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Conserved domains on  [gi|614086889|sp|P9WMV3|]
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RecName: Full=D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase; AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase; Short=HBP phosphatase

Protein Classification

HAD family hydrolase( domain architecture ID 11492994)

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
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 10-147 3.01e-68

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: 204.94  E-value: 3.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   10 WCLFLDRDGVINRQVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDG 89
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 614086889   90 VLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHPdSEPLLSIVVGDSLSDLELAHNV 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLG-VDASRSLVVGDRLRDLQAARNA 137
 
Name Accession Description Interval E-value
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 10-147 3.01e-68

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: 204.94  E-value: 3.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   10 WCLFLDRDGVINRQVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDG 89
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 614086889   90 VLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHPdSEPLLSIVVGDSLSDLELAHNV 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLG-VDASRSLVVGDRLRDLQAARNA 137
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 10-147 8.75e-61

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: 185.81  E-value: 8.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  10 WCLFLDRDGVINRQVvgDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDG 89
Cdd:cd07503    1 KALFLDRDGVINVDV--PYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 614086889  90 VLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLELAHNV 147
Cdd:cd07503   79 VEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKEL-GIDLARSFVIGDRLSDIQAARNA 135
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 9-179 7.51e-55

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: 171.82  E-value: 7.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   9 QWCLFLDRDGVINRQVvgDYVRNWRQFEWLPGAARALKKLRAwAPY-IVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLAS 87
Cdd:COG0241    3 KKAVFLDRDGTINEDV--GYVKSPEEFEFLPGVLEALARLNE-AGYrLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  88 DGVLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLELAHNVAAAAGACASVQIGGASSGGV 167
Cdd:COG0241   80 EGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERL-GIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEAL 158

                        170
                 ....*....|..
gi 614086889 168 ADASFDSLWEFA 179
Cdd:COG0241  159 PDTVADDLAEAV 170
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
12-144 1.58e-30

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 109.91  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  12 LFLDRDGVINRQVVGdYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGVL 91
Cdd:PRK08942   6 IFLDRDGVINVDSDG-YVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRGGR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 614086889  92 IDGFQVCPHHRSQRCGCRKPRPGLVLDwLGRHPDSEPLLSIVVGDSLSDLELA 144
Cdd:PRK08942  85 LDGIYYCPHHPEDGCDCRKPKPGMLLS-IAERLNIDLAGSPMVGDSLRDLQAA 136
 
Name Accession Description Interval E-value
Histidinol-ppas TIGR01656
histidinol-phosphate phosphatase family domain; This domain is found in authentic ...
 10-147 3.01e-68

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: 204.94  E-value: 3.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   10 WCLFLDRDGVINRQVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDG 89
Cdd:TIGR01656   1 PALFLDRDGVINEDTVSDYPRSLDDWQLRPGAVPALLTLRAAGYTVVVVTNQSGIGRGYFSAEAFRAPNGRLLELLRQLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 614086889   90 VLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHPdSEPLLSIVVGDSLSDLELAHNV 147
Cdd:TIGR01656  81 VAVDGVLFCPHHPADNCSCRKPKPGLILEALKRLG-VDASRSLVVGDRLRDLQAARNA 137
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 10-147 8.75e-61

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: 185.81  E-value: 8.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  10 WCLFLDRDGVINRQVvgDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDG 89
Cdd:cd07503    1 KALFLDRDGVINVDV--PYVHKPEDLEFLPGVIEALKKLKDAGYLVVVVTNQSGIARGYFSEADFEALHDKMRELLASQG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 614086889  90 VLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLELAHNV 147
Cdd:cd07503   79 VEIDDIYYCPHHPDDGCPCRKPKPGMLLDAAKEL-GIDLARSFVIGDRLSDIQAARNA 135
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 9-179 7.51e-55

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: 171.82  E-value: 7.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   9 QWCLFLDRDGVINRQVvgDYVRNWRQFEWLPGAARALKKLRAwAPY-IVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLAS 87
Cdd:COG0241    3 KKAVFLDRDGTINEDV--GYVKSPEEFEFLPGVLEALARLNE-AGYrLVVVTNQSGIGRGLFTEEDLNAVHAKMLELLAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  88 DGVLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLELAHNVAAAAGACASVQIGGASSGGV 167
Cdd:COG0241   80 EGGRIDAIYYCPHHPDDNCDCRKPKPGMLLQAAERL-GIDLSNSYMIGDRLSDLQAAKAAGCKGILVLTGKGAEELAEAL 158

                        170
                 ....*....|..
gi 614086889 168 ADASFDSLWEFA 179
Cdd:COG0241  159 PDTVADDLAEAV 170
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 10-147 8.98e-39

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: 8.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   10 WCLFLDRDGVINRQVvgDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSavdvMVIHRHLQMQLASDG 89
Cdd:TIGR01662   1 KAVVLDLDGTLTDDV--PYVSDEDERILYPEVPDALAELKEAGYKVVIVTNQSGIGRGYFS----RSFSGRVARRLEELG 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 614086889   90 VLIDGFQVCPHhrsqrcgCRKPRPGLVLDWLGRHPDSEPLLSIVVGD-SLSDLELAHNV 147
Cdd:TIGR01662  75 VPIDILYACPG-------CRKPKPGMFLEALKRFNEIDPEESVYVGDqDLTDLQAAKRV 126
PRK08942 PRK08942
D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
12-144 1.58e-30

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


Pssm-ID: 236354 [Multi-domain]  Cd Length: 181  Bit Score: 109.91  E-value: 1.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  12 LFLDRDGVINRQVVGdYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGVL 91
Cdd:PRK08942   6 IFLDRDGVINVDSDG-YVKSPDEWIPIPGSIEAIARLKQAGYRVVVATNQSGIARGLFTEAQLNALHEKMDWSLADRGGR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 614086889  92 IDGFQVCPHHRSQRCGCRKPRPGLVLDwLGRHPDSEPLLSIVVGDSLSDLELA 144
Cdd:PRK08942  85 LDGIYYCPHHPEDGCDCRKPKPGMLLS-IAERLNIDLAGSPMVGDSLRDLQAA 136
GmhB_yaeD TIGR00213
D,D-heptose 1,7-bisphosphate phosphatase; This family of proteins formerly designated yaeD ...
 12-175 9.27e-25

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: 94.99  E-value: 9.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   12 LFLDRDGVINrqVVGDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGVL 91
Cdd:TIGR00213   4 IFLDRDGTIN--IDHGYVHEIDNFEFIDGVIDALRELKKMGYALVLVTNQSGIARGYFTEAQFEQLTEWMDWSLAERDVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   92 IDGFQVCPHH------RSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLE--LAHNVAAAAGACASVQIGGAS 163
Cdd:TIGR00213  82 LDGIYYCPHHpegveeFRQVCDCRKPKPGMLLQARKEL-HIDMAQSYMVGDKLEDMQagVAAKVKTNVLVRTGKPITPEA 160

                         170
                  ....*....|..
gi 614086889  164 SgGVADASFDSL 175
Cdd:TIGR00213 161 E-NIADWVLNSL 171
PRK05446 PRK05446
bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;
12-146 2.34e-18

bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase HisB;


Pssm-ID: 235471 [Multi-domain]  Cd Length: 354  Bit Score: 80.99  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  12 LFLDRDGVINRQVVGDY-VRNWRQFEWLPGAARALKKLRAwAPY-IVVVTNQQGVGAGLMSAVDVMVIHRHLqMQ-LASD 88
Cdd:PRK05446   5 LFIDRDGTLIEEPPTDFqVDSLDKLAFEPGVIPALLKLQK-AGYkLVMVTNQDGLGTDSFPQEDFDPPHNLM-MQiFESQ 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 614086889  89 GVLIDGFQVCPHHRSQRCGCRKPRPGLVLDWLgrhpdSEPLL----SIVVGDSLSDLELAHN 146
Cdd:PRK05446  83 GIKFDEVLICPHFPEDNCSCRKPKTGLVEEYL-----AEGAIdlanSYVIGDRETDVQLAEN 139
hisB_Nterm TIGR01261
histidinol-phosphatase; This model describes histidinol phosphatase. All known examples in the ...
 12-147 5.60e-18

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: 76.67  E-value: 5.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889   12 LFLDRDGVINRQVVGDY-VRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDVMVIHRHLQMQLASDGV 90
Cdd:TIGR01261   4 LFIDRDGTLIEEPPSDFqVDALEKLRFEKGVIPALLKLKKAGYKFVMVTNQDGLGTPSFPQADFDGPHNLMLQIFRSQGI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 614086889   91 LIDGFQVCPHHRSQRCGCRKPRPGLVLDWLgRHPDSEPLLSIVVGDSLSDLELAHNV 147
Cdd:TIGR01261  84 IFDDVLICPHFPDDNCDCRKPKIKLLEPYL-KKNLIDKARSYVIGDRETDMQLAENL 139
PRK06769 PRK06769
HAD-IIIA family hydrolase;
12-147 3.35e-12

HAD-IIIA family hydrolase;


Pssm-ID: 180686 [Multi-domain]  Cd Length: 173  Bit Score: 61.67  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 614086889  12 LFLDRDGVINRQvvgDYVRNWRQFEWLPGAARALKKLRAWAPYIVVVTNQQGVGAGLMSAVDvmvihrhLQMQLASDGvl 91
Cdd:PRK06769   7 IFIDRDGTIGGD---TTIHYPGSFTLFPFTKASLQKLKANHIKIFSFTNQPGIADGIATIAD-------FVQELKGFG-- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 614086889  92 IDGFQVCPHHRSQRCGCRKPRPGLVLDWLGRHpDSEPLLSIVVGDSLSDLELAHNV 147
Cdd:PRK06769  75 FDDIYLCPHKHGDGCECRKPSTGMLLQAAEKH-GLDLTQCAVIGDRWTDIVAAAKV 129
 
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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