NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|515950470|ref|WP_017381053|]
View 

HAD-IIIA family hydrolase [Paenisporosarcina sp. TG-14]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-172 5.07e-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: 224.98  E-value: 5.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINEvlteRVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISEL 80
Cdd:COG0241    2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFLGK-------SDP 153
Cdd:COG0241   78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTgkgaeelAEA 157

                        170
                 ....*....|....*....
gi 515950470 154 LADAVFPDLLSAVDWIIED 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 5.07e-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: 224.98  E-value: 5.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINEvlteRVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISEL 80
Cdd:COG0241    2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFLGK-------SDP 153
Cdd:COG0241   78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTgkgaeelAEA 157

                        170
                 ....*....|....*....
gi 515950470 154 LADAVFPDLLSAVDWIIED 172
Cdd:COG0241  158 LPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 3-148 1.40e-64

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: 194.67  E-value: 1.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   3 KALFLDRDGVINEVlterVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISELKK 82
Cdd:cd07503    1 KALFLDRDGVINVD----VPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLAS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515950470  83 EGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL 148
Cdd:cd07503   77 QGVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-170 3.15e-45

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 146.89  E-value: 3.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINevlTERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISEL 80
Cdd:PRK08942   2 SMKAIFLDRDGVIN---VDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGT--------KGV-FLGKS 151
Cdd:PRK08942  79 ADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVtpvlvrtgKGVtTLAEG 158

                        170
                 ....*....|....*....
gi 515950470 152 DPLADAVFPDLLSAVDWII 170
Cdd:PRK08942 159 AAPGTWVLDSLADLPQALK 177
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 3-148 8.76e-39

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: 129.44  E-value: 8.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470    3 KALFLDRDGVINEVltERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISELKK 82
Cdd:TIGR01656   1 PALFLDRDGVINED--TVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515950470   83 EGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL 148
Cdd:TIGR01656  79 LGVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLL 144
Hydrolase_like pfam13242
HAD-hyrolase-like;
103-165 7.71e-09

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 49.92  E-value: 7.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515950470  103 CRKPNSKLITDLSKKYDIDLFQSYMVGDT-DTDIIAGKKAGTKGVFL--GKSDP--------LADAVFPDLLSA 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 5.07e-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: 224.98  E-value: 5.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINEvlteRVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISEL 80
Cdd:COG0241    2 MKKAVFLDRDGTINE----DVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFLGK-------SDP 153
Cdd:COG0241   78 AAEGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTgkgaeelAEA 157

                        170
                 ....*....|....*....
gi 515950470 154 LADAVFPDLLSAVDWIIED 172
Cdd:COG0241  158 LPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 3-148 1.40e-64

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: 194.67  E-value: 1.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   3 KALFLDRDGVINEVlterVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISELKK 82
Cdd:cd07503    1 KALFLDRDGVINVD----VPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLAS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515950470  83 EGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL 148
Cdd:cd07503   77 QGVEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-170 3.15e-45

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 146.89  E-value: 3.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINevlTERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISEL 80
Cdd:PRK08942   2 SMKAIFLDRDGVIN---VDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGT--------KGV-FLGKS 151
Cdd:PRK08942  79 ADRGGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVtpvlvrtgKGVtTLAEG 158

                        170
                 ....*....|....*....
gi 515950470 152 DPLADAVFPDLLSAVDWII 170
Cdd:PRK08942 159 AAPGTWVLDSLADLPQALK 177
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 3-148 8.76e-39

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: 129.44  E-value: 8.76e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470    3 KALFLDRDGVINEVltERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISELKK 82
Cdd:TIGR01656   1 PALFLDRDGVINED--TVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQ 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515950470   83 EGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL 148
Cdd:TIGR01656  79 LGVAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLL 144
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
1-148 1.03e-29

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 111.42  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDG-VINEVLTErvKFVNKPHELYFLPGVPEAIKKLNPFfDFIFV-VTNQGGVGLGFMKETELNKIHDHMIS 78
Cdd:PRK05446   1 MQKILFIDRDGtLIEEPPTD--FQVDSLDKLAFEPGVIPALLKLQKA-GYKLVmVTNQDGLGTDSFPQEDFDPPHNLMMQ 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  79 ELKKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL 148
Cdd:PRK05446  78 IFESQGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIRY 147
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 3-172 1.91e-26

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: 98.84  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470    3 KALFLDRDGVINEvlteRVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELNKIHDHMISELKK 82
Cdd:TIGR00213   2 KAIFLDRDGTINI----DHGYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   83 EGAIIHDVAYCPHKP------KSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFLGKSDPLad 156
Cdd:TIGR00213  78 RDVDLDGIYYCPHHPegveefRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTNVLVRTGKP-- 155

                         170
                  ....*....|....*.
gi 515950470  157 aVFPDLLSAVDWIIED 172
Cdd:TIGR00213 156 -ITPEAENIADWVLNS 170
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 3-146 3.19e-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: 95.16  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470    3 KALFLDRDG-VINEVLTE-RVKFVNKpheLYFLPGVPEAIKKLNPFfDFIFV-VTNQGGVGLGFMKETELNKIHDHMISE 79
Cdd:TIGR01261   2 KILFIDRDGtLIEEPPSDfQVDALEK---LRFEKGVIPALLKLKKA-GYKFVmVTNQDGLGTPSFPQADFDGPHNLMLQI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515950470   80 LKKEGAIIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGV 146
Cdd:TIGR01261  78 FRSQGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGIRGI 144
PRK06769 PRK06769
HAD-IIIA family hydrolase;
1-171 1.12e-23

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 91.33  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   1 MKKALFLDRDGVINEvlTERVKFvnkPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKETELnkihdhmISEL 80
Cdd:PRK06769   3 NIQAIFIDRDGTIGG--DTTIHY---PGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADGIATIADF-------VQEL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  81 KKEGaiIHDVAYCPHKPKSGCACRKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL----GKS----- 151
Cdd:PRK06769  71 KGFG--FDDIYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVrtgaGYDalhty 148

                        170       180
                 ....*....|....*....|....*
gi 515950470 152 -DPLADA----VFPDLLSAVDWIIE 171
Cdd:PRK06769 149 rDKWAHIepnyIAENFEDAVNWILN 173
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 3-148 6.10e-20

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: 80.91  E-value: 6.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470    3 KALFLDRDGVinevLTERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNQGGVGLGFMKEtelnKIHDHMISELKK 82
Cdd:TIGR01662   1 KAVVLDLDGT----LTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSR----SFSGRVARRLEE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515950470   83 EGAIIHDVAYCPHkpksgcaCRKPNSKLITDLSKKY-DIDLFQSYMVGDTD-TDIIAGKKAGTKGVFL 148
Cdd:TIGR01662  73 LGVPIDILYACPG-------CRKPKPGMFLEALKRFnEIDPEESVYVGDQDlTDLQAAKRVGLATILV 133
Hydrolase_like pfam13242
HAD-hyrolase-like;
103-165 7.71e-09

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 49.92  E-value: 7.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515950470  103 CRKPNSKLITDLSKKYDIDLFQSYMVGDT-DTDIIAGKKAGTKGVFL--GKSDP--------LADAVFPDLLSA 165
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRlDTDILGAREAGARTILVltGVTRPadlekapiRPDYVVDDLAEA 75
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
28-169 4.03e-08

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 50.70  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  28 HELYFLPGVPEAIKKLNpffdfifvvtnQGGVGLGFMkeTelNKIHDHMISELKKEGAIIH-DVAYCPhkpkSGCACRKP 106
Cdd:COG0546   81 DETRLFPGVRELLEALK-----------ARGIKLAVV--T--NKPREFAERLLEALGLDDYfDAIVGG----DDVPPAKP 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515950470 107 NSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGVFL----GKSDPL----ADAVFPDLLSAVDWI 169
Cdd:COG0546  142 KPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVtwgyGSAEELeaagADYVIDSLAELLALL 212
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
15-144 6.76e-06

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 44.11  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   15 EVLTERVKFVNKPHELYFLPGVPEAIKKLNPFFDFIFVVTNqgGVGLGFMKETELNKIHDHMiselkkegaiihDVAYC- 93
Cdd:pfam13419  63 EFYLRKYNEELHDKLVKPYPGIKELLEELKEQGYKLGIVTS--KSRENVEEFLKQLGLEDYF------------DVIVGg 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515950470   94 ---PHKpksgcacrKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTK 144
Cdd:pfam13419 129 ddvEGK--------KPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIK 174
HAD_YsbA-like cd07523
uncharacterized family of the haloacid dehalogenase-like superfamily, similar to the ...
 104-146 1.37e-05

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: 43.13  E-value: 1.37e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515950470 104 RKPNSKLITDLSKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGV 146
Cdd:cd07523  129 RKPNPEAINYLLNKYQLNPEETVMIGDRELDIEAGHNAGISTI 171
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 36-146 5.71e-05

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: 40.46  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470  36 VPEAIKKLNPFFDFIFVVTNqggvglgfmketelnKIHDHMISELKKEGAIIH-DVAYCPHkpksGCACRKPNSKLITDL 114
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTN---------------RSREALRALLEKLGLGDLfDGIIGSD----GGGTPKPKPKPLLLL 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515950470 115 SKKYDIDLFQSYMVGDTDTDIIAGKKAGTKGV 146
Cdd:cd01427   73 LLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 103-146 3.80e-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: 36.98  E-value: 3.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 515950470 103 CRKPNSKLITDLSKKYDIDLFQSYMVGDT-DTDIIAGKKAGTKGV 146
Cdd:cd07510  202 VGKPSRFMFDCISSKFSIDPARTCMVGDRlDTDILFGQNCGLKTL 246
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 22-145 3.87e-03

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: 36.08  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515950470   22 KFVNKPHE-LYFLPGVPEAIKKL--NPFFDFIFvvTNQGGVGLGFMK--ETELNKIhDHMISELKkegaiIHDVAYCPHK 96
Cdd:pfam08645  19 VFPRNPDDwKWLYPSVPEKLKKLheDGYKIVIF--TNQGGIGRKGKKslEKFKNKI-EAILKKLG-----VPLQVYAATK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515950470   97 PKsgcACRKPNSKLITDLSKKYD----IDLFQSYMVGDTdtdiiAGKKAGTKG 145
Cdd:pfam08645  91 KD---IYRKPNTGMWDEMKKDYNdgveIDLEKSFYVGDA-----AGRPYDTRR 135
PLN02645 PLN02645
phosphoglycolate phosphatase
 105-144 5.85e-03

phosphoglycolate phosphatase


Pssm-ID: 178251  Cd Length: 311  Bit Score: 36.23  E-value: 5.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515950470 105 KPNSKLITDLSKKYDIDLFQSYMVGDT-DTDIIAGKKAGTK 144
Cdd:PLN02645 230 KPSTFMMDYLANKFGIEKSQICMVGDRlDTDILFGQNGGCK 270
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 105-142 9.06e-03

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: 35.49  E-value: 9.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 515950470 105 KPNSKLITDLSKKYDIDLFQSYMVGD-TDTDIIAGKKAG 142
Cdd:cd16422  177 KPNPIILDPVLEKFDYSKEETVMVGDrLYTDIVLGINAG 215
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH