTEELLTWIlemkNAGIPVVVVSNNNS----KRVARA-IEK-FDLLYVARAM---KPLARGIN 99
Cdd:cd04305    1 AIIFDLDDTLL-----PGAKELLEEL----KKGYKLGIITNGPTevqwEKLEQLgIHKyFDHIVISEEVgvqKPNPEIFD 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488219640 100 IAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSI 134
Cdd:cd04305   72 YALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
45-136 6.26e-12

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 60.68  E-value: 6.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEKFDLLY-----VARAM----KPLARGINIAKKQLDLADDEIVMV 115
Cdd:pfam13419  82 PGIKELLEEL---KEQGYKLGIVTSKSRENVEEFLKQLGLEDyfdviVGGDDvegkKPDPDPILKALEQLGLKPEEVIYV 158

                          90       100
                  ....*....|....*....|.
gi 488219640  116 GDQImTDIRGANRAGIRSILV 136
Cdd:pfam13419 159 GDSP-RDIEAAKNAGIKVIAV 178
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
92-136 1.76e-11

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 60.51  E-value: 1.76e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488219640  92 KPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:COG0647  186 KPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLV 230
Hydrolase_like pfam13242
HAD-hyrolase-like;
92-137 4.41e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 53.39  E-value: 4.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488219640   92 KPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVK 137
Cdd:pfam13242   4 KPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVL 49
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 29-138 1.75e-09

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: 53.06  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIAwnnpdgtEELLTWIlemKNAGIPVVVVSNNNSK-----RVARAIEKFDLLYV---ARAMKPLARGINI 100
Cdd:cd16415    1 LITFDVTGTLLA-------VETLKDL---KEKGLKLAVVSNFDRRlrellEALGLDDYFDFVVFsyeVGYEKPDPRIFQK 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488219640 101 AKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVKP 138
Cdd:cd16415   71 ALERLGVSPEEALHVGDDLKNDYLGARAVGWHALLVDR 108
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 6-130 1.08e-08

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: 52.20  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640    6 KPTWMVEA-IYQITPAQLKNLGIKAVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVSNNNSKRVARAIEKFDL 84
Cdd:pfam00702  58 KRDWLEELdILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGL 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488219640   85 L---------YVARAMKPLARGINIAKKQLDLADDEIVMVGDQImTDIRGANRAG 130
Cdd:pfam00702 138 DdyfdvvisgDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 92-136 2.13e-07

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: 49.13  E-value: 2.13e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488219640  92 KPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:cd07530  177 KPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLV 221
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 92-137 3.41e-06

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: 45.73  E-value: 3.41e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488219640  92 KPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVK 137
Cdd:cd07509  172 KPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVR 217
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 7-136 3.66e-06

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: 45.10  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640    7 PTWMVEAIYQITPAQLKNLGIKAVLTDLDNTLIAwnnpdgteelltwileMKNAGIPVVVVSNNN--SKRVARAIE---K 81
Cdd:TIGR01509  58 PEDAQLLYKQLFYEQIEEEAKLKPLPGVRALLEA----------------LRARGKKLALLTNSPraHKLVLALLGlrdL 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488219640   82 FDLLYVA---RAMKPLARGINIAKKQLDLADDEIVMVGDQIMtDIRGANRAGIRSILV 136
Cdd:TIGR01509 122 FDVVIDSsdvGLGKPDPDIYLQALKALGLEPSECVFVDDSPA-GIEAAKAAGMHTVGV 178
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 48-140 1.02e-05

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 43.87  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  48 EELLTWILEMKNAGIPVVVVSNNN-------SKRVARAIEKFDLLYV---ARAMKPLARGINIAKKQLDLADDEIVMVgD 117
Cdd:cd02603   87 PEMLDLLEALRAKGYKVYLLSNTWpdhfkfqLELLPRRGDLFDGVVEscrLGVRKPDPEIYQLALERLGVKPEEVLFI-D 165

                         90       100
                 ....*....|....*....|...
gi 488219640 118 QIMTDIRGANRAGIRSILVKPII 140
Cdd:cd02603  166 DREENVEAARALGIHAILVTDAE 188
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
45-136 2.53e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 42.87  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEKFDL-----LYVA----RAMKPLARGINIAKKQLDLADDEIVMV 115
Cdd:PRK13222  96 PGVKETLAAL---KAAGYPLAVVTNKPTPFVAPLLEALGIadyfsVVIGgdslPNKKPDPAPLLLACEKLGLDPEEMLFV 172

                         90       100
                 ....*....|....*....|.
gi 488219640 116 GDQImTDIRGANRAGIRSILV 136
Cdd:PRK13222 173 GDSR-NDIQAARAAGCPSVGV 192
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 106-136 2.72e-05

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


Pssm-ID: 319827 [Multi-domain]  Cd Length: 253  Bit Score: 43.08  E-value: 2.72e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488219640 106 DLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:cd07525  198 RPAKARILAVGDGLHTDILGANAAGLDSLFV 228
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
45-136 3.09e-05

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 42.50  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEK------FDLLY----VARAmKP-----LArginiAKKQLDLAD 109
Cdd:COG0637   89 PGVVELLEAL---KEAGIKIAVATSSPRENAEAVLEAaglldyFDVIVtgddVARG-KPdpdiyLL-----AAERLGVDP 159

                         90       100
                 ....*....|....*....|....*..
gi 488219640 110 DEIVMVGDqIMTDIRGANRAGIRSILV 136
Cdd:COG0637  160 EECVVFED-SPAGIRAAKAAGMRVVGV 185
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 92-137 4.13e-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: 42.31  E-value: 4.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 488219640   92 KPLARGINIAKKQLDLADDEI-VMVGDQIMTDIRGANRAGIRSILVK 137
Cdd:TIGR01460 188 KPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVL 234
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 54-130 5.36e-05

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: 41.61  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   54 ILEMKNAGIPVVVVSNNNSKRVARAIEKFDLL--------YVARAMKPLARGINIAKKQLDLaDDEIVMVGDQImTDIRG 125
Cdd:TIGR01549  82 LARLKSAGIKLGIISNGSLRAQKLLLRLFGLGdyfelilvSDEPGSKPEPEIFLAALESLGV-PPEVLHVGDNL-NDIEG 159


                  ....*
gi 488219640  126 ANRAG 130
Cdd:TIGR01549 160 ARNAG 164
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 45-136 5.61e-05

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: 41.84  E-value: 5.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTWileMKNAGIPVVVVSNNNSKRVARAIEKFDLL-YVA--------RAMKPLARGINIAKKQLDLADDEIVMV 115
Cdd:cd16417   90 PGVKEGLAA---LKAQGYPLACVTNKPERFVAPLLEALGISdYFSlvlggdslPEKKPDPAPLLHACEKLGIAPAQMLMV 166

                         90       100
                 ....*....|....*....|.
gi 488219640 116 GDQImTDIRGANRAGIRSILV 136
Cdd:cd16417  167 GDSR-NDILAARAAGCPSVGL 186
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 92-136 1.00e-04

uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid dehalogenase-like superfamily; This uncharacterized 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: 319858 [Multi-domain]  Cd Length: 247  Bit Score: 41.27  E-value: 1.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488219640  92 KPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:cd16422  177 KPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILV 221
HAD_BPGM-like cd07505
beta-phosphoglucomutase-like family of the haloacid dehalogenase-like (HAD) hydrolase ...
 29-136 1.39e-04

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: 39.91  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLI--------AWN-------------------NPDGTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIEK 81
Cdd:cd07505    1 AVIFDMDGVLIdteplhrqAWQllerknallleliaseglkLKPGVVELLDAL---KAAGIPVAVATSSSRRNVELLLLE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488219640  82 FDLLY----------VARAMKPLARGINIAKKQLDLADDEIVMVGDqIMTDIRGANRAGIRSILV 136
Cdd:cd07505   78 LGLLRgyfdvivsgdDVERGKPAPDIYLLAAERLGVDPERCLVFED-SLAGIEAAKAAGMTVVAV 141
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 45-136 2.96e-04

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: 39.88  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  45 DGTEELLTwilEMKNAGIPVVVVSnnnSKR--VARAI-EKFDLL----YVARAMKPLARG-----INIAKKQLDLADDEI 112
Cdd:cd04302   84 PGIPELLE---KLKAAGYRLYVAT---SKPevFARRIlEHFGLDeyfdGIAGASLDGSRVhkadvIRYALDTLGIAPEQA 157

                         90       100
                 ....*....|....*....|....
gi 488219640 113 VMVGDQiMTDIRGANRAGIRSILV 136
Cdd:cd04302  158 VMIGDR-KHDIIGARANGIDSIGV 180
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 87-136 4.24e-04

HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the Class IIA subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. The sequences modelled by this equivalog are all gram negative and primarily alpha proteobacteria. Only one sequence hase been annotated as other than "hypothetical." That one, from Brucella, is annotated as related to NagD, but only by sequence similarity and should be treated with some skepticism. (See comments for Class IIA subfamily model)


Pssm-ID: 130526 [Multi-domain]  Cd Length: 242  Bit Score: 39.49  E-value: 4.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488219640   87 VARAMKPLARGINIAKKQL-DLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:TIGR01459 190 VIYSGKPYPAIFHKALKECsNIPKNRMLMVGDSFYTDILGANRLGIDTALV 240
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 30-83 5.01e-04

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 37.83  E-value: 5.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488219640   30 VLTDLDNTLIAWNNP-DGTEELLTWileMKNAGIPVVVVSNNNSKRVARAIEKFD 83
Cdd:pfam13344   1 FLFDIDGVLWRGGEPiPGAAEALRA---LRAAGKPVVFVTNNSSRSREEYAEKLR 52
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 28-136 8.75e-04

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 37.90  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  28 KAVLTDLDNTLI----AWNNPD------GTEELLtwiLEMKNAGIPVVVVSNNNSkrVAR------AIEK---------- 81
Cdd:cd07503    1 KALFLDRDGVINvdvpYVHKPEdleflpGVIEAL---KKLKDAGYLVVVVTNQSG--IARgyfseaDFEAlhdkmrella 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488219640  82 -----FDLLYVARAM--------KPLARGINIAKKQLDLADDEIVMVGDQImTDIRGANRAGIRSILV 136
Cdd:cd07503   76 sqgveIDDIYYCPHHpddgcpcrKPKPGMLLDAAKELGIDLARSFVIGDRL-SDIQAARNAGCKGILV 142
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 27-68 9.70e-04

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 38.19  E-value: 9.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488219640  27 IKAVLTDLDNTLIawnNPDGT--EELLTWILEMKNAGIPVVVVS 68
Cdd:COG0561    2 IKLIALDLDGTLL---NDDGEisPRTKEALRRLREKGIKVVIAT 42
HAD_PGPase cd16421
Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to ...
 29-136 1.09e-03

Rhodobacter capsulatus Cbbz phosphoglycolate phosphatase and related proteins; ; belongs to the haloacid dehalogenase-like superfamily; Phosphoglycolate phosphatase (PGPase; EC 3.1.3.18) catalyzes the conversion of 2-phosphoglycolate into glycolate and phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319857 [Multi-domain]  Cd Length: 105  Bit Score: 37.05  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  29 AVLTDLDNTLIawnnpdgTEELLTWIlemKNAGIPVVVVSNNNSKRVARAIE-----KFDLLYVAR---AMKPLARGINI 100
Cdd:cd16421    1 AVIFDLDGTLL-------ILELLKAL---RQKGIKLAVLSNKPNEAVQVLVEelfpgSFDFVLGEKegiRRKPDPT*ALE 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488219640 101 AKKQLDLADDEIVMVGDQiMTDIRGANRAGIRSILV 136
Cdd:cd16421   71 CAKVLGVPPDEVLYVGDS-GVDMQTARNAGMDEIGV 105
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 28-138 1.30e-03

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 37.77  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  28 KAVLTDLDNTLIA----WNNPDgtE-ELLTWILE----MKNAGIPVVVVSN-----------------NNskRVARAIEK 81
Cdd:COG0241    4 KAVFLDRDGTINEdvgyVKSPE--EfEFLPGVLEalarLNEAGYRLVVVTNqsgigrglfteedlnavHA--KMLELLAA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488219640  82 ----FDLLYVA----------RamKP-----LArginIAKK-QLDLAddEIVMVGDqIMTDIRGANRAGIRSILVKP 138
Cdd:COG0241   80 eggrIDAIYYCphhpddncdcR--KPkpgmlLQ----AAERlGIDLS--NSYMIGD-RLSDLQAAKAAGCKGILVLT 147
PRK10748 PRK10748
5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB;
63-144 1.37e-03

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


Pssm-ID: 182696 [Multi-domain]  Cd Length: 238  Bit Score: 37.79  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  63 PVVVVSNNNSKRVARAIEKFdLLYVARA-----MKPLARGINIAKKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILVK 137
Cdd:PRK10748 130 PLVAITNGNAQPELFGLGDY-FEFVLRAgphgrSKPFSDMYHLAAEKLNVPIGEILHVGDDLTTDVAGAIRCGMQACWIN 208

                         90
                 ....*....|..
gi 488219640 138 P-----IIATDS 144
Cdd:PRK10748 209 PengdlMQTWDS 220
HAD_L2-DEX cd02588
L-2-haloacid dehalogenase; L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation ...
 22-136 1.73e-03

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: 37.63  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640  22 LKNLGIKAVLTDLDNTLIAWNN----PDgTEELLTwilEMKNAGIPVVVVSNNNSKRVARAIEK------FDLLYVA--- 88
Cdd:cd02588   68 AAELGLELDESDLDELGDAYLRlppfPD-VVAGLR---RLREAGYRLAILSNGSPDLIEDVVANaglrdlFDAVLSAedv 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488219640  89 RAMKPLARGINIAKKQLDLADDEIVMVGdQIMTDIRGANRAGIRSILV 136
Cdd:cd02588  144 RAYKPAPAVYELAAERLGVPPDEILHVA-SHAWDLAGARALGLRTAWI 190
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 29-68 2.28e-03

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 37.36  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 488219640   29 AVLTDLDNTLIAWNNPDGTEELLTWILEMKNAGIPVVVVS 68
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVT 40
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 28-73 7.35e-03

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: 35.65  E-value: 7.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488219640  28 KAVLTDLDNTLIAWNNP-DGTEELLTWIlemKNAGIPVVVVSNNNSK 73
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAiPGAVEFIERL---REKGIPFLFLTNNSTR 44
FkbH TIGR01686
FkbH-like domain; This model describes a domain of a family of proteins of unknown overall ...
 28-135 7.98e-03

FkbH-like domain; This model describes a domain of a family of proteins of unknown overall function. One of these, however, is a modular polyketide synthase 4800 amino acids in length from Streptomyces avermilitis in which this domain is the C-terminal segment. By contrast, the FkbH protein from Streptomyces hygroscopicus aparently contains only this domain. The remaining members of the family all contain an additional N-terminal domain of between 200 and 275 amino acids which show less than 20% identity to one another. It seems likely then that these proteins are involved in disparate functions, probably the biosynthesis of different natural products. For instance, the FkbH gene is found in a gene cluster believed to be responsible for the biosynthesis of unususal "PKS extender units" in the ascomycin pathway. This domain is composed of two parts, the first of which is a member of subfamily IIIC (TIGR01681) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases are present in this domain. The C-terminal portion of this domain is unique to this family (by BLAST).


Pssm-ID: 273757 [Multi-domain]  Cd Length: 320  Bit Score: 35.98  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   28 KAVLTDLDNTL----IAWNNPDGT------EELLTWILEMKNAGIPVVVVSNNNSKRVARAIEKF-DLLYVAR------- 89
Cdd:TIGR01686   4 KVLVLDLDNTLwggvLGEDGIDNLnlsplhKTLQEKIKTLKKQGFLLALASKNDEDDAKKVFERRkDFILQAEdfdarsi 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488219640   90 AMKPLARGINIAKKQLDLADDEIVMVGDQImtdirgANRAGIRSIL 135
Cdd:TIGR01686  84 NWGPKSESLRKIAKKLNLGTDSFLFIDDNP------AERANVKITL 123
YjjG/YfnB TIGR02254
noncanonical pyrimidine nucleotidase, YjjG family; This HAD superfamily includes including ...
 1-138 9.42e-03

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: 35.54  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640    1 MFSNYKPT----WMVEAIYQITPAQLKNLGIKAVLTDLDNTL--IAWNNP------------DGTEELLTWILEMKNAGI 62
Cdd:TIGR02254  38 MFAQYKEInqglWRAYEEGKITKDEVVNTRFSALLKEYNTEAdeALLNQKylrfleeghqllPGAFELMENLQQKFRLYI 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219640   63 PVVVVSNNNSKRVARA--IEKFDLLYV---ARAMKPLARGINIA-KKQLDLADDEIVMVGDQIMTDIRGANRAGIRSILV 136
Cdd:TIGR02254 118 VTNGVRETQYKRLRKSglFPFFDDIFVsedAGIQKPDKEIFNYAlERMPKFSKEEVLMIGDSLTADIKGGQNAGLDTCWM 197


                  ..
gi 488219640  137 KP 138
Cdd:TIGR02254 198 NP 199
 
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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