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Conserved domains on  [gi|2524517646|ref|WP_286639627|]
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D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase [Thiopseudomonas alkaliphila]

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;
1-176 2.22e-103

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


:

Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 294.42  E-value: 2.22e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:PRK08942    3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPAD 160
Cdd:PRK08942   83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                         170
                  ....*....|....*.
gi 2524517646 161 TLIFSDLAAVAEYLIS 176
Cdd:PRK08942  163 TWVLDSLADLPQALKK 178
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-176 2.22e-103

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 294.42  E-value: 2.22e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:PRK08942    3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPAD 160
Cdd:PRK08942   83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                         170
                  ....*....|....*.
gi 2524517646 161 TLIFSDLAAVAEYLIS 176
Cdd:PRK08942  163 TWVLDSLADLPQALKK 178
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-176 9.59e-92

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: 264.65  E-value: 9.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDaYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:COG0241     3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPad 160
Cdd:COG0241    82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                         170
                  ....*....|....*.
gi 2524517646 161 TLIFSDLAAVAEYLIS 176
Cdd:COG0241   160 DTVADDLAEAVDYLLA 175
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 2-144 4.05e-65

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: 196.21  E-value: 4.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   2 QLIILDRDGVINQDSDaYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAGG 81
Cdd:cd07503     1 KALFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524517646  82 ELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLV 144
Cdd:cd07503    80 EIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 2-147 3.11e-48

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: 153.71  E-value: 3.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   2 QLIILDRDGVINQDSDA-YIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
Hydrolase_like pfam13242
HAD-hyrolase-like;
98-168 1.35e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.93  E-value: 1.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524517646  98 NCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLR-DLEAAVAIKAKPVLVKTGK-GVETVNKRLPADTLIFSDLA 168
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVtRPADLEKAPIRPDYVVDDLA 73
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-176 2.22e-103

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 294.42  E-value: 2.22e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:PRK08942    3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPAD 160
Cdd:PRK08942   83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                         170
                  ....*....|....*.
gi 2524517646 161 TLIFSDLAAVAEYLIS 176
Cdd:PRK08942  163 TWVLDSLADLPQALKK 178
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-176 9.59e-92

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: 264.65  E-value: 9.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDaYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:COG0241     3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPad 160
Cdd:COG0241    82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                         170
                  ....*....|....*.
gi 2524517646 161 TLIFSDLAAVAEYLIS 176
Cdd:COG0241   160 DTVADDLAEAVDYLLA 175
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 2-144 4.05e-65

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: 196.21  E-value: 4.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   2 QLIILDRDGVINQDSDaYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAGG 81
Cdd:cd07503     1 KALFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524517646  82 ELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLV 144
Cdd:cd07503    80 EIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 2-147 3.11e-48

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: 153.71  E-value: 3.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   2 QLIILDRDGVINQDSDA-YIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 4-148 1.33e-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: 114.64  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   4 IILDRDGVINQDSdAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAGGEL 83
Cdd:TIGR00213   4 IFLDRDGTINIDH-GYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDVDL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2524517646  84 GYIAYCPHGPD------DGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAK-PVLVKTGK 148
Cdd:TIGR00213  83 DGIYYCPHHPEgveefrQVCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKtNVLVRTGK 154
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 3-144 2.91e-31

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: 109.80  E-value: 2.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   3 LIILDRDGVINQDSDaYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQtlhaMHAKLRALVQAAGGE 82
Cdd:TIGR01662   2 AVVLDLDGTLTDDVP-YVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFSRS----FSGRVARRLEELGVP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524517646  83 LGYIAYCPHgpddgcnCRKPLPGLLEQIAAHYQT-DLTDVWFVGD-SLRDLEAAVAIKAKPVLV 144
Cdd:TIGR01662  77 IDILYACPG-------CRKPKPGMFLEALKRFNEiDPEESVYVGDqDLTDLQAAKRVGLATILV 133
PRK06769 PRK06769
HAD-IIIA family hydrolase;
1-155 4.86e-21

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 84.78  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDayIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGyysEQTLHAMHAKLRALvqaag 80
Cdd:PRK06769    4 IQAIFIDRDGTIGGDTT--IHYPGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADG---IATIADFVQELKGF----- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2524517646  81 gelGY--IAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNK 155
Cdd:PRK06769   74 ---GFddIYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTGAGYDALHT 147
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
29-174 2.71e-17

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 75.74  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  29 LPGAIEAMAQLSQAGWTVAIATNqsglargyyseqtlhAMHAKLRALVQAAGGElGYIAYCpHGPDDGCNcRKPLPGLLE 108
Cdd:COG0546    86 FPGVRELLEALKARGIKLAVVTN---------------KPREFAERLLEALGLD-DYFDAI-VGGDDVPP-AKPKPEPLL 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524517646 109 QIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKRLPADtLIFSDLAAVAEYL 174
Cdd:COG0546   148 EALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGAD-YVIDSLAELLALL 212
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 3-134 3.81e-17

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: 74.36  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   3 LIILDRDGVINQD--SDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:TIGR01261   3 ILFIDRDGTLIEEppSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRSQG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAA 134
Cdd:TIGR01261  83 IIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLA 136
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
3-140 1.44e-15

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 72.90  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   3 LIIlDRDGVINQD--SDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHAMHAKLRALVQAAG 80
Cdd:PRK05446    5 LFI-DRDGTLIEEppTDFQVDSLDKLAFEPGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQIFESQG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  81 GELGYIAYCPHGPDDGCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAK 140
Cdd:PRK05446   84 IKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIK 143
Hydrolase_like pfam13242
HAD-hyrolase-like;
98-168 1.35e-10

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 54.93  E-value: 1.35e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524517646  98 NCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLR-DLEAAVAIKAKPVLVKTGK-GVETVNKRLPADTLIFSDLA 168
Cdd:pfam13242   1 VCGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVtRPADLEKAPIRPDYVVDDLA 73
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 17-174 2.27e-09

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: 54.65  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  17 DAYIKTVDEWIAL-PGAIEAMAQLSQAGWTVAIATNQSGLArgyyseQTLHAMHAKLRALVQAA--GGELGYiaycphgp 93
Cdd:COG1011    82 EAFLAALPELVEPyPDALELLEALKARGYRLALLTNGSAEL------QEAKLRRLGLDDLFDAVvsSEEVGV-------- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  94 ddgcncRKPLPGLLEQIAAHYQTDLTDVWFVGDSLR-DLEAAVAIKAKPVLVKTGKGVETVNkrlPADTLIFSDLAAVAE 172
Cdd:COG1011   148 ------RKPDPEIFELALERLGVPPEEALFVGDSPEtDVAGARAAGMRTVWVNRSGEPAPAE---PRPDYVISDLAELLE 218


                  ..
gi 2524517646 173 YL 174
Cdd:COG1011   219 LL 220
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 7-136 4.54e-09

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: 53.36  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   7 DRDGVINQDSDAYIKTVDEWIALPGAIEAMAQLSQAGWTVAIATNQSglargyyseqtLHAMHAKLRALvqaagGELGYI 86
Cdd:pfam00702  78 EGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDN-----------PEAAEALLRLL-----GLDDYF 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2524517646  87 AYCPHGPDDGCncRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVA 136
Cdd:pfam00702 142 DVVISGDDVGV--GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKA 189
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 32-144 2.15e-06

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: 44.31  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  32 AIEAMAQLSQAGWTVAIATNQSglargyyseqtLHAMHAKLRALVQAAGGELGYiayCPHGPDDGCNCRKPLPGLLEQIA 111
Cdd:cd01427    12 AVELLKRLRAAGIKLAIVTNRS-----------REALRALLEKLGLGDLFDGII---GSDGGGTPKPKPKPLLLLLLKLG 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2524517646 112 AHYQtdltDVWFVGDSLRDLEAAVAIKAKPVLV 144
Cdd:cd01427    78 VDPE----EVLFVGDSENDIEAARAAGGRTVAV 106
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 30-172 5.81e-06

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: 44.61  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  30 PGAIEAMAQLSQAGWTVAIATNqsglargyyseQTLHAMHAKLRALvqaagGELGYIAYCPHGpdDGCNCRKPLPGLLEQ 109
Cdd:cd07512    89 PGVIEALERLRAAGWRLAICTN-----------KPEAPARALLSAL-----GLADLFAAVVGG--DTLPQRKPDPAPLRA 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524517646 110 IAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGKGVETVNKrLPADTLI--FSDLAAVAE 172
Cdd:cd07512   151 AIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHAPVAE-LPHDAVFsdFDALPDLLA 214
HAD_like cd07533
uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily, similar ...
 30-147 1.90e-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: 43.16  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  30 PGAIEAMAQLSQAGWTVAIATNQSglARGYYSEQTLHAMHAKLRAlVQAAggelgyiaycphgpDDGCNcrKPLPGLLEQ 109
Cdd:cd07533    87 PGVREALDALAAQGVLLAVATGKS--RRGLDRVLEQHGLGGYFDA-TRTA--------------DDTPS--KPHPEMLRE 147

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2524517646 110 IAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTG 147
Cdd:cd07533   148 ILAELGVDPSRAVMVGDTAYDMQMAANAGAHAVGVAWG 185
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
5-144 1.60e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 40.26  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   5 ILDRDGVINQDSDAYIKTVDEWIA---------LPGAIEAMAQLSQAGWTVAIATNqsglargyyseqtlhamhaKLRAL 75
Cdd:pfam13419  48 IFRYLGVSEDEEEKIEFYLRKYNEelhdklvkpYPGIKELLEELKEQGYKLGIVTS-------------------KSREN 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524517646  76 VQAAGGELGYIAYCPH--GPDDgCNCRKPLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLV 144
Cdd:pfam13419 109 VEEFLKQLGLEDYFDVivGGDD-VEGKKPDPDPILKALEQLGLKPEEVIYVGDSPRDIEAAKNAGIKVIAV 178
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 24-126 1.80e-04

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


Pssm-ID: 370030  Cd Length: 161  Bit Score: 39.93  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  24 DEWIAL-PGAIEAMAQLSQAGWTVAIATNQSGLARGyySEQTLHAMHAKLRALVQAAGGELG-YIAycphgPDDGCNcRK 101
Cdd:pfam08645  25 DDWKWLyPSVPEKLKKLHEDGYKIVIFTNQGGIGRK--GKKSLEKFKNKIEAILKKLGVPLQvYAA-----TKKDIY-RK 96

                          90       100
                  ....*....|....*....|....*....
gi 2524517646 102 PLPGLLEQIAAHY----QTDLTDVWFVGD 126
Cdd:pfam08645  97 PNTGMWDEMKKDYndgvEIDLEKSFYVGD 125
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 4-68 2.23e-04

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 38.60  E-value: 2.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524517646   4 IILDRDGVINQDSDAYiktvdewialPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQtLHAM 68
Cdd:pfam13344   1 FLFDIDGVLWRGGEPI----------PGAAEALRALRAAGKPVVFVTNNSSRSREEYAEK-LRKL 54
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-171 1.20e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 38.17  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646   1 MQLIILDRDGVINQDSDAYiktvdewialPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQ----------------- 63
Cdd:COG0647     8 YDAFLLDLDGVLYRGDEPI----------PGAVEALARLRAAGKPVLFLTNNSSRTPEDVAEKlrrlgipvaedeivtsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  64 --TLHAMH----------------------------------------------AKLRALVQAAGGELGYIA-----YCP 90
Cdd:COG0647    78 daTAAYLAerhpgarvyvigeeglreeleeagltlvddeepdavvvgldrtftyEKLAEALRAIRRGAPFIAtnpdrTVP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  91 HG----PDDGCNCR--------------KPLPGLLEQIAAHYQTDLTDVWFVGDSLR-DLEAAVAIKAKPVLVKTGK-GV 150
Cdd:COG0647   158 TEdgliPGAGALAAaleaatggeplvvgKPSPPIYELALERLGVDPERVLMVGDRLDtDILGANAAGLDTLLVLTGVtTA 237

                         250       260
                  ....*....|....*....|.
gi 2524517646 151 ETVNKRLPADTLIFSDLAAVA 171
Cdd:COG0647   238 EDLEAAPIRPDYVLDSLAELL 258
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
28-170 1.50e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 37.88  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  28 ALPGAIEAMAQLSQAGWTVAIATNqSGLARgyyseqtlhaMHAKLRALvqaagGELGYIAYC------PHGpddgcncrK 101
Cdd:COG0637    87 LIPGVVELLEALKEAGIKIAVATS-SPREN----------AEAVLEAA-----GLLDYFDVIvtgddvARG--------K 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2524517646 102 PLPGLLEQIAAHYQTDLTDVWFVGDSLRDLEAAVAIKAKPVLVKTGkgvETVNKRLPADTLIFSDLAAV 170
Cdd:COG0637   143 PDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDG---GTAEEELAGADLVVDDLAEL 208
HAD_Pase_UmpH-like cd07508
haloacid dehalogenase-like superfamily phosphatases, UmpH/NagD family; Phosphatases in this ...
 3-67 1.78e-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: 37.73  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2524517646   3 LIILDRDGVINQDSDayiktvdewiALPGAIEAMAQLSQAGWTVAIATNQSGLARGYYSEQTLHA 67
Cdd:cd07508     1 LVISDCDGVLWHDER----------AIPGAAEFLEALKEAGKKIVFVSNNSSRSRQDYAEKFRKF 55
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 107-143 1.81e-03

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 37.51  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2524517646 107 LEQIAAHYQTDLTDVWFVGDSLRD---LEAA---VAIKAKPVL 143
Cdd:COG0560   160 LRELAAELGIDLEQSYAYGDSANDlpmLEAAglpVAVNPDPAL 202
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 29-134 2.62e-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: 36.60  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524517646  29 LPGAIEAMAQLSQAGWTVAIATNqsglarGYYSEQTLhamhaklraLVQAAGGE--LGYIAYcphgpdDGCNCRKPLPGL 106
Cdd:TIGR01549  75 IRGAADLLARLKSAGIKLGIISN------GSLRAQKL---------LLRLFGLGdyFELILV------SDEPGSKPEPEI 133

                          90       100
                  ....*....|....*....|....*...
gi 2524517646 107 LEQIAAHYQTDlTDVWFVGDSLRDLEAA 134
Cdd:TIGR01549 134 FLAALESLGVP-PEVLHVGDNLNDIEGA 160
 
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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