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Conserved domains on  [gi|190624332|gb|EDV39856|]
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uncharacterized protein Dana_GF10231 [Drosophila ananassae]

Protein Classification

HAD family hydrolase( domain architecture ID 11576405)

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_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 19-303 1.08e-156

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: 439.05  E-value: 1.08e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  19 KWVKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIAN 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  99 FLKNKGMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDK--SMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLR 176
Cdd:cd07532   81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKddSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 177 NPDVIVVGTSMDAAYPFDEhRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKF 256
Cdd:cd07532  161 NPDVLFLATNMDATFPGPV-GRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILF 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 190624332 257 AHNCGFHSLLVGTGVHSFEDAQKIKDSGDKKKKSFIPDTYLPSFGHL 303
Cdd:cd07532  240 ANNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 19-303 1.08e-156

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: 439.05  E-value: 1.08e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  19 KWVKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIAN 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  99 FLKNKGMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDK--SMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLR 176
Cdd:cd07532   81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKddSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 177 NPDVIVVGTSMDAAYPFDEhRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKF 256
Cdd:cd07532  161 NPDVLFLATNMDATFPGPV-GRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILF 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 190624332 257 AHNCGFHSLLVGTGVHSFEDAQKIKDSGDKKKKSFIPDTYLPSFGHL 303
Cdd:cd07532  240 ANNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 24-303 8.93e-67

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: 210.11  E-value: 8.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   24 IETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNK 103
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  104 GM-RRKVFVMGEIGIRAELDKVGIAHM-EVDEKLDKSMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPDVI 181
Cdd:TIGR01452  82 PDaGKAVYVIGEEGLRAELDAAGIRLAgDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAHLREPGCL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  182 VVGTSMDAAYPF-DEHRkvIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNC 260
Cdd:TIGR01452 162 FVATNRDPWHPLsDGSR--TPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRC 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 190624332  261 GFHSLLVGTGVHSFEDAQkikDSGDKKKKSFIPDTYLPSFGHL 303
Cdd:TIGR01452 240 GMTTVLVLSGVSQLEEAQ---EYLMAGQDDLVPDYVVESLADL 279
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
21-304 3.65e-56

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 182.23  E-value: 3.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  21 VKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFL 100
Cdd:COG0647    5 ADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 101 KNKGMRRKVFVMGEIGIRAELDKVGIahmevdekldksmyefakELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPdV 180
Cdd:COG0647   85 AERHPGARVYVIGEEGLREELEEAGL------------------TLVDDEEPDAVVVGLDRTFTYEKLAEALRAIRRG-A 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 181 IVVGTSMDAAYPFDehRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNC 260
Cdd:COG0647  146 PFIATNPDRTVPTE--DGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAA 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 190624332 261 GFHSLLVGTGVHSFEDAQkikdsgdkkKKSFIPDTYLPSFGHLL 304
Cdd:COG0647  224 GLDTLLVLTGVTTAEDLE---------AAPIRPDYVLDSLAELL 258
PLN02645 PLN02645
phosphoglycolate phosphatase
 21-278 1.18e-46

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 159.49  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  21 VKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFL 100
Cdd:PLN02645  25 IDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 101 K--NKGMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDKSMYEFAKEL-EIDPDVGAVVIGRDERYNMARLIRTSAYLR- 176
Cdd:PLN02645 105 KsiNFPKDKKVYVIGEEGILEELELAGFQYLGGPEDGDKKIELKPGFLmEHDKDVGAVVVGFDRYINYYKIQYATLCIRe 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 177 NPDVIVVGTSMDAAYPFDEHRKvIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKF 256
Cdd:PLN02645 185 NPGCLFIATNRDAVTHLTDAQE-WAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILF 263

                        250       260
                 ....*....|....*....|..
gi 190624332 257 AHNCGFHSLLVGTGVHSFEDAQ 278
Cdd:PLN02645 264 GQNGGCKTLLVLSGVTSESMLL 285
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 27-126 3.90e-36

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 125.27  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMR 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|
gi 190624332  107 RKVFVMGEIGIRAELDKVGI 126
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGF 100
 
Name Accession Description Interval E-value
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 19-303 1.08e-156

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: 439.05  E-value: 1.08e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  19 KWVKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIAN 98
Cdd:cd07532    1 EWLANIDTVIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFNVKENNILSSAAVIAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  99 FLKNKGMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDK--SMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLR 176
Cdd:cd07532   81 YLKEKGFKKKVYVIGEEGIRKELEEAGIVSCGGDGEDEKddSMGDFAHNLELDPDVGAVVVGRDEHFSYPKLMKACNYLR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 177 NPDVIVVGTSMDAAYPFDEhRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKF 256
Cdd:cd07532  161 NPDVLFLATNMDATFPGPV-GRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILF 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 190624332 257 AHNCGFHSLLVGTGVHSFEDAQKIKDSGDKKKKSFIPDTYLPSFGHL 303
Cdd:cd07532  240 ANNCGFQSLLVGTGVNSLEDAEKIKKEGDPKKKDLVPDTYLPSLGHL 286
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 27-302 4.51e-86

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: 259.22  E-value: 4.51e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMR 106
Cdd:cd07508    2 VISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDVPEDQIVTSAKATARFLRSRKFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 107 RKVFVMGEIGIRAELDKVGIAHMEVDEKLDKSMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPDVIVVGTS 186
Cdd:cd07508   82 KKVYVLGEEGLKEELRAAGFRIAGGPSKGIETYAELVEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNPGCLFIATA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 187 MDAAYPFDEHRkVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHSLL 266
Cdd:cd07508  162 PDRIHPLKDGG-PIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKACGFQTLL 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 190624332 267 VGTGVHSFEDAQkikdsgDKKKKSFIPDTYLPSFGH 302
Cdd:cd07508  241 VLTGVTTLEDLQ------AYIDHELVPDYYADSLAD 270
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 24-307 2.02e-75

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: 232.28  E-value: 2.02e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  24 IETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGF-MIDEDHCRTSSTSIANFLKN 102
Cdd:cd07510    1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFtGLKEEEIFSSAYCAARYLRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 103 K---GMRRKVFVMGEIGIRAELDKVGIAHMEV-DEKLDKSMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNP 178
Cdd:cd07510   81 RlpgPADGKVYVLGGEGLRAELEAAGVAHLGGpDDGLRRAAPKDWLLAGLDPDVGAVLVGLDEHVNYLKLAKATQYLRDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 179 DVIVVGTSMDAAYPFdEHRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAH 258
Cdd:cd07510  161 GCLFVATNRDPWHPL-SDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFGQ 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 190624332 259 NCGFHSLLVGTGVHSFEDAQKIKDSGDkkkksfIPDTYLPSFGHLLEFL 307
Cdd:cd07510  240 NCGLKTLLVLTGVSTLEEALAKLSNDL------VPDYYVESLADLLELL 282
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 24-303 8.93e-67

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: 210.11  E-value: 8.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   24 IETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNK 103
Cdd:TIGR01452   2 AQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGLAEQLFSSALCAARLLRQP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  104 GM-RRKVFVMGEIGIRAELDKVGIAHM-EVDEKLDKSMYEFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPDVI 181
Cdd:TIGR01452  82 PDaGKAVYVIGEEGLRAELDAAGIRLAgDPGEKKQDEADGFMYDIKLDERVGAVVVGYDEHFSYVKLMEACAHLREPGCL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  182 VVGTSMDAAYPF-DEHRkvIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNC 260
Cdd:TIGR01452 162 FVATNRDPWHPLsDGSR--TPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILFGHRC 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 190624332  261 GFHSLLVGTGVHSFEDAQkikDSGDKKKKSFIPDTYLPSFGHL 303
Cdd:TIGR01452 240 GMTTVLVLSGVSQLEEAQ---EYLMAGQDDLVPDYVVESLADL 279
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
21-304 3.65e-56

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 182.23  E-value: 3.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  21 VKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFL 100
Cdd:COG0647    5 ADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIPVAEDEIVTSGDATAAYL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 101 KNKGMRRKVFVMGEIGIRAELDKVGIahmevdekldksmyefakELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPdV 180
Cdd:COG0647   85 AERHPGARVYVIGEEGLREELEEAGL------------------TLVDDEEPDAVVVGLDRTFTYEKLAEALRAIRRG-A 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 181 IVVGTSMDAAYPFDehRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNC 260
Cdd:COG0647  146 PFIATNPDRTVPTE--DGLIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAA 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 190624332 261 GFHSLLVGTGVHSFEDAQkikdsgdkkKKSFIPDTYLPSFGHLL 304
Cdd:COG0647  224 GLDTLLVLTGVTTAEDLE---------AAPIRPDYVLDSLAELL 258
PLN02645 PLN02645
phosphoglycolate phosphatase
 21-278 1.18e-46

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 159.49  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  21 VKNIETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFL 100
Cdd:PLN02645  25 IDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLNVTEEEIFSSSFAAAAYL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 101 K--NKGMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDKSMYEFAKEL-EIDPDVGAVVIGRDERYNMARLIRTSAYLR- 176
Cdd:PLN02645 105 KsiNFPKDKKVYVIGEEGILEELELAGFQYLGGPEDGDKKIELKPGFLmEHDKDVGAVVVGFDRYINYYKIQYATLCIRe 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 177 NPDVIVVGTSMDAAYPFDEHRKvIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKF 256
Cdd:PLN02645 185 NPGCLFIATNRDAVTHLTDAQE-WAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILF 263

                        250       260
                 ....*....|....*....|..
gi 190624332 257 AHNCGFHSLLVGTGVHSFEDAQ 278
Cdd:PLN02645 264 GQNGGCKTLLVLSGVTSESMLL 285
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 25-278 2.16e-42

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: 146.20  E-value: 2.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  25 ETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKG 104
Cdd:cd07530    1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGIDVPEEDVYTSALATAQYLAEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 105 MRRKVFVMGEIGIRAELDKVGiahmevdekldksmYEFAKEleiDPDvgAVVIGRDERYNMARLiRTSAYLRNPDVIVVG 184
Cdd:cd07530   81 PGAKVYVIGEEGLRTALHEAG--------------LTLTDE---NPD--YVVVGLDRDLTYEKL-AEATLAIRNGAKFIA 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 185 TSMDAAYPfdEHRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHS 264
Cdd:cd07530  141 TNPDLTLP--TERGLLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDT 218

                        250
                 ....*....|....
gi 190624332 265 LLVGTGVHSFEDAQ 278
Cdd:cd07530  219 LLVLTGVTTREDLA 232
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 27-270 3.63e-41

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: 142.85  E-value: 3.63e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGL-GFMIDEDHCRTSSTSIANFLKNKGM 105
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLlGVDVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  106 RRKVFVMGEIGIRAELDKVGIAHMEVDekldksmyeFAKELEIDPDVGAVVIGRDERYNMARLIRTSAYLRNPDVIVVGT 185
Cdd:TIGR01460  81 GEKVYVIGVGELRESLEGLGFRNDFFD---------DIDHLAIEKIPAAVIVGEPSDFSYDELAKAAYLLAEGDVPFIAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  186 SMDAAYPFDEHRKVIvGASAMMTSVRALSGRQPLILGKPNPWILDPLLK-CGVIKPDTTLMVGDTMTADMKFAHNCGFHS 264
Cdd:TIGR01460 152 NRDDLVRLGDGRFRP-GAGAIAAGIKELSGREPTVVGKPSPAIYRAALNlLQARPERRDVMVGDNLRTDILGAKNAGFDT 230


                  ....*.
gi 190624332  265 LLVGTG 270
Cdd:TIGR01460 231 LLVLTG 236
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 27-126 3.90e-36

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 125.27  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMR 106
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGFDIDEDEIITSGTAAADYLKERKFG 80

                          90       100
                  ....*....|....*....|
gi 190624332  107 RKVFVMGEIGIRAELDKVGI 126
Cdd:pfam13344  81 KKVLVIGSEGLREELEEAGF 100
PRK10444 PRK10444
HAD-IIA family hydrolase;
24-276 3.90e-26

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 103.72  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  24 IETIICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNK 103
Cdd:PRK10444   1 IKNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 104 gMRRKVFVMGEIGIRAELDKVGIAHMevdekldksmyefakelEIDPDVgaVVIGRDERYNMaRLIRTSAYLrnpdvIVV 183
Cdd:PRK10444  81 -EGKKAYVIGEGALIHELYKAGFTIT-----------------DINPDF--VIVGETRSYNW-DMMHKAAYF-----VAN 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 184 GTSMDAAYPfDEHRKVIVGA-SAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGF 262
Cdd:PRK10444 135 GARFIATNP-DTHGRGFYPAcGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGL 213

                        250
                 ....*....|....
gi 190624332 263 HSLLVGTGVHSFED 276
Cdd:PRK10444 214 ETILVLSGVSTLDD 227
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 28-278 3.72e-25

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: 100.97  E-value: 3.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  28 ICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMRR 107
Cdd:cd16422    3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGLDRVFTSGEATIDHLKKEFIKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 108 KVFVMGEIGIRAELDKVGIahmEVDEKldksmyefakeleiDPDVgaVVIGRDERYNMARLIRTSAYLRNPdVIVVGTSM 187
Cdd:cd16422   83 KIFLLGTKSLREEFEKAGF---TLDGD--------------DIDV--VVLGFDTELTYEKLRTACLLLRRG-IPYIATHP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 188 DAAYPFDEhrKVIVGASAMMTSVRALSGRQP-LILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHSLL 266
Cdd:cd16422  143 DINCPSEE--GPIPDAGSIIALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSIL 220

                        250
                 ....*....|..
gi 190624332 267 VGTGVHSFEDAQ 278
Cdd:cd16422  221 VLSGETTREDLE 232
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 30-270 6.20e-21

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: 89.65  E-value: 6.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  30 DADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMRRKV 109
Cdd:cd07509    6 DLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFDVSEEEIFTSLTAARQYLEEKGLRPHL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 110 FVMGEIgiraeldkvgiahMEVDEKLDKSmyefakeleiDPDvgAVVIGR-DERYNMARLIRTSAYLRN-PDVIVVGTSM 187
Cdd:cd07509   86 LVDDDA-------------LEDFIGIDTS----------DPN--AVVIGDaGEHFNYQTLNRAFRLLLDgAPLIALHKGR 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 188 daaYpFDEHRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHSLLV 267
Cdd:cd07509  141 ---Y-YKRKDGLALDPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILV 216


                 ...
gi 190624332 268 GTG 270
Cdd:cd07509  217 RTG 219
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 27-276 1.16e-19

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: 86.08  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFLKNKGMR 106
Cdd:cd07531    3 YIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLAREKPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 107 RKVFVMGEIGIRAELDKVGIahmEVDEKLDKSMYefakeleidpdvgaVVIGRDERYNMARL-IRTSAYLRNPDVIvvGT 185
Cdd:cd07531   83 AKVFVTGEEGLIEELRLAGL---EIVDKYDEAEY--------------VVVGSNRKITYELLtKAFRACLRGARYI--AT 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 186 SMDAAYPFDEHRkvIVGASAMMTSVRALSGRQP-LILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHS 264
Cdd:cd07531  144 NPDRIFPAEDGP--IPDTAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMET 221

                        250
                 ....*....|..
gi 190624332 265 LLVGTGVHSFED 276
Cdd:cd07531  222 ALVLTGVTTREN 233
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 24-270 9.04e-14

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: 69.89  E-value: 9.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   24 IETIICDADGVLW----HFTKAIDGAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANF 99
Cdd:TIGR01458   1 VKGVLLDISGVLYisdaGGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFDISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  100 LKNKGMRRKVFVmgEIGIRAELDKVgiahmevdeklDKSmyefakeleiDPDvgAVVIGRDERY----NMARLIRTSAYL 175
Cdd:TIGR01458  81 LEEKQLRPMLLV--DDRVLPDFDGI-----------DTS----------DPN--CVVMGLAPEHfsyqILNQAFRLLLDG 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  176 RNPDVIVVGtsmDAAYpFDEHRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMK 255
Cdd:TIGR01458 136 AKPVLIAIG---KGRY-YKRKDGLALDVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVG 211

                         250
                  ....*....|....*
gi 190624332  256 FAHNCGFHSLLVGTG 270
Cdd:TIGR01458 212 GAQDCGMRGIQVRTG 226
Hydrolase_like pfam13242
HAD-hyrolase-like;
220-278 1.19e-13

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 64.94  E-value: 1.19e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 190624332  220 ILGKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHSLLVGTGVHSFEDAQ 278
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLE 59
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 27-277 2.24e-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: 65.81  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  27 IICDADGVLWHFTKAIDGAPEVFKRVTESGRNLFIVTNnSSMPSEAFAKRAQGLGFMIDEDHCRTSSTSIANFL--KNKG 104
Cdd:cd07525    3 FLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTN-APRPAESVVRQLAKLGVPPSTYDAIITSGEVTRELlaREAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 105 MRRKVFVMG---EIGIRAELDKVGIAhmEVDEKLDKSMYEFAKELEIDPDvgavviGRDERYNMARLIRTSAYLRNPDVI 181
Cdd:cd07525   82 LGRKVYHLGperDANVLEGLDVVATD--DAEKAEFILCTGLYDDETETPE------DYRKLLKAAAARGLPLICANPDLV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 182 VvgtsmdaaypfDEHRKVIVGASAMMTSVRALSGRQpLILGKPNPWILDPLLK-CGVIKPDTTLMVGDTMTADMKFAHNC 260
Cdd:cd07525  154 V-----------PRGGKLIYCAGALAELYEELGGEV-IYFGKPHPPIYDLALArLGRPAKARILAVGDGLHTDILGANAA 221

                        250
                 ....*....|....*..
gi 190624332 261 GFHSLLVGTGVHSFEDA 277
Cdd:cd07525  222 GLDSLFVTGGIHRRLAA 238
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
212-307 1.07e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 54.55  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332 212 ALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTmTADMKFAHNCGFHSLLVGTGVHSFEDAQKIKdsgdkkkksf 291
Cdd:COG0546  129 AIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVPFIGVTWGYGSAEELEAAG---------- 197

                         90
                 ....*....|....*.
gi 190624332 292 iPDTYLPSFGHLLEFL 307
Cdd:COG0546  198 -ADYVIDSLAELLALL 212
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 222-276 4.39e-08

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; 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: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 52.40  E-value: 4.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 190624332 222 GKPNPWILDPLL-KCGViKPDTTLMVGDTmTADMKFAHNCGFHSLLVGTGVHSFED 276
Cdd:cd07533  138 SKPHPEMLREILaELGV-DPSRAVMVGDT-AYDMQMAANAGAHAVGVAWGYHSLED 191
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 223-264 5.46e-05

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: 41.76  E-value: 5.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 190624332 223 KPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHS 264
Cdd:cd04305   64 KPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKT 105
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 24-261 9.25e-05

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: 42.57  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332   24 IETIICDADGVLWhftkaiDGAPEVFKRVTESGRNLFIvtnnssmpSEAFAKRAQGLGFmidedhcrtsstSIANFLKNK 103
Cdd:pfam00702   1 IKAVVFDLDGTLT------DGEPVVTEAIAELASEHPL--------AKAIVAAAEDLPI------------PVEDFTARL 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  104 GMRRKVFVMGEIGIRAELDKVGIAHMEVDEKLDKSMYEFAKELEIDPDVGAVVigrderynmarlirtsAYLRNPDV-IV 182
Cdd:pfam00702  55 LLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEAL----------------KALKERGIkVA 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190624332  183 VGTSmdaayPFDEHRKVIVGASAMMTSVRALSGRQPLILGKPNPWILDPLLKCGVIKPDTTLMVGDTMtADMKFAHNCG 261
Cdd:pfam00702 119 ILTG-----DNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 222-267 2.01e-04

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: 39.94  E-value: 2.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 190624332 222 GKPNPWILDPLLKCGVIKPDTTLMVGDTMTADMKFAHNCGFHSLLV 267
Cdd:cd16416   63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTILV 108
HAD_dREG-2_like cd16415
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to ...
 223-268 3.74e-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: 36.89  E-value: 3.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 190624332 223 KPNPWILD-PLLKCGViKPDTTLMVGDTMTADMKFAHNCGFHSLLVG 268
Cdd:cd16415   62 KPDPRIFQkALERLGV-SPEEALHVGDDLKNDYLGARAVGWHALLVD 107
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 27-113 5.46e-03

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: 35.83  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190624332  27 IICDADGVLWhftkaidgAPEVFKRVTESGRNLFIVTNNSSMPSEAFAKRaqgLGFMIDEDHCRTSSTSIANFLKNKGMR 106
Cdd:cd01427    2 VLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREALRALLEK---LGLGDLFDGIIGSDGGGTPKPKPKPLL 70


                 ....*..
gi 190624332 107 RKVFVMG 113
Cdd:cd01427   71 LLLLKLG 77
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 223-267 7.18e-03

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: 37.32  E-value: 7.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 190624332 223 KPNP----WILDpllKCGViKPDTTLMVGDTMTADMKFAHNCGFHSLLV 267
Cdd:COG1011  149 KPDPeifeLALE---RLGV-PPEEALFVGDSPETDVAGARAAGMRTVWV 193
 
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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