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Conserved domains on  [gi|281332119|ref|NP_001162623|]
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glycerol-3-phosphate phosphatase [Rattus norvegicus]

Protein Classification

HAD family hydrolase( domain architecture ID 11576291)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 28-319 3.32e-164

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: 458.39  E-value: 3.32e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMgPEaglEVFGTAYCSAL 107
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLK-EE---EIFSSAYCAAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 108 YLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:cd07510   77 YLRQRLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVGLDEHVNYLKLAKATQY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 188 LQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL 267
Cdd:cd07510  157 LRDPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDIL 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281332119 268 LGSTCSLKTILTLTGVSSLEDVKSNQesdcmfKKKMVPDFYVDSIADLLPAL 319
Cdd:cd07510  237 FGQNCGLKTLLVLTGVSTLEEALAKL------SNDLVPDYYVESLADLLELL 282
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 28-319 3.32e-164

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: 458.39  E-value: 3.32e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMgPEaglEVFGTAYCSAL 107
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLK-EE---EIFSSAYCAAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 108 YLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:cd07510   77 YLRQRLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVGLDEHVNYLKLAKATQY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 188 LQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL 267
Cdd:cd07510  157 LRDPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDIL 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281332119 268 LGSTCSLKTILTLTGVSSLEDVKSNQesdcmfKKKMVPDFYVDSIADLLPAL 319
Cdd:cd07510  237 FGQNCGLKTLLVLTGVSTLEEALAKL------SNDLVPDYYVESLADLLELL 282
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 28-315 2.05e-100

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: 296.39  E-value: 2.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGpmgpeAGLEVFGTAYCSAL 107
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNG-----LAEQLFSSALCAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  108 YLRQrlAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:TIGR01452  77 LLRQ--PPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  188 LQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL 267
Cdd:TIGR01452 155 LREPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDIL 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281332119  268 LGSTCSLKTILTLTGVSSLEDVKSNQESDcmfKKKMVPDFYVDSIADL 315
Cdd:TIGR01452 235 FGHRCGMTTVLVLSGVSQLEEAQEYLMAG---QDDLVPDYVVESLADL 279
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-320 5.13e-88

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 266.19  E-value: 5.13e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   1 MAEAEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEK 80
Cdd:PLN02645   1 SSNVTPAAMAAAAQLLTLENADELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  81 LRRLGFGGPmgpEAglEVFGTAYCSALYLRQrLAGVPDPKAYVLGSPALAAELEAVGVTSVGvGPDvlHGDGPSDWLAVP 160
Cdd:PLN02645  81 FESLGLNVT---EE--EIFSSSFAAAAYLKS-INFPKDKKVYVIGEEGILEELELAGFQYLG-GPE--DGDKKIELKPGF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 161 L---EPDVRAVVVGFDPHFSYMKL---TKAVRylQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIG 234
Cdd:PLN02645 152 LmehDKDVGAVVVGFDRYINYYKIqyaTLCIR--ENPGCLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 235 KPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQesdcmfkKKMVPDFYVDSIAD 314
Cdd:PLN02645 230 KPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLVLSGVTSESMLLSPE-------NKIQPDFYTSKISD 302


                 ....*.
gi 281332119 315 LLPALQ 320
Cdd:PLN02645 303 FLTLKA 308
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
24-316 4.56e-81

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 246.56  E-value: 4.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  24 LLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggPMGPEaglEVFGTAY 103
Cdd:COG0647    4 LADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGI--PVAED---EIVTSGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 104 CSALYLRQRlagVPDPKAYVLGSPALAAELEAVGVTsvgvgpdvlhgdgpsdwLAVPLEPDvrAVVVGFDPHFSYMKLTK 183
Cdd:COG0647   79 ATAAYLAER---HPGARVYVIGEEGLREELEEAGLT-----------------LVDDEEPD--AVVVGLDRTFTYEKLAE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 184 AVRYLQQPdCLLVGTNMDNRLPLENGrFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLD 263
Cdd:COG0647  137 ALRAIRRG-APFIATNPDRTVPTEDG-LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLD 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281332119 264 TDILLGSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDSIADLL 316
Cdd:COG0647  215 TDILGANAAGLDTLLVLTGVTTAEDLE---------AAPIRPDYVLDSLAELL 258
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 31-139 9.74e-37

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 127.20  E-value: 9.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   31 LLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggpmgPEAGLEVFGTAYCSALYLR 110
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGF-----DIDEDEIITSGTAAADYLK 75

                          90       100
                  ....*....|....*....|....*....
gi 281332119  111 QRLagvPDPKAYVLGSPALAAELEAVGVT 139
Cdd:pfam13344  76 ERK---FGKKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 28-319 3.32e-164

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: 458.39  E-value: 3.32e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMgPEaglEVFGTAYCSAL 107
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLK-EE---EIFSSAYCAAR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 108 YLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:cd07510   77 YLRQRLPGPADGKVYVLGGEGLRAELEAAGVAHLGGPDDGLRRAAPKDWLLAGLDPDVGAVLVGLDEHVNYLKLAKATQY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 188 LQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL 267
Cdd:cd07510  157 LRDPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDIL 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281332119 268 LGSTCSLKTILTLTGVSSLEDVKSNQesdcmfKKKMVPDFYVDSIADLLPAL 319
Cdd:cd07510  237 FGQNCGLKTLLVLTGVSTLEEALAKL------SNDLVPDYYVESLADLLELL 282
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 28-315 2.05e-100

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: 296.39  E-value: 2.05e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGpmgpeAGLEVFGTAYCSAL 107
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNG-----LAEQLFSSALCAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  108 YLRQrlAGVPDPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:TIGR01452  77 LLRQ--PPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  188 LQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL 267
Cdd:TIGR01452 155 LREPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDIL 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 281332119  268 LGSTCSLKTILTLTGVSSLEDVKSNQESDcmfKKKMVPDFYVDSIADL 315
Cdd:TIGR01452 235 FGHRCGMTTVLVLSGVSQLEEAQEYLMAG---QDDLVPDYVVESLADL 279
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 24-315 1.42e-98

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: 292.29  E-value: 1.42e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  24 LLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPmgpeaGLEVFGTAY 103
Cdd:cd07532    2 WLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVK-----ENNILSSAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 104 CSALYLRQRLAGvpdPKAYVLGSPALAAELEAVGVTSVGVGPDVLHGDGPSDWLAVP-LEPDVRAVVVGFDPHFSYMKLT 182
Cdd:cd07532   77 VIADYLKEKGFK---KKVYVIGEEGIRKELEEAGIVSCGGDGEDEKDDSMGDFAHNLeLDPDVGAVVVGRDEHFSYPKLM 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 183 KAVRYLQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRL 262
Cdd:cd07532  154 KACNYLRNPDVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRL 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281332119 263 DTDILLGSTCSLKTILTLTGVSSLEDVKSNQESDCMFKKKMVPDFYVDSIADL 315
Cdd:cd07532  234 KTDILFANNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
PLN02645 PLN02645
phosphoglycolate phosphatase
 1-320 5.13e-88

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 266.19  E-value: 5.13e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   1 MAEAEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEK 80
Cdd:PLN02645   1 SSNVTPAAMAAAAQLLTLENADELIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  81 LRRLGFGGPmgpEAglEVFGTAYCSALYLRQrLAGVPDPKAYVLGSPALAAELEAVGVTSVGvGPDvlHGDGPSDWLAVP 160
Cdd:PLN02645  81 FESLGLNVT---EE--EIFSSSFAAAAYLKS-INFPKDKKVYVIGEEGILEELELAGFQYLG-GPE--DGDKKIELKPGF 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 161 L---EPDVRAVVVGFDPHFSYMKL---TKAVRylQQPDCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIG 234
Cdd:PLN02645 152 LmehDKDVGAVVVGFDRYINYYKIqyaTLCIR--ENPGCLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 235 KPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQesdcmfkKKMVPDFYVDSIAD 314
Cdd:PLN02645 230 KPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNGGCKTLLVLSGVTSESMLLSPE-------NKIQPDFYTSKISD 302


                 ....*.
gi 281332119 315 LLPALQ 320
Cdd:PLN02645 303 FLTLKA 308
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 32-314 2.92e-87

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: 262.69  E-value: 2.92e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  32 LFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRlgFGGPMGPEaglEVFGTAYCSALYLRQ 111
Cdd:cd07508    3 ISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRK--FGVDVPED---QIVTSAKATARFLRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 112 RLagvPDPKAYVLGSPALAAELEAVGVTSVGvGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQP 191
Cdd:cd07508   78 RK---FGKKVYVLGEEGLKEELRAAGFRIAG-GPSKGIETYAELVEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 192 DCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGST 271
Cdd:cd07508  154 GCLFIATAPDRIHPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKA 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 281332119 272 CSLKTILTLTGVSSLEDVksnqesDCMFKKKMVPDFYVDSIAD 314
Cdd:cd07508  234 CGFQTLLVLTGVTTLEDL------QAYIDHELVPDYYADSLAD 270
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
24-316 4.56e-81

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 246.56  E-value: 4.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  24 LLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggPMGPEaglEVFGTAY 103
Cdd:COG0647    4 LADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGI--PVAED---EIVTSGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 104 CSALYLRQRlagVPDPKAYVLGSPALAAELEAVGVTsvgvgpdvlhgdgpsdwLAVPLEPDvrAVVVGFDPHFSYMKLTK 183
Cdd:COG0647   79 ATAAYLAER---HPGARVYVIGEEGLREELEEAGLT-----------------LVDDEEPD--AVVVGLDRTFTYEKLAE 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 184 AVRYLQQPdCLLVGTNMDNRLPLENGrFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLD 263
Cdd:COG0647  137 ALRAIRRG-APFIATNPDRTVPTEDG-LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLD 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 281332119 264 TDILLGSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDSIADLL 316
Cdd:COG0647  215 TDILGANAAGLDTLLVLTGVTTAEDLE---------AAPIRPDYVLDSLAELL 258
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 29-314 2.50e-67

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: 210.91  E-value: 2.50e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  29 DTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggPMGPEaglEVFGTAYCSALY 108
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGI--DVPEE---DVYTSALATAQY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 109 LRQRLAGVpdpKAYVLGSPALAAELEAVGVTSVGVGPDvlhgdgpsdwlavplepdvrAVVVGFDPHFSYMKLTKAVRYL 188
Cdd:cd07530   76 LAEQLPGA---KVYVIGEEGLRTALHEAGLTLTDENPD--------------------YVVVGLDRDLTYEKLAEATLAI 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 189 QQpDCLLVGTNMDNRLPLENGrFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILL 268
Cdd:cd07530  133 RN-GAKFIATNPDLTLPTERG-LLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAA 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 281332119 269 GSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDSIAD 314
Cdd:cd07530  211 GIAAGIDTLLVLTGVTTREDLA---------KPPYRPTYIVPSLRE 247
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 32-282 7.33e-53

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: 173.67  E-value: 7.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   32 LFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGfGGPMGPEaglEVFGTAYCSALYLRQ 111
Cdd:TIGR01460   2 LFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLL-GVDVSPD---QIITSGSVTKDLLRQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  112 RLagvPDPKAYVLGSPALAAELEAVGVTSVGVgPDVLHGDgpsdwlavpLEPDVRAVVVGFDPHFSYMKLTKAVRYLQQP 191
Cdd:TIGR01460  78 RF---EGEKVYVIGVGELRESLEGLGFRNDFF-DDIDHLA---------IEKIPAAVIVGEPSDFSYDELAKAAYLLAEG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  192 DCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERT-VMVGDRLDTDILLGS 270
Cdd:TIGR01460 145 DVPFIAANRDDLVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAK 224

                         250
                  ....*....|..
gi 281332119  271 TCSLKTILTLTG 282
Cdd:TIGR01460 225 NAGFDTLLVLTG 236
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 32-289 3.42e-47

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: 159.14  E-value: 3.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  32 LFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggpmgpEAGLE-VFGTAYCSALYLR 110
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGI------DAGLDrVFTSGEATIDHLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 111 QRLAGvpdPKAYVLGSPALAAELEAVGVTSVGVGPDVlhgdgpsdwlavplepdvraVVVGFDPHFSYMKLTKAVRYLQQ 190
Cdd:cd16422   77 KEFIK---PKIFLLGTKSLREEFEKAGFTLDGDDIDV--------------------VVLGFDTELTYEKLRTACLLLRR 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 191 PdCLLVGTNMDNRLPLENGrFIAGTGCLVRAVEMAAQRQAD-IIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLG 269
Cdd:cd16422  134 G-IPYIATHPDINCPSEEG-PIPDAGSIIALIETSTGRRPDlVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLG 211

                        250       260
                 ....*....|....*....|
gi 281332119 270 STCSLKTILTLTGVSSLEDV 289
Cdd:cd16422  212 INAGVDSILVLSGETTREDL 231
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 29-316 1.62e-42

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: 147.33  E-value: 1.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  29 DTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggpmgpEAGL-EVFGTAYCSAL 107
Cdd:cd07531    1 KGYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGI------EVGEdEILVSSYVTAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 108 YLrqrLAGVPDPKAYVLGSPALAAELEAVGVTSVGvGPDvlhgdgpSDWLavplepdvraVVVGFDPHFSYMKLTKAVRY 187
Cdd:cd07531   75 FL---AREKPNAKVFVTGEEGLIEELRLAGLEIVD-KYD-------EAEY----------VVVGSNRKITYELLTKAFRA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 188 LQQpDCLLVGTNMDNRLPLENGRfIAGTGCLVRAVEMAAQRQAD-IIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDI 266
Cdd:cd07531  134 CLR-GARYIATNPDRIFPAEDGP-IPDTAAIIGAIEWCTGREPEvVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDI 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 281332119 267 LLGSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDSIADLL 316
Cdd:cd07531  212 AMGKAIGMETALVLTGVTTRENLD---------RHGYKPDYVLNSIKDLV 252
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 31-139 9.74e-37

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 127.20  E-value: 9.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   31 LLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggpmgPEAGLEVFGTAYCSALYLR 110
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGF-----DIDEDEIITSGTAAADYLK 75

                          90       100
                  ....*....|....*....|....*....
gi 281332119  111 QRLagvPDPKAYVLGSPALAAELEAVGVT 139
Cdd:pfam13344  76 ERK---FGKKVLVIGSEGLREELEEAGFE 101
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 31-282 6.73e-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: 6.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  31 LLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFggPMGPEaglEVFGTAYCSALYLR 110
Cdd:cd07509    3 VLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGF--DVSEE---EIFTSLTAARQYLE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 111 QRlaGVPdpkayvlgsPALaaeleavgvtsvgvgpdVLHGDGPSDWLAV-PLEPDvrAVVVGFDP-HFSYMKLTKAVRYL 188
Cdd:cd07509   78 EK--GLR---------PHL-----------------LVDDDALEDFIGIdTSDPN--AVVIGDAGeHFNYQTLNRAFRLL 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 189 QQPDCLLVgtnmdnrlpLENGRFIA-------GTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDR 261
Cdd:cd07509  128 LDGAPLIA---------LHKGRYYKrkdglalDPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDD 198

                        250       260
                 ....*....|....*....|.
gi 281332119 262 LDTDILLGSTCSLKTILTLTG 282
Cdd:cd07509  199 LRDDVGGAQACGMRGILVRTG 219
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 32-314 8.19e-31

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: 116.49  E-value: 8.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   32 LFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGPMGpeaglEVFGTAYCSALYL-R 110
Cdd:TIGR01457   5 LIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATEE-----QVFTTSMATAQYIaQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  111 QRLagvpDPKAYVLGSPALAAELEAVGVTSVGVGPDVlhgdgpsdwlavplepdvraVVVGFDPHFSYMKLTKAVRYLQQ 190
Cdd:TIGR01457  80 QKK----DASVYVIGEEGLREAIKENGLTFGGENPDY--------------------VVVGLDRSITYEKFAVACLAIRN 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  191 pDCLLVGTNMDNRLPLENGrFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGS 270
Cdd:TIGR01457 136 -GARFISTNGDIAIPTERG-LLPGNGSLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGI 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 281332119  271 TCSLKTILTLTGVSSLEDVKSNQESdcmfkkkmvPDFYVDSIAD 314
Cdd:TIGR01457 214 NAGIDTLLVHTGVTKREHMTDDMEK---------PTHAIDSLAE 248
PRK10444 PRK10444
HAD-IIA family hydrolase;
34-291 2.05e-25

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 102.18  E-value: 2.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  34 DCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEklrRLGFGGPMGPEaglEVFGT-AYCSALYLRQR 112
Cdd:PRK10444   7 DIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLAN---RFATAGVDVPD---SVFYTsAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 113 LAGvpdpKAYVLGSPALAAELEAVGVTSVGVGPDVlhgdgpsdwlavplepdvraVVVGFDPHFSYMKLTKAVRYLQQpD 192
Cdd:PRK10444  81 EGK----KAYVIGEGALIHELYKAGFTITDINPDF--------------------VIVGETRSYNWDMMHKAAYFVAN-G 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 193 CLLVGTNMDNRLPlengRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTC 272
Cdd:PRK10444 136 ARFIATNPDTHGR----GFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQA 211

                        250
                 ....*....|....*....
gi 281332119 273 SLKTILTLTGVSSLEDVKS 291
Cdd:PRK10444 212 GLETILVLSGVSTLDDIDS 230
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 28-314 4.90e-20

HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of the IIA subfamily (TIGR01460) of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. One sequence (GP|10716807) has been annotated as a "phospholysine phosphohistidine inorganic pyrophosphatase," probably in reference to studies on similarly described (but unsequenced) enzymes from bovine and rat tissues. However, the supporting information for this annotation has never been published. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 162372 [Multi-domain]  Cd Length: 257  Bit Score: 87.61  E-value: 4.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   28 VDTLLFDCDGVLW----RGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGgpmgpEAGLEVFGTAY 103
Cdd:TIGR01458   1 VKGVLLDISGVLYisdaGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFD-----ISEDEVFTPAP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  104 CSALYLRQRlagvpdpkayvlgspalaaeleavgvtsvGVGPDVLHGDGPSDWLAVPLEPDVRAVVVGFDP-HFSYMKLT 182
Cdd:TIGR01458  76 AARQLLEEK-----------------------------QLRPMLLVDDRVLPDFDGIDTSDPNCVVMGLAPeHFSYQILN 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  183 KAVRYL-QQPDCLLVGtnmdnrlpLENGRFIA-------GTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPER 254
Cdd:TIGR01458 127 QAFRLLlDGAKPVLIA--------IGKGRYYKrkdglalDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEE 198

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  255 TVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDSIAD 314
Cdd:TIGR01458 199 AVMIGDDCRDDVGGAQDCGMRGIQVRTGKYRPSDEE---------KINVPPDLTCDSLPH 249
Hydrolase_like pfam13242
HAD-hyrolase-like;
232-315 1.99e-18

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 78.04  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  232 IIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKsnqesdcmfKKKMVPDFYVDS 311
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLE---------KAPIRPDYVVDD 71


                  ....
gi 281332119  312 IADL 315
Cdd:pfam13242  72 LAEA 75
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 29-307 7.79e-12

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: 64.27  E-value: 7.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  29 DTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITnNSSKTRTAYAEKLRRLGFggpmgPEAGLEVFGTAYCSALY 108
Cdd:cd07525    1 DAFLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVT-NAPRPAESVVRQLAKLGV-----PPSTYDAIITSGEVTRE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 109 LRQRLAGVPdPKAYVLGSPALAAELEAVGVTSVGVGP--DVLHGDGPSDWLAVPLEpdvravvvgfdphfsymKLTKAVR 186
Cdd:cd07525   75 LLAREAGLG-RKVYHLGPERDANVLEGLDVVATDDAEkaEFILCTGLYDDETETPE-----------------DYRKLLK 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 187 YLQQPDCLLVGTNMDNRLPLEnGRFIAGTGCLVRAVEMAAQRqADIIGKPSRFIFDCVSQEYGINP-ERTVMVGDRLDTD 265
Cdd:cd07525  137 AAAARGLPLICANPDLVVPRG-GKLIYCAGALAELYEELGGE-VIYFGKPHPPIYDLALARLGRPAkARILAVGDGLHTD 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 281332119 266 ILLGSTCSLKTILTLTGVSSLEDvksnqeSDCMFKKKMVPDF 307
Cdd:cd07525  215 ILGANAAGLDSLFVTGGIHRRLA------AEAGIKSQIVPDF 250
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 24-281 3.18e-08

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: 53.36  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   24 LLAEVDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAeKLRRLGFGGPMgPEAGLEVFGTAY 103
Cdd:TIGR01459   4 LINDYDVFLLDLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIFSLHK-TLKSLGINADL-PEMIISSGEIAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  104 CSALYLRQRlAGVPDPKAYVLGspalaaeleavgvtsvgvgpdvlHGDGPSDWLAVPLEPDVR-----AVVVGF---DPH 175
Cdd:TIGR01459  82 QMILESKKR-FDIRNGIIYLLG-----------------------HLENDIINLMQCYTTDDEnkanaSLITIYrseNEK 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  176 FSYMKLTKAVRYLQQPDCLLVGTNMDnRLPLENGRFIAGTGCLvraVEMAAQRQADII--GKPSRFIFDCVSQEYGINPE 253
Cdd:TIGR01459 138 LDLDEFDELFAPIVARKIPNICANPD-RGINQHGIYRYGAGYY---AELIKQLGGKVIysGKPYPAIFHKALKECSNIPK 213

                         250       260
                  ....*....|....*....|....*....
gi 281332119  254 RTV-MVGDRLDTDILLGSTCSLKTILTLT 281
Cdd:TIGR01459 214 NRMlMVGDSFYTDILGANRLGIDTALVLT 242
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 233-277 3.24e-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: 51.00  E-value: 3.24e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 281332119 233 IGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTI 277
Cdd:cd04305   62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 234-278 9.75e-08

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: 49.57  E-value: 9.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 281332119 234 GKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTIL 278
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTIL 107
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 234-316 1.20e-07

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 51.63  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  234 GKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSsledvkSNQESDCMFKkkmvPDFYVDSIA 313
Cdd:TIGR02253 149 EKPHPKIFYAALKRLGVKPEEAVMVGDRLDKDIKGAKNAGMKTVWINQGKS------SKMEDDVYPY----PDYEISSLR 218


                  ...
gi 281332119  314 DLL 316
Cdd:TIGR02253 219 ELL 221
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
234-320 2.56e-07

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.31  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 234 GKPSRFIFDCVSQEYGINPERTVMVGDRLdTDILLGSTCSLKTILTLTGVSSLEDVKSNQesdcmfkkkmvPDFYVDSIA 313
Cdd:COG0546  139 AKPKPEPLLEALERLGLDPEEVLMVGDSP-HDIEAARAAGVPFIGVTWGYGSAEELEAAG-----------ADYVIDSLA 206


                 ....*..
gi 281332119 314 DLLPALQ 320
Cdd:COG0546  207 ELLALLA 213
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 31-143 6.25e-07

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: 47.39  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  31 LLFDCDGVLWrgetavpgAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGGP---MGPEAGLEVFGTAYCSAL 107
Cdd:cd01427    2 VLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGiigSDGGGTPKPKPKPLLLLL 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 281332119 108 ylrqRLAGVPDPKAYVLG-SPALAAELEAVGVTSVGV 143
Cdd:cd01427   74 ----LKLGVDPEEVLFVGdSENDIEAARAAGGRTVAV 106
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
234-278 3.12e-06

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 46.66  E-value: 3.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 281332119 234 GKPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL----LGstcsLKTIL 278
Cdd:COG2179   90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLggnrAG----LYTIL 134
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 28-267 4.18e-06

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: 46.43  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119   28 VDTLLFDCDGVLWRGETAVPGAPETLRALRARGKRLGfitnnssktrtAYAEKLRRLGfggpmgpeaglevfgtaycsAL 107
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIV-----------AAAEDLPIPV--------------------ED 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  108 YLRQRLAGVPDPKAYVLGSPALAAELEAVGVTSVGVgpdvlhgdgpsdwlavplepDVRAVVVGFDPHFSYMKLTKAVRY 187
Cdd:pfam00702  50 FTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLV--------------------ELLGVIALADELKLYPGAAEALKA 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  188 LQQPDC-LLVGTNmDNRLPLENGRFIAGtgcLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDtDI 266
Cdd:pfam00702 110 LKERGIkVAILTG-DNPEAAEALLRLLG---LDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVN-DI 184


                  .
gi 281332119  267 L 267
Cdd:pfam00702 185 P 185
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 235-319 1.04e-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: 45.79  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119 235 KPSRFIFDCVSQEYGINPERTVMVGDRLDTDIL----LGstcsLKTILtltgvssLEDVKSNQESDCmfkkkmVPDFYVD 310
Cdd:COG1011  149 KPDPEIFELALERLGVPPEEALFVGDSPETDVAgaraAG----MRTVW-------VNRSGEPAPAEP------RPDYVIS 211


                 ....*....
gi 281332119 311 SIADLLPAL 319
Cdd:COG1011  212 DLAELLELL 220
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 44-122 1.09e-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: 45.79  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  44 TAVPGAPETLRALRARGKRLGFITNNSsktRTAYAEKLRRLGFGGPmgpeaglevFGTAYCSAlylrqrLAGV--PDPKA 121
Cdd:COG1011   93 EPYPDALELLEALKARGYRLALLTNGS---AELQEAKLRRLGLDDL---------FDAVVSSE------EVGVrkPDPEI 154


                 .
gi 281332119 122 Y 122
Cdd:COG1011  155 F 155
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 235-293 2.01e-05

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: 44.32  E-value: 2.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281332119  235 KPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGSTCSLKTILTLTGVSSLEDVKSNQ 293
Cdd:TIGR01668  91 KPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQWFIKRI 149
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 246-314 4.58e-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: 43.16  E-value: 4.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281332119 246 QEYGINPERTVMVGDRLdTDILLGSTCSLKTILTLTGVSSLEDvksnqesdcmfkKKMVPDFYVDSIAD 314
Cdd:COG0241  113 ERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLTGKGAEEL------------AEALPDTVADDLAE 168
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
47-158 6.30e-05

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 43.38  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119  47 PGAPETLRALRARGKRLGFITNNSsktrTAYAEK-LRRLGFGGPMGPEAGLEVFGTAYCSALYLRQ--RLAGVPDPKAYV 123
Cdd:COG0546   87 PGVRELLEALKARGIKLAVVTNKP----REFAERlLEALGLDDYFDAIVGGDDVPPAKPKPEPLLEalERLGLDPEEVLM 162

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 281332119 124 LG-SPA--LAAelEAVGVTSVGVGPDVLHGDGPSDWLA 158
Cdd:COG0546  163 VGdSPHdiEAA--RAAGVPFIGVTWGYGSAEELEAAGA 198
HAD_like cd07511
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 31-84 1.98e-04

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: 40.83  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 281332119  31 LLFDCDGVLWRGETAVPGAPETLRALraRGKRLGFI--TNNSSKTRTAYAEKLRRL 84
Cdd:cd07511    3 FAFDIDGVLVRGKKPIPGAPKALKFL--NDNKIPFIflTNGGGFPESKRADFLSKL 56
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
44-88 3.39e-04

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 41.49  E-value: 3.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 281332119  44 TAVPGAPETLRALRARGKRLGFITNNSSKTRTAYAEKLRRLGFGG 88
Cdd:COG2503  123 TAVPGAVEFLNYANSKGVTVFYISNRKAEEKAATLANLKALGFPV 167
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-155 1.58e-03

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: 39.11  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281332119    4 AEAGGDEVRCVRLSAERAKLLLAEVDTLLFDCDGVlwrgeTAVPGAPETLRALRARGKRLGFITNNSsktRTAYAEKLRR 83
Cdd:pfam00702  63 EELDILRGLVETLEAEGLTVVLVELLGVIALADEL-----KLYPGAAEALKALKERGIKVAILTGDN---PEAAEALLRL 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281332119   84 LGFGGPMGPEAGLEVFGtaycsalylrqrlAGVPDPKAYVlgspALAAELeavgvtsvGVGP-DVLH-GDGPSD 155
Cdd:pfam00702 135 LGLDDYFDVVISGDDVG-------------VGKPKPEIYL----AALERL--------GVKPeEVLMvGDGVND 183
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 249-317 1.70e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 39.24  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281332119 249 GINPERTVMVGDRLDtDILLGSTCSLKTIL---TLTGVSSLEdvksnqesdcmfkkKMVPDFYVDSIADLLP 317
Cdd:PRK13288 152 GAKPEEALMVGDNHH-DILAGKNAGTKTAGvawTIKGREYLE--------------QYKPDFMLDKMSDLLA 208
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 246-319 2.60e-03

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: 38.34  E-value: 2.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281332119 246 QEYGINPERTVMVGDRlDTDILLGSTCSLKTILTLTGVSSLEDVKSNQesdcmfkkkmvPDFYVDSIADLLPAL 319
Cdd:cd04302  148 DTLGIAPEQAVMIGDR-KHDIIGARANGIDSIGVLYGYGSEDELEEAG-----------ATYIVETPAELLELL 209
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 30-85 3.88e-03

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: 36.37  E-value: 3.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 281332119  30 TLLFDCDgvlwrgETAVPGAPETLRALRArGKRLGFITNNSSKTRTayaEKLRRLG 85
Cdd:cd04305    1 AIIFDLD------DTLLPGAKELLEELKK-GYKLGIITNGPTEVQW---EKLEQLG 46
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 249-281 4.01e-03

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: 37.00  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 281332119  249 GINPERTVMVGDRLDTDILLGSTCSLKTILTLT 281
Cdd:TIGR01662 103 EIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 249-317 4.01e-03

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: 38.03  E-value: 4.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281332119 249 GINPERTVMVGDRlDTDILLGSTCSLKTILTLTGVSSLEDVKSNQesdcmfkkkmvPDFYVDSIADLLP 317
Cdd:cd02616  150 GAEPEEALMVGDS-PHDILAGKNAGVKTVGVTWGYKGREYLKAFN-----------PDFIIDKMSDLLT 206
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 246-278 5.23e-03

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: 36.74  E-value: 5.23e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 281332119 246 QEYGINPERTVMVGDRlDTDILLGSTCSLKTIL 278
Cdd:cd07503  110 KELGIDLARSFVIGDR-LSDIQAARNAGCKGIL 141
 
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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