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Conserved domains on  [gi|518524211|ref|WP_019694418|]
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D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase [Pseudomonas fluorescens]

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;
1-177 1.05e-113

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


:

Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 320.23  E-value: 1.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVINYDSDAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:PRK08942   3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPVG 160
Cdd:PRK08942  83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                        170
                 ....*....|....*..
gi 518524211 161 TLIFDDLAAIAAELIHN 177
Cdd:PRK08942 163 TWVLDSLADLPQALKKQ 179
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-177 1.05e-113

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 320.23  E-value: 1.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVINYDSDAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:PRK08942   3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPVG 160
Cdd:PRK08942  83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                        170
                 ....*....|....*..
gi 518524211 161 TLIFDDLAAIAAELIHN 177
Cdd:PRK08942 163 TWVLDSLADLPQALKKQ 179
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-175 6.17e-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: 265.04  E-value: 6.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVINYDSDaYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPvg 160
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                        170
                 ....*....|....*
gi 518524211 161 TLIFDDLAAIAAELI 175
Cdd:COG0241  160 DTVADDLAEAVDYLL 174
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 2-144 2.46e-69

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: 206.61  E-value: 2.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   2 KLLILDRDGVINYDSDaYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQGG 81
Cdd:cd07503    1 KALFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518524211  82 EVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLV 144
Cdd:cd07503   80 EIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 2-147 6.92e-50

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: 157.56  E-value: 6.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    2 KLLILDRDGVINYDSDA-YIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518524211   81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
Hydrolase_like pfam13242
HAD-hyrolase-like;
99-168 1.81e-12

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 59.55  E-value: 1.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518524211   99 CRKPKPGMLKTIAAHYDVALTNLWFVGDSLG-DLEAAKAVDCQPVLVKTGKGEKTQGLTLPV-GTLIFDDLA 168
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKAPIrPDYVVDDLA 73
 
Name Accession Description Interval E-value
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
1-177 1.05e-113

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 320.23  E-value: 1.05e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVINYDSDAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:PRK08942   3 MKAIFLDRDGVINVDSDGYVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPVG 160
Cdd:PRK08942  83 GRLDGIYYCPHHPEDGCDCRKPKPGMLLSIAERLNIDLAGSPMVGDSLRDLQAAAAAGVTPVLVRTGKGVTTLAEGAAPG 162

                        170
                 ....*....|....*..
gi 518524211 161 TLIFDDLAAIAAELIHN 177
Cdd:PRK08942 163 TWVLDSLADLPQALKKQ 179
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-175 6.17e-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: 265.04  E-value: 6.17e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVINYDSDaYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:COG0241    3 KKAVFLDRDGTINEDVG-YVKSPEEFEFLPGVLEALARLNEAGYRLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAAEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPvg 160
Cdd:COG0241   82 GRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERLGIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEALP-- 159

                        170
                 ....*....|....*
gi 518524211 161 TLIFDDLAAIAAELI 175
Cdd:COG0241  160 DTVADDLAEAVDYLL 174
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 2-144 2.46e-69

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: 206.61  E-value: 2.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   2 KLLILDRDGVINYDSDaYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQGG 81
Cdd:cd07503    1 KALFLDRDGVINVDVP-YVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQGV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518524211  82 EVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLV 144
Cdd:cd07503   80 EIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKELGIDLARSFVIGDRLSDIQAARNAGCKGILV 142
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 2-147 6.92e-50

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: 157.56  E-value: 6.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    2 KLLILDRDGVINYDSDA-YIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQG 80
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSdYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518524211   81 GEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTG 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLGVDASRSLVVGDRLRDLQAARNAGAAAGLLVSG 147
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 2-148 3.41e-33

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: 116.18  E-value: 3.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    2 KLLILDRDGVINYDSdAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQGG 81
Cdd:TIGR00213   2 KAIFLDRDGTINIDH-GYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDV 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518524211   82 EVGLIVYCPHGPDEG------CDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQ-PVLVKTGK 148
Cdd:TIGR00213  81 DLDGIYYCPHHPEGVeefrqvCDCRKPKPGMLLQARKELHIDMAQSYMVGDKLEDMQAGVAAKVKtNVLVRTGK 154
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 2-144 2.72e-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: 2.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    2 KLLILDRDGVINYDSDaYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDvatlDAMHERLRTLVAEQGG 81
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVP-YVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFS----RSFSGRVARRLEELGV 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518524211   82 EVGLIVYCPHgpdegcdCRKPKPGMLKTIAAHY-DVALTNLWFVGDSLG-DLEAAKAVDCQPVLV 144
Cdd:TIGR01662  76 PIDILYACPG-------CRKPKPGMFLEALKRFnEIDPEESVYVGDQDLtDLQAAKRVGLATILV 133
PRK06769 PRK06769
HAD-IIIA family hydrolase;
6-152 3.37e-21

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 85.17  E-value: 3.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   6 LDRDGVINYDSDayiksveewIPLPGSI-------DAIAQLSKAGWTVAVATNQSGIARGyydVATLDAMHERLRTLVAE 78
Cdd:PRK06769   9 IDRDGTIGGDTT---------IHYPGSFtlfpftkASLQKLKANHIKIFSFTNQPGIADG---IATIADFVQELKGFGFD 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518524211  79 QggevglIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKT 152
Cdd:PRK06769  77 D------IYLCPHKHGDGCECRKPSTGMLLQAAEKHGLDLTQCAVIGDRWTDIVAAAKVNATTILVRTGAGYDA 144
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 2-135 5.59e-19

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: 78.99  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    2 KLLILDRDGVINYD--SDAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTLVAEQ 79
Cdd:TIGR01261   2 KILFIDRDGTLIEEppSDFQVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRSQ 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 518524211   80 GGEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAK 135
Cdd:TIGR01261  82 GIIFDDVLICPHFPDDNCDCRKPKIKLLEPYLKKNLIDKARSYVIGDRETDMQLAE 137
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
2-140 8.52e-19

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 81.76  E-value: 8.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   2 KLLILDRDG------VINYDSDAYIKSVEEwiplPGSIDAIAQLSKAGWTVAVATNQSGIARGYYDVATLDAMHERLRTL 75
Cdd:PRK05446   3 KILFIDRDGtlieepPTDFQVDSLDKLAFE----PGVIPALLKLQKAGYKLVMVTNQDGLGTDSFPQEDFDPPHNLMMQI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518524211  76 VAEQGGEVGLIVYCPHGPDEGCDCRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQ 140
Cdd:PRK05446  79 FESQGIKFDEVLICPHFPEDNCSCRKPKTGLVEEYLAEGAIDLANSYVIGDRETDVQLAENMGIK 143
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
28-174 6.37e-17

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 74.58  E-value: 6.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  28 PLPGSIDAIAQLSKAGWTVAVATNqsgiargyydvatldAMHERLRTLVAEqggeVGLIVYCPH--GPDEGCDcRKPKPG 105
Cdd:COG0546   85 LFPGVRELLEALKARGIKLAVVTN---------------KPREFAERLLEA----LGLDDYFDAivGGDDVPP-AKPKPE 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518524211 106 MLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKTQGLTLPVgTLIFDDLAAIAAEL 174
Cdd:COG0546  145 PLLEALERLGLDPEEVLMVGDSPHDIEAARAAGVPFIGVTWGYGSAEELEAAGA-DYVIDSLAELLALL 212
Hydrolase_like pfam13242
HAD-hyrolase-like;
99-168 1.81e-12

HAD-hyrolase-like;


Pssm-ID: 433056 [Multi-domain]  Cd Length: 75  Bit Score: 59.55  E-value: 1.81e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518524211   99 CRKPKPGMLKTIAAHYDVALTNLWFVGDSLG-DLEAAKAVDCQPVLVKTGKGEKTQGLTLPV-GTLIFDDLA 168
Cdd:pfam13242   2 CGKPNPGMLERALARLGLDPERTVMIGDRLDtDILGAREAGARTILVLTGVTRPADLEKAPIrPDYVVDDLA 73
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 17-174 2.98e-10

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: 56.96  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  17 DAYIKSVEEWIPL-PGSIDAIAQLSKAGWTVAVATNqsgiargyydvATLDAMHERLRTLvaeqggevGL-------IVY 88
Cdd:COG1011   82 EAFLAALPELVEPyPDALELLEALKARGYRLALLTN-----------GSAELQEAKLRRL--------GLddlfdavVSS 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  89 CPHGpdegcdCRKPKPGMLKTIAAHYDVALTNLWFVGDSL-GDLEAAKAVDCQPVLVkTGKGEKTQGLTLPvgTLIFDDL 167
Cdd:COG1011  143 EEVG------VRKPDPEIFELALERLGVPPEEALFVGDSPeTDVAGARAAGMRTVWV-NRSGEPAPAEPRP--DYVISDL 213


                 ....*..
gi 518524211 168 AAIAAEL 174
Cdd:COG1011  214 AELLELL 220
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 33-144 3.55e-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: 49.32  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  33 IDAIAQLSKAGWTVAVATNQSgiargyydvatLDAMHERLRTLVAEQGGEVGLIVycphgpdEGCDCRKPKPGMLKTIAA 112
Cdd:cd01427   13 VELLKRLRAAGIKLAIVTNRS-----------REALRALLEKLGLGDLFDGIIGS-------DGGGTPKPKPKPLLLLLL 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518524211 113 HYDVALTNLWFVGDSLGDLEAAKAVDCQPVLV 144
Cdd:cd01427   75 KLGVDPEEVLFVGDSENDIEAARAAGGRTVAV 106
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-138 2.46e-07

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: 48.35  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211    4 LILDRDGVINYDSDAYIKSVEEWIPLPGSIDAIAQLSKAGWTVAVATNQSgiargyydvatldamhERLRTLVAEQGGEV 83
Cdd:pfam00702  75 LEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDN----------------PEAAEALLRLLGLD 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518524211   84 GLIVYCPHGPDEGCdcRKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVD 138
Cdd:pfam00702 139 DYFDVVISGDDVGV--GKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PNK3P pfam08645
Polynucleotide kinase 3 phosphatase; Polynucleotide kinase 3 phosphatases play a role in the ...
 30-129 3.78e-06

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: 44.56  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   30 PGSIDAIAQLSKAGWTVAVATNQSGIARGyyDVATLDAMHERLRTLVAEQGGEvgLIVYCPHGPDEgcdCRKPKPGMLKT 109
Cdd:pfam08645  32 PSVPEKLKKLHEDGYKIVIFTNQGGIGRK--GKKSLEKFKNKIEAILKKLGVP--LQVYAATKKDI---YRKPNTGMWDE 104

                          90       100
                  ....*....|....*....|....
gi 518524211  110 IAAHYD----VALTNLWFVGDSLG 129
Cdd:pfam08645 105 MKKDYNdgveIDLEKSFYVGDAAG 128
PRK13222 PRK13222
N-acetylmuramic acid 6-phosphate phosphatase MupP;
28-174 1.14e-05

N-acetylmuramic acid 6-phosphate phosphatase MupP;


Pssm-ID: 237310 [Multi-domain]  Cd Length: 226  Bit Score: 44.03  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  28 PLPGSIDAIAQLSKAGWTVAVATN-----------QSGIARgYYDVATldamherlrtlvaeqGGevglivycphgpdeg 96
Cdd:PRK13222  94 LYPGVKETLAALKAAGYPLAVVTNkptpfvaplleALGIAD-YFSVVI---------------GG--------------- 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  97 cDC---RKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVktgkgekTQGLTLPVG------TLIFDDL 167
Cdd:PRK13222 143 -DSlpnKKPDPAPLLLACEKLGLDPEEMLFVGDSRNDIQAARAAGCPSVGV-------TYGYNYGEPialsepDVVIDHF 214


                 ....*..
gi 518524211 168 AAIAAEL 174
Cdd:PRK13222 215 AELLPLL 221
PGP_bact TIGR01449
2-phosphoglycolate phosphatase, prokaryotic; PGP is an essential enzyme in the glycolate ...
 28-147 1.87e-05

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: 43.27  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   28 PLPGSIDAIAQLSKAGWTVAVATNQ-SGIARgyyDVATLDAMHERLRTLVaeqGGEvglivycphgpdeGCDCRKPKPGM 106
Cdd:TIGR01449  86 VFPGVEATLGALRAKGLRLGLVTNKpTPLAR---PLLELLGLAKYFSVLI---GGD-------------SLAQRKPHPDP 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 518524211  107 LKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTG 147
Cdd:TIGR01449 147 LLLAAERLGVAPQQMVYVGDSRVDIQAARAAGCPSVLLTYG 187
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-171 4.46e-05

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 42.40  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   1 MKLLILDRDGVInYDSDAyiksveewiPLPGSIDAIAQLSKAGWTVAVATN--------------QSGIARGYYDV---- 62
Cdd:COG0647    8 YDAFLLDLDGVL-YRGDE---------PIPGAVEALARLRAAGKPVLFLTNnssrtpedvaeklrRLGIPVAEDEIvtsg 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  63 -ATLDAMHER-------------LRTLVAEQGGEV-------------------------------GLIVYCPH----GP 93
Cdd:COG0647   78 dATAAYLAERhpgarvyvigeegLREELEEAGLTLvddeepdavvvgldrtftyeklaealrairrGAPFIATNpdrtVP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  94 DE------------------GCDCR---KPKPGMLKTIAAHYDVALTNLWFVGDSL-GDLEAAKAVDCQPVLVKTGKGEK 151
Cdd:COG0647  158 TEdglipgagalaaaleaatGGEPLvvgKPSPPIYELALERLGVDPERVLMVGDRLdTDILGANAAGLDTLLVLTGVTTA 237

                        250       260
                 ....*....|....*....|.
gi 518524211 152 TQGLTLPVG-TLIFDDLAAIA 171
Cdd:COG0647  238 EDLEAAPIRpDYVLDSLAELL 258
HAD_PGPase cd07512
haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter ...
 28-175 7.09e-05

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: 41.53  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  28 PLPGSIDAIAQLSKAGWTVAVATNQ-SGIARgyydvATLDAMHerLRTLVAeqggevgLIVycphgpdeGCDC---RKPK 103
Cdd:cd07512   87 PYPGVIEALERLRAAGWRLAICTNKpEAPAR-----ALLSALG--LADLFA-------AVV--------GGDTlpqRKPD 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518524211 104 PGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGEKtqgltlPVGTL----IFDDLAAIAAELI 175
Cdd:cd07512  145 PAPLRAAIRRLGGDVSRALMVGDSETDAATARAAGVPFVLVTFGYRHA------PVAELphdaVFSDFDALPDLLA 214
HAD_PGPase cd16417
Escherichia coli Gph phosphoglycolate phosphatase and related proteins; belongs to the ...
 100-170 4.74e-04

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: 39.14  E-value: 4.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518524211 100 RKPKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGKGE-KTQGLTLPvgTLIFDDLAAI 170
Cdd:cd16417  142 KKPDPAPLLHACEKLGIAPAQMLMVGDSRNDILAARAAGCPSVGLTYGYNYgEDIAASGP--DAVIDSLAEL 211
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 30-144 2.15e-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: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  30 PGSIDAIAQLSKAGWTVAVAtnqSGiarGYYDVAtlDAMHERLR-------TLVAEQG---GEV-GLIVYcphgpDEGcd 98
Cdd:COG0560   91 PGARELIAEHRAAGHKVAIV---SG---GFTFFV--EPIAERLGidhvianELEVEDGrltGEVvGPIVD-----GEG-- 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 518524211  99 crkpKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDcQPVLV 144
Cdd:COG0560  156 ----KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAG-LPVAV 196
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 4-75 2.87e-03

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 35.52  E-value: 2.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518524211    4 LILDRDGVINYDSDayiksveewiPLPGSIDAIAQLSKAGWTVAVATNQSGIARgyydvatlDAMHERLRTL 75
Cdd:pfam13344   1 FLFDIDGVLWRGGE----------PIPGAAEALRALRAAGKPVVFVTNNSSRSR--------EEYAEKLRKL 54
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
28-170 4.08e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 36.34  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211  28 PLPGSIDAIAQLSKAGWTVAVATNqsgiargyYDVATLDAMHERLR------TLVAeqGGEVglivycPHGpdegcdcrK 101
Cdd:COG0637   87 LIPGVVELLEALKEAGIKIAVATS--------SPRENAEAVLEAAGlldyfdVIVT--GDDV------ARG--------K 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518524211 102 PKPGMLKTIAAHYDVALTNLWFVGDSLGDLEAAKAVDCQPVLVKTGkgeKTQGLTLPVGTLIFDDLAAI 170
Cdd:COG0637  143 PDPDIYLLAAERLGVDPEECVVFEDSPAGIRAAKAAGMRVVGVPDG---GTAEEELAGADLVVDDLAEL 208
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 29-137 6.26e-03

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


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 35.45  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518524211   29 LPGSIDAIAQLSKAGWTVAVATNQSgiargyydvatldamhERLRTLVAEQGGEVGLIVYcPHGPDEGCdcRKPKPGMLK 108
Cdd:TIGR01549  75 IRGAADLLARLKSAGIKLGIISNGS----------------LRAQKLLLRLFGLGDYFEL-ILVSDEPG--SKPEPEIFL 135

                          90       100
                  ....*....|....*....|....*....
gi 518524211  109 TIAAHYDVALTNLwFVGDSLGDLEAAKAV 137
Cdd:TIGR01549 136 AALESLGVPPEVL-HVGDNLNDIEGARNA 163
 
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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