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Conserved domains on  [gi|499623336|ref|WP_011304070|]
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MULTISPECIES: HAD-IIB family hydrolase [Staphylococcus]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 3-233 8.63e-34

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member pfam08282:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 255  Bit Score: 122.73  E-value: 8.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNGSLI-LSKGKIIKSVSFS 81
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIyDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   82 LSEMEKIKQLINEFDATYLI--DGDWdYAYTGPQNHSILKNLDPLNSANLVNLDSL----KSVVKVLILTSSNN-----E 150
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLytDDGV-YILNDNELEKILKELNYTKSFVPEIDDFElledEDINKILILLDEEDldeleK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  151 LLSKKLNELDVYVNKHGneNVLDISPKGIHKWAAL----KMLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRS 225
Cdd:pfam08282 160 ELKELFGSLITITSSGP--GYLEIMPKGVSKGTALkalaKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNaSPEVKA 237


                  ....*...
gi 499623336  226 FAKEFIES 233
Cdd:pfam08282 238 AADYVTDS 245
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 3-233 8.63e-34

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 122.73  E-value: 8.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNGSLI-LSKGKIIKSVSFS 81
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIyDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   82 LSEMEKIKQLINEFDATYLI--DGDWdYAYTGPQNHSILKNLDPLNSANLVNLDSL----KSVVKVLILTSSNN-----E 150
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLytDDGV-YILNDNELEKILKELNYTKSFVPEIDDFElledEDINKILILLDEEDldeleK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  151 LLSKKLNELDVYVNKHGneNVLDISPKGIHKWAAL----KMLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRS 225
Cdd:pfam08282 160 ELKELFGSLITITSSGP--GYLEIMPKGVSKGTALkalaKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNaSPEVKA 237


                  ....*...
gi 499623336  226 FAKEFIES 233
Cdd:pfam08282 238 AADYVTDS 245
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 3-233 1.14e-30

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 114.67  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNG-SLILSKGKIIKSVSFS 81
Cdd:TIGR00099   2 IFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGaAVIDDQGEILYKKPLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   82 LSEMEKIKQLINEFDATYLIDGDWDYAYTGPQNH--SILKNLDPLNSANLVNLDSLKS-VVKVLILTSSNNELLS----K 154
Cdd:TIGR00099  82 LDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEyfTIFKKFLGEPKLEVVDIQYLPDdILKILLLFLDPEDLDLlieaL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  155 KLNELDVYVNKHG-NENVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENALYTV-MVGHHEELRSFAK 228
Cdd:TIGR00099 162 NKLELEENVSVVSsGPYSIEITAKGVSKGSALQSLaealGISLEDVIAFGDGMNDIEMLEAAGYGVaMGNADEELKALAD 241


                  ....*
gi 499623336  229 EFIES 233
Cdd:TIGR00099 242 YVTDS 246
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-248 3.68e-26

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 100.98  E-value: 3.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISK-DFHDYtMIGGNGSLILS-KGKIIKSVSF 80
Cdd:COG0561    5 IALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEElGLDDP-LITSNGALIYDpDGEVLYERPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  81 SLSEMEKIKQLINEFDatylidgdwdyaytgpqnhsilknldplnsanlvnldslksvVKVLILTSSnnellskklneld 160
Cdd:COG0561   84 DPEDVREILELLREHG------------------------------------------LHLQVVVRS------------- 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336 161 vyvnkhgNENVLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRSFAKEFIESeg 235
Cdd:COG0561  109 -------GPGFLEILPKGVSKGSALKklaeRLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNaPPEVKAAADYVTGS-- 179

                        250
                 ....*....|...
gi 499623336 236 NLELKIVEKIEEI 248
Cdd:COG0561  180 NDEDGVAEALEKL 192
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-211 6.40e-24

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 96.51  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   4 VFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISK-DFHDYtMIGGNGSLILSK-GKIIKSVSFS 81
Cdd:cd07516    3 ALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEElGLDSP-LITFNGALVYDPtGKEILERLIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  82 LSEMEKIKQLINEFDAT---YLIDGDWDYAYTGPQNHSILKNLDPLNsanLVNLDSLKSVVKVLILTSSNN--ELLSKKL 156
Cdd:cd07516   82 KEDVKELEEFLRKLGIGiniYTNDDWADTIYEENEDDEIIKPAEILD---DLLLPPDEDITKILFVGEDEEldELIAKLP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499623336 157 NEL--DVYVNKhGNENVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENA 211
Cdd:cd07516  159 EEFfdDLSVVR-SAPFYLEIMPKGVSKGNALKKLaeylGISLEEVIAFGDNENDLSMLEYA 218
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-218 7.97e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 42.65  E-value: 7.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   1 MKF---VFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASArpirDMLPVI---SKdfhdytMIGGNGSLILSKGKI 74
Cdd:PRK01158   1 MKIkaiAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATG----NVLCFAraaAK------LIGTSGPVIAENGGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  75 IKSvsfslsemekikqlinEFDATYLIDGDWDYAYTGpqnHSILKNLDPLNSANLVNLDSLKSVVKVLILTSSNNELLSK 154
Cdd:PRK01158  71 ISV----------------GFDGKRIFLGDIEECEKA---YSELKKRFPEASTSLTKLDPDYRKTEVALRRTVPVEEVRE 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499623336 155 KLNELDVYVNKHGNENVLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVG 218
Cdd:PRK01158 132 LLEELGLDLEIVDSGFAIHIKSPGVNKGTGLKklaeLMGIDPEEVAAIGDSENDLEMFEVAGFGVAVA 199
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 3-233 8.63e-34

haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 122.73  E-value: 8.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNGSLI-LSKGKIIKSVSFS 81
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIyDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   82 LSEMEKIKQLINEFDATYLI--DGDWdYAYTGPQNHSILKNLDPLNSANLVNLDSL----KSVVKVLILTSSNN-----E 150
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLytDDGV-YILNDNELEKILKELNYTKSFVPEIDDFElledEDINKILILLDEEDldeleK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  151 LLSKKLNELDVYVNKHGneNVLDISPKGIHKWAAL----KMLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRS 225
Cdd:pfam08282 160 ELKELFGSLITITSSGP--GYLEIMPKGVSKGTALkalaKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNaSPEVKA 237


                  ....*...
gi 499623336  226 FAKEFIES 233
Cdd:pfam08282 238 AADYVTDS 245
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 3-233 1.14e-30

Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272905 [Multi-domain]  Cd Length: 256  Bit Score: 114.67  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNG-SLILSKGKIIKSVSFS 81
Cdd:TIGR00099   2 IFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGaAVIDDQGEILYKKPLD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   82 LSEMEKIKQLINEFDATYLIDGDWDYAYTGPQNH--SILKNLDPLNSANLVNLDSLKS-VVKVLILTSSNNELLS----K 154
Cdd:TIGR00099  82 LDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEyfTIFKKFLGEPKLEVVDIQYLPDdILKILLLFLDPEDLDLlieaL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  155 KLNELDVYVNKHG-NENVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENALYTV-MVGHHEELRSFAK 228
Cdd:TIGR00099 162 NKLELEENVSVVSsGPYSIEITAKGVSKGSALQSLaealGISLEDVIAFGDGMNDIEMLEAAGYGVaMGNADEELKALAD 241


                  ....*
gi 499623336  229 EFIES 233
Cdd:TIGR00099 242 YVTDS 246
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-248 3.68e-26

Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440327 [Multi-domain]  Cd Length: 192  Bit Score: 100.98  E-value: 3.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISK-DFHDYtMIGGNGSLILS-KGKIIKSVSF 80
Cdd:COG0561    5 IALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEElGLDDP-LITSNGALIYDpDGEVLYERPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  81 SLSEMEKIKQLINEFDatylidgdwdyaytgpqnhsilknldplnsanlvnldslksvVKVLILTSSnnellskklneld 160
Cdd:COG0561   84 DPEDVREILELLREHG------------------------------------------LHLQVVVRS------------- 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336 161 vyvnkhgNENVLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRSFAKEFIESeg 235
Cdd:COG0561  109 -------GPGFLEILPKGVSKGSALKklaeRLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNaPPEVKAAADYVTGS-- 179

                        250
                 ....*....|...
gi 499623336 236 NLELKIVEKIEEI 248
Cdd:COG0561  180 NDEDGVAEALEKL 192
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-211 6.40e-24

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-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, 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: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 96.51  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   4 VFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISK-DFHDYtMIGGNGSLILSK-GKIIKSVSFS 81
Cdd:cd07516    3 ALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEElGLDSP-LITFNGALVYDPtGKEILERLIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  82 LSEMEKIKQLINEFDAT---YLIDGDWDYAYTGPQNHSILKNLDPLNsanLVNLDSLKSVVKVLILTSSNN--ELLSKKL 156
Cdd:cd07516   82 KEDVKELEEFLRKLGIGiniYTNDDWADTIYEENEDDEIIKPAEILD---DLLLPPDEDITKILFVGEDEEldELIAKLP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499623336 157 NEL--DVYVNKhGNENVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENA 211
Cdd:cd07516  159 EEFfdDLSVVR-SAPFYLEIMPKGVSKGNALKKLaeylGISLEEVIAFGDNENDLSMLEYA 218
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 3-217 1.70e-13

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 67.41  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTIC-FKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNGSLILSKGKI--IKSVS 79
Cdd:TIGR01484   2 LFFDLDGTLLdPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEIlyIEPSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   80 FSLSEMEKIKQLINEFdaTYLIDGDWDyaYTGPQNHSILKNLDP-LNSANLVNLDSLKSVVKVLILTssnnellskkLNE 158
Cdd:TIGR01484  82 VFEEILGIKFEEIGAE--LKSLSEHYV--GTFIEDKAIAVAIHYvGAELGQELDSKMRERLEKIGRN----------DLE 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499623336  159 LDVYVNkhgNENVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENALYTVMV 217
Cdd:TIGR01484 148 LEAIYS---GKTDLEVLPAGVNKGSALQALlqelNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 5-228 2.64e-09

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 55.69  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   5 FDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPiRDMLPVISKDFHDYTMIGGNGSLILSKGKIIKSVSFSLSE 84
Cdd:cd07517    5 FDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRA-PFEIQPIVKALGIDSYVSYNGQYVFFEGEVIYKNPLPQEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  85 MEKIKQLINEFDAtylidgdwDYAYtgpqnhsilknldplnsanlvnldslksvvkvliltsSNNELLSKKLNELDVYVN 164
Cdd:cd07517   84 VERLTEFAKEQGH--------PVSF-------------------------------------YGQLLLFEDEEEEQKYEE 118

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499623336 165 KHG-------NENVLDISPKGIHKWAALKM----LGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRSFAK 228
Cdd:cd07517  119 LRPelrfvrwHPLSTDVIPKGGSKAKGIQKviehLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNaHEELKEIAD 194
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-211 3.79e-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: 49.12  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    3 FVFDLDGTICfKGEPVSDKILNslknLTNSGHQVIFASARPIRDMLPVIskdfHDYTMIGGNGSLILSKgkiiksvsfSL 82
Cdd:pfam00702   4 VVFDLDGTLT-DGEPVVTEAIA----ELASEHPLAKAIVAAAEDLPIPV----EDFTARLLLGKRDWLE---------EL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   83 SEMEKIKQLINEFDATyLIDGDWDYAYTGPQNHSILKNLDPLnsanlvnLDSLKSV-VKVLILTSSNNELLSKKLNELDV 161
Cdd:pfam00702  66 DILRGLVETLEAEGLT-VVLVELLGVIALADELKLYPGAAEA-------LKALKERgIKVAILTGDNPEAAEALLRLLGL 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 499623336  162 YvnkHGNENVLDISPKGIHKW------AALKMLGIDKGDYIAFGNDSNDISMFENA 211
Cdd:pfam00702 138 D---DYFDVVISGDDVGVGKPkpeiylAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 170-233 2.97e-06

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


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 46.42  E-value: 2.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499623336 170 NVLDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENALYT-VMVGHHEELRSFAKEFIES 233
Cdd:cd07518  105 GSIDIIPPGVNKATGLKQLlkhwGISPDEVMAFGDGGNDIEMLKYAGYSyAMENAPEEVKAAAKYVAPS 173
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 6-218 8.41e-06

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 45.50  E-value: 8.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336    6 DLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIrdmlPVISKDfhdYTMIGGNGSLILSKGKII--KSVSFSLS 83
Cdd:TIGR01487   7 DIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTV----PFARAL---AVLIGTSGPVVAENGGVIfyNKEDIFLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   84 EMEKIKQLINEFDATYLIDgDWDYAYtgpqnhsilknldplnsanlvnldslKSVVKVLILTSSNNELLSKKLNELDVYV 163
Cdd:TIGR01487  80 NMEEEWFLDEEKKKRFPRD-RLSNEY--------------------------PRASLVIMREGKDVDEVREIIKERGLNL 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499623336  164 NKHGNEnvLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVG 218
Cdd:TIGR01487 133 VASGFA--IHIMKKGVDKGVGVEklkeLLGIKPEEVAAIGDSENDIDLFRVVGFKVAVA 189
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 146-249 1.79e-05

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 44.76  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  146 SSNNELLSKKLNELDVYVNKHGNENVLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-H 220
Cdd:TIGR01482 115 GIDVDTVREIIKELGLNLVAVDSGFDIHILPQGVNKGVAVKklkeKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANaQ 194

                          90       100       110
                  ....*....|....*....|....*....|..
gi 499623336  221 EELRSFAKEFIES---EGNLElKIVEKIEEIA 249
Cdd:TIGR01482 195 PELKEWADYVTESpygEGGAE-AIGEILQAIG 225
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-218 7.97e-05

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 42.65  E-value: 7.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   1 MKF---VFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASArpirDMLPVI---SKdfhdytMIGGNGSLILSKGKI 74
Cdd:PRK01158   1 MKIkaiAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATG----NVLCFAraaAK------LIGTSGPVIAENGGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336  75 IKSvsfslsemekikqlinEFDATYLIDGDWDYAYTGpqnHSILKNLDPLNSANLVNLDSLKSVVKVLILTSSNNELLSK 154
Cdd:PRK01158  71 ISV----------------GFDGKRIFLGDIEECEKA---YSELKKRFPEASTSLTKLDPDYRKTEVALRRTVPVEEVRE 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499623336 155 KLNELDVYVNKHGNENVLDISPKGIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVG 218
Cdd:PRK01158 132 LLEELGLDLEIVDSGFAIHIKSPGVNKGTGLKklaeLMGIDPEEVAAIGDSENDLEMFEVAGFGVAVA 199
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
 149-233 1.09e-04

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 43.37  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336 149 NEL---LSKKLNELDVYV---NKhgnenVLDISPKGIHKW-AALKMLGIDKGDYI-AFGNDSNDISMFEnAL----YTVM 216
Cdd:PRK14501 625 NELilaLSSLLSNAPLEVlrgNK-----VVEVRPAGVNKGrAVRRLLEAGPYDFVlAIGDDTTDEDMFR-ALpetaITVK 698

                         90       100
                 ....*....|....*....|....*...
gi 499623336 217 VGH-----------HEELRSFAKEFIES 233
Cdd:PRK14501 699 VGPgesraryrlpsQREVRELLRRLLDI 726
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 178-228 2.82e-04

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 39.88  E-value: 2.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499623336 178 GIHKWAALK----MLGIDKGDYIAFGNDSNDISMFENALYTVMVGH-HEELRSFAK 228
Cdd:cd07514   65 GVDKGTGLEklaeRLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANaDEELKEAAD 120
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 172-248 2.95e-04

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. 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: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 41.18  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336 172 LDISPKGIHKWAALKML----GIDKGDYIAFGNDSNDISMFENALYTVMVGHH-EELRSFAKE---FIESEGNLELKIVE 243
Cdd:cd02605  161 LDILPLGAGKGEALRYLqekwNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAqPELLKWADRvtrSRLAKGPYAGGILE 240


                 ....*
gi 499623336 244 KIEEI 248
Cdd:cd02605  241 GLAHF 245
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 139-211 1.29e-03

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: 37.38  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499623336 139 VKVLILTSSNNELLSKKLNELDVYVNKH---GNENVLDISPKGIHKWAALKMLGIDKGDYIAFGNDSNDISMFENA 211
Cdd:cd01427   24 IKLAIVTNRSREALRALLEKLGLGDLFDgiiGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAA 99
PRK15126 PRK15126
HMP-PP phosphatase;
5-70 1.87e-03

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 38.91  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499623336   5 FDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPIRDMLPVISKDFHDYTMIGGNGSLILS 70
Cdd:PRK15126   7 FDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHS 72
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 176-230 8.15e-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: 36.74  E-value: 8.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499623336 176 PKGIHKWAALkmLGIDKGDYIAFGNDSNDISMFENALYTVMVGHHEELRSFAKEF 230
Cdd:COG0560  157 AEALRELAAE--LGIDLEQSYAYGDSANDLPMLEAAGLPVAVNPDPALREAADRE 209
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 3-79 8.87e-03

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 35.64  E-value: 8.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499623336   3 FVFDLDGTICFKGEPVSDKILNSLKNLTNSGHQVIFASARPirdmLPVIskdFHDYTMIGGNGSLI-----LSKGKIIKS 77
Cdd:cd07514    2 IAVDIDGTLTDRRRSIDLRAIEAIRKLEKAGIPVVLVTGNS----LPVA---RALAKYLGLSGPVVaenggVDKGTGLEK 74


                 ..
gi 499623336  78 VS 79
Cdd:cd07514   75 LA 76
 
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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