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Conserved domains on  [gi|10092677|ref|NP_064711|]
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chronophin [Homo sapiens]

Protein Classification

PGP_euk family protein( domain architecture ID 11492666)

PGP_euk family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 18-290 2.00e-168

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: 467.80  E-value: 2.00e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    18 RAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLrAEQLFSSALCAARLLR 97
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGL-AEQLFSSALCAARLLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    98 QrlpgPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-----------PRVRAVLVGYDEHFSFAKLREACAHL 166
Cdd:TIGR01452  80 Q----PPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEadgfmydikldERVGAVVVGYDEHFSYVKLMEACAHL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   167 RDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILF 246
Cdd:TIGR01452 156 REPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 10092677   247 GHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADL 290
Cdd:TIGR01452 236 GHRCGMTTVLVLSGVSQLEEAQEYLMAGQDDLVPDYVVESLADL 279
 
Name Accession Description Interval E-value
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 18-290 2.00e-168

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: 467.80  E-value: 2.00e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    18 RAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLrAEQLFSSALCAARLLR 97
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGL-AEQLFSSALCAARLLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    98 QrlpgPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-----------PRVRAVLVGYDEHFSFAKLREACAHL 166
Cdd:TIGR01452  80 Q----PPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEadgfmydikldERVGAVVVGYDEHFSYVKLMEACAHL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   167 RDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILF 246
Cdd:TIGR01452 156 REPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 10092677   247 GHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADL 290
Cdd:TIGR01452 236 GHRCGMTTVLVLSGVSQLEEAQEYLMAGQDDLVPDYVVESLADL 279
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 19-294 5.42e-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: 456.85  E-value: 5.42e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  19 AQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQ 98
Cdd:cd07510   1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEEEIFSSAYCAARYLRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  99 RLPGPPDapGAVFVLGGEGLRAELRAAGLRLAGDPSAGD-----------GAAPRVRAVLVGYDEHFSFAKLREACAHLR 167
Cdd:cd07510  81 RLPGPAD--GKVYVLGGEGLRAELEAAGVAHLGGPDDGLrraapkdwllaGLDPDVGAVLVGLDEHVNYLKLAKATQYLR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 168 DPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFG 247
Cdd:cd07510 159 DPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFG 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 10092677 248 HRCGMTTVLTLTGVSRLEEAQAYLaagQHDLVPHYYVESIADLTEGL 294
Cdd:cd07510 239 QNCGLKTLLVLTGVSTLEEALAKL---SNDLVPDYYVESLADLLELL 282
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
12-290 1.23e-86

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 259.66  E-value: 1.23e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  12 LRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALC 91
Cdd:COG0647   1 MSELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIP-VAEDEIVTSGDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  92 AARLLRQRLPGppdapGAVFVLGGEGLRAELRAAGLRLAGDPSAGdgaaprvrAVLVGYDEHFSFAKLREACAHLRDPeC 171
Cdd:COG0647  80 TAAYLAERHPG-----ARVYVIGEEGLREELEEAGLTLVDDEEPD--------AVVVGLDRTFTYEKLAEALRAIRRG-A 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 172 LLVATDRDPWHPLSDGsRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCG 251
Cdd:COG0647 146 PFIATNPDRTVPTEDG-LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAG 224

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 10092677 252 MTTVLTLTGVSRLEEAQAYlaagqhDLVPHYYVESIADL 290
Cdd:COG0647 225 LDTLLVLTGVTTAEDLEAA------PIRPDYVLDSLAEL 257
PLN02645 PLN02645
phosphoglycolate phosphatase
 23-290 3.82e-69

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 216.89  E-value: 3.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   23 LFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQrLPG 102
Cdd:PLN02645  32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLN-VTEEEIFSSSFAAAAYLKS-INF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  103 PPDapGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-----------PRVRAVLVGYDEHFSFAKLREACAHLR-DPE 170
Cdd:PLN02645 110 PKD--KKVYVIGEEGILEELELAGFQYLGGPEDGDKKIelkpgflmehdKDVGAVVVGFDRYINYYKIQYATLCIReNPG 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  171 CLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRC 250
Cdd:PLN02645 188 CLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNG 267

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10092677  251 GMTTVLTLTGVSRLEEaqayLAAGQHDLVPHYYVESIADL 290
Cdd:PLN02645 268 GCKTLLVLSGVTSESM----LLSPENKIQPDFYTSKISDF 303
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 22-128 4.05e-35

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 122.19  E-value: 4.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    22 VLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFgGLRAEQLFSSALCAARLLRQRLP 101
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGF-DIDEDEIITSGTAAADYLKERKF 79

                          90       100
                  ....*....|....*....|....*..
gi 10092677   102 GppdapGAVFVLGGEGLRAELRAAGLR 128
Cdd:pfam13344  80 G-----KKVLVIGSEGLREELEEAGFE 101
 
Name Accession Description Interval E-value
PGP_euk TIGR01452
phosphoglycolate/pyridoxal phosphate phosphatase family; PGP is an essential enzyme in the ...
 18-290 2.00e-168

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: 467.80  E-value: 2.00e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    18 RAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLrAEQLFSSALCAARLLR 97
Cdd:TIGR01452   1 TAQGFIFDCDGVLWLGERVVPGAPELLDRLARAGKQILFVTNNSTKSRAEYALKFARLGFNGL-AEQLFSSALCAARLLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    98 QrlpgPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-----------PRVRAVLVGYDEHFSFAKLREACAHL 166
Cdd:TIGR01452  80 Q----PPDAGKAVYVIGEEGLRAELDAAGIRLAGDPGEKKQDEadgfmydikldERVGAVVVGYDEHFSYVKLMEACAHL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   167 RDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILF 246
Cdd:TIGR01452 156 REPGCLFVATNRDPWHPLSDGSRTPGTGSLVAAIETASGRQPLVVGKPSPYMFNCITEKFSIDPARTLMVGDRLETDILF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 10092677   247 GHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADL 290
Cdd:TIGR01452 236 GHRCGMTTVLVLSGVSQLEEAQEYLMAGQDDLVPDYVVESLADL 279
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 19-294 5.42e-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: 456.85  E-value: 5.42e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  19 AQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQ 98
Cdd:cd07510   1 VDTFLFDCDGVLWNGEKAIPGAPETLNLLRSLGKRLVFVTNNSTKSREAYAKKFARLGFTGLKEEEIFSSAYCAARYLRQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  99 RLPGPPDapGAVFVLGGEGLRAELRAAGLRLAGDPSAGD-----------GAAPRVRAVLVGYDEHFSFAKLREACAHLR 167
Cdd:cd07510  81 RLPGPAD--GKVYVLGGEGLRAELEAAGVAHLGGPDDGLrraapkdwllaGLDPDVGAVLVGLDEHVNYLKLAKATQYLR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 168 DPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFG 247
Cdd:cd07510 159 DPGCLFVATNRDPWHPLSDGSFIPGTGSLVAALETASGRQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDTDILFG 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 10092677 248 HRCGMTTVLTLTGVSRLEEAQAYLaagQHDLVPHYYVESIADLTEGL 294
Cdd:cd07510 239 QNCGLKTLLVLTGVSTLEEALAKL---SNDLVPDYYVESLADLLELL 282
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 21-289 8.63e-118

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: 339.34  E-value: 8.63e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  21 GVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGlRAEQLFSSALCAARLLRQRL 100
Cdd:cd07508   1 LVISDCDGVLWHDERAIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKFGVDV-PEDQIVTSAKATARFLRSRK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 101 PGppdapGAVFVLGGEGLRAELRAAGLRLAGDPS----------AGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPE 170
Cdd:cd07508  80 FG-----KKVYVLGEEGLKEELRAAGFRIAGGPSkgietyaelvEHLEDDENVDAVIVGSDFKLNFAKLRKACRYLRNPG 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 171 CLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRC 250
Cdd:cd07508 155 CLFIATAPDRIHPLKDGGPIPGTGAFAAAVEAATGRQPLVLGKPSPWLGELALEKFGIDPERVLFVGDRLATDVLFGKAC 234

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 10092677 251 GMTTVLTLTGVSRLEEAQAYLaagQHDLVPHYYVESIAD 289
Cdd:cd07508 235 GFQTLLVLTGVTTLEDLQAYI---DHELVPDYYADSLAD 270
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
12-290 1.23e-86

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 259.66  E-value: 1.23e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  12 LRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALC 91
Cdd:COG0647   1 MSELADRYDAFLLDLDGVLYRGDEPIPGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKLRRLGIP-VAEDEIVTSGDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  92 AARLLRQRLPGppdapGAVFVLGGEGLRAELRAAGLRLAGDPSAGdgaaprvrAVLVGYDEHFSFAKLREACAHLRDPeC 171
Cdd:COG0647  80 TAAYLAERHPG-----ARVYVIGEEGLREELEEAGLTLVDDEEPD--------AVVVGLDRTFTYEKLAEALRAIRRG-A 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 172 LLVATDRDPWHPLSDGsRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCG 251
Cdd:COG0647 146 PFIATNPDRTVPTEDG-LIPGAGALAAALEAATGGEPLVVGKPSPPIYELALERLGVDPERVLMVGDRLDTDILGANAAG 224

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 10092677 252 MTTVLTLTGVSRLEEAQAYlaagqhDLVPHYYVESIADL 290
Cdd:COG0647 225 LDTLLVLTGVTTAEDLEAA------PIRPDYVLDSLAEL 257
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 22-290 1.11e-85

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: 258.39  E-value: 1.11e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  22 VLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQRLP 101
Cdd:cd07532   9 VIFDADGVLWTGDKPIPGAVEVFNALLDKGKKVFIVTNNSTKTREELAKKAKKLGFN-VKENNILSSAAVIADYLKEKGF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 102 GppdapGAVFVLGGEGLRAELRAAG---LRLAGDPSAGDGA---------APRVRAVLVGYDEHFSFAKLREACAHLRDP 169
Cdd:cd07532  88 K-----KKVYVIGEEGIRKELEEAGivsCGGDGEDEKDDSMgdfahnlelDPDVGAVVVGRDEHFSYPKLMKACNYLRNP 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 170 ECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHR 249
Cdd:cd07532 163 DVLFLATNMDATFPGPVGRVIPGAGAMVAAIEAVSGRKPLVLGKPNPQILNFLMKSGVIKPERTLMIGDRLKTDILFANN 242

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 10092677 250 CGMTTVLTLTGVSRLEEAQ---AYLAAGQHDLVPHYYVESIADL 290
Cdd:cd07532 243 CGFQSLLVGTGVNSLEDAEkikKEGDPKKKDLVPDTYLPSLGHL 286
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 20-289 7.45e-73

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: 224.01  E-value: 7.45e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  20 QGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQR 99
Cdd:cd07530   1 KGYLIDLDGTVYRGGTAIPGAVEFIERLREKGIPFLFLTNNSTRTPEDVAAKLAEMGID-VPEEDVYTSALATAQYLAEQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 100 LPGppdapGAVFVLGGEGLRAELRAAGLRLAGDpsagdgaapRVRAVLVGYDEHFSFAKLREACAHLRDPeCLLVATDRD 179
Cdd:cd07530  80 LPG-----AKVYVIGEEGLRTALHEAGLTLTDE---------NPDYVVVGLDRDLTYEKLAEATLAIRNG-AKFIATNPD 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 180 PWHPLSDGsRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLT 259
Cdd:cd07530 145 LTLPTERG-LLPGNGSVVAALEAATGVKPLFIGKPEPIMMRAALEKLGLKSEETLMVGDRLDTDIAAGIAAGIDTLLVLT 223

                       250       260       270
                ....*....|....*....|....*....|
gi 10092677 260 GVSRLEEAQAYLAAgqhdlvPHYYVESIAD 289
Cdd:cd07530 224 GVTTREDLAKPPYR------PTYIVPSLRE 247
PLN02645 PLN02645
phosphoglycolate phosphatase
 23-290 3.82e-69

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 216.89  E-value: 3.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   23 LFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQrLPG 102
Cdd:PLN02645  32 IFDCDGVIWKGDKLIEGVPETLDMLRSMGKKLVFVTNNSTKSRAQYGKKFESLGLN-VTEEEIFSSSFAAAAYLKS-INF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  103 PPDapGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-----------PRVRAVLVGYDEHFSFAKLREACAHLR-DPE 170
Cdd:PLN02645 110 PKD--KKVYVIGEEGILEELELAGFQYLGGPEDGDKKIelkpgflmehdKDVGAVVVGFDRYINYYKIQYATLCIReNPG 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  171 CLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRC 250
Cdd:PLN02645 188 CLFIATNRDAVTHLTDAQEWAGAGSMVGAIKGSTEREPLVVGKPSTFMMDYLANKFGIEKSQICMVGDRLDTDILFGQNG 267

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 10092677  251 GMTTVLTLTGVSRLEEaqayLAAGQHDLVPHYYVESIADL 290
Cdd:PLN02645 268 GCKTLLVLSGVTSESM----LLSPENKIQPDFYTSKISDF 303
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 22-260 3.11e-59

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: 189.07  E-value: 3.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    22 VLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLP 101
Cdd:TIGR01460   1 FLFDIDGVLWLGHKPIPGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKLSSLLGVDVSPDQIITSGSVTKDLLRQRFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   102 GPPdapgaVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVR-AVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP 180
Cdd:TIGR01460  81 GEK-----VYVIGVGELRESLEGLGFRNDFFDDIDHLAIEKIPaAVIVGEPSDFSYDELAKAAYLLAEGDVPFIAANRDD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   181 WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPART-LMVGDRLETDILFGHRCGMTTVLTLT 259
Cdd:TIGR01460 156 LVRLGDGRFRPGAGAIAAGIKELSGREPTVVGKPSPAIYRAALNLLQARPERRdVMVGDNLRTDILGAKNAGFDTLLVLT 235


                  .
gi 10092677   260 G 260
Cdd:TIGR01460 236 G 236
HAD_Pase_UmpH-like cd07531
UmpH/NagD family phosphatase, similar to Bacillus AraL phosphatase, a putative sugar ...
 21-291 1.58e-47

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: 159.66  E-value: 1.58e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  21 GVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQrl 100
Cdd:cd07531   2 GYIIDLDGTIGKGVTLIPGAVEGVKTLRRLGKKIIFLSNNSTRSRRILLERLRSFGIEVGEDEILVSSYVTARFLARE-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 101 pgppdAPGA-VFVLGGEGLRAELRAAGLRLAGDPSAgdgaaprVRAVLVGYDEHFSFAKLREAC-AHLRDPEclLVATDR 178
Cdd:cd07531  80 -----KPNAkVFVTGEEGLIEELRLAGLEIVDKYDE-------AEYVVVGSNRKITYELLTKAFrACLRGAR--YIATNP 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 179 DPWHPLSDGSrTPGTGSLAAAVETASGRQA-LVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLT 257
Cdd:cd07531 146 DRIFPAEDGP-IPDTAAIIGAIEWCTGREPeVVVGKPSEVMAREALDILGLDAKDCAIVGDQIDVDIAMGKAIGMETALV 224

                       250       260       270
                ....*....|....*....|....*....|....
gi 10092677 258 LTGVSRLEEAQaylaagQHDLVPHYYVESIADLT 291
Cdd:cd07531 225 LTGVTTRENLD------RHGYKPDYVLNSIKDLV 252
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 23-287 2.32e-41

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: 143.35  E-value: 2.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  23 LFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRaEQLFSSALCAARLLRQRLPG 102
Cdd:cd16422   3 IFDMDGTIYLGDDLIPGTLEFLERLHEKKRRYIFLTNNSSKNLADYVEKLNRLGIDAGL-DRVFTSGEATIDHLKKEFIK 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 103 PpdapgAVFVLGGEGLRAELRAAGLRLAGDpsagdgaapRVRAVLVGYDEHFSFAKLREACAHLRDPeCLLVATDRDPWH 182
Cdd:cd16422  82 P-----KIFLLGTKSLREEFEKAGFTLDGD---------DIDVVVLGFDTELTYEKLRTACLLLRRG-IPYIATHPDINC 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 183 PLSDGSrTPGTGSLAAAVETASGRQA-LVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGV 261
Cdd:cd16422 147 PSEEGP-IPDAGSIIALIETSTGRRPdLVIGKPNPIILDPVLEKFDYSKEETVMVGDRLYTDIVLGINAGVDSILVLSGE 225

                       250       260
                ....*....|....*....|....*.
gi 10092677 262 SRLEEAQaylaagQHDLVPHYYVESI 287
Cdd:cd16422 226 TTREDLE------DLERKPTYVFDNV 245
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 20-260 6.25e-38

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: 134.33  E-value: 6.25e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  20 QGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQR 99
Cdd:cd07509   1 KAVLLDLSGTLYISGAAIPGAAEALKRLRHAGLKVRFLTNTTKESRRTLAERLQRLGFD-VSEEEIFTSLTAARQYLEEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 100 LPGPpdapgavFVLGGEGLRAELRAAglrlagDPSAGDgaaprvrAVLVG-YDEHFSFAKLREACAHLRDpECLLVATDR 178
Cdd:cd07509  80 GLRP-------HLLVDDDALEDFIGI------DTSDPN-------AVVIGdAGEHFNYQTLNRAFRLLLD-GAPLIALHK 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 179 DPWHPLSDGSRTpGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTL 258
Cdd:cd07509 139 GRYYKRKDGLAL-DPGAFVTGLEYATGIKATVVGKPSPEFFLSALRSLGVDPEEAVMIGDDLRDDVGGAQACGMRGILVR 217


                ..
gi 10092677 259 TG 260
Cdd:cd07509 218 TG 219
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 22-128 4.05e-35

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 122.19  E-value: 4.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    22 VLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFgGLRAEQLFSSALCAARLLRQRLP 101
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAEKLRKLGF-DIDEDEIITSGTAAADYLKERKF 79

                          90       100
                  ....*....|....*....|....*..
gi 10092677   102 GppdapGAVFVLGGEGLRAELRAAGLR 128
Cdd:pfam13344  80 G-----KKVLVIGSEGLREELEEAGFE 101
HAD-SF-IIA-hyp2 TIGR01457
HAD-superfamily subfamily IIA hydrolase, TIGR01457; This hypothetical equivalog is a member of ...
 20-289 2.28e-33

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: 122.66  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    20 QGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRaEQLFSSALCAARLLRQR 99
Cdd:TIGR01457   2 KGYLIDLDGTMYNGTEKIEEACEFVRTLKKRGVPYLFVTNNSTRTPEQVADKLVSFDIPATE-EQVFTTSMATAQYIAQQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   100 lpgppDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAgdgaaprvrAVLVGYDEHFSFAKLREACAHLRDpECLLVATDRD 179
Cdd:TIGR01457  81 -----KKDASVYVIGEEGLREAIKENGLTFGGENPD---------YVVVGLDRSITYEKFAVACLAIRN-GARFISTNGD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   180 PWHPLSDGsRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLT 259
Cdd:TIGR01457 146 IAIPTERG-LLPGNGSLTSVLTVSTGVKPVFIGKPESIIMEQAMRVLGTDVEETLMVGDNYATDIMAGINAGIDTLLVHT 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 10092677   260 GVSRLEEAQAYLAAgqhdlvPHYYVESIAD 289
Cdd:TIGR01457 225 GVTKREHMTDDMEK------PTHAIDSLAE 248
HAD-SF-IIA-hyp3 TIGR01458
HAD-superfamily subfamily IIA hydrolase, TIGR01458; This hypothetical equivalog is a member of ...
 20-289 1.89e-25

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: 101.86  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    20 QGVLFDCDGVLWN----GERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARL 95
Cdd:TIGR01458   2 KGVLLDISGVLYIsdagGGTAVPGSQEAVKRLRGASVKVRFVTNTTKESKQDLLERLQRLGFD-ISEDEVFTPAPAARQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    96 LRQRLPGPpdapgavFVLGGEGLRAELRAAGlrlAGDPSAgdgaaprvrAVLVGYDEHFSFAKLREACAHLRD-PECLLV 174
Cdd:TIGR01458  81 LEEKQLRP-------MLLVDDRVLPDFDGID---TSDPNC---------VVMGLAPEHFSYQILNQAFRLLLDgAKPVLI 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   175 ATDRDPWHPLSDGSRTpGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTT 254
Cdd:TIGR01458 142 AIGKGRYYKRKDGLAL-DVGPFVTALEYATDTKATVVGKPSKTFFLEALRATGCEPEEAVMIGDDCRDDVGGAQDCGMRG 220

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 10092677   255 VLTLTGVSRLEEAQaylaagQHDLVPHYYVESIAD 289
Cdd:TIGR01458 221 IQVRTGKYRPSDEE------KINVPPDLTCDSLPH 249
PRK10444 PRK10444
HAD-IIA family hydrolase;
20-266 2.69e-24

HAD-IIA family hydrolase;


Pssm-ID: 182466 [Multi-domain]  Cd Length: 248  Bit Score: 98.33  E-value: 2.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   20 QGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGgLRAEQLFSSALCAARLLRQR 99
Cdd:PRK10444   2 KNVICDIDGVLMHDNVAVPGAAEFLHRILDKGLPLVLLTNYPSQTGQDLANRFATAGVD-VPDSVFYTSAMATADFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  100 lpgppDAPGAvFVLGGEGLRAELRAAGLRLAG-DPSAgdgaaprvraVLVGYDEHFSFAKLREAcAHLRDPECLLVATDR 178
Cdd:PRK10444  81 -----EGKKA-YVIGEGALIHELYKAGFTITDiNPDF----------VIVGETRSYNWDMMHKA-AYFVANGARFIATNP 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  179 DPWHPlsdgSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTL 258
Cdd:PRK10444 144 DTHGR----GFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVL 219


                 ....*...
gi 10092677  259 TGVSRLEE 266
Cdd:PRK10444 220 SGVSTLDD 227
Hydrolase_like pfam13242
HAD-hyrolase-like;
210-290 4.53e-21

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 84.97  E-value: 4.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   210 VVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAgqhdlvPHYYVESIAD 289
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDTDILGAREAGARTILVLTGVTRPADLEKAPIR------PDYVVDDLAE 74


                  .
gi 10092677   290 L 290
Cdd:pfam13242  75 A 75
HAD_like cd07525
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 22-282 4.61e-19

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: 84.30  E-value: 4.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  22 VLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRArPELALRFARLGFGGLRAEQLFSSALCAARLLRQRlp 101
Cdd:cd07525   3 FLLDLWGVLHDGNEPYPGAVEALAALRAAGKTVVLVTNAPRPA-ESVVRQLAKLGVPPSTYDAIITSGEVTRELLARE-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 102 gpPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGaaprvrAVLVGY--DEHFSFAKLREACAHLRDPECLLVATDRD 179
Cdd:cd07525  80 --AGLGRKVYHLGPERDANVLEGLDVVATDDAEKAEF------ILCTGLydDETETPEDYRKLLKAAAARGLPLICANPD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 180 PWHPLSdGSRTPGTGSLAAAVEtASGRQALVVGKPSPYMFECITENFS-IDPARTLMVGDRLETDILFGHRCGMTTVLTL 258
Cdd:cd07525 152 LVVPRG-GKLIYCAGALAELYE-ELGGEVIYFGKPHPPIYDLALARLGrPAKARILAVGDGLHTDILGANAAGLDSLFVT 229

                       250       260
                ....*....|....*....|....
gi 10092677 259 TGVSRLEEAQAYLaagQHDLVPHY 282
Cdd:cd07525 230 GGIHRRLAAEAGI---KSQIVPDF 250
HAD-SF-IIA-hyp4 TIGR01459
HAD-superfamily class IIA hydrolase, TIGR01459; This hypothetical equivalog is a member of the ...
 12-259 5.23e-19

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: 83.79  E-value: 5.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    12 LRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPeLALRFARLGFGGLRAEQLFSSALC 91
Cdd:TIGR01459   1 IFDLINDYDVFLLDLWGVIIDGNHTYPGAVQNLNKIIAQGKPVYFVSNSPRNIFS-LHKTLKSLGINADLPEMIISSGEI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    92 AARLLRQRLPGPPDAPGAVFVLgGEGLRAELRAAGLRLAGDPSAGDGaaprvrAVLVGY---DEHFSFAKLREACAHL-- 166
Cdd:TIGR01459  80 AVQMILESKKRFDIRNGIIYLL-GHLENDIINLMQCYTTDDENKANA------SLITIYrseNEKLDLDEFDELFAPIva 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   167 RDPECLLVATDRDpwhPLSDGSRTPGTGSLAAAVETASGrQALVVGKPSPYMFECITENFSIDPART-LMVGDRLETDIL 245
Cdd:TIGR01459 153 RKIPNICANPDRG---INQHGIYRYGAGYYAELIKQLGG-KVIYSGKPYPAIFHKALKECSNIPKNRmLMVGDSFYTDIL 228

                         250
                  ....*....|....
gi 10092677   246 FGHRCGMTTVLTLT 259
Cdd:TIGR01459 229 GANRLGIDTALVLT 242
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
20-295 1.01e-10

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 60.33  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  20 QGVLFDCDGVLWNGERAVPGApeLLERLARAGKAALFVSNNSRRARPELALRFARLgFGGLRAEQL------FSSALCAA 93
Cdd:COG0546   2 KLVLFDLDGTLVDSAPDIAAA--LNEALAELGLPPLDLEELRALIGLGLRELLRRL-LGEDPDEELeellarFRELYEEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  94 RLLRQRLpgppdAPGAVfvlggEGLrAELRAAGLRLAgdpsagdgaaprvraVLVGYDEHFsfakLREACAHLRdpecll 173
Cdd:COG0546  79 LLDETRL-----FPGVR-----ELL-EALKARGIKLA---------------VVTNKPREF----AERLLEALG------ 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 174 vatdrdpwhplsdgsrtpgtgsLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRlETDILFGHRCGMT 253
Cdd:COG0546 123 ----------------------LDDYFDAIVGGDDVPPAKPKPEPLLEALERLGLDPEEVLMVGDS-PHDIEAARAAGVP 179

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 10092677 254 TVLTLTGVSRLEEAQAYLaagqhdlvPHYYVESIADLTEGLE 295
Cdd:COG0546 180 FIGVTWGYGSAEELEAAG--------ADYVIDSLAELLALLA 213
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 22-251 1.30e-10

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 59.52  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677    22 VLFDCDGVLWNGEravPGAPELLERLAragkaalfvsnnsrrARPELALRFARLGfgglraeqlfssalcaarllrQRLP 101
Cdd:pfam00702   4 VVFDLDGTLTDGE---PVVTEAIAELA---------------SEHPLAKAIVAAA---------------------EDLP 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   102 GPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAA-PRVRAVLVGYDEHFSFAKLREACAHLRDPEC-LLVATDrD 179
Cdd:pfam00702  45 IPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVlVELLGVIALADELKLYPGAAEALKALKERGIkVAILTG-D 123

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10092677   180 PWHPLSDGSRTPGtgsLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCG 251
Cdd:pfam00702 124 NPEAAEALLRLLG---LDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGV-NDIPAAKAAG 191
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 213-294 1.79e-10

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: 58.57  E-value: 1.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 213 KPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCGMTTVLTLTGVSRLEEAQAylaagqhdlVPHYYVESIADLTE 292
Cdd:COG0241 102 KPKPGMLLQAAERLGIDLSNSYMIGDRL-SDLQAAKAAGCKGILVLTGKGAEELAEA---------LPDTVADDLAEAVD 171


                ..
gi 10092677 293 GL 294
Cdd:COG0241 172 YL 173
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 213-256 4.15e-10

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: 56.77  E-value: 4.15e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 10092677 213 KPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCGMTTVL 256
Cdd:cd07503  99 KPKPGMLLDAAKELGIDLARSFVIGDRL-SDIQAARNAGCKGIL 141
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 22-292 4.40e-10

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: 58.50  E-value: 4.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  22 VLFDCDGVLWNGERAV-PGAPELLERLARAGKAALFvsnnSRRARPELALRFARLGFGGLRAEQLFSSAL---------C 91
Cdd:COG1011   4 VLFDLDGTLLDFDPVIaEALRALAERLGLLDEAEEL----AEAYRAIEYALWRRYERGEITFAELLRRLLeelgldlaeE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  92 AARLLRQRLPGPPDA-PGAVFVLggeglrAELRAAGLRLAGdpsAGDGAAPRVRAVL--VGYDEHFsfaklreacahlrd 168
Cdd:COG1011  80 LAEAFLAALPELVEPyPDALELL------EALKARGYRLAL---LTNGSAELQEAKLrrLGLDDLF-------------- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677 169 pECLLVAtdrdpwhplsdgsrtpgtgslaaavetasgrQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGH 248
Cdd:COG1011 137 -DAVVSS-------------------------------EEVGVRKPDPEIFELALERLGVPPEEALFVGDSPETDVAGAR 184

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 10092677 249 RCGMTTVLtltgVSRleeaqaYLAAGQHDLVPHYYVESIADLTE 292
Cdd:COG1011 185 AAGMRTVW----VNR------SGEPAPAEPRPDYVISDLAELLE 218
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 211-255 5.52e-10

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: 55.63  E-value: 5.52e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 10092677 211 VGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTV 255
Cdd:cd04305  62 VQKPNPEIFDYALNQLGVKPEETLMVGDSLESDILGAKNAGIKTV 106
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 213-259 8.50e-09

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: 53.18  E-value: 8.50e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 10092677   213 KPSPYMFECITENFS-IDPARTLMVGDRLETDILFGHRCGMTTVLTLT 259
Cdd:TIGR01662  88 KPKPGMFLEALKRFNeIDPEESVYVGDQDLTDLQAAKRVGLATILVAP 135
YqeG COG2179
Predicted phosphohydrolase YqeG, HAD superfamily [General function prediction only];
212-256 1.31e-08

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


Pssm-ID: 441782  Cd Length: 164  Bit Score: 53.21  E-value: 1.31e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 10092677 212 GKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVL 256
Cdd:COG2179  90 KKPLPRGFRKALKLMGLPPEETAVVGDQLFTDVLGGNRAGLYTIL 134
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
213-290 3.03e-08

D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 52.51  E-value: 3.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10092677  213 KPSPYMFECITENFSIDPARTLMVGDRLEtDILFGHRCGMTTVLTLTGVSRLEEAQaylAAGQHDLVphyyVESIADL 290
Cdd:PRK08942 103 KPKPGMLLSIAERLNIDLAGSPMVGDSLR-DLQAAAAAGVTPVLVRTGKGVTTLAE---GAAPGTWV----LDSLADL 172
HAD_BsYqeG-like cd16416
Uncharacterized family of the the haloacid dehalogenase-like superfamily, similar to the ...
 212-256 1.62e-07

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: 48.80  E-value: 1.62e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 10092677 212 GKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVL 256
Cdd:cd16416  63 GKPRPRAFRRALKEMDLPPEQVAMVGDQLFTDILGGNRAGLYTIL 107
YqeG_hyp_ppase TIGR01668
HAD superfamily (subfamily IIIA) phosphatase, TIGR01668; This family of hypothetical proteins ...
 194-265 8.99e-06

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


Pssm-ID: 273744  Cd Length: 170  Bit Score: 45.09  E-value: 8.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 10092677   194 GSLAAAVETASGRQALVVG-KPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLE 265
Cdd:TIGR01668  71 EQRAKAVEKALGIPVLPHAvKPPGCAFRRAHPEMGLTSEQVAVVGDRLFTDVMGGNRNGSYTILVEPLVHPDQ 143
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
 195-296 2.09e-05

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 44.85  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  195 SLAAAVETASGRqalvvgkPSPYMFECITENFSIDPARTLM-VGDRlETDILFGHRCGMTTV----------LTLTGVSR 263
Cdd:PRK13478 147 HVVTTDDVPAGR-------PYPWMALKNAIELGVYDVAACVkVDDT-VPGIEEGLNAGMWTVgvilsgnelgLSEEEYQA 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 10092677  264 LEEA----------QAYLAAGqhdlvPHYYVESIADLTEGLED 296
Cdd:PRK13478 219 LSAAelaarrerarARLRAAG-----AHYVIDTIADLPAVIAD 256
HAD_5NT cd02604
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p ...
 211-259 9.95e-05

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to Saccharomyces cerevisiae Phm8p and Sdt1p; This family includes Saccharomyces cerevisiae Phm8p (phosphate metabolism protein 8) and Sdt1p (Suppressor of disruption of TFIIS). Phm8p participates in the ribose salvage pathway, it catalyzes the dephosphorylation of nucleotide monophosphates to nucleosides, its preferred substrates are nucleotide monophosphates AMP, GMP, CMP, and UMP. Phm8p is also a lysophosphatidic acid phosphatase, dephosphorylating lysophosphatidic acids (LPAs) to monoacylglycerol in response to phosphate starvation. Sdt1p is a pyrimidine and pyridine-specific 5'-nucleotidase; it is an NMN/NaMN 5'-nucleotidases involved in the production of nicotinamide riboside and nicotinic acid riboside, and is a pyrimidine 5'-nucleotidase with high specificity for UMP and 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: 319791 [Multi-domain]  Cd Length: 182  Bit Score: 42.24  E-value: 9.95e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 10092677 211 VGKPSPYMFECITENFSIDPARTLMVGDrLETDILFGHRCGMTTVLTLT 259
Cdd:cd02604 135 DPKPHPAAFEKAIREAGLDPKRAAFFDD-SIRNLLAAKALGMKTVLVGP 182
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 213-256 2.44e-04

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


Pssm-ID: 319825 [Multi-domain]  Cd Length: 173  Bit Score: 40.82  E-value: 2.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 10092677 213 KPSPYMFECITENFSIDPARTLMVGDRlETDILFGHRCGMTTVL 256
Cdd:cd07523 130 KPNPEAINYLLNKYQLNPEETVMIGDR-ELDIEAGHNAGISTIL 172
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 228-294 4.17e-04

haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 40.65  E-value: 4.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 10092677 228 IDPARTLMVGDRlETDILFGHRCGMTTVLTLTGVSRLEEAQaylAAGqhdlvPHYYVESIADLTEGL 294
Cdd:cd04302 152 IAPEQAVMIGDR-KHDIIGARANGIDSIGVLYGYGSEDELE---EAG-----ATYIVETPAELLELL 209
PRK09449 PRK09449
dUMP phosphatase; Provisional
 211-290 4.95e-04

dUMP phosphatase; Provisional


Pssm-ID: 181865 [Multi-domain]  Cd Length: 224  Bit Score: 40.65  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  211 VGKPSPYMFE-CITENFSIDPARTLMVGDRLETDILFGHRCGMTTV-LTLTGVSRleeaqaylaagQHDLVPHYYVESIA 288
Cdd:PRK09449 148 VAKPDVAIFDyALEQMGNPDRSRVLMVGDNLHSDILGGINAGIDTCwLNAHGREQ-----------PEGIAPTYQVSSLS 216


                 ..
gi 10092677  289 DL 290
Cdd:PRK09449 217 EL 218
PRK06769 PRK06769
HAD-IIIA family hydrolase;
213-292 6.79e-04

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 39.71  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677  213 KPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCGMTTVLTLTGV--SRLEEAQAYLAagqhDLVPHYYVESIADL 290
Cdd:PRK06769  93 KPSTGMLLQAAEKHGLDLTQCAVIGDRW-TDIVAAAKVNATTILVRTGAgyDALHTYRDKWA----HIEPNYIAENFEDA 167


                 ..
gi 10092677  291 TE 292
Cdd:PRK06769 168 VN 169
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 213-290 9.23e-04

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: 39.57  E-value: 9.23e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10092677 213 KPSPYMFECITENFSIDPARTLMVGDRlETDILFGHRCGMTTVLTLTGVSRLEEAQAYlaagqhdlVPHYYVESIADL 290
Cdd:cd02616 136 KPDPEPVLKALELLGAEPEEALMVGDS-PHDILAGKNAGVKTVGVTWGYKGREYLKAF--------NPDFIIDKMSDL 204
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 213-290 1.07e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 39.63  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10092677  213 KPSPYMFECITENFSIDPARTLMVGDRLEtDILFGHRCGMTTVltltGVSRLEEAQAYLAagQHDlvPHYYVESIADL 290
Cdd:PRK13288 138 KPDPEPVLKALELLGAKPEEALMVGDNHH-DILAGKNAGTKTA----GVAWTIKGREYLE--QYK--PDFMLDKMSDL 206
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 21-94 1.81e-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: 37.38  E-value: 1.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10092677  21 GVLFDCDGVLWngeravpgAPELLERLARAGKAALFVSNNSRRArpelALRFARLGFGGLRAEQLFSSALCAAR 94
Cdd:cd01427   1 AVLFDLDGTLL--------AVELLKRLRAAGIKLAIVTNRSREA----LRALLEKLGLGDLFDGIIGSDGGGTP 62
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 210-256 1.92e-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: 36.99  E-value: 1.92e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 10092677 210 VVGKPSPYMFECITENFSIDPARTLMVGDRlETDILFGHRCGMTTVL 256
Cdd:cd01427  60 GTPKPKPKPLLLLLLKLGVDPEEVLFVGDS-ENDIEAARAAGGRTVA 105
PGP_phosphatase pfam09419
Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial ...
 185-262 2.10e-03

Mitochondrial PGP phosphatase; This is a family of proteins that acts as a mitochondrial phosphatase in cardiolipin biosynthesis. Cardiolipin is a unique dimeric phosphoglycerolipid predominantly present in mitochondrial membranes. The inverted phosphatase motif includes the highly conserved DKD triad.


Pssm-ID: 430598  Cd Length: 168  Bit Score: 38.08  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10092677   185 SDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPART-----LMVGDRLETDILFGHRCGMTTVLTLT 259
Cdd:pfam09419  86 SAGSNDDKDGEQAKALEKSTGIPVLRHPVKKPGCGEEVLEYFKERGVVTrpseiAVVGDRLFTDILMANMMGSWGVWLTD 165


                  ...
gi 10092677   260 GVS 262
Cdd:pfam09419 166 GVG 168
CECR5 TIGR01456
HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; This hypothetical equivalog is a member ...
 21-67 2.97e-03

HAD-superfamily class IIA hydrolase, TIGR01456, CECR5; 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 eukaryotes. One sequence (GP|13344995) is called "Cat Eye Syndrome critical region protein 5" (CECR5). This gene has been cloned from a pericentromere region of human chromosome 22 believed to be the location of the gene or genes responsible for Cat Eye Syndrome. This is one of a number of candidate genes. The Schizosaccharomyces pombe sequence (EGAD|138276) is annotated as "phosphatidyl synthase," however this is due entirely to a C-terminal region of the protein (outside the region of similarity of this model) which is highly homologous to a family of CDP-alcohol phosphatidyltransferases. (Thus, the annotation of GP|4226073 from C. elegans as similar to phosphatidyl synthase, is a mistake as this gene does not contain the C-terminal portion). The physical connection of the phosphatidyl synthase and the HAD-superfamily hydrolase domain in S. pombe may, however, be an important clue to the substrate for the hydrolases in this equivalog.


Pssm-ID: 200106 [Multi-domain]  Cd Length: 321  Bit Score: 38.70  E-value: 2.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 10092677    21 GVLFDCDGVLWNGERAVPGAPELLERLARAGKAA----LFVSNN---SRRARPE 67
Cdd:TIGR01456   2 GFAFDIDGVLFRGKKPIAGASDALRRLNRNQGQLkipyIFLTNGggfSERARAE 55
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 213-260 3.32e-03

histidinol-phosphate phosphatase family domain; This domain is found in authentic histidinol-phosphate phosphatases which are sometimes found as stand-alone entities and sometimes as fusions with imidazoleglycerol-phosphate dehydratase (TIGR01261). Additionally, a family of proteins including YaeD from E. coli (TIGR00213) and various other proteins are closely related but may not have the same substrate specificity. This domain is a member of the haloacid-dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. This superfamily is distinguished by the presence of three motifs: an N-terminal motif containing the nucleophilic aspartate, a central motif containing an conserved serine or threonine, and a C-terminal motif containing a conserved lysine (or arginine) and conserved aspartates. More specifically, the domian modelled here is a member of subfamily III of the HAD-superfamily by virtue of lacking a "capping" domain in either of the two common positions, between motifs 1 and 2, or between motifs 2 and 3.


Pssm-ID: 273737  Cd Length: 147  Bit Score: 37.38  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 10092677   213 KPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCGMTTVLTLTG 260
Cdd:TIGR01656 101 KPKPGLILEALKRLGVDASRSLVVGDRL-RDLQAARNAGAAAGLLVSG 147
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
213-255 9.92e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 36.41  E-value: 9.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 10092677   213 KPSPYMFECITENFSIDPARTLMVGDRLeTDILFGHRCGMTTV 255
Cdd:pfam13419 135 KPDPDPILKALEQLGLKPEEVIYVGDSP-RDIEAAKNAGIKVI 176
 
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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