NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499531746|emb|CCI78111|]
View 

nagD [Klebsiella pneumoniae subsp. rhinoscleromatis SB3432]

Protein Classification

HAD-IIA family hydrolase( domain architecture ID 11484729)

HAD-IIA family hydrolase similar to Escherichia coli ribonucleotide monophosphatase NagD, which catalyzes the dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


:

Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 532.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   3 IQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  83 EGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTHGRGFYPACGALCAG 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 163 IEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240


                 ....*...
gi 499531746 243 SVAEIDIF 250
Cdd:PRK10444 241 SVADIDVI 248
 
Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 532.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   3 IQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  83 EGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTHGRGFYPACGALCAG 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 163 IEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240


                 ....*...
gi 499531746 243 SVAEIDIF 250
Cdd:PRK10444 241 SVADIDVI 248
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 4-246 2.18e-127

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: 360.75  E-value: 2.18e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   4 QNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE 83
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 -GKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTHG---RGFYPACGAL 159
Cdd:cd07530   81 pGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLpteRGLLPGNGSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 160 CAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSW 239
Cdd:cd07530  161 VAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPTY 240


                 ....*..
gi 499531746 240 IYPSVAE 246
Cdd:cd07530  241 IVPSLRE 247
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-249 3.36e-107

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 310.12  E-value: 3.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   1 MTIQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLR 80
Cdd:COG0647    6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  81 RQ-EGKKAYVVGEGALIHELYKAGFTIT-DVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDT---HGRGFYPA 155
Cdd:COG0647   86 ERhPGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRtvpTEDGLIPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 156 CGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPF 235
Cdd:COG0647  166 AGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPI 245

                        250
                 ....*....|....
gi 499531746 236 RPSWIYPSVAEIDI 249
Cdd:COG0647  246 RPDYVLDSLAELLL 259
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 6-223 6.29e-77

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: 232.60  E-value: 6.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFAT-AGIDVPDSAFYTSAMATADFLR-RQE 83
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSlLGVDVSPDQIITSGSVTKDLLRqRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   84 GKKAYVVGEGALIHELYKAGF---TITDVN-------PDFVIVGETRSFNWEMMHKAAFFVANG-ARFIATNPDT---HG 149
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrndFFDDIDhlaiekiPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDlvrLG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499531746  150 RG-FYPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQT-VIVGDNLRTDILAGFQAGLETILMLSG 223
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVLTG 236
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 6-105 3.46e-29

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 105.63  E-value: 3.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE-G 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKfG 80

                          90       100
                  ....*....|....*....|.
gi 499531746   85 KKAYVVGEGALIHELYKAGFT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
PRK10444 PRK10444
HAD-IIA family hydrolase;
3-250 0e+00

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 532.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   3 IQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQ 82
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  83 EGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTHGRGFYPACGALCAG 162
Cdd:PRK10444  81 EGKKAYVIGEGALIHELYKAGFTITDINPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 163 IEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIYP 242
Cdd:PRK10444 161 IEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSTLDDIDSMPFRPSWIYP 240


                 ....*...
gi 499531746 243 SVAEIDIF 250
Cdd:PRK10444 241 SVADIDVI 248
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 4-246 2.18e-127

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: 360.75  E-value: 2.18e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   4 QNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE 83
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 -GKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTHG---RGFYPACGAL 159
Cdd:cd07530   81 pGAKVYVIGEEGLRTALHEAGLTLTDENPDYVVVGLDRDLTYEKLAEATLAIRNGAKFIATNPDLTLpteRGLLPGNGSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 160 CAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSW 239
Cdd:cd07530  161 VAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLTGVTTREDLAKPPYRPTY 240


                 ....*..
gi 499531746 240 IYPSVAE 246
Cdd:cd07530  241 IVPSLRE 247
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 5-246 1.31e-107

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 311.61  E-value: 1.31e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   5 NIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE- 83
Cdd:cd07508    1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 GKKAYVVGEGALIHELYKAGFTI-------------------TDVNPDFVIVGETRSFNWEMMHKAAFFVAN-GARFIAT 143
Cdd:cd07508   81 GKKVYVLGEEGLKEELRAAGFRIaggpskgietyaelvehleDDENVDAVIVGSDFKLNFAKLRKACRYLRNpGCLFIAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 144 NPDTHGR----GFYPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETIL 219
Cdd:cd07508  161 APDRIHPlkdgGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 499531746 220 MLSGVSTLDDIDS---MPFRPSWIYPSVAE 246
Cdd:cd07508  241 VLTGVTTLEDLQAyidHELVPDYYADSLAD 270
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-249 3.36e-107

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 310.12  E-value: 3.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   1 MTIQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLR 80
Cdd:COG0647    6 DRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  81 RQ-EGKKAYVVGEGALIHELYKAGFTIT-DVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDT---HGRGFYPA 155
Cdd:COG0647   86 ERhPGARVYVIGEEGLREELEEAGLTLVdDEEPDAVVVGLDRTFTYEKLAEALRAIRRGAPFIATNPDRtvpTEDGLIPG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 156 CGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPF 235
Cdd:COG0647  166 AGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAGLDTLLVLTGVTTAEDLEAAPI 245

                        250
                 ....*....|....
gi 499531746 236 RPSWIYPSVAEIDI 249
Cdd:COG0647  246 RPDYVLDSLAELLL 259
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 6-223 6.29e-77

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: 232.60  E-value: 6.29e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFAT-AGIDVPDSAFYTSAMATADFLR-RQE 83
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSlLGVDVSPDQIITSGSVTKDLLRqRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   84 GKKAYVVGEGALIHELYKAGF---TITDVN-------PDFVIVGETRSFNWEMMHKAAFFVANG-ARFIATNPDT---HG 149
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFrndFFDDIDhlaiekiPAAVIVGEPSDFSYDELAKAAYLLAEGdVPFIAANRDDlvrLG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499531746  150 RG-FYPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQT-VIVGDNLRTDILAGFQAGLETILMLSG 223
Cdd:TIGR01460 161 DGrFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVLTG 236
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 7-246 6.17e-59

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: 186.87  E-value: 6.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   7 ICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQEGK- 85
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  86 KAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTH---GRGFYPACGALCAG 162
Cdd:cd16422   83 KIFLLGTKSLREEFEKAGFTLDGDDIDVVVLGFDTELTYEKLRTACLLLRRGIPYIATHPDINcpsEEGPIPDAGSIIAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 163 IEKISGRKP-FYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIY 241
Cdd:cd16422  163 IETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGETTREDLEDLERKPTYVF 242


                 ....*
gi 499531746 242 PSVAE 246
Cdd:cd16422  243 DNVGE 247
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 9-246 3.99e-56

HAD-superfamily subfamily IIA hydrolase, TIGR01457; 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 positive (low-GC) bacteria. Sequences found in this model are annotated variously as related to NagD or 4-nitrophenyl phosphatase, and this hypothetical equivalog, of all of those within the Class IIA subfamily, is most closely related to the E. coli NagD enzyme and the PGP_euk equivalog (TIGR01452). However, there is presently no evidence that this hypothetical equivalog has the same function of either those. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 130524  Cd Length: 249  Bit Score: 180.05  E-value: 3.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    9 DIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQ-EGKKA 87
Cdd:TIGR01457   7 DLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEEQVFTTSMATAQYIAQQkKDASV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   88 YVVGEGALIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGARFIATNPDTH---GRGFYPACGALCAGIE 164
Cdd:TIGR01457  87 YVIGEEGLREAIKENGLTFGGENPDYVVVGLDRSITYEKFAVACLAIRNGARFISTNGDIAiptERGLLPGNGSLTSVLT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  165 KISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIYPSV 244
Cdd:TIGR01457 167 VSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHTGVTKREHMTDDMEKPTHAIDSL 246


                  ..
gi 499531746  245 AE 246
Cdd:TIGR01457 247 AE 248
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 6-247 7.44e-50

UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar phosphatase; Bacillus subtilis AraL is a phosphatase displaying activity towards different sugar phosphate substrates; it is encoded by the arabinose metabolic operon araABDLMNPQ-abfA and may play a role in the dephosphorylation of substrates related to l-arabinose metabolism. 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: 319833 [Multi-domain]  Cd Length: 252  Bit Score: 163.89  E-value: 7.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE-G 84
Cdd:cd07531    3 YIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREKpN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  85 KKAYVVGEGALIHELYKAGFTITDvNPD---FVIVGETRSFNWEMMHKAAFFVANGARFIATNPD---THGRGFYPACGA 158
Cdd:cd07531   83 AKVFVTGEEGLIEELRLAGLEIVD-KYDeaeYVVVGSNRKITYELLTKAFRACLRGARYIATNPDrifPAEDGPIPDTAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 159 LCAGIEKISGRKP-FYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRP 237
Cdd:cd07531  162 IIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALVLTGVTTRENLDRHGYKP 241

                        250
                 ....*....|
gi 499531746 238 SWIYPSVAEI 247
Cdd:cd07531  242 DYVLNSIKDL 251
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 2-230 8.94e-49

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. 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: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 162.09  E-value: 8.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   2 TIQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFL-R 80
Cdd:cd07532    5 NIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIADYLkE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  81 RQEGKKAYVVGEGALIHELYKAGF---------------------TITDVNPDFVIVGETRSFNWEMMHKAAFFVAN-GA 138
Cdd:cd07532   85 KGFKKKVYVIGEEGIRKELEEAGIvscggdgedekddsmgdfahnLELDPDVGAVVVGRDEHFSYPKLMKACNYLRNpDV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 139 RFIATNPDThgrgFYPAC--------GALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAG 210
Cdd:cd07532  165 LFLATNMDA----TFPGPvgrvipgaGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFA 240

                        250       260
                 ....*....|....*....|
gi 499531746 211 FQAGLETILMLSGVSTLDDI 230
Cdd:cd07532  241 NNCGFQSLLVGTGVNSLEDA 260
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 3-247 1.04e-43

UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase; This subfamily includes the phosphoglycolate phosphatases (human PGP and Arabidopsis thaliana PGLP2) and p-nitrophenylphosphatases (Schizosaccharomyces pombe PHO2 and Saccharomyces PHO13p). It belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319813 [Multi-domain]  Cd Length: 282  Bit Score: 149.07  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   3 IQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDS-AFYTSAMATA----D 77
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEeEIFSSAYCAArylrQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  78 FLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDF--------------------VIVGETRSFNWEMMHKAAFFVAN- 136
Cdd:cd07510   81 RLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGlrraapkdwllagldpdvgaVLVGLDEHVNYLKLAKATQYLRDp 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 137 GARFIATNPD-----THGRgFYPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGF 211
Cdd:cd07510  161 GCLFVATNRDpwhplSDGS-FIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQ 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499531746 212 QAGLETILMLSGVSTLDDI---DSMPFRPSWIYPSVAEI 247
Cdd:cd07510  240 NCGLKTLLVLTGVSTLEEAlakLSNDLVPDYYVESLADL 278
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 2-230 4.14e-39

phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In mammals, PGP is found in many tissues, notably in red blood cells where P-glycolate is and important activator of the hydrolysis of 2,3-bisphosphoglycerate, a major modifier of the oxygen affinity of hemoglobin. Pyridoxal phosphate (PLP, Vitamin B6) phosphatase is involved in the degradation of PLP in mammals and is widely distributed in human tissues including erythrocyes. The enzymes described here are members of the Haloacid dehalogenase superfamily of hydrolase enzymes (pfam00702). Unlike the bacterial PGP equivalog (TIGR01449), which is a member of class (subfamily) I, these enzymes are members of class (subfamily) II. These two families have almost certainly arisen from convergent evolution (although these two ancestors may themselves have diverged from a more distant HAD superfamily progenitor). The primary seed sequence for this model comes from Chlamydomonas reinhardtii, a photosynthetic alga. The enzyme has been purified and characterized and these data are fully consistent with the assignment of function as a PGPase involved in photorespiration. The second seed, from Homo sapiens chromosome 22 has been characterized as a pyridoxal phosphatase. Biochemical characterization of partially purified PGP's from various tissues including red blood cells have been performed while one gene for PGP has been localized to chromosome 16p13.3. The sequence used here maps to chromosome 22. There is indeed a related gene on chromosome 16 (and it is expressed, since EST's are found) which shows 46% identity. The chromosome 16 gene is not in evidence in nraa but translated from the genomic sequence. The third seed, from C. elegans, is only supported by sequence similarity. This model is limited to eukaryotic species including S. pombe and S. cerevisiae, although several archaea score between the trusted and noise cutoffs. This model is closely related to a family of bacterial sequences including the E. coli NagD and B. subtilus AraL genes which are characterized by the ability to hydrolyze para-nitrophenylphosphate (pNPPases or NPPases). The chlamydomonas PGPase d


Pssm-ID: 273635 [Multi-domain]  Cd Length: 279  Bit Score: 136.92  E-value: 4.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    2 TIQNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRR 81
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   82 Q--EGKKAYVVGEGALIHELYKAG--------------------FTITDVNPDFVIVGETRSFNWEMMHKAAFFVAN-GA 138
Cdd:TIGR01452  81 PpdAGKAVYVIGEEGLRAELDAAGirlagdpgekkqdeadgfmyDIKLDERVGAVVVGYDEHFSYVKLMEACAHLREpGC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  139 RFIATNPD--THGRG--FYPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAG 214
Cdd:TIGR01452 161 LFVATNRDpwHPLSDgsRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRCG 240

                         250
                  ....*....|....*.
gi 499531746  215 LETILMLSGVSTLDDI 230
Cdd:TIGR01452 241 MTTVLVLSGVSQLEEA 256
PLN02645 PLN02645
phosphoglycolate phosphatase
 7-232 5.50e-39

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 137.54  E-value: 5.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   7 ICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRR---QE 83
Cdd:PLN02645  32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYLKSinfPK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 GKKAYVVGEGALIHELYKAGFTI----------TDVNPDF----------VIVGETRSFNWEMMHKAAFFVAN--GARFI 141
Cdd:PLN02645 112 DKKVYVIGEEGILEELELAGFQYlggpedgdkkIELKPGFlmehdkdvgaVVVGFDRYINYYKIQYATLCIREnpGCLFI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 142 ATNPD--THGRGF--YPACGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLET 217
Cdd:PLN02645 192 ATNRDavTHLTDAqeWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKT 271

                        250
                 ....*....|....*
gi 499531746 218 ILMLSGVSTLDDIDS 232
Cdd:PLN02645 272 LLVLSGVTSESMLLS 286
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 4-250 1.05e-34

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: 124.70  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   4 QNIICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE 83
Cdd:cd07509    1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 GKKAYVVGEGALihELYKAgftITDVNPDFVIVGET-RSFNWEMMHKAAFFVANGARFIATnpdthGRGFYPA------- 155
Cdd:cd07509   81 LRPHLLVDDDAL--EDFIG---IDTSDPNAVVIGDAgEHFNYQTLNRAFRLLLDGAPLIAL-----HKGRYYKrkdglal 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 156 -CGALCAGIEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGvSTLDDIDSMP 234
Cdd:cd07509  151 dPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVRTG-KYRPSDEKKP 229

                        250
                 ....*....|....*...
gi 499531746 235 FRPSWIY--PSVAEIDIF 250
Cdd:cd07509  230 NVPPDLTadSFADAVDHI 247
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 6-105 3.46e-29

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 105.63  E-value: 3.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRFATAGIDVPDSAFYTSAMATADFLRRQE-G 84
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKfG 80

                          90       100
                  ....*....|....*....|.
gi 499531746   85 KKAYVVGEGALIHELYKAGFT 105
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGFE 101
Hydrolase_like pfam13242
HAD-hyrolase-like;
175-246 4.96e-23

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 88.83  E-value: 4.96e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499531746  175 GKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFRPSWIYPSVAE 246
Cdd:pfam13242   3 GKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIRPDYVVDDLAE 74
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 6-242 9.40e-14

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: 68.51  E-value: 9.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   6 IICDIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQdLANRFATAGIDVPD-SAFYTSAMATADFLRRQE- 83
Cdd:cd07525    3 FLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPAES-VVRQLAKLGVPPSTyDAIITSGEVTRELLAREAg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  84 -GKKAYVVG--------EG---ALIHELYKAGFTITDVNPDFvivgETRSFN--WEMMHKAAffvANGARFIATNPD--- 146
Cdd:cd07525   82 lGRKVYHLGperdanvlEGldvVATDDAEKAEFILCTGLYDD----ETETPEdyRKLLKAAA---ARGLPLICANPDlvv 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 147 -THGRGFYPAcGALCAGIEKISGRKPFYvGKPSPWIIRSALNKMQAHSEQTVI-VGDNLRTDILAGFQAGLETILMLSGV 224
Cdd:cd07525  155 pRGGKLIYCA-GALAELYEELGGEVIYF-GKPHPPIYDLALARLGRPAKARILaVGDGLHTDILGANAAGLDSLFVTGGI 232

                        250       260
                 ....*....|....*....|..
gi 499531746 225 STLDD----IDSMPFrPSWIYP 242
Cdd:cd07525  233 HRRLAaeagIKSQIV-PDFVIP 253
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 175-219 7.35e-13

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: 63.06  E-value: 7.35e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499531746 175 GKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETIL 219
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTIL 107
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 9-222 7.68e-13

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: 66.07  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    9 DIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTgQDLANRFATAGIDVPDSAFYTSAMATA-----DFLRRQE 83
Cdd:TIGR01459  14 DLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNI-FSLHKTLKSLGINADLPEMIISSGEIAvqmilESKKRFD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   84 GKKA--YVVGEG----ALIHELYKAgFTITDVNPDFVIVGETRSFNWEMMHKAAFFVANGAR---FIATNPD----THGR 150
Cdd:TIGR01459  93 IRNGiiYLLGHLendiINLMQCYTT-DDENKANASLITIYRSENEKLDLDEFDELFAPIVARkipNICANPDrginQHGI 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499531746  151 GFYPAcGALCAGIEKISGrKPFYVGKPSPWIIRSALNKMQAHSEQTVI-VGDNLRTDILAGFQAGLETILMLS 222
Cdd:TIGR01459 172 YRYGA-GYYAELIKQLGG-KVIYSGKPYPAIFHKALKECSNIPKNRMLmVGDSFYTDILGANRLGIDTALVLT 242
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
98-237 7.15e-12

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 61.68  E-value: 7.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  98 ELYKAGFT--ITDVnpDFVIVGETRSF------NW-EMMHKAAFFVangarFIATNpDTHGRGFYPACgalCAGIEKISG 168
Cdd:COG2179   20 KLKEKGIKglILDL--DNTLVPWDEPEatpeviEWlEELKEAGFKV-----CIVSN-NSEKRVKRFAE---KLGIPYIAR 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499531746 169 RKpfyvgKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILmlsgVSTLDDIDSMPFRP 237
Cdd:COG2179   89 AK-----KPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTIL----VKPLVDKEFWFTRI 148
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-214 2.99e-10

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: 57.98  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746    3 IQNIICDIDGVLMHDNvavPGAAEFIKRILdkgmplvmltnypsqTGQDLANRFATAGIDVPDSA--FYTSAMA-TADFL 79
Cdd:pfam00702   1 IKAVVFDLDGTLTDGE---PVVTEAIAELA---------------SEHPLAKAIVAAAEDLPIPVedFTARLLLgKRDWL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   80 RRQEGKKAyvvgegaLIHELYKAGFTITDVNPDFVIVGETRSFNWEMMHKA-AFFVANGAR-FIATNPDTHG-RGFYPAC 156
Cdd:pfam00702  63 EELDILRG-------LVETLEAEGLTVVLVELLGVIALADELKLYPGAAEAlKALKERGIKvAILTGDNPEAaEALLRLL 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499531746  157 GALCAGIEKISGRkPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLrTDILAGFQAG 214
Cdd:pfam00702 136 GLDDYFDVVISGD-DVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-247 6.87e-10

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 57.25  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   3 IQNIICDIDGVLMHDNvavPGAAEFIKRILDK-GMPLVMLTNYPSQTGQDLANRFATAgidVPDSAFYTSAMATADFLR- 80
Cdd:COG0546    1 IKLVLFDLDGTLVDSA---PDIAAALNEALAElGLPPLDLEELRALIGLGLRELLRRL---LGEDPDEELEELLARFREl 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  81 -RQEGKKAYVVGEGA--LIHELYKAGFTItdvnpdfvivgetrsfnwemmhkaaffvangarFIATNPDThgRGFYPACG 157
Cdd:COG0546   75 yEEELLDETRLFPGVreLLEALKARGIKL---------------------------------AVVTNKPR--EFAERLLE 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 158 ALcaGIEK----ISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRtDILAGFQAGLETILMLSGVSTLDDIDSm 233
Cdd:COG0546  120 AL--GLDDyfdaIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDSPH-DIEAARAAGVPFIGVTWGYGSAEELEA- 195

                        250
                 ....*....|....
gi 499531746 234 pFRPSWIYPSVAEI 247
Cdd:COG0546  196 -AGADYVIDSLAEL 208
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 174-218 3.21e-08

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: 50.23  E-value: 3.21e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499531746 174 VGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETI 218
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
163-218 1.56e-06

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 47.19  E-value: 1.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499531746  163 IEKISGRKPFYVGKPSPWIIRSALNKMQAHSEQTVIVGDNLRtDILAGFQAGLETI 218
Cdd:pfam13419 122 FDVIVGGDDVEGKKPDPDPILKALEQLGLKPEEVIYVGDSPR-DIEAAKNAGIKVI 176
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 162-236 2.27e-06

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: 46.63  E-value: 2.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499531746  162 GIEKISGRKpfyvgKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILMLSGVSTLDDIDSMPFR 236
Cdd:TIGR01668  82 GIPVLPHAV-----KPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRIWR 151
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 176-232 3.60e-05

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


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 43.42  E-value: 3.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDNLRtDILAGFQAGLETILMLSGVSTLDDIDS 232
Cdd:cd02616  136 KPDPEPVLKALELLGAEPEEALMVGDSPH-DILAGKNAGVKTVGVTWGYKGREYLKA 191
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-247 5.01e-05

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: 42.78  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   1 MTIQNIICDIDGVLMHDN---------VAVPGAAEFIKRILDKGMPLVMLTNypsqtgqdlanrfatagidvpdsafyts 71
Cdd:COG0241    1 MMKKAVFLDRDGTINEDVgyvkspeefEFLPGVLEALARLNEAGYRLVVVTN---------------------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746  72 amatadflrrQEGkkayvVGEGAlihelykagFTITDVNPdfvivgetrsFNwEMMHKAafFVANGARFIATNPDTHGrg 151
Cdd:COG0241   53 ----------QSG-----IGRGL---------FTEEDLNA----------VH-AKMLEL--LAAEGGRIDAIYYCPHH-- 93

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746 152 fyPACGALCagiekisgRKPfyvgkpSPWIIRSALNKMQAHSEQTVIVGDNLRtDILAGFQAGLETILMLSGVSTLDDID 231
Cdd:COG0241   94 --PDDNCDC--------RKP------KPGMLLQAAERLGIDLSNSYMIGDRLS-DLQAAKAAGCKGILVLTGKGAEELAE 156

                        250
                 ....*....|....*.
gi 499531746 232 SmpfRPSWIYPSVAEI 247
Cdd:COG0241  157 A---LPDTVADDLAEA 169
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 174-247 6.77e-05

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: 42.71  E-value: 6.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499531746 174 VGKPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETILmlsgVSTLDDIDSMPFRPSWIYPSVAEI 247
Cdd:COG1011  147 VRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGARAAGMRTVW----VNRSGEPAPAEPRPDYVISDLAEL 216
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 176-217 7.98e-05

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 42.32  E-value: 7.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDNLRtDILAGFQAGLET 217
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNHH-DILAGKNAGTKT 178
PRK09449 PRK09449
dUMP phosphatase; Provisional
 174-217 1.69e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 41.43  E-value: 1.69e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499531746 174 VGKPSPWIIRSALNKM-QAHSEQTVIVGDNLRTDILAGFQAGLET 217
Cdd:PRK09449 148 VAKPDVAIFDYALEQMgNPDRSRVLMVGDNLHSDILGGINAGIDT 192
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
175-247 4.69e-04

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 40.19  E-value: 4.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499531746 175 GKPSPWIIRSALNKMQAHSEQTVIVGDNLrTDILAGFQAGLETIlmlsGVSTLDDIDSMPFRPSWIYPSVAEI 247
Cdd:COG0637  141 GKPDPDIYLLAAERLGVDPEECVVFEDSP-AGIRAAKAAGMRVV----GVPDGGTAEEELAGADLVVDDLAEL 208
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 176-219 1.03e-03

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: 38.04  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDNLRTDILAGFQAGLETIL 219
Cdd:cd16415   62 KPDPRIFQKALERLGVSPEEALHVGDDLKNDYLGARAVGWHALL 105
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 9-103 1.08e-03

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to the uncharacterized human CECR5 (cat eye syndrome critical region protein 5); 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: 319814  Cd Length: 136  Bit Score: 38.14  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499531746   9 DIDGVLMHDNVAVPGAAEFIKRILDKGMPLVMLTNYPSQTGQDLANRF-ATAGIDVPDSAFYTS------AMATADFLRR 81
Cdd:cd07511    6 DIDGVLVRGKKPIPGAPKALKFLNDNKIPFIFLTNGGGFPESKRADFLsKLLGVEVSPDQVIQShspgkpTELTYDFAEH 85

                         90       100
                 ....*....|....*....|..
gi 499531746  82 QEGKKAYVVGEGALIHELYKAG 103
Cdd:cd07511   86 VLQRQAKRLGKTEPFKYVYMVG 107
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 176-247 1.72e-03

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: 38.37  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDNlRTDILAGFQAGLETILMLSGVSTLDDIDSMpfRPSWIYPSVAEI 247
Cdd:cd16417  143 KPDPAPLLHACEKLGIAPAQMLMVGDS-RNDILAARAAGCPSVGLTYGYNYGEDIAAS--GPDAVIDSLAEL 211
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 176-219 1.87e-03

uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the uncharacterized Lactococcus lactis YsbA; The specific function of Lactococcus lactis YsbA is unknown. 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: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 38.13  E-value: 1.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDnlRT-DILAGFQAGLETIL 219
Cdd:cd07523  130 KPNPEAINYLLNKYQLNPEETVMIGD--RElDIEAGHNAGISTIL 172
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
176-247 2.07e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 38.25  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499531746 176 KPSPWIIRSALNKMQAHSEQTVIVGDNlRTDILAGFQAGLETILMLSGVSTLDDIDSMPfrPSWIYPSVAEI 247
Cdd:PRK13222 149 KPDPAPLLLACEKLGLDPEEMLFVGDS-RNDIQAARAAGCPSVGVTYGYNYGEPIALSE--PDVVIDHFAEL 217
 
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