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Conserved domains on  [gi|88194322|ref|YP_499114|]
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hypothetical protein SAOUHSC_00542 [Staphylococcus aureus subsp. aureus NCTC 8325]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576297)

Cof-type HAD-IIB family hydrolase, part of the HAD (haloacid dehalogenase) family that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-282 2.59e-79

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: 240.57  E-value: 2.59e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHL 83
Cdd:cd07516   1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  84 NKSLVHKITNVLKDAGIYYQVYTSRA----IYTEDPQRDLDIYIDIaeragqhanverikngiqrridngtlkvvdnYDA 159
Cdd:cd07516  81 SKEDVKELEEFLRKLGIGINIYTNDDwadtIYEENEDDEIIKPAEI-------------------------------LDD 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 160 IENIPGELIMKILAFDGNLEKIDKASKILAES-PNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNL 238
Cdd:cd07516 130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 88194322 239 NDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:cd07516 210 NDLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-282 2.59e-79

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: 240.57  E-value: 2.59e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHL 83
Cdd:cd07516   1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  84 NKSLVHKITNVLKDAGIYYQVYTSRA----IYTEDPQRDLDIYIDIaeragqhanverikngiqrridngtlkvvdnYDA 159
Cdd:cd07516  81 SKEDVKELEEFLRKLGIGINIYTNDDwadtIYEENEDDEIIKPAEI-------------------------------LDD 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 160 IENIPGELIMKILAFDGNLEKIDKASKILAES-PNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNL 238
Cdd:cd07516 130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 88194322 239 NDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:cd07516 210 NDLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-280 1.40e-75

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 231.36  E-value: 1.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     5 IATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHLN 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    85 KSLVHKITNVLKDAGIYYQVYTSRAIYTEDPQRDLDIYIDIaeragqhanverikngiqrridNGTLKVVDNYDAIENIP 164
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKEL----------------------NYTKSFVPEIDDFELLE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   165 GELIMKILaFDGNLEKIDKASKILAESPN--LAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDLS 242
Cdd:pfam08282 139 DEDINKIL-ILLDEEDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIE 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 88194322   243 MLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:pfam08282 218 MLEAAGLGVAMGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-280 3.83e-63

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: 199.42  E-value: 3.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    84 NKSLVHKITNVLKDAGIYYQVYTSRAIYTEDPQRDldiYIDIAERAGQHANVERIKNgiqrridngtlkvvdnydaieNI 163
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPE---YFTIFKKFLGEPKLEVVDI---------------------QY 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   164 PGELIMKILAFDGNLEKIDKASKIL---AESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLND 240
Cdd:TIGR00099 137 LPDDILKILLLFLDPEDLDLLIEALnklELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMND 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 88194322   241 LSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:TIGR00099 217 IEMLEAAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-283 2.25e-62

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: 195.35  E-value: 2.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMST 80
Cdd:COG0561   1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  81 SHLNKSLVHKITNVLKDAGIYYQVYTSraiytedpqrdldiyidiaeragqhanverikngiqrridngtlkvvdnydai 160
Cdd:COG0561  81 RPLDPEDVREILELLREHGLHLQVVVR----------------------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 161 enipgelimkilafdgnlekidkaskilaespnlaissSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLND 240
Cdd:COG0561 108 --------------------------------------SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGND 149

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 88194322 241 LSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKL 283
Cdd:COG0561 150 LEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-282 5.59e-39

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 137.52  E-value: 5.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    2 IKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVP--Y-ICLNGAEV-RDETFNV 77
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdYcITNNGALVqKAADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   78 MSTSHLNKSLVHKITNVLKDAGIYYQVYTSRAIYTedPQRDLDIYIdIAEragqhANVERIkngiqrridngTLKvvdnY 157
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT--ANRDISYYT-VHE-----SFLTGI-----------PLV----F 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  158 DAIENI-PGELIMKILAFDgNLEKIDKA-SKILAES-PNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSI 234
Cdd:PRK10513 140 REVEKMdPNLQFPKVMMID-EPEILDAAiARIPAEVkERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAI 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 88194322  235 GDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10513 219 GDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-282 2.59e-79

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: 240.57  E-value: 2.59e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHL 83
Cdd:cd07516   1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  84 NKSLVHKITNVLKDAGIYYQVYTSRA----IYTEDPQRDLDIYIDIaeragqhanverikngiqrridngtlkvvdnYDA 159
Cdd:cd07516  81 SKEDVKELEEFLRKLGIGINIYTNDDwadtIYEENEDDEIIKPAEI-------------------------------LDD 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 160 IENIPGELIMKILAFDGNLEKIDKASKILAES-PNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNL 238
Cdd:cd07516 130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 88194322 239 NDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:cd07516 210 NDLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-280 1.40e-75

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 231.36  E-value: 1.40e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     5 IATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHLN 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    85 KSLVHKITNVLKDAGIYYQVYTSRAIYTEDPQRDLDIYIDIaeragqhanverikngiqrridNGTLKVVDNYDAIENIP 164
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKEL----------------------NYTKSFVPEIDDFELLE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   165 GELIMKILaFDGNLEKIDKASKILAESPN--LAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDLS 242
Cdd:pfam08282 139 DEDINKIL-ILLDEEDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIE 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 88194322   243 MLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:pfam08282 218 MLEAAGLGVAMGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-280 3.83e-63

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: 199.42  E-value: 3.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMSTSHL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    84 NKSLVHKITNVLKDAGIYYQVYTSRAIYTEDPQRDldiYIDIAERAGQHANVERIKNgiqrridngtlkvvdnydaieNI 163
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPE---YFTIFKKFLGEPKLEVVDI---------------------QY 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   164 PGELIMKILAFDGNLEKIDKASKIL---AESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLND 240
Cdd:TIGR00099 137 LPDDILKILLLFLDPEDLDLLIEALnklELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMND 216

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 88194322   241 LSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:TIGR00099 217 IEMLEAAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-283 2.25e-62

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: 195.35  E-value: 2.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMST 80
Cdd:COG0561   1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  81 SHLNKSLVHKITNVLKDAGIYYQVYTSraiytedpqrdldiyidiaeragqhanverikngiqrridngtlkvvdnydai 160
Cdd:COG0561  81 RPLDPEDVREILELLREHGLHLQVVVR----------------------------------------------------- 107

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 161 enipgelimkilafdgnlekidkaskilaespnlaissSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLND 240
Cdd:COG0561 108 --------------------------------------SGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGND 149

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 88194322 241 LSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKL 283
Cdd:COG0561 150 LEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-282 5.59e-39

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 137.52  E-value: 5.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    2 IKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVP--Y-ICLNGAEV-RDETFNV 77
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdYcITNNGALVqKAADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   78 MSTSHLNKSLVHKITNVLKDAGIYYQVYTSRAIYTedPQRDLDIYIdIAEragqhANVERIkngiqrridngTLKvvdnY 157
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT--ANRDISYYT-VHE-----SFLTGI-----------PLV----F 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  158 DAIENI-PGELIMKILAFDgNLEKIDKA-SKILAES-PNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSI 234
Cdd:PRK10513 140 REVEKMdPNLQFPKVMMID-EPEILDAAiARIPAEVkERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAI 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 88194322  235 GDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10513 219 GDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 3-283 2.19e-35

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: 126.57  E-value: 2.19e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   3 KLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVpYICLNGAEVRDETfNVMSTSH 82
Cdd:cd07517   1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFFEG-EVIYKNP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  83 LNKSLVHKITNVLKDAGIYYQVYTsraiytedpqrdldiyidiaeragqhanverikngiqrridngtlkvvdnydaien 162
Cdd:cd07517  79 LPQELVERLTEFAKEQGHPVSFYG-------------------------------------------------------- 102

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 163 ipgeliMKILAFDGNLEKidkasKILAESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDLS 242
Cdd:cd07517 103 ------QLLLFEDEEEEQ-----KYEELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIE 171

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 88194322 243 MLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKL 283
Cdd:cd07517 172 MLEAVGIGIAMGNAHEELKEIADYVTKDVDEDGILKALKHF 212
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 3-282 1.17e-33

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 123.60  E-value: 1.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    3 KLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGR------AFYEAQApvadtdLTVPYICLNGAEVRD-ETF 75
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRhhvaihPFYQALA------LDTPAICCNGTYLYDyQAK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   76 NVMSTSHLNKSLVHKITNVLKDAGIYYQVYTSRAIYTEDPqrdldiyidiaeragqHANVERIKNGI------QRRidng 149
Cdd:PRK10530  78 KVLEADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHP----------------TGHVIRTLNWAqtlppeQRP---- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  150 TLKVVDN-YDAIENIpgELIMKILAFDGNLEKIDKASKILAESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEM 228
Cdd:PRK10530 138 TFTQVDSlAQAARQV--NAIWKFALTHEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSM 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 88194322  229 KEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10530 216 KNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 3-276 1.16e-27

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: 105.36  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   3 KLIATDMDGTLLNAAHEISQPNIDAIKYA-QEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVrdetfnvmsts 81
Cdd:cd07518   1 KLIATDMDGTFLNDDKTYDHERFFAILDQlLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV----------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  82 hlnkslVHKITNVLKDagiyyqvytsraiytedpqrdldiyidiaeragqhanverikngiqrridngtlkvvdnyDAIE 161
Cdd:cd07518  70 ------YFKFTLNVPD------------------------------------------------------------EAAP 83

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 162 NIPGELIMKilaFDGNLEkidkaskilaespnlaISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDL 241
Cdd:cd07518  84 DIIDELNQK---FGGILR----------------AVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDI 144

                       250       260       270
                ....*....|....*....|....*....|....*
gi 88194322 242 SMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGV 276
Cdd:cd07518 145 EMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGV 179
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-285 9.50e-26

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 101.59  E-value: 9.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDEtfnvmst 80
Cdd:PRK01158   2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVG------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   81 shlnkslvhkitnvlkdagiyyqvYTSRAIYTEDPQRDLDIYIDIAERAGQhANVERIKNGIQRRIDNGTLKvvdnydai 160
Cdd:PRK01158  75 ------------------------FDGKRIFLGDIEECEKAYSELKKRFPE-ASTSLTKLDPDYRKTEVALR-------- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  161 ENIPGELIMKILA-FDGNLEKIDkaskilaespnlaisssSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLN 239
Cdd:PRK01158 122 RTVPVEEVRELLEeLGLDLEIVD-----------------SGFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSEN 184

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 88194322  240 DLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKLLR 285
Cdd:PRK01158 185 DLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLLL 230
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-253 1.54e-19

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: 84.35  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     4 LIATDMDGTLLN-AAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDetfnvmstsh 82
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFY---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    83 lnkslvhkitnvlkDAGIYYQVYTSRAIYTEDPQRDlDIYiDIAERAGQHANVERIKNgiqrridngtLKVVDNYDAIEN 162
Cdd:TIGR01484  71 --------------PGEILYIEPSDVFEEILGIKFE-EIG-AELKSLSEHYVGTFIED----------KAIAVAIHYVGA 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   163 IPG-ELIMKIlafdgnlekIDKASKILAESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDL 241
Cdd:TIGR01484 125 ELGqELDSKM---------RERLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDE 195

                         250
                  ....*....|..
gi 88194322   242 SMLEKVGYPVAM 253
Cdd:TIGR01484 196 EMFEVAGLAVAV 207
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 2-280 4.69e-19

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: 83.25  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     2 IKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDEtfnvmsts 81
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIFYN-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    82 HLNKSLVHKITNVLKDagiyyqvytsraiytedpqrdldiyidiaERAGQHANVERIKNGIQRridngtlkvvdnydaie 161
Cdd:TIGR01487  73 KEDIFLANMEEEWFLD-----------------------------EEKKKRFPRDRLSNEYPR----------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   162 nipgelimKILAFDGNLEKIDKASKIlAESPNLAISSSsRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDL 241
Cdd:TIGR01487 107 --------ASLVIMREGKDVDEVREI-IKERGLNLVAS-GFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDI 176

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 88194322   242 SMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:TIGR01487 177 DLFRVVGFKVAVANADDQLKEIADYVTSNPYGEGVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 213-284 1.92e-18

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: 79.56  E-value: 1.92e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88194322 213 KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKLL 284
Cdd:cd07514  68 KGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-285 2.23e-16

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: 76.35  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322     5 IATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRA--FYEA---QAPVADtdltvPYICLNGAEVRDEtfnvms 79
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSvqFARAlakLIGTPD-----PVIAENGGEISYN------ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    80 tshlnkslvhkitnvlkdagiyyqvYTSRAIYTEDPQRDLDIYIDIAERAGqhanVERIKNGIQRRidngtlkvvdnyda 159
Cdd:TIGR01482  70 -------------------------EGLDDIFLAYLEEEWFLDIVIAKTFP----FSRLKVQYPRR-------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   160 ienipgelimKILAFDGNLEKIDKASKILAESPNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDNLN 239
Cdd:TIGR01482 107 ----------ASLVKMRYGIDVDTVREIIKELGLNLVAVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSEN 176

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 88194322   240 DLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKLLR 285
Cdd:TIGR01482 177 DIDLFEVPGFGVAVANAQPELKEWADYVTESPYGEGGAEAIGEILQ 222
PLN02887 PLN02887
hydrolase family protein
 3-280 1.32e-15

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 76.45  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    3 KLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAfyeaqapvadtdltvpyiclngaevRDETFNVMSTSH 82
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKA-------------------------RPAVIDILKMVD 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   83 LNKSlvhkiTNVLKDA--GIYYQ---VY--TSRAIYTEDpqRDLDIYIDIAERAGQHaNVERIKNGIQRRIDNGTLKVVD 155
Cdd:PLN02887 364 LAGK-----DGIISESspGVFLQgllVYgrQGREIYRSN--LDQEVCREACLYSLEH-KIPLIAFSQDRCLTLFDHPLVD 435

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  156 NYDAIENIPGELIMKilAFDGNLEKIDKASKILAESPNlAISSS----------SRGNI--------EITHSDAQKGIAL 217
Cdd:PLN02887 436 SLHTIYHEPKAEIMS--SVDQLLAAADIQKVIFLDTAE-GVSSVlrpywseatgDRANVvqaqpdmlEIVPPGTSKGNGV 512

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88194322  218 ETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAI 280
Cdd:PLN02887 513 KMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 213-271 3.24e-13

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 66.23  E-value: 3.24e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 88194322 213 KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTN 271
Cdd:COG1778  84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKP 142
PRK15126 PRK15126
HMP-PP phosphatase;
1-255 7.42e-13

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 67.03  E-value: 7.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMST 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   81 SHLNKSLVHKITNVLKDAGIYYQVYTSRAIYTEDpqrdldiyiDIAERAGQHanverikngiqrRIDNGTLKVVDnydaI 160
Cdd:PRK15126  81 QDLPADVAELVLHQQWDTRASMHVFNDDGWFTGK---------EIPALLQAH------------VYSGFRYQLID----L 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  161 ENIPGELIMKILAFDGNLEKID---KASKILAESPNLAIssSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMSIGDN 237
Cdd:PRK15126 136 KRLPAHGVTKICFCGDHDDLTRlqiQLNEALGERAHLCF--SATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDA 213

                        250
                 ....*....|....*...
gi 88194322  238 LNDLSMLEKVGYPVAMEN 255
Cdd:PRK15126 214 MNDREMLGSVGRGFIMGN 231
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-287 2.55e-11

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 62.65  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVrdetfnvmst 80
Cdd:PRK00192   3 MKLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAI---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   81 sHLNKSLVHKITNVLKDAGIYYQVYTSRAiYTEdpqrdldiyidiaeragqhanVERIKNGIQRRIDnGTLKVVDNYDA- 159
Cdd:PRK00192  73 -YIPKNYFPFQPDGERLKGDYWVIELGPP-YEE---------------------LREILDEISDELG-YPLKGFGDLSAe 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  160 -IENI---PGELI-----------MKILAFDGNLEKIdkasKILAESPNLAIsssSRGNIEIT-HSDAQKGIALETIAER 223
Cdd:PRK00192 129 eVAELtglSGESArlakdrefsepFLWNGSEAAKERF----EEALKRLGLKV---TRGGRFLHlLGGGDKGKAVRWLKEL 201

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88194322  224 LGIEMK-EVMSIGDNLNDLSMLEKVGYPVAMEN----GAEEVKKIAKY-VTDTNENSGVG--KAIMKLLREQ 287
Cdd:PRK00192 202 YRRQDGvETIALGDSPNDLPMLEAADIAVVVPGpdgpNPPLLPGIADGeFILASAPGPEGwaEAINKLLSKL 273
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 213-268 5.33e-11

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. 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: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 59.46  E-value: 5.33e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 88194322 213 KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVT 268
Cdd:cd01630  77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 205-288 1.03e-09

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 55.99  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   205 EITHSDAQKGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSGVGKAIMKLL 284
Cdd:TIGR01670  69 HLYQGQSNKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELL 148


                  ....
gi 88194322   285 REQQ 288
Cdd:TIGR01670 149 LLAQ 152
PRK10976 PRK10976
putative hydrolase; Provisional
 1-263 1.22e-09

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 57.75  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322    1 MIKLIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGAEVRDETFNVMST 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   81 SHLNKSLVHKITNVLKD-AGIYYQVYtsraiytedpqRDLDIYIdiaeragqhaNVERIKngiQRRIDNGTlkvVDNYDA 159
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDnPDIITNVY-----------RDDEWFM----------NRHRPE---EMRFFKEA---VFKYQL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  160 IE--NIPGELIMKILAFDGNLEK-IDKASKILA---ESPNlaISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMS 233
Cdd:PRK10976 134 YEpgLLEPDGVSKVFFTCDSHEKlLPLEQAINArwgDRVN--VSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIA 211

                        250       260       270
                 ....*....|....*....|....*....|
gi 88194322  234 IGDNLNDLSMLEKVGYPVAMENGAEEVKKI 263
Cdd:PRK10976 212 FGDGMNDAEMLSMAGKGCIMGNAHQRLKDL 241
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 202-264 1.88e-09

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: 56.38  E-value: 1.88e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88194322 202 GNIEITHSDAQ-KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMeNGAEEVKKIA 264
Cdd:COG0560 144 GEVVGPIVDGEgKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAA 206
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 4-251 2.34e-06

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 47.74  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGA--------EVRDETF 75
Cdd:cd07507   1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGaifiprgyFKFPGRC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  76 N--------VMSTSHlnKSLVHKITNVLKDAGIyyqVYTSRAIYTEDP-QRDLDIYIDIAERAGQHANVERIkngIQRRI 146
Cdd:cd07507  81 KseggyeviELGKPY--REIRAALEKIREETGF---KITGFGDLTEEEiAELTGLPRERAALAKEREYSETI---ILRSD 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 147 DNGTLKVVDNYDAIenipGELIMKILAF----DGNLEKiDKASKILAEspnlaissssrgnieithsdaqkgialetIAE 222
Cdd:cd07507 153 EEEDEKVLEALEER----GLKITKGGRFyhvlGAGADK-GKAVAILAA-----------------------------LYR 198

                       250       260
                ....*....|....*....|....*....
gi 88194322 223 RLGiEMKEVMSIGDNLNDLSMLEKVGYPV 251
Cdd:cd07507 199 QLY-EAIVTVGLGDSPNDLPMLEAVDIAF 226
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 4-68 5.66e-06

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 46.63  E-value: 5.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88194322     4 LIATDMDGTLLNAAHEISQPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGA 68
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGG 65
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 210-252 7.42e-06

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 45.62  E-value: 7.42e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 88194322 210 DAQ-KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVA 252
Cdd:cd07500 134 DAQrKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 4-68 8.31e-06

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 46.36  E-value: 8.31e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88194322   4 LIATDMDGTLLNaAHEIS-QPNIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTVPYICLNGA 68
Cdd:COG3769   5 LVFTDLDGTLLD-HDTYSwAAALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGA 69
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 4-275 1.16e-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: 42.72  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322   4 LIATDMDGTLLnaAHEISQPNIDAIKYAQEQ-----GITVVIATGRAFYEAQAPVADTDLTVPyiclngaevrDETFNVM 78
Cdd:cd02605   1 LLVSDLDETLV--GHDTNLQALERLQDLLEQltadnDVILVYATGRSPESVLELIKEVMLPKP----------DFIISDV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322  79 STShlnkslvhkitnvlkdagIYY---QVYTSRAIYTE--DPQRDLDIYIDIAeragqhANVERIKNgiQRRIDNGTLKV 153
Cdd:cd02605  69 GTE------------------IYYgesGYLEPDTYWNEvlSEGWERFLFEAIA------DLFKQLKP--QSELEQNPHKI 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88194322 154 vdNYdaieNIPGELIMKILAfdgNLEKIDKASKILAespNLAISSSSRGNIEITHSDAQKGIALETIAERLGIEMKEVMS 233
Cdd:cd02605 123 --SF----YLDPQNDAAVIE---QLEEMLLKAGLTV---RIIYSSGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLV 190

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 88194322 234 IGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTNENSG 275
Cdd:cd02605 191 CGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKG 232
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 4-71 5.79e-04

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: 38.53  E-value: 5.79e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88194322   4 LIATDMDGTLLNaaheisqpnIDAIKYAQEQGITVVIATGRAFYEAQAPVADTDLTV---PYICLNGAEVR 71
Cdd:cd01427   1 AVLFDLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDlfdGIIGSDGGGTP 62
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
206-271 1.08e-03

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 39.14  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88194322  206 ITH-----SDaqKGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMENGAEEVKKIAKYVTDTN 271
Cdd:PRK09484  87 ITHlyqgqSN--KLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIA 155
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 213-248 1.22e-03

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: 39.11  E-value: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 88194322   213 KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVG 248
Cdd:pfam00702 156 KPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 202-264 1.52e-03

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 38.88  E-value: 1.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88194322   202 GNIEITHSDAQ-KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVAMeNGAEEVKKIA 264
Cdd:TIGR00338 141 GLVEGPIVDASyKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKA 203
serB PRK11133
phosphoserine phosphatase; Provisional
 210-252 4.73e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.01  E-value: 4.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 88194322  210 DAQ-KGIALETIAERLGIEMKEVMSIGDNLNDLSMLEKVGYPVA 252
Cdd:PRK11133 245 DAQyKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
 
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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