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Conserved domains on  [gi|1288460206|ref|WP_100546183|]
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HAD-IIIA family hydrolase [Lysinibacillus xylanilyticus]

Protein Classification

D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase( domain architecture ID 11415520)

D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase removes the C-7 phosphate from D-glycero-D-manno-heptose-1,7-bisphosphate, which is the third essential step of lipopolysaccharide heptose biosynthesis; belongs to the haloacid dehalogenase (HAD) superfamily of hydrolases that use a nucleophilic aspartate in the phosphoryl transfer reaction

CATH:  3.30.1240.10
EC:  3.1.3.83
Gene Ontology:  GO:0034200|GO:0046872
PubMed:  16889794|15337123|33940035|37786806

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-172 2.10e-76

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: 225.75  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINEvltdRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:COG0241     2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFLG-------AKDP 153
Cdd:COG0241    78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLtgkgaeeLAEA 157

                         170
                  ....*....|....*....
gi 1288460206 154 LADAIFPDLISAADWIIKD 172
Cdd:COG0241   158 LPDTVADDLAEAVDYLLAE 176
 
Name Accession Description Interval E-value
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-172 2.10e-76

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: 225.75  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINEvltdRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:COG0241     2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFLG-------AKDP 153
Cdd:COG0241    78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLtgkgaeeLAEA 157

                         170
                  ....*....|....*....
gi 1288460206 154 LADAIFPDLISAADWIIKD 172
Cdd:COG0241   158 LPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 3-148 6.59e-66

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: 198.14  E-value: 6.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVINEVltdrVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELKK 82
Cdd:cd07503     1 KALFLDRDGVINVD----VPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLAS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288460206  83 EGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL 148
Cdd:cd07503    77 QGVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-174 1.94e-49

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 157.67  E-value: 1.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINevlTDRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:PRK08942    2 SMKAIFLDRDGVIN---VDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGT--------KGV-FLGAK 151
Cdd:PRK08942   79 ADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVtpvlvrtgKGVtTLAEG 158

                         170       180
                  ....*....|....*....|...
gi 1288460206 152 DPLADAIFPDLISAADWIIKDAT 174
Cdd:PRK08942  159 AAPGTWVLDSLADLPQALKKQQK 181
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 3-148 1.83e-42

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: 138.69  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVINEvltDRVK-FVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELK 81
Cdd:TIGR01656   1 PALFLDRDGVINE---DTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288460206  82 KEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL 148
Cdd:TIGR01656  78 QLGVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLL 144
Hydrolase_like pfam13242
HAD-hyrolase-like;
103-165 4.01e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 53.39  E-value: 4.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288460206 103 CRKPNSKLIVDLGEKYNIDLANSYMVGDT-DTDIIAGKRAGTKGVF----------LGAKDPLADAIFPDLISA 165
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREAGARTILvltgvtrpadLEKAPIRPDYVVDDLAEA 75
 
Name Accession Description Interval E-value
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-172 2.10e-76

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: 225.75  E-value: 2.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINEvltdRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:COG0241     2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFLG-------AKDP 153
Cdd:COG0241    78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLtgkgaeeLAEA 157

                         170
                  ....*....|....*....
gi 1288460206 154 LADAIFPDLISAADWIIKD 172
Cdd:COG0241   158 LPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 3-148 6.59e-66

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: 198.14  E-value: 6.59e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVINEVltdrVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELKK 82
Cdd:cd07503     1 KALFLDRDGVINVD----VPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLAS 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1288460206  83 EGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL 148
Cdd:cd07503    77 QGVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-174 1.94e-49

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 157.67  E-value: 1.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINevlTDRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:PRK08942    2 SMKAIFLDRDGVIN---VDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGT--------KGV-FLGAK 151
Cdd:PRK08942   79 ADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVtpvlvrtgKGVtTLAEG 158

                         170       180
                  ....*....|....*....|...
gi 1288460206 152 DPLADAIFPDLISAADWIIKDAT 174
Cdd:PRK08942  159 AAPGTWVLDSLADLPQALKKQQK 181
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 3-148 1.83e-42

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: 138.69  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVINEvltDRVK-FVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELK 81
Cdd:TIGR01656   1 PALFLDRDGVINE---DTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLR 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288460206  82 KEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL 148
Cdd:TIGR01656  78 QLGVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLL 144
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
1-165 6.95e-30

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 111.81  E-value: 6.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDG-VINEVLTDrvKFVNKPKDFYFLPHVPKAIKKLNKyFDYIFV-VTNQGGVGLGFMKETQLQKIHEHMVK 78
Cdd:PRK05446    1 MQKILFIDRDGtLIEEPPTD--FQVDSLDKLAFEPGVIPALLKLQK-AGYKLVmVTNQDGLGTDSFPQEDFDPPHNLMMQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  79 ELKKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFLGAKDPLADAI 158
Cdd:PRK05446   78 IFESQGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRYARETLNWDAI 157


                  ....*..
gi 1288460206 159 FPDLISA 165
Cdd:PRK05446  158 AEQLTKR 164
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 3-172 1.89e-29

D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD resembles the histidinol phosphatase domain of the bifunctional protein HisB. The member from E. coli has been characterized as D,D-heptose 1,7-bisphosphate phosphatase, GmhB, involved in inner core LPS assembly (). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129317 [Multi-domain]  Cd Length: 176  Bit Score: 106.55  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVINevlTDRvKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELKK 82
Cdd:TIGR00213   2 KAIFLDRDGTIN---IDH-GYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  83 EGATIHEVVYCPHKP------KSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFLGAKDPLad 156
Cdd:TIGR00213  78 RDVDLDGIYYCPHHPegveefRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTNVLVRTGKP-- 155

                         170
                  ....*....|....*.
gi 1288460206 157 aIFPDLISAADWIIKD 172
Cdd:TIGR00213 156 -ITPEAENIADWVLNS 170
PRK06769 PRK06769
HAD-IIIA family hydrolase;
1-171 8.48e-27

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 99.42  E-value: 8.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   1 MKKAVFLDRDGVINEvlTDRVKFvnkPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLqkihehmVKEL 80
Cdd:PRK06769    3 NIQAIFIDRDGTIGG--DTTIHY---PGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADGIATIADF-------VQEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  81 KKEGatIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL--GA-------- 150
Cdd:PRK06769   71 KGFG--FDDIYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVrtGAgydalhty 148

                         170       180
                  ....*....|....*....|....*.
gi 1288460206 151 KDPLADaIFPDLIS-----AADWIIK 171
Cdd:PRK06769  149 RDKWAH-IEPNYIAenfedAVNWILN 173
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 3-146 2.41e-25

histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the scope of this model are bifunctional proteins with a histidinol phosphatase domain followed by an imidazoleglycerol-phosphate dehydratase domain. These enzymatic domains catalyze the ninth and seventh steps, respectively, of histidine biosynthesis. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 130328 [Multi-domain]  Cd Length: 161  Bit Score: 95.55  E-value: 2.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDG-VINEVLTD-RVKFVNKPKdfyFLPHVPKAIKKLNKyFDYIFV-VTNQGGVGLGFMKETQLQKIHEHMVKE 79
Cdd:TIGR01261   2 KILFIDRDGtLIEEPPSDfQVDALEKLR---FEKGVIPALLKLKK-AGYKFVmVTNQDGLGTPSFPQADFDGPHNLMLQI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288460206  80 LKKEGATIHEVVYCPHKPKSGCACRKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGV 146
Cdd:TIGR01261  78 FRSQGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGIRGI 144
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 3-148 1.90e-24

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: 92.47  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   3 KAVFLDRDGVinevLTDRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKEtqlqKIHEHMVKELKK 82
Cdd:TIGR01662   1 KAVVLDLDGT----LTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSR----SFSGRVARRLEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1288460206  83 EGATIHEVVYCPHkpksgcaCRKPNSKLIVDLGEKYN-IDLANSYMVGDTD-TDIIAGKRAGTKGVFL 148
Cdd:TIGR01662  73 LGVPIDILYACPG-------CRKPKPGMFLEALKRFNeIDPEESVYVGDQDlTDLQAAKRVGLATILV 133
Hydrolase_like pfam13242
HAD-hyrolase-like;
103-165 4.01e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 53.39  E-value: 4.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1288460206 103 CRKPNSKLIVDLGEKYNIDLANSYMVGDT-DTDIIAGKRAGTKGVF----------LGAKDPLADAIFPDLISA 165
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREAGARTILvltgvtrpadLEKAPIRPDYVVDDLAEA 75
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
32-169 7.45e-10

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 55.71  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  32 FLPHVPKAIKKLNKYFDYIFVVTNqggvglgfmketqlqKIHEHMVKELKKEGATIH-EVVYCPhkpkSGCACRKPNSKL 110
Cdd:COG0546    85 LFPGVRELLEALKARGIKLAVVTN---------------KPREFAERLLEALGLDDYfDAIVGG----DDVPPAKPKPEP 145

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1288460206 111 IVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGVFL----GAKDPL----ADAIFPDLISAADWI 169
Cdd:COG0546   146 LLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgyGSAEELeaagADYVIDSLAELLALL 212
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 36-146 8.46e-07

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 45.46  E-value: 8.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  36 VPKAIKKLNKYFDYIFVVTNqggvglgfmketqlqKIHEHMVKELKKEGATIH-EVVYCPHkpksGCACRKPNSKLIVDL 114
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTN---------------RSREALRALLEKLGLGDLfDGIIGSD----GGGTPKPKPKPLLLL 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1288460206 115 GEKYNIDLANSYMVGDTDTDIIAGKRAGTKGV 146
Cdd:cd01427    73 LLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 104-146 3.27e-06

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: 45.06  E-value: 3.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1288460206 104 RKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTKGV 146
Cdd:cd07523   129 RKPNPEAINYLLNKYQLNPEETVMIGDRELDIEAGHNAGISTI 171
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
15-144 2.59e-05

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 42.57  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  15 EVLTDRVKFVNKPKDFYFLPHVPKAIKKLNKYFDYIFVVTNqggvglgfmketqlqKIHEHMVKELKKEGATIH-EVVYC 93
Cdd:pfam13419  63 EFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTS---------------KSRENVEEFLKQLGLEDYfDVIVG 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1288460206  94 ----PHKpksgcacrKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTK 144
Cdd:pfam13419 128 gddvEGK--------KPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIK 174
PNK-3'Pase TIGR01663
polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5 ...
 8-159 5.24e-05

polynucleotide 5'-kinase 3'-phosphatase; This model represents the metazoan 5'-polynucleotide-kinase-3'-phosphatase, PNKP, which is believed to be involved in repair of oxidative DNA damage. Removal of 3' phosphates is essential for the further processing of the break by DNA polymerases. The central phosphatase domain is a member of the IIIA subfamily (TIGR01662) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. As is common in this superfamily, the enzyme is magnesium dependent. A difference between this enzyme and other HAD-superfamily phosphatases is in the third conserved catalytic motif which usually contains two conserved aspartate residues believed to be involved in binding the magnesium ion. Here, the second aspartate is replaced by a conserved arginine residue which may indicate an interaction with the phosphate backbone of the substrate. Very close relatives of this domain are also found separate from the N- and C-terminal domains seen here, as in the 3'-phosphatase found in plants. The larger family of these domains is described by TIGR01664. Outside of the phosphatase domain is a P-loop ATP-binding motif associated with the kinase activity. The entry for the mouse homolog appears to be missing a large piece of sequence corresponding to the first conserved catalytic motif of the phosphatase domain as well as the conserved threonine of the second motif. Either this is a sequencing artifact or this may represent a pseudo- or non-functional gene. Note that the EC number for the kinase function is: 2.7.1.78


Pssm-ID: 130724 [Multi-domain]  Cd Length: 526  Bit Score: 42.70  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   8 DRDGVINEVLTDRVkFVNKPKDFYFL-PHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKELK---KE 83
Cdd:TIGR01663 174 DLDGTIIKTKSGKV-FPKGPDDWQIIfPEIPEKLKELEADGFKICIFTNQGGIARGKINADDFKAKIEAIVAKLGvpfQV 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  84 GATIHEVVYcphkpksgcacRKPNSKLIVDLGEKYN----IDLANSYMVGDTdtdiiAGKRAGTKGVFLGAKD-PLADAI 158
Cdd:TIGR01663 253 FIAIGAGFY-----------RKPLTGMWDHLKEEANdgteIQEDDCFFVGDA-----AGRPANGKAAGKKKKDfSCADRL 316


                  .
gi 1288460206 159 F 159
Cdd:TIGR01663 317 F 317
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 22-145 6.18e-04

Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the repair of single breaks in DNA induced by DNA-damaging agents such as gamma radiation and camptothecin.


Pssm-ID: 370030  Cd Length: 161  Bit Score: 38.39  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  22 KFVNKPKDFYFL-PHVPKAIKKLNKYfDYIFVV-TNQGGVGLGFMK--ETQLQKIhEHMVKELKkegatIHEVVYCPHKP 97
Cdd:pfam08645  19 VFPRNPDDWKWLyPSVPEKLKKLHED-GYKIVIfTNQGGIGRKGKKslEKFKNKI-EAILKKLG-----VPLQVYAATKK 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1288460206  98 KsgcACRKPNSKLIVDLGEKYN----IDLANSYMVGDTdtdiiAGKRAGTKG 145
Cdd:pfam08645  92 D---IYRKPNTGMWDEMKKDYNdgveIDLEKSFYVGDA-----AGRPYDTRR 135
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 104-142 3.14e-03

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


Pssm-ID: 319854 [Multi-domain]  Cd Length: 212  Bit Score: 36.83  E-value: 3.14e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1288460206 104 RKPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAG 142
Cdd:cd16417   142 KKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAG 180
HAD_Neu5Ac-Pase_like cd04305
human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase ...
 33-148 3.85e-03

human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases; N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319800 [Multi-domain]  Cd Length: 109  Bit Score: 35.21  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206  33 LPHVPKAIKKLNKYFDyIFVVTNqggvglGFmKETQLQKIHEHMVKELKKEGATIHEVVYcphkpksgcacRKPNSKlIV 112
Cdd:cd04305    11 LPGAKELLEELKKGYK-LGIITN------GP-TEVQWEKLEQLGIHKYFDHIVISEEVGV-----------QKPNPE-IF 70

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1288460206 113 DLG-EKYNIDLANSYMVGDT-DTDIIAGKRAGTKGVFL 148
Cdd:cd04305    71 DYAlNQLGVKPEETLMVGDSlESDILGAKNAGIKTVWF 108
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 2-130 4.14e-03

polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional enzyme polynucleotide 5'-kinase/3'-phosphatase; Polynucleotide 3'-phosphatase (PNP) domain. This domain dephosphorylates single-stranded as well as double-stranded 3'-phospho termini. It is found in bifunctional enzyme polynucleotide kinase/phosphatase (PNKP) which contain both kinase and phosphatase domains. PNKP plays a key role in both base excision repair and non-homologous end-joining DNA repair pathway. DNA strand breaks can result from DNA damage by ionizing radiation and chemical agents, such as alkylating agents or anticancer agents. Such DNA damage often results in DNA strands with 5'-hydroxyl and 3'-phosphate termini. However, the repair of DNA damage by DNA polymerases and ligases requires 5'-phosphate and 3'-hydroxyl termini. PNKP acts as a 5'-kinase/3'-phosphatase to create 5'-phosphate/3'-hydroxyl termini, which are a necessary prerequisite for ligation during repair. 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: 319766  Cd Length: 154  Bit Score: 36.17  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1288460206   2 KKAVFlDRDGVINEVLTDRVkFVNKPKDFYFL-PHVPKAIKKLNKYFDYIFVVTNQGGVGLGFMKETQLQKIHEHMVKEL 80
Cdd:cd01625     1 KVAAF-DLDGTLIKTKSGKV-FPTNASDWQILyPSVPEKLKALHKDGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILEKL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1288460206  81 KkegatIHEVVYCPHKPKsgcACRKPNS----KLIVDLGEKYNIDLANSYMVGD 130
Cdd:cd01625    79 G-----VPIQVYAATKKG---KYRKPVTgmwdHLKEDLNSGIPINLKDSFYVGD 124
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 105-142 4.26e-03

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 36.41  E-value: 4.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1288460206 105 KPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAG 142
Cdd:pfam00702 154 KPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK13288 PRK13288
pyrophosphatase PpaX; Provisional
 105-153 4.95e-03

pyrophosphatase PpaX; Provisional


Pssm-ID: 237336 [Multi-domain]  Cd Length: 214  Bit Score: 36.16  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1288460206 105 KPNSKLIVDLGEKYNIDLANSYMVGDTDTDIIAGKRAGTK--GVFLGAKDP 153
Cdd:PRK13288  138 KPDPEPVLKALELLGAKPEEALMVGDNHHDILAGKNAGTKtaGVAWTIKGR 188
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 103-146 5.81e-03

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: 36.21  E-value: 5.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1288460206 103 CRKPNSKLIVDLGEKYNIDLANSYMVGDT-DTDIIAGKRAGTKGV 146
Cdd:cd07510   202 VGKPSRFMFDCISSKFSIDPARTCMVGDRlDTDILFGQNCGLKTL 246
 
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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