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MULTISPECIES: D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase [Enterobacter]

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;
3-188 2.95e-121

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


:

Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 339.87  E-value: 2.95e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   3 KSVPAIFLDRDGTINVDH-GYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLAD 81
Cdd:PRK08942   1 KSMKAIFLDRDGVINVDSdGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  82 RGVDLDGIYYCPHHPQGtveayrqTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVgTKILVRTGKPV 161
Cdd:PRK08942  81 RGGRLDGIYYCPHHPED-------GCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV-TPVLVRTGKGV 152

                        170       180
                 ....*....|....*....|....*....
gi 495777300 162 TPEAENAA--DWVINSLADLPKEIKKHQK 188
Cdd:PRK08942 153 TTLAEGAApgTWVLDSLADLPQALKKQQK 181
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
3-188 2.95e-121

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 339.87  E-value: 2.95e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   3 KSVPAIFLDRDGTINVDH-GYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLAD 81
Cdd:PRK08942   1 KSMKAIFLDRDGVINVDSdGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  82 RGVDLDGIYYCPHHPQGtveayrqTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVgTKILVRTGKPV 161
Cdd:PRK08942  81 RGGRLDGIYYCPHHPED-------GCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV-TPVLVRTGKGV 152

                        170       180
                 ....*....|....*....|....*....
gi 495777300 162 TPEAENAA--DWVINSLADLPKEIKKHQK 188
Cdd:PRK08942 153 TTLAEGAApgTWVLDSLADLPQALKKQQK 181
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 5-181 2.10e-114

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: 322.64  E-value: 2.10e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    5 VPAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRGV 84
Cdd:TIGR00213   1 NKAIFLDRDGTINIDHGYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   85 DLDGIYYCPHHPQGtVEAYRQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTKILVRTGKPVTPE 164
Cdd:TIGR00213  81 DLDGIYYCPHHPEG-VEEFRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTNVLVRTGKPITPE 159

                         170
                  ....*....|....*..
gi 495777300  165 AENAADWVINSLADLPK 181
Cdd:TIGR00213 160 AENIADWVLNSLADLPQ 176
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-186 1.59e-96

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: 277.36  E-value: 1.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   1 MAKsvPAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLA 80
Cdd:COG0241    1 MMK--KAVFLDRDGTINEDVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  81 DRGVDLDGIYYCPHHPQGtveayrqTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTGKP 160
Cdd:COG0241   79 AEGGRIDAIYYCPHHPDD-------NCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKG-ILVLTGKG 150

                        170       180
                 ....*....|....*....|....*.
gi 495777300 161 VTPEAENAADWVINSLADLPKEIKKH 186
Cdd:COG0241  151 AEELAEALPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 6-155 2.64e-78

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: 229.73  E-value: 2.64e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   6 PAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRGVD 85
Cdd:cd07503    1 KALFLDRDGVINVDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  86 LDGIYYCPHHPQgtveayrQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILV 155
Cdd:cd07503   81 IDDIYYCPHHPD-------DGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKG-ILV 142
Hydrolase_like pfam13242
HAD-hyrolase-like;
109-179 1.85e-14

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 64.94  E-value: 1.85e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777300  109 CRKPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVRTGK---PVTPEAENAADWVINSLADL 179
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGART-ILVLTGVtrpADLEKAPIRPDYVVDDLAEA 75
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
3-188 2.95e-121

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 339.87  E-value: 2.95e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   3 KSVPAIFLDRDGTINVDH-GYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLAD 81
Cdd:PRK08942   1 KSMKAIFLDRDGVINVDSdGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  82 RGVDLDGIYYCPHHPQGtveayrqTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVgTKILVRTGKPV 161
Cdd:PRK08942  81 RGGRLDGIYYCPHHPED-------GCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGV-TPVLVRTGKGV 152

                        170       180
                 ....*....|....*....|....*....
gi 495777300 162 TPEAENAA--DWVINSLADLPKEIKKHQK 188
Cdd:PRK08942 153 TTLAEGAApgTWVLDSLADLPQALKKQQK 181
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 5-181 2.10e-114

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: 322.64  E-value: 2.10e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    5 VPAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRGV 84
Cdd:TIGR00213   1 NKAIFLDRDGTINIDHGYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   85 DLDGIYYCPHHPQGtVEAYRQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTKILVRTGKPVTPE 164
Cdd:TIGR00213  81 DLDGIYYCPHHPEG-VEEFRQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKTNVLVRTGKPITPE 159

                         170
                  ....*....|....*..
gi 495777300  165 AENAADWVINSLADLPK 181
Cdd:TIGR00213 160 AENIADWVLNSLADLPQ 176
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-186 1.59e-96

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: 277.36  E-value: 1.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   1 MAKsvPAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLA 80
Cdd:COG0241    1 MMK--KAVFLDRDGTINEDVGYVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  81 DRGVDLDGIYYCPHHPQGtveayrqTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTGKP 160
Cdd:COG0241   79 AEGGRIDAIYYCPHHPDD-------NCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKG-ILVLTGKG 150

                        170       180
                 ....*....|....*....|....*.
gi 495777300 161 VTPEAENAADWVINSLADLPKEIKKH 186
Cdd:COG0241  151 AEELAEALPDTVADDLAEAVDYLLAE 176
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 6-155 2.64e-78

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: 229.73  E-value: 2.64e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   6 PAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRGVD 85
Cdd:cd07503    1 KALFLDRDGVINVDVPYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGVE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  86 LDGIYYCPHHPQgtveayrQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILV 155
Cdd:cd07503   81 IDDIYYCPHHPD-------DGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKG-ILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 6-157 2.09e-40

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: 134.06  E-value: 2.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    6 PAIFLDRDGTINVD--HGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRG 83
Cdd:TIGR01656   1 PALFLDRDGVINEDtvSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777300   84 VDLDGIYYCPHHPQgtveayrQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTKILVRT 157
Cdd:TIGR01656  81 VAVDGVLFCPHHPA-------DNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 6-157 1.00e-38

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: 129.45  E-value: 1.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    6 PAIFLDRDGTINVDHGYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAqfetLTEWMDWSLADRGVD 85
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRS----FSGRVARRLEELGVP 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777300   86 LDGIYYCPHhpqgtveayrqtcdCRKPHPGMFISAQ-EFLHIDMAASYMVGDK-LEDMQAAAAAGVGTkILVRT 157
Cdd:TIGR01662  77 IDILYACPG--------------CRKPKPGMFLEALkRFNEIDPEESVYVGDQdLTDLQAAKRVGLAT-ILVAP 135
PRK06769 PRK06769
HAD-IIIA family hydrolase;
7-174 9.71e-32

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 112.51  E-value: 9.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   7 AIFLDRDGTINVDHgYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETltEWMdwsladrGVDL 86
Cdd:PRK06769   6 AIFIDRDGTIGGDT-TIHYPGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADGIATIADFVQ--ELK-------GFGF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  87 DGIYYCPHHpqgtveaYRQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGvGTKILVRTG-------- 158
Cdd:PRK06769  76 DDIYLCPHK-------HGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVN-ATTILVRTGagydalht 147

                        170       180
                 ....*....|....*....|....*.
gi 495777300 159 -----KPVTPE--AEN---AADWVIN 174
Cdd:PRK06769 148 yrdkwAHIEPNyiAENfedAVNWILN 173
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
6-149 7.73e-26

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 101.41  E-value: 7.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   6 PAIFLDRDGTInvdhgyVHE---------IDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMD 76
Cdd:PRK05446   3 KILFIDRDGTL------IEEpptdfqvdsLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMM 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495777300  77 WSLADRGVDLDGIYYCPHHPQgtveayrQTCDCRKPHPGMFisaQEFLH---IDMAASYMVGDKLEDMQAAAAAGV 149
Cdd:PRK05446  77 QIFESQGIKFDEVLICPHFPE-------DNCSCRKPKTGLV---EEYLAegaIDLANSYVIGDRETDVQLAENMGI 142
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 6-149 3.34e-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: 3.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    6 PAIFLDRDGTINVDHGYVHEIDEFE---FIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADR 82
Cdd:TIGR01261   2 KILFIDRDGTLIEEPPSDFQVDALEklrFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRSQ 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777300   83 GVDLDGIYYCPHHPQgtveayrQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGV 149
Cdd:TIGR01261  82 GIIFDDVLICPHFPD-------DNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAENLGI 141
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
24-185 1.53e-17

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 76.89  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  24 HEIDEFEFIEGVIDAMRQLKEMGYALVVVTNqsgiARGKFTEAQFETLtEWMDWsladrgvdLDGIYYCPHHPQgtveay 103
Cdd:COG0546   78 ELLDETRLFPGVRELLEALKARGIKLAVVTN----KPREFAERLLEAL-GLDDY--------FDAIVGGDDVPP------ 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300 104 rqtcdcRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTG-KPVTPEAENAADWVINSLADLPKE 182
Cdd:COG0546  139 ------AKPKPEPLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPF-IGVTWGyGSAEELEAAGADYVIDSLAELLAL 211


                 ...
gi 495777300 183 IKK 185
Cdd:COG0546  212 LAE 214
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 10-181 1.67e-15

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 71.60  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  10 LDRDGTINVDHGYVHEIDE-FEFIEGVIDAMRQLKEMGYALVVVTNqsgiargkfteAQFETLTEWMDWS-LADRgvdLD 87
Cdd:COG1011   72 LGLDLAEELAEAFLAALPElVEPYPDALELLEALKARGYRLALLTN-----------GSAELQEAKLRRLgLDDL---FD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  88 GIYycphhpqgTVEAYRqtcdCRKPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVrTGKPVTPEAE 166
Cdd:COG1011  138 AVV--------SSEEVG----VRKPDPEIFELALERLGVPPEEALFVGDSPEtDVAGARAAGMRT-VWV-NRSGEPAPAE 203

                        170
                 ....*....|....*
gi 495777300 167 NAADWVINSLADLPK 181
Cdd:COG1011  204 PRPDYVISDLAELLE 218
Hydrolase_like pfam13242
HAD-hyrolase-like;
109-179 1.85e-14

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 64.94  E-value: 1.85e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777300  109 CRKPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVRTGK---PVTPEAENAADWVINSLADL 179
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGART-ILVLTGVtrpADLEKAPIRPDYVVDDLAEA 75
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
34-183 1.13e-13

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 66.37  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  34 GVIDAMRQLKEMGYALVVVTNQSGiargKFTEAQFETLtewmdwSLADRGVDLDGiyycphhpqG-TVEAyrqtcdcRKP 112
Cdd:PRK13222  97 GVKETLAALKAAGYPLAVVTNKPT----PFVAPLLEAL------GIADYFSVVIG---------GdSLPN-------KKP 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777300 113 HPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILV----RTGKPVtpeAENAADWVINSLADLPKEI 183
Cdd:PRK13222 151 DPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPS-VGVtygyNYGEPI---ALSEPDVVIDHFAELLPLL 221
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-179 4.35e-11

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 59.74  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   1 MAKSVPAIFLDRDGTINVDHgyvheidefEFIEGVIDAMRQLKEMGYALVVVTN--------------QSGI-------- 58
Cdd:COG0647    4 LADRYDAFLLDLDGVLYRGD---------EPIPGAVEALARLRAAGKPVLFLTNnssrtpedvaeklrRLGIpvaedeiv 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  59 -------------ARGK-------------FTEAQFETLTEW----------MDWSLAD---------RGVDL------- 86
Cdd:COG0647   75 tsgdataaylaerHPGArvyvigeeglreeLEEAGLTLVDDEepdavvvgldRTFTYEKlaealrairRGAPFiatnpdr 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  87 -----DGIYYCPhhpqGT-VEAYRQTCDCR-----KPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkIL 154
Cdd:COG0647  155 tvpteDGLIPGA----GAlAAALEAATGGEplvvgKPSPPIYELALERLGVDPERVLMVGDRLDtDILGANAAGLDT-LL 229

                        250       260
                 ....*....|....*....|....*....
gi 495777300 155 VRTGKPvTPEAENAA----DWVINSLADL 179
Cdd:COG0647  230 VLTGVT-TAEDLEAApirpDYVLDSLAEL 257
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 34-183 9.90e-11

haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319815 [Multi-domain]  Cd Length: 214  Bit Score: 58.48  E-value: 9.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  34 GVIDAMRQLKEMGYALVVVTNQSGIArgkfTEAQFETLtewmdwSLADRGVDLDGiyycphhpqgtveayRQTCDCRKPH 113
Cdd:cd07512   90 GVIEALERLRAAGWRLAICTNKPEAP----ARALLSAL------GLADLFAAVVG---------------GDTLPQRKPD 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300 114 PGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTGKPVTPEAENAADWVINSLADLPKEI 183
Cdd:cd07512  145 PAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPF-VLVTFGYRHAPVAELPHDAVFSDFDALPDLL 213
CTE7 TIGR02253
HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and ...
 34-180 6.30e-10

HAD superfamily (subfamily IA) hydrolase, TIGR02253; This family of sequences from archaea and metazoans includes the human uncharacterized protein CTE7. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same function. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).


Pssm-ID: 274057 [Multi-domain]  Cd Length: 221  Bit Score: 56.26  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   34 GVIDAMRQLKEMGYALVVVTNQSgiargkfTEAQFETLTEWmdwsladrGVD--LDGIYYCPHHPQGtveayrqtcdcrK 111
Cdd:TIGR02253  98 GVRDTLMELRESGYRLGIITDGL-------PVKQWEKLERL--------GVRdfFDAVITSEEEGVE------------K 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495777300  112 PHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTKILVRTG-KPVTPEAENAADWVINSLADLP 180
Cdd:TIGR02253 151 PHPKIFYAALKRLGVKPEEAVMVGDRLDkDIKGAKNAGMKTVWINQGKsSKMEDDVYPYPDYEISSLRELL 221
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
25-179 2.30e-09

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 54.44  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  25 EIDEFEFIEGVIDAMRQLKEMGYALVVVTNqsgiargkfteaqfeTLTEWMDWSLADRGVD--LDGIYYCPHHPQGtvea 102
Cdd:COG0637   81 AEEGLPLIPGVVELLEALKEAGIKIAVATS---------------SPRENAEAVLEAAGLLdyFDVIVTGDDVARG---- 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777300 103 yrqtcdcrKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTGKPVTPEAEnAADWVINSLADL 179
Cdd:COG0637  142 --------KPDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRV-VGVPDGGTAEEELA-GADLVVDDLAEL 208
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 34-180 1.66e-08

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: 52.24  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  34 GVIDAMRQLKEMGYALVVVTNQSGiargKFTE---AQFEtLTEWMDWSLAdrGVDLdgiyycphhPQgtveayrqtcdcR 110
Cdd:cd16417   91 GVKEGLAALKAQGYPLACVTNKPE----RFVApllEALG-ISDYFSLVLG--GDSL---------PE------------K 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777300 111 KPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTkILVRTG----KPVtpeAENAADWVINSLADLP 180
Cdd:cd16417  143 KPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPS-VGLTYGynygEDI---AASGPDAVIDSLAELL 212
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 21-148 4.73e-08

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: 50.66  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   21 GYVHEIDEFEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEaqfetLTEWMDWSLADRGVDLDGIYycphhpqgtv 100
Cdd:pfam00702  89 GVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLR-----LLGLDDYFDVVISGDDVGVG---------- 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 495777300  101 eayrqtcdcrKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAG 148
Cdd:pfam00702 154 ----------KPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 7-155 5.72e-08

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: 48.93  E-value: 5.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   7 AIFLDRDGTInvdhgYVHEidefefiegvidAMRQLKEMGYALVVVTNQSGiargKFTEAQFETLtewmdwslaDRGVDL 86
Cdd:cd01427    1 AVLFDLDGTL-----LAVE------------LLKRLRAAGIKLAIVTNRSR----EALRALLEKL---------GLGDLF 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495777300  87 DGIYYCPHHPQgtveayrqtcdcRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGvGTKILV 155
Cdd:cd01427   51 DGIIGSDGGGT------------PKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAG-GRTVAV 106
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 7-136 2.36e-07

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: 48.41  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300    7 AIFlDRDGT-INVDHGYVHEIDEFEFI---EGVIDAMRQLKEMGYALVVVTNQSGIARGkfTEAQFETLTEWMDWSLADR 82
Cdd:pfam08645   3 AAF-DLDGTlIKTKSGKVFPRNPDDWKwlyPSVPEKLKKLHEDGYKIVIFTNQGGIGRK--GKKSLEKFKNKIEAILKKL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495777300   83 GVDLDgIYYCPHHpqgtvEAYrqtcdcRKPHPGMFISAQE----FLHIDMAASYMVGD 136
Cdd:pfam08645  80 GVPLQ-VYAATKK-----DIY------RKPNTGMWDEMKKdyndGVEIDLEKSFYVGD 125
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
27-149 2.83e-07

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 48.35  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   27 DEFEFIEGVIDAMRQLKEMGYALVVVTNQS-GIARGKFTEAQFETLtewmdwsladrgvdLDGIYycphhpqGTVEAYRq 105
Cdd:pfam13419  76 KLVKPYPGIKELLEELKEQGYKLGIVTSKSrENVEEFLKQLGLEDY--------------FDVIV-------GGDDVEG- 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 495777300  106 tcdcRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGV 149
Cdd:pfam13419 134 ----KKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGI 173
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 34-180 4.35e-07

2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate salvage pathway in higher organisms (photorespiration in plants). Phosphoglycolate results from the oxidase activity of RubisCO in the Calvin cycle when concentrations of carbon dioxide are low relative to oxygen. In Ralstonia (Alcaligenes) eutropha and Rhodobacter sphaeroides, the PGP gene (CbbZ) is located on an operon along with other Calvin cycle enzymes including RubisCO. The only other pertinent experimental evidence concerns the gene from E. coli. The in vitro activity of the Ralstonia and Escherichia enzymes was determined with crude cell extracts of strains containing PGP on expression plasmids and compared to controls. In E. coli, however, there does not appear to be a functional Calvin cycle (RubisCO is absent), although the E. coli PGP gene (gph) is on the same operon (dam) with ribulose-5-phosphate-3-epimerase (rpe), a gene in the pentose-phosphate pathway (along with other, unrelated genes). The E. coli enzyme is not expressed under normal laboratory conditions; the pathway to which it belongs has not been determined. In fact, the possibility exists, although unlikely, that the E. coli enzyme and others within this equivalog have as their physiological substrate another, closely related molecule. The other seed chosen for this model, from Xylella fastidiosa has no experimental evidence, but is a plant pathogen and thus may obtain phosphoglycolate from its host. This model has been restricted to encompass only proteobacteria as no related PGP has been verified outside of this clade. Sequences from Aquifex aeolicus and Treponema pallidum fall between the trusted and noise cutoffs. Just below the noise cutoff is a gene which is part of the operon for the biosynthesis of the blue pigment, indigoidine, from Erwinia (Pectobacterium) chrysanthemi, a plant pathogen. It does not seem likely, considering the proposed biosynthetic mechanism, that the dephosphorylation of phosphoglycolate or a closely related compound is required. Possibly, this gene is fortuitously located in this operon, or has an indirect relationship to the necessity for the biosynthesis of this compound. Sequences from 11 species have been annotated as PGP or putative PGP but fall below the noise cutoff. None of these have experimental validation. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolase enzymes (pfam00702). [Energy metabolism, Sugars]


Pssm-ID: 130516 [Multi-domain]  Cd Length: 213  Bit Score: 48.28  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   34 GVIDAMRQLKEMGYALVVVTNQSgiargKFTEAQFETLTEWMDWSLADRGVDldgiyycphhpqgtveayrqTCDCRKPH 113
Cdd:TIGR01449  89 GVEATLGALRAKGLRLGLVTNKP-----TPLARPLLELLGLAKYFSVLIGGD--------------------SLAQRKPH 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495777300  114 PGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTKILVRTGKPVTPEAENAADWVINSLADLP 180
Cdd:TIGR01449 144 PDPLLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYGYRYGEAIDLLPPDVLYDSLNELP 210
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 8-71 8.14e-07

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 45.53  E-value: 8.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777300    8 IFLDRDGTINVDHgyvheidefEFIEGVIDAMRQLKEMGYALVVVTNQSGIARGKFTEaQFETL 71
Cdd:pfam13344   1 FLFDIDGVLWRGG---------EPIPGAAEALRALRAAGKPVVFVTNNSSRSREEYAE-KLRKL 54
HAD_Pase_UmpH-like cd07510
UmpH/NagD family phosphatase, similar to human PGP phosphoglycolate phosphatase and ...
 104-179 5.32e-06

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: 45.46  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300 104 RQTCDCRKPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVRTGKPVTPEAEN------AADWVINSL 176
Cdd:cd07510  197 RQAIVVGKPSRFMFDCISSKFSIDPARTCMVGDRLDtDILFGQNCGLKT-LLVLTGVSTLEEALAklsndlVPDYYVESL 275


                 ...
gi 495777300 177 ADL 179
Cdd:cd07510  276 ADL 278
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 34-179 1.79e-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: 43.54  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  34 GVIDAMRQLKEMGYALvvvtnqsGIARGKfteaqfetltewmdwslADRGVD--LDGiyycpHHPQGTVEAYRQTCDCR- 110
Cdd:cd07533   88 GVREALDALAAQGVLL-------AVATGK-----------------SRRGLDrvLEQ-----HGLGGYFDATRTADDTPs 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300 111 KPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVgTKILVRTGKPVTPE-AENAADWVINSLADL 179
Cdd:cd07533  139 KPHPEMLREILAELGVDPSRAVMVGDTAYDMQMAANAGA-HAVGVAWGYHSLEDlRSAGADAVVDHFSEL 207
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 100-183 1.99e-05

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: 43.81  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300 100 VEAYRQTCDCR-----KPHPGMFISAQEFLHIDMAASYMVGDKL-EDMQAAAAAGVgTKILVRTGK--PVTPEAEN-AAD 170
Cdd:cd07509  156 VTGLEYATGIKatvvgKPSPEFFLSALRSLGVDPEEAVMIGDDLrDDVGGAQACGM-RGILVRTGKyrPSDEKKPNvPPD 234

                         90
                 ....*....|...
gi 495777300 171 WVINSLADLPKEI 183
Cdd:cd07509  235 LTADSFADAVDHI 247
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 22-148 5.97e-05

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: 41.61  E-value: 5.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300   22 YVHEIDEFE-FIEGVIDAMRQLKEMGYALVVVTNqsgiargKFTEAQfetltewmdwslaDRGVDLDGIYycphhpQGTV 100
Cdd:TIGR01549  64 FWSEYDAEEaYIRGAADLLARLKSAGIKLGIISN-------GSLRAQ-------------KLLLRLFGLG------DYFE 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 495777300  101 EAYRQTCDCRKPHPGMFISAQEflHIDMAASY-MVGDKLEDMQAAAAAG 148
Cdd:TIGR01549 118 LILVSDEPGSKPEPEIFLAALE--SLGVPPEVlHVGDNLNDIEGARNAG 164
HAD_PPase cd02616
pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX ...
 22-179 6.32e-05

pyrophosphatase similar to Bacillus subtilis PpaX; This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319797 [Multi-domain]  Cd Length: 207  Bit Score: 41.88  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  22 YVHEIDEF-EFIEGVIDAMRQLKEMGYALVVVTNqsgiargKFTEaqfetltewmdwsLADRGVDLDGI--YYcphhpqG 98
Cdd:cd02616   71 YREHNDDLtKEYPGVYETLARLKSQGIKLGVVTT-------KLRE-------------TALKGLKLLGLdkYF------D 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  99 TVEAYRQTCDcRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAGVGTKILVRTGKPVTPEAENAADWVINSLAD 178
Cdd:cd02616  125 VIVGGDDVTH-HKPDPEPVLKALELLGAEPEEALMVGDSPHDILAGKNAGVKTVGVTWGYKGREYLKAFNPDFIIDKMSD 203


                 .
gi 495777300 179 L 179
Cdd:cd02616  204 L 204
HAD_Pase_UmpH-like cd07530
UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide ...
 111-178 6.95e-05

UmpH/NagD family phosphatase, similar to Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase and Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase; Escherichia coli UmpH/NagD is a ribonucleoside tri-, di-, and monophosphatase with a preference for purines, it shows peak activity with UMP and functions in UMP-degradation. It is also an effective phosphatase with AMP, GMP and CMP. Mycobacterium tuberculosis phosphatase, Rv1692 is a glycerol 3-phosphate phosphatase. Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319832 [Multi-domain]  Cd Length: 247  Bit Score: 42.19  E-value: 6.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495777300 111 KPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVRTGkpVTPEAENAA-----DWVINSLAD 178
Cdd:cd07530  177 KPEPIMMRAALEKLGLKSEETLMVGDRLDtDIAAGIAAGIDT-LLVLTG--VTTREDLAKppyrpTYIVPSLRE 247
HAD_sEH-N_like cd02603
N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX ...
 29-148 5.83e-04

N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive; This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. 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: 319790 [Multi-domain]  Cd Length: 195  Bit Score: 38.86  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  29 FEFIEGVIDAMRQLKEMGYALVVVTNQSgiargkfteaqFETLTEWMDWsLADRGVDLDGIYYcphhpqgtveayrqTCD 108
Cdd:cd02603   83 VDPNPEMLDLLEALRAKGYKVYLLSNTW-----------PDHFKFQLEL-LPRRGDLFDGVVE--------------SCR 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495777300 109 --CRKPHPGMFISAQEFLHIDMAASYMVGDKLEDMQAAAAAG 148
Cdd:cd02603  137 lgVRKPDPEIYQLALERLGVKPEEVLFIDDREENVEAARALG 178
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 111-178 1.49e-03

haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this UmpH/NagD family include Escherichia coli UmpH UMP phosphatase/NagD nucleotide phosphatase , Mycobacterium tuberculosis Rv1692 glycerol 3-phosphate phosphatase, human PGP phosphoglycolate phosphatase, Schizosaccharomyces pombe PHO2 p-nitrophenylphosphatase, Bacillus AraL a putative sugar phosphatase, and Plasmodium falciparum para nitrophenyl phosphate phosphatase PNPase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319811 [Multi-domain]  Cd Length: 270  Bit Score: 38.11  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777300 111 KPHPGMFISAQEFLHIDMAASYMVGDKLE-DMQAAAAAGVGTkILVRTGKPVTPEAENAA------DWVINSLAD 178
Cdd:cd07508  197 KPSPWLGELALEKFGIDPERVLFVGDRLAtDVLFGKACGFQT-LLVLTGVTTLEDLQAYIdhelvpDYYADSLAD 270
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 31-81 3.14e-03

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 37.09  E-value: 3.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495777300  31 FIEGVIDAMRQLKEMGYALVVVTNqsgiarGKFTEAQFETLTEWMDWSLAD 81
Cdd:COG1180   87 QPEFLLDLAKLAKELGLHTALDTN------GYIPEEALEELLPYLDAVNID 131
PTZ00412 PTZ00412
leucyl aminopeptidase; Provisional
 125-188 3.68e-03

leucyl aminopeptidase; Provisional


Pssm-ID: 240407 [Multi-domain]  Cd Length: 569  Bit Score: 37.26  E-value: 3.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495777300 125 HIDMAASYMVGDKLEDMQAAAAAGVGTKILVRTGKPVTPEAENAADWVINSLADLP-KEIKKHQK 188
Cdd:PTZ00412 501 HLDIAGVGMGGDKPKGFQPAGAPGFGVQLLVDYFRHNKPPKRKGIKKAQNAKKDLKvVQKKRHGR 565
HAD_PNP cd01625
polynucleotide 3'-phosphatase domain similar to the phosphatase domain of the bifunctional ...
 40-136 3.72e-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: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495777300  40 RQLKEM---GYALVVVTNQSGIARGKFTEAQFETLTEWMDWSLADRGVdldgIYYCPHhpqgtVEAYrqtcdcRKPHPGM 116
Cdd:cd01625   36 EKLKALhkdGYKIVIFTNQGGIVRGKLTPEVFKGKIEAILEKLGVPIQ----VYAATK-----KGKY------RKPVTGM 100

                         90       100
                 ....*....|....*....|....
gi 495777300 117 FISAQEFLH----IDMAASYMVGD 136
Cdd:cd01625  101 WDHLKEDLNsgipINLKDSFYVGD 124
 
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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