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Conserved domains on  [gi|394256717|gb|EJE01644|]
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Cof-like hydrolase [Staphylococcus epidermidis NIHLM040]

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 9.77e-78

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: 236.72  E-value: 9.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHL 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  84 NHDLVHKITTALKNNHIYYQIYTN----RGIYTEDPKRDLAIYIDIaeragqkadvakirnniqkridngtlkvvdnYDS 159
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINIYTNddwaDTIYEENEDDEIIKPAEI-------------------------------LDD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 160 IEDIPGELIMKVLAFDADLSKIDQVGQELASS-PNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNL 238
Cdd:cd07516  130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 394256717 239 NDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 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 9.77e-78

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: 236.72  E-value: 9.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHL 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  84 NHDLVHKITTALKNNHIYYQIYTN----RGIYTEDPKRDLAIYIDIaeragqkadvakirnniqkridngtlkvvdnYDS 159
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINIYTNddwaDTIYEENEDDEIIKPAEI-------------------------------LDD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 160 IEDIPGELIMKVLAFDADLSKIDQVGQELASS-PNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNL 238
Cdd:cd07516  130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 394256717 239 NDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 282
Cdd:cd07516  210 NDLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-280 1.00e-76

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 234.05  E-value: 1.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    5 IATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHLN 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   85 HDLVHKITTALKNNHIYYQIYTNRGIYTEDPKRDlaiyidiaeragqkadvakirnNIQKRIDNGTLKVVDNYDSIEDIP 164
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNEL----------------------EKILKELNYTKSFVPEIDDFELLE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  165 GELIMKVLaFDADLSKIDQVGQELASSPN--LAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDIS 242
Cdd:pfam08282 139 DEDINKIL-ILLDEEDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIE 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 394256717  243 MLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:pfam08282 218 MLEAAGLGVAMGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-283 6.25e-57

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: 181.49  E-value: 6.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMST 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  81 SHLNHDLVHKITTALKNNHIYYQIYTnrgiytedpkrdlaiyidiaeragqkadvakirnniqkridngtlkvvdnydsi 160
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQVVV------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 161 edipgelimkvlafdadlskidqvgqelasspnlavsSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLND 240
Cdd:COG0561  107 -------------------------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGND 149

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 394256717 241 ISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKI 283
Cdd:COG0561  150 LEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-280 8.18e-57

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: 183.24  E-value: 8.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   84 NHDLVHKITTALKNNHIYYQIYTNRGIYTedPKRDLAIYidiaeragqKADVAKIRNNIQKRIDNgtlkvvdNYDSIEDI 163
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYA--SKNDPEYF---------TIFKKFLGEPKLEVVDI-------QYLPDDIL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  164 pgeLIMKVLAFDADLSKIDQVGQELASSPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDISM 243
Cdd:TIGR00099 143 ---KILLLFLDPEDLDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEM 219

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 394256717  244 LERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:TIGR00099 220 LEAAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-282 9.88e-36

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 129.04  E-value: 9.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   2 IKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVP--Y-ICLNGAEV-RDESFNI 77
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdYcITNNGALVqKAADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  78 MSTSHLNHD---LVHKITTALKnnhIYYQIYTNRGIYTedPKRDLAIYIdIAEragqkADVAKIrnniqkridngTLKvv 154
Cdd:PRK10513  83 VAQTALSYDdylYLEKLSREVG---VHFHALDRNTLYT--ANRDISYYT-VHE-----SFLTGI-----------PLV-- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 155 dnYDSIEDI-PGELIMKVL------AFDADLSKIDQVGQElasspNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGID 227
Cdd:PRK10513 139 --FREVEKMdPNLQFPKVMmidepeILDAAIARIPAEVKE-----RYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIK 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394256717 228 LTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10513 212 PEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 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 9.77e-78

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: 236.72  E-value: 9.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHL 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  84 NHDLVHKITTALKNNHIYYQIYTN----RGIYTEDPKRDLAIYIDIaeragqkadvakirnniqkridngtlkvvdnYDS 159
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINIYTNddwaDTIYEENEDDEIIKPAEI-------------------------------LDD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 160 IEDIPGELIMKVLAFDADLSKIDQVGQELASS-PNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNL 238
Cdd:cd07516  130 LLLPPDEDITKILFVGEDEELDELIAKLPEEFfDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 394256717 239 NDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 282
Cdd:cd07516  210 NDLSMLEYAGLGVAMGNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-280 1.00e-76

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 234.05  E-value: 1.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    5 IATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHLN 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   85 HDLVHKITTALKNNHIYYQIYTNRGIYTEDPKRDlaiyidiaeragqkadvakirnNIQKRIDNGTLKVVDNYDSIEDIP 164
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNEL----------------------EKILKELNYTKSFVPEIDDFELLE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  165 GELIMKVLaFDADLSKIDQVGQELASSPN--LAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDIS 242
Cdd:pfam08282 139 DEDINKIL-ILLDEEDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIE 217

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 394256717  243 MLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:pfam08282 218 MLEAAGLGVAMGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-283 6.25e-57

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: 181.49  E-value: 6.25e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMST 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  81 SHLNHDLVHKITTALKNNHIYYQIYTnrgiytedpkrdlaiyidiaeragqkadvakirnniqkridngtlkvvdnydsi 160
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQVVV------------------------------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 161 edipgelimkvlafdadlskidqvgqelasspnlavsSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLND 240
Cdd:COG0561  107 -------------------------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGND 149

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 394256717 241 ISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKI 283
Cdd:COG0561  150 LEMLEAAGLGVAMGNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-280 8.18e-57

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: 183.24  E-value: 8.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMSTSHL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   84 NHDLVHKITTALKNNHIYYQIYTNRGIYTedPKRDLAIYidiaeragqKADVAKIRNNIQKRIDNgtlkvvdNYDSIEDI 163
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYA--SKNDPEYF---------TIFKKFLGEPKLEVVDI-------QYLPDDIL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  164 pgeLIMKVLAFDADLSKIDQVGQELASSPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDISM 243
Cdd:TIGR00099 143 ---KILLLFLDPEDLDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEM 219

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 394256717  244 LERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:TIGR00099 220 LEAAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-282 9.88e-36

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 129.04  E-value: 9.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   2 IKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVP--Y-ICLNGAEV-RDESFNI 77
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdYcITNNGALVqKAADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  78 MSTSHLNHD---LVHKITTALKnnhIYYQIYTNRGIYTedPKRDLAIYIdIAEragqkADVAKIrnniqkridngTLKvv 154
Cdd:PRK10513  83 VAQTALSYDdylYLEKLSREVG---VHFHALDRNTLYT--ANRDISYYT-VHE-----SFLTGI-----------PLV-- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 155 dnYDSIEDI-PGELIMKVL------AFDADLSKIDQVGQElasspNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGID 227
Cdd:PRK10513 139 --FREVEKMdPNLQFPKVMmidepeILDAAIARIPAEVKE-----RYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIK 211

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394256717 228 LTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10513 212 PEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 3-282 2.70e-29

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 112.42  E-value: 2.70e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   3 KLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGR------AFYEAqtpvaeTDLKVPYICLNGAEVRD-ESF 75
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRhhvaihPFYQA------LALDTPAICCNGTYLYDyQAK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  76 NIMSTSHLNHDLVHKITTALKNNHIYYQIYTNRGIYTEDPKRDLAIYIDIAER--AGQKAdvakirnniqkridngTLKV 153
Cdd:PRK10530  78 KVLEADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTlpPEQRP----------------TFTQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 154 VDN-YDSIEDIpgELIMKVLAFDADLSKIDQVGQELASSPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVV 232
Cdd:PRK10530 142 VDSlAQAARQV--NAIWKFALTHEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVV 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 394256717 233 AIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMK 282
Cdd:PRK10530 220 AFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 3-279 4.55e-29

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: 110.00  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   3 KLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVpYICLNGAEVRDESfNIMSTSH 82
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFFEG-EVIYKNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  83 LNHDLVHKITTALKNNHIYYQIYTNRGIY-TEDPKRDLAIYIDiaeragqkadvakirnniqkridngTLKVVDNYDsie 161
Cdd:cd07517   79 LPQELVERLTEFAKEQGHPVSFYGQLLLFeDEEEEQKYEELRP-------------------------ELRFVRWHP--- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 162 dipgelimkvlaFDADlskidqvgqelasspnlavssssrgnleITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDI 241
Cdd:cd07517  131 ------------LSTD----------------------------VIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDI 170

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 394256717 242 SMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKA 279
Cdd:cd07517  171 EMLEAVGIGIAMGNAHEELKEIADYVTKDVDEDGILKA 208
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 3-276 7.68e-23

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: 92.65  E-value: 7.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   3 KLIATDMDGTLLNAGHE-ITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVrdesfnimsts 81
Cdd:cd07518    1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  82 hlnhdlVHKITtalknnhiyyqiytnrgIYTEDPKRDlaiyiDIAERAGQKAdvakirnniqkridNGTLKVVdnydsie 161
Cdd:cd07518   70 ------YFKFT-----------------LNVPDEAAP-----DIIDELNQKF--------------GGILRAV------- 100

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 162 dipgelimkvlafdadlskidqvgqelasspnlavsSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDI 241
Cdd:cd07518  101 ------------------------------------TSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDI 144

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 394256717 242 SMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGV 276
Cdd:cd07518  145 EMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGV 179
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-284 2.39e-21

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 90.03  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAfyeaqTPVAETDLKV-----PYICLNGAEVRDEsf 75
Cdd:PRK01158   2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNV-----LCFARAAAKLigtsgPVIAENGGVISVG-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  76 nimstshlnhdlvhkittalknnhiyyqiYTNRGIYTEDpkrdlaiyIDIAERAgqkadvakiRNNIQKRIDNGTLKVVD 155
Cdd:PRK01158  75 -----------------------------FDGKRIFLGD--------IEECEKA---------YSELKKRFPEASTSLTK 108

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 156 NYDSI--------EDIPGELIMKVLA-FDADLSKIDqvgqelasspnlavsssSRGNLEITHSDAQKGIALSAIAHQLGI 226
Cdd:PRK01158 109 LDPDYrktevalrRTVPVEEVRELLEeLGLDLEIVD-----------------SGFAIHIKSPGVNKGTGLKKLAELMGI 171

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 394256717 227 DLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKIL 284
Cdd:PRK01158 172 DPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLL 229
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 213-284 1.29e-16

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: 74.93  E-value: 1.29e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394256717 213 KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKIL 284
Cdd:cd07514   68 KGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-253 1.92e-16

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: 75.88  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    4 LIATDMDGTLLNAG-HEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDesfnimstsh 82
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFY---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   83 lnhdlvhkittalkNNHIYYQIYTNRGIYTEDPKRDLaIYIDIAERAGQKADVAKIRNNIQKRIDNGTLKVVDNYDSIED 162
Cdd:TIGR01484  71 --------------PGEILYIEPSDVFEEILGIKFEE-IGAELKSLSEHYVGTFIEDKAIAVAIHYVGAELGQELDSKMR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  163 IPGELImkvlafdadlsKIDQvgqelassPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDIS 242
Cdd:TIGR01484 136 ERLEKI-----------GRND--------LELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEE 196

                         250
                  ....*....|.
gi 394256717  243 MLERVGYPVAM 253
Cdd:TIGR01484 197 MFEVAGLAVAV 207
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-284 9.53e-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: 74.42  E-value: 9.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    5 IATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRA---FYEAQTPVAETDlkvPYICLNGAEVRDEsfnimsts 81
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSvqfARALAKLIGTPD---PVIAENGGEISYN-------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   82 hlnhDLVHKITTALKNNHIyyqiytnrgiytedpkrdlaiyidiaeragqkadvakIRNNIQKRID-NGTLKVvdnydsi 160
Cdd:TIGR01482  70 ----EGLDDIFLAYLEEEW-------------------------------------FLDIVIAKTFpFSRLKV------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  161 eDIPGElimKVLAFDADLSKIDQVgQELASSPNLAVSSSSRGN-LEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLN 239
Cdd:TIGR01482 102 -QYPRR---ASLVKMRYGIDVDTV-REIIKELGLNLVAVDSGFdIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSEN 176

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 394256717  240 DISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKIL 284
Cdd:TIGR01482 177 DIDLFEVPGFGVAVANAQPELKEWADYVTESPYGEGGAEAIGEIL 221
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 2-280 1.86e-15

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: 73.62  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    2 IKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDEsfnimsts 81
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIFYN-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   82 hlnhdlvhkittalknnhiyyqiytnrgiytedpkrdlaiYIDIaeRAGQKADVAKIRNNIQKRIDNGTLKVvdnydsie 161
Cdd:TIGR01487  73 ----------------------------------------KEDI--FLANMEEEWFLDEEKKKRFPRDRLSN-------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  162 dipgELIMKVLAFDADLSKIDQVgQELASSPNLAVSSSsRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDI 241
Cdd:TIGR01487 103 ----EYPRASLVIMREGKDVDEV-REIIKERGLNLVAS-GFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDI 176

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 394256717  242 SMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:TIGR01487 177 DLFRVVGFKVAVANADDQLKEIADYVTSNPYGEGVVEVL 215
PRK15126 PRK15126
HMP-PP phosphatase;
1-261 4.47e-15

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 73.57  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMST 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  81 SHLNHDLVHKITTALKNNHIYYQIYTNRGIYTEdpkrdlaiyidiaeragqKADVAKIRNNiqkRIDNGTLKVVDnydsI 160
Cdd:PRK15126  81 QDLPADVAELVLHQQWDTRASMHVFNDDGWFTG------------------KEIPALLQAH---VYSGFRYQLID----L 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 161 EDIPGELIMKVlAFDAD---LSKID-QVGQELASSPNLAVSSssRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGD 236
Cdd:PRK15126 136 KRLPAHGVTKI-CFCGDhddLTRLQiQLNEALGERAHLCFSA--TDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGD 212

                        250       260
                 ....*....|....*....|....*
gi 394256717 237 NLNDISMLERVGYPVAMNNAIDEVK 261
Cdd:PRK15126 213 AMNDREMLGSVGRGFIMGNAMPQLR 237
PLN02887 PLN02887
hydrolase family protein
 3-280 4.71e-14

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 72.21  E-value: 4.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   3 KLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLK---------VPYICLNGAEVRDE 73
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYGR 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  74 SFNIMSTSHLNHDLVHKITTALKNNHIYYQIYTNRGIYT--EDPKRDLAIYIdiaeragQKADVAKIRNNIQKRIDNGTL 151
Cdd:PLN02887 389 QGREIYRSNLDQEVCREACLYSLEHKIPLIAFSQDRCLTlfDHPLVDSLHTI-------YHEPKAEIMSSVDQLLAAADI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 152 KVVDNYDSIEDIPGELimkvlafdadlskidqvgqelasSPNLAVSSSSRGN--------LEITHSDAQKGIALSAIAHQ 223
Cdd:PLN02887 462 QKVIFLDTAEGVSSVL-----------------------RPYWSEATGDRANvvqaqpdmLEIVPPGTSKGNGVKMLLNH 518

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 394256717 224 LGIDLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAI 280
Cdd:PLN02887 519 LGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 213-271 2.97e-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: 2.97e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 394256717 213 KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTN 271
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKP 142
PRK10976 PRK10976
putative hydrolase; Provisional
 1-256 6.58e-13

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 67.38  E-value: 6.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVRDESFNIMST 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  81 SHLNHDLVHKITTALKNNHiyyQIYTNrgIYtedpkRDLAIYIDiAERAGQKadvakirNNIQKRIDNGTLKVVDNydsi 160
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDNP---DIITN--VY-----RDDEWFMN-RHRPEEM-------RFFKEAVFKYQLYEPGL---- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 161 edIPGELIMKVLAFDADLSKIDQVGQELAS--SPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNL 238
Cdd:PRK10976 139 --LEPDGVSKVFFTCDSHEKLLPLEQAINArwGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGM 216

                        250
                 ....*....|....*...
gi 394256717 239 NDISMLERVGYPVAMNNA 256
Cdd:PRK10976 217 NDAEMLSMAGKGCIMGNA 234
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-286 1.04e-10

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 60.72  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   1 MIKLIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAevrdesfnimst 80
Cdd:PRK00192   3 MKLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGA------------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  81 shlnhdlvhkittalknnhiyyQIYTNRGIYTEDPKRDLAIYIDIAERAGQKadVAKIR---NNIQKRIDnGTLKVVDNY 157
Cdd:PRK00192  71 ----------------------AIYIPKNYFPFQPDGERLKGDYWVIELGPP--YEELReilDEISDELG-YPLKGFGDL 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 158 dSIEDI------PGELI-----------MKVLAFDADLSKIdqvgQELASSPNLAVsssSRGNLEIT-HSDAQKGIALSA 219
Cdd:PRK00192 126 -SAEEVaeltglSGESArlakdrefsepFLWNGSEAAKERF----EEALKRLGLKV---TRGGRFLHlLGGGDKGKAVRW 197

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394256717 220 IAHQLGI-DLTDVVAIGDNLNDISMLERVGYPVAMNNA----IDEVKHIAKY-VTDTNENSGVG--KAIMKILKE 286
Cdd:PRK00192 198 LKELYRRqDGVETIALGDSPNDLPMLEAADIAVVVPGPdgpnPPLLPGIADGeFILASAPGPEGwaEAINKLLSK 272
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 202-254 1.09e-10

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: 60.24  E-value: 1.09e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 394256717 202 GNLEITHSDAQ-KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMN 254
Cdd:COG0560  144 GEVVGPIVDGEgKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN 197
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 205-290 4.71e-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: 54.07  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  205 EITHSDAQKGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSGVGKAIMKIL 284
Cdd:TIGR01670  69 HLYQGQSNKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELL 148


                  ....*.
gi 394256717  285 KEENNL 290
Cdd:TIGR01670 149 LLAQGK 154
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 213-268 2.82e-08

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: 51.75  E-value: 2.82e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 394256717 213 KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMNNAIDEVKHIAKYVT 268
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 4-251 4.65e-08

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: 52.79  E-value: 4.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717    4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAevrdesfnimstshl 83
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGG--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   84 nhdlvhkittalknnhiyyQIYTNRGIYTedpkRDLAIYIDIAERagqkadVAKIRNNIQKrIDNGTLKVVDNYDSIEDI 163
Cdd:TIGR01486  66 -------------------AIYGPRGWRP----EPEYPVIALGIP------YEKIRARLRE-LSEELGFKFRGLGDLTDE 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  164 PGELIMKVLAFDADLSKIDQVGQELASSPN----LAVSSSSRGnLEITH---------SDAQKGIALSAIA---HQLGID 227
Cdd:TIGR01486 116 EIAELTGLSRELARLAQRREYSETILWSEErrerFTEALVAVG-LEVTHggrfyhvlgAGSDKGKAVNALKafyNQPGGA 194

                         250       260
                  ....*....|....*....|....
gi 394256717  228 LTdVVAIGDNLNDISMLERVGYPV 251
Cdd:TIGR01486 195 IK-VVGLGDSPNDLPLLEVVDLAV 217
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 4-275 1.40e-06

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: 48.50  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   4 LIATDMDGTLLnaGHEITT-----MNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPyiclngaevrdesfnim 78
Cdd:cd02605    1 LLVSDLDETLV--GHDTNLqalerLQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKP----------------- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  79 stSHLNHDLVHKITTAlknNHIYYQiytnrgiytedPKRDLAIYIDIAERAGQKADVAKIRNNI--QKRIDNGTLKVVDN 156
Cdd:cd02605   62 --DFIISDVGTEIYYG---ESGYLE-----------PDTYWNEVLSEGWERFLFEAIADLFKQLkpQSELEQNPHKISFY 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 157 YDSIEDipgelimkvlafDADLSKIDQVGQELASSPNLAVSSSSRGNLEITHSDAQKGIALSAIAHQLGIDLTDVVAIGD 236
Cdd:cd02605  126 LDPQND------------AAVIEQLEEMLLKAGLTVRIIYSSGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGD 193

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 394256717 237 NLNDISMLERVGYPVAMNNAIDEVKHIAKYVTDTNENSG 275
Cdd:cd02605  194 SGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKG 232
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 4-251 1.09e-05

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: 45.82  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717   4 LIATDMDGTLLNAGHEITTMNQEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGAEVR--DESFNImsts 81
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIFipRGYFKF---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717  82 hlnhdlvhkittALKNNHIYYQIYTNRGIytedPKRDLAIYID-IAERAGqkadvakirnniQKRIDNGTLkvvdNYDSI 160
Cdd:cd07507   77 ------------PGRCKSEGGYEVIELGK----PYREIRAALEkIREETG------------FKITGFGDL----TEEEI 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256717 161 EDIPG------ELIMK-----VLAFDADLSKIDQVGQELASSPNLAVSSSSRGNLEITHSDAQKGIA-LSAIAHQLGIDL 228
Cdd:cd07507  125 AELTGlpreraALAKEreyseTIILRSDEEEDEKVLEALEERGLKITKGGRFYHVLGAGADKGKAVAiLAALYRQLYEAI 204

                        250       260
                 ....*....|....*....|...
gi 394256717 229 TdVVAIGDNLNDISMLERVGYPV 251
Cdd:cd07507  205 V-TVGLGDSPNDLPMLEAVDIAF 226
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 210-254 1.53e-05

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: 44.46  E-value: 1.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 394256717 210 DAQ-KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMN 254
Cdd:cd07500  134 DAQrKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIAFH 179
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 4-68 3.53e-04

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 41.35  E-value: 3.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394256717   4 LIATDMDGTLLNagHEitTMN----QEAIKFAQAHGITVVIATGRAFYEAQTPVAETDLKVPYICLNGA 68
Cdd:COG3769    5 LVFTDLDGTLLD--HD--TYSwaaaLPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGA 69
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 210-254 8.00e-04

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: 40.03  E-value: 8.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 394256717  210 DAQ-KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMN 254
Cdd:TIGR00338 149 DASyKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAFN 194
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 4-50 8.33e-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: 38.15  E-value: 8.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 394256717   4 LIATDMDGTLLNagheittmnQEAIKFAQAHGITVVIATGRAFYEAQ 50
Cdd:cd01427    1 AVLFDLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALR 38
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 202-254 8.34e-04

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 39.60  E-value: 8.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 394256717 202 GNLEITHSD-AQKGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVGYPVAMN 254
Cdd:cd02612  140 GRIIGPPCYgEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVAVN 193
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 2-63 1.87e-03

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: 37.89  E-value: 1.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 394256717   2 IKLIATDMDGTLLN-------AGHEITTMNQE---AIKFAQAHGITVVIATGRafyeaQTPVAET---DLKVPYI 63
Cdd:cd01630    1 IKLLVLDVDGVLTDgriyydsNGEELKSFNVRdglGIKLLQKSGIEVAIITGR-----QSEAVRRrakELGIEDL 70
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 213-248 2.94e-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: 37.95  E-value: 2.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 394256717  213 KGIALSAIAHQLGIDLTDVVAIGDNLNDISMLERVG 248
Cdd:pfam00702 156 KPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD pfam12710
haloacid dehalogenase-like hydrolase;
215-245 8.43e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 36.74  E-value: 8.43e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 394256717  215 IALSAIAHQLGIDLTDVVAIGDNLNDISMLE 245
Cdd:pfam12710 158 LRAWLAARGLGLDLADSVAYGDSPSDLPMLR 188
 
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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