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Conserved domains on  [gi|519005719|ref|WP_020161594|]
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D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase [Cycloclasticus pugetii]

Protein Classification

HAD family hydrolase( domain architecture ID 11483476)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
6-181 1.08e-87

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


:

Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 254.74  E-value: 1.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   6 NKPDIILDRDGVINIDSDSYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQA 85
Cdd:PRK08942   2 SMKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  86 GGEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQENPEL 165
Cdd:PRK08942  82 GGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAP 161

                        170
                 ....*....|....*.
gi 519005719 166 PYPIFETLYDASQNIL 181
Cdd:PRK08942 162 GTWVLDSLADLPQALK 177
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
6-181 1.08e-87

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 254.74  E-value: 1.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   6 NKPDIILDRDGVINIDSDSYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQA 85
Cdd:PRK08942   2 SMKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  86 GGEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQENPEL 165
Cdd:PRK08942  82 GGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAP 161

                        170
                 ....*....|....*.
gi 519005719 166 PYPIFETLYDASQNIL 181
Cdd:PRK08942 162 GTWVLDSLADLPQALK 177
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 7-181 5.38e-83

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: 242.69  E-value: 5.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   7 KPDIILDRDGVINIDSDsYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAG 86
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  87 GEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQEnpELP 166
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAE--ALP 159

                        170
                 ....*....|....*
gi 519005719 167 YPIFETLYDASQNIL 181
Cdd:COG0241  160 DTVADDLAEAVDYLL 174
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 10-150 9.90e-60

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: 182.73  E-value: 9.90e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  10 IILDRDGVINIDSDsYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAGGEI 89
Cdd:cd07503    3 LFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVEI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519005719  90 TGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILV 150
Cdd:cd07503   82 DDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 8-153 1.24e-54

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: 169.89  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719    8 PDIILDRDGVINIDSDS-YVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAG 86
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519005719   87 GEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTG 153
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
Hydrolase_like pfam13242
HAD-hyrolase-like;
105-176 3.50e-13

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 61.48  E-value: 3.50e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519005719  105 CRKPKPGLLHDLSLEFNIDLNAAIVIGDSLR-DLQAATEVGSKAILVLTGKGKKTQQENPEL-PYPIFETLYDA 176
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKAPIrPDYVVDDLAEA 75
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
6-181 1.08e-87

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 254.74  E-value: 1.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   6 NKPDIILDRDGVINIDSDSYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQA 85
Cdd:PRK08942   2 SMKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  86 GGEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQENPEL 165
Cdd:PRK08942  82 GGRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAP 161

                        170
                 ....*....|....*.
gi 519005719 166 PYPIFETLYDASQNIL 181
Cdd:PRK08942 162 GTWVLDSLADLPQALK 177
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 7-181 5.38e-83

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: 242.69  E-value: 5.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   7 KPDIILDRDGVINIDSDsYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAG 86
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  87 GEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQEnpELP 166
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAE--ALP 159

                        170
                 ....*....|....*
gi 519005719 167 YPIFETLYDASQNIL 181
Cdd:COG0241  160 DTVADDLAEAVDYLL 174
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 10-150 9.90e-60

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: 182.73  E-value: 9.90e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  10 IILDRDGVINIDSDsYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAGGEI 89
Cdd:cd07503    3 LFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVEI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519005719  90 TGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILV 150
Cdd:cd07503   82 DDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 8-153 1.24e-54

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: 169.89  E-value: 1.24e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719    8 PDIILDRDGVINIDSDS-YVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAG 86
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519005719   87 GEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTG 153
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 10-152 1.98e-33

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: 115.58  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   10 IILDRDGVINIDSDsYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSldtlTAMHNKMLDLIHQAGGEI 89
Cdd:TIGR01662   3 VVLDLDGTLTDDVP-YVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFS----RSFSGRVARRLEELGVPI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 519005719   90 TGIAFCPHtpddhctCRKPKPGLLHDLSLEFN-IDLNAAIVIGD-SLRDLQAATEVGSKAILVLT 152
Cdd:TIGR01662  78 DILYACPG-------CRKPKPGMFLEALKRFNeIDPEESVYVGDqDLTDLQAAKRVGLATILVAP 135
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 8-162 2.15e-32

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: 114.25  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719    8 PDIILDRDGVINIDSdSYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQAGG 87
Cdd:TIGR00213   2 KAIFLDRDGTINIDH-GYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   88 EITGIAFCPHTPD------DHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAA--TEVGSKaILVLTGKGKKTQ 159
Cdd:TIGR00213  81 DLDGIYYCPHHPEgveefrQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGvaAKVKTN-VLVRTGKPITPE 159


                  ...
gi 519005719  160 QEN 162
Cdd:TIGR00213 160 AEN 162
PRK06769 PRK06769
HAD-IIIA family hydrolase;
10-158 2.85e-22

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 87.86  E-value: 2.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  10 IILDRDGVINIDSDSYVKSVNEWLPIqsSILAIANLHKAGHRIFIATNQSGLGRGyfsldtltamHNKMLDLIHqaggEI 89
Cdd:PRK06769   7 IFIDRDGTIGGDTTIHYPGSFTLFPF--TKASLQKLKANHIKIFSFTNQPGIADG----------IATIADFVQ----EL 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519005719  90 TGIAF-----CPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKT 158
Cdd:PRK06769  71 KGFGFddiylCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTGAGYDA 144
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
6-149 1.43e-21

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 89.47  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   6 NKPDIILDRDGVInIDS-------DSYVKSVNEwlpiQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKM 78
Cdd:PRK05446   1 MQKILFIDRDGTL-IEEpptdfqvDSLDKLAFE----PGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLM 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519005719  79 LDLIhqaggEITGIAF-----CPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAIL 149
Cdd:PRK05446  76 MQIF-----ESQGIKFdevliCPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIKGIR 146
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 8-148 2.26e-21

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: 85.53  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719    8 PDIILDRDGVInID---SDSYVKSVNEWLPIQSSILAIANLHKAGHRIFIATNQSGLGRGYFSLDTLTAMHNKMLDLIHQ 84
Cdd:TIGR01261   2 KILFIDRDGTL-IEeppSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519005719   85 AGGEITGIAFCPHTPDDHCTCRKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAI 148
Cdd:TIGR01261  81 QGIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGIRGI 144
Hydrolase_like pfam13242
HAD-hyrolase-like;
105-176 3.50e-13

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 61.48  E-value: 3.50e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519005719  105 CRKPKPGLLHDLSLEFNIDLNAAIVIGDSLR-DLQAATEVGSKAILVLTGKGKKTQQENPEL-PYPIFETLYDA 176
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKAPIrPDYVVDDLAEA 75
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
41-153 5.31e-12

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 61.87  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  41 AIANLHKAGHRIFIATNqsglGRGYFSLDTLTAmhnkmLDLIHQAGGEITGiafcphtpdDHCTCRKPKPGLLHDLSLEF 120
Cdd:COG0546   92 LLEALKARGIKLAVVTN----KPREFAERLLEA-----LGLDDYFDAIVGG---------DDVPPAKPKPEPLLEALERL 153

                         90       100       110
                 ....*....|....*....|....*....|...
gi 519005719 121 NIDLNAAIVIGDSLRDLQAATEVGSKAILVLTG 153
Cdd:COG0546  154 GLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWG 186
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 41-150 1.55e-07

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 47.39  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  41 AIANLHKAGHRIFIATNQSglgrgyfsldtltamHNKMLDLIHQAGGEITGIAFCphTPDDHCTcRKPKPGLLHDLSLEF 120
Cdd:cd01427   15 LLKRLRAAGIKLAIVTNRS---------------REALRALLEKLGLGDLFDGII--GSDGGGT-PKPKPKPLLLLLLKL 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 519005719 121 NIDLNAAIVIGDSLRDLQAATEVGSKAILV 150
Cdd:cd01427   77 GVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
mtnX PRK09552
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
 96-175 1.21e-05

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed


Pssm-ID: 236562  Cd Length: 219  Bit Score: 43.81  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  96 PHTPDDHCT--CRKPKPGLLHDLSLefniDLNAAIVIGDSLRDLQAAtevgSKAILVLTGKGKKTQQENPELPYPIFETL 173
Cdd:PRK09552 134 PHPCDEHCQnhCGCCKPSLIRKLSD----TNDFHIVIGDSITDLEAA----KQADKVFARDFLITKCEELGIPYTPFETF 205


                 ..
gi 519005719 174 YD 175
Cdd:PRK09552 206 HD 207
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 13-132 1.77e-05

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: 43.02  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   13 DRDGVInIDSDS---YVKSVNEWLPIQSSILA-IANLHKAGHRIFIATNQSGLGR-GYFSLDTLTamhNKMLDLIHQAGG 87
Cdd:pfam08645   6 DLDGTL-IKTKSgkvFPRNPDDWKWLYPSVPEkLKKLHEDGYKIVIFTNQGGIGRkGKKSLEKFK---NKIEAILKKLGV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 519005719   88 EITgiAFCPHTPDDHctcRKPKPG----LLHDLSLEFNIDLNAAIVIGD 132
Cdd:pfam08645  82 PLQ--VYAATKKDIY---RKPNTGmwdeMKKDYNDGVEIDLEKSFYVGD 125
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 41-144 1.83e-05

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 43.34  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   41 AIANLHKAGHRIFIATNQSglgrgYFSLDTLTAMHNKMLDLIHQAGGEITGIAfcphtpddhctcrKPKPGLLHDLSLEF 120
Cdd:pfam00702 106 ALKALKERGIKVAILTGDN-----PEAAEALLRLLGLDDYFDVVISGDDVGVG-------------KPKPEIYLAALERL 167

                          90       100
                  ....*....|....*....|....
gi 519005719  121 NIDLNAAIVIGDSLRDLQAATEVG 144
Cdd:pfam00702 168 GVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 98-153 4.59e-05

uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar to Parvibaculum lavamentivorans HAD-superfamily hydrolase, subfamily IA, variant 1; This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319835 [Multi-domain]  Cd Length: 207  Bit Score: 42.39  E-value: 4.59e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 519005719  98 TPDDHCTcrKPKPGLLHDLSLEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTG 153
Cdd:cd07533  132 TADDTPS--KPHPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWG 185
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 95-177 3.45e-04

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 39.62  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  95 CPHTPDDHCTCRKPKPGLLHDLSLEFNIdlnaAIVIGDSLRDLQAATEvgskAILVLTGKGK--KTQQENpeLPYPIFET 172
Cdd:cd07524  132 WPHECDCTNGCGCCKSSIIRKYSKPRPF----IIVIGDSVTDLEAAKE----ADLVFARDGLilKCEEEN--LPYPPFET 201


                 ....*
gi 519005719 173 LYDAS 177
Cdd:cd07524  202 FTDID 206
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 127-181 6.48e-04

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: 39.19  E-value: 6.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519005719 127 AIVIGDSLR-DLQAATEVGSKAILVLTGKGKKTQQENPEL-PYPIFETLYDASQNIL 181
Cdd:cd07509  192 AVMIGDDLRdDVGGAQACGMRGILVRTGKYRPSDEKKPNVpPDLTADSFADAVDHIL 248
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
45-150 1.39e-03

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 37.56  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   45 LHKAGHRIFIATNqsglGRGYFSLDTLTamHNKMLDLIHQAggeITGiafcphtpdDHCTCRKPKPGLLHDLSLEFNIDL 124
Cdd:pfam13419  91 LKEQGYKLGIVTS----KSRENVEEFLK--QLGLEDYFDVI---VGG---------DDVEGKKPDPDPILKALEQLGLKP 152

                          90       100
                  ....*....|....*....|....*.
gi 519005719  125 NAAIVIGDSLRDLQAATEVGSKAILV 150
Cdd:pfam13419 153 EEVIYVGDSPRDIEAAKNAGIKVIAV 178
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
107-154 1.42e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 38.17  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 519005719 107 KPKPgLLHDLSLE-FNIDLNAAIVIGDSLR-DLQAATEVGSKAILVLTGK 154
Cdd:COG0647  186 KPSP-PIYELALErLGVDPERVLMVGDRLDtDILGANAAGLDTLLVLTGV 234
HAD_like cd07506
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily; The ...
 121-153 4.40e-03

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: 319809  Cd Length: 115  Bit Score: 35.43  E-value: 4.40e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 519005719 121 NIDLNAAIVIGDSLRDLQAATEVGSKAILVLTG 153
Cdd:cd07506   83 AFDPHQVVVIGDTPNDVACARALGARSVAVATG 115
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
41-150 4.74e-03

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 36.33  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  41 AIANLHKAGHRIFIATNQ---------SGLG-RGYFSLdtltamhnkmldLIhqaGGeitgiafcphtpdDHCTCRKPKP 110
Cdd:PRK13222 101 TLAALKAAGYPLAVVTNKptpfvapllEALGiADYFSV------------VI---GG-------------DSLPNKKPDP 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 519005719 111 G-LLHDLSLeFNIDLNAAIVIGDSLRDLQAATEVGSKAILV 150
Cdd:PRK13222 153 ApLLLACEK-LGLDPEEMLFVGDSRNDIQAARAAGCPSVGV 192
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 41-144 5.52e-03

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies 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. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 35.83  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719   41 AIANLHKAGHRIFIATNqsglgrGYFSLDTLTAMHNKMLDLIHQAGGeitgiafcphtpDDHcTCRKPKPGLLHDLSLEF 120
Cdd:TIGR01549  81 LLARLKSAGIKLGIISN------GSLRAQKLLLRLFGLGDYFELILV------------SDE-PGSKPEPEIFLAALESL 141

                          90       100
                  ....*....|....*....|....
gi 519005719  121 NIDlNAAIVIGDSLRDLQAATEVG 144
Cdd:TIGR01549 142 GVP-PEVLHVGDNLNDIEGARNAG 164
HAD_5NT cd04302
haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065; ...
 42-162 5.76e-03

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


Pssm-ID: 319798 [Multi-domain]  Cd Length: 209  Bit Score: 36.03  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  42 IANLHKAGHRIFIAT--NQSGLGR--GYFSLDTLtamhnkmLDLIHQAggeitgiafcphTPDDHctcRKPKPGLLHDLS 117
Cdd:cd04302   90 LEKLKAAGYRLYVATskPEVFARRilEHFGLDEY-------FDGIAGA------------SLDGS---RVHKADVIRYAL 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 519005719 118 LEFNIDLNAAIVIGDSLRDLQAATEVGSKAILVLTGKGKKTQQEN 162
Cdd:cd04302  148 DTLGIAPEQAVMIGDRKHDIIGARANGIDSIGVLYGYGSEDELEE 192
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 13-132 6.73e-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: 35.40  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519005719  13 DRDGVInIDSDS---YVKSVNEWLPIQSSILA-IANLHKAGHRIFIATNQSGLGRGYFSLDTLTamhNKMLDLIHQAGGE 88
Cdd:cd01625    6 DLDGTL-IKTKSgkvFPTNASDWQILYPSVPEkLKALHKDGYKIVIFTNQGGIVRGKLTPEVFK---GKIEAILEKLGVP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 519005719  89 ITGIAFCphtPDDHctCRKPKPGLLHDLSLEFN----IDLNAAIVIGD 132
Cdd:cd01625   82 IQVYAAT---KKGK--YRKPVTGMWDHLKEDLNsgipINLKDSFYVGD 124
HAD_Pase_UmpH-like cd16422
uncharacterized subfamily of the UmpH/NagD phosphatase family, belongs to the haloacid ...
 107-173 8.05e-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: 35.88  E-value: 8.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 519005719 107 KPKPGLLHDLSLEFNIDLNAAIVIGDSL-RDLQAATEVGSKAILVLTGKGKKTQQENPEL-PYPIFETL 173
Cdd:cd16422  177 KPNPIILDPVLEKFDYSKEETVMVGDRLyTDIVLGINAGVDSILVLSGETTREDLEDLERkPTYVFDNV 245
 
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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