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Conserved domains on  [gi|498254215|ref|WP_010568371|]
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HAD hydrolase family protein [Leptospira broomii]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 20-284 4.63e-46

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


The actual alignment was detected with superfamily member pfam08282:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 255  Bit Score: 155.86  E-value: 4.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRAsPTGVRVAETYL 99
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYD-ENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  100 SPNAVAAVLDSGKKSGFDPILhvdhYEEGvDILAESPITDPKFHNYSGGDLKRSRVVKNCLDYGSDRILvACFLSQQKEH 179
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILL----YTDD-GVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDIN-KILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  180 LVELESNLLSLPESVQFrtvITRIHGvaYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAM 259
Cdd:pfam08282 154 LDELEKELKELFGSLIT---ITSSGP--GYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAM 228

                         250       260
                  ....*....|....*....|....*
gi 498254215  260 KNAISYLRDHAPYITRySNDEDAIA 284
Cdd:pfam08282 229 GNASPEVKAAADYVTD-SNNEDGVA 252
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 20-284 4.63e-46

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 155.86  E-value: 4.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRAsPTGVRVAETYL 99
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYD-ENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  100 SPNAVAAVLDSGKKSGFDPILhvdhYEEGvDILAESPITDPKFHNYSGGDLKRSRVVKNCLDYGSDRILvACFLSQQKEH 179
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILL----YTDD-GVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDIN-KILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  180 LVELESNLLSLPESVQFrtvITRIHGvaYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAM 259
Cdd:pfam08282 154 LDELEKELKELFGSLIT---ITSSGP--GYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAM 228

                         250       260
                  ....*....|....*....|....*
gi 498254215  260 KNAISYLRDHAPYITRySNDEDAIA 284
Cdd:pfam08282 229 GNASPEVKAAADYVTD-SNNEDGVA 252
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 20-287 1.50e-44

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: 151.59  E-value: 1.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRaSPTGVRVAETYL 99
Cdd:cd07516    2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVY-DPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 100 SPNAVAAVLDSGKKSGFdpilhvdhyeeGVDILAESPITDPKFHNYSGGDLKRSRVVKNCLDYGSDRILVACFLSQQKEH 179
Cdd:cd07516   81 SKEDVKELEEFLRKLGI-----------GINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 180 LVELESNllsLPESVQFRTVITRihGVAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAM 259
Cdd:cd07516  150 LDELIAK---LPEEFFDDLSVVR--SAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAM 224

                        250       260
                 ....*....|....*....|....*...
gi 498254215 260 KNAISYLRDHAPYITRySNDEDAIAMTL 287
Cdd:cd07516  225 GNAIDEVKEAADYVTL-TNNEDGVAKAI 251
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 17-284 2.95e-37

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: 131.03  E-value: 2.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  17 IHTIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRaSPTGVRVAE 96
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIY-DPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  97 TYLSPNAVAAVLDSGKKSGFDPILHVdhyeegvdilaespitdpkfhnYSGGdlkrsrvvkncldygsdrilvacflsqq 176
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQVVV----------------------RSGP---------------------------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 177 kehlvelesnllslpesvqfrtvitrihgvaYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFG 256
Cdd:COG0561  111 -------------------------------GFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLG 159

                        250       260
                 ....*....|....*....|....*...
gi 498254215 257 FAMKNAISYLRDHAPYITRySNDEDAIA 284
Cdd:COG0561  160 VAMGNAPPEVKAAADYVTG-SNDEDGVA 186
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 20-284 4.21e-36

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: 129.70  E-value: 4.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRASPTGVrVAETYL 99
Cdd:TIGR00099   2 IFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI-LYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  100 SPNAVAAVLDSGKKSGFDPIL-----------HVDHYEEGVDILAESPITDPKFHNYSGGDLKrsrVVKNCLDYgsdril 168
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILygddsiyasknDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK---ILLLFLDP------ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  169 VACFLSQQKEHLVELESNLlslpeSVQFRTvitrihgvAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWE 248
Cdd:TIGR00099 152 EDLDLLIEALNKLELEENV-----SVVSSG--------PYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIE 218

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 498254215  249 MISHAGFGFAMKNAISYLRDHAPYITRySNDEDAIA 284
Cdd:TIGR00099 219 MLEAAGYGVAMGNADEELKALADYVTD-SNNEDGVA 253
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 17-285 2.21e-21

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 90.91  E-value: 2.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  17 IHTIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPF----ALEFSGDlFVVSNNGQVLRASPTGV 92
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYlkelHMEQPGD-YCITNNGALVQKAADGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  93 RVAETYLSpnavaavldsgkksgFDPILHVDHY--EEGV---------------DI----LAESPITdpkfhnysGGDLK 151
Cdd:PRK10513  82 TVAQTALS---------------YDDYLYLEKLsrEVGVhfhaldrntlytanrDIsyytVHESFLT--------GIPLV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 152 RSRVVKncLDYGSDRILVACFlsqqkEHLVELESNLLSLPESVQFRTVITRihGVAYCLEVLEKNVSKWSAIDTFLRANQ 231
Cdd:PRK10513 139 FREVEK--MDPNLQFPKVMMI-----DEPEILDAAIARIPAEVKERYTVLK--SAPYFLEILDKRVNKGTGVKSLAEHLG 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498254215 232 LDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRySNDEDAIAM 285
Cdd:PRK10513 210 IKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTK-SNLEDGVAF 262
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 20-284 4.63e-46

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 155.86  E-value: 4.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRAsPTGVRVAETYL 99
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYD-ENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  100 SPNAVAAVLDSGKKSGFDPILhvdhYEEGvDILAESPITDPKFHNYSGGDLKRSRVVKNCLDYGSDRILvACFLSQQKEH 179
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILL----YTDD-GVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDIN-KILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  180 LVELESNLLSLPESVQFrtvITRIHGvaYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAM 259
Cdd:pfam08282 154 LDELEKELKELFGSLIT---ITSSGP--GYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAM 228

                         250       260
                  ....*....|....*....|....*
gi 498254215  260 KNAISYLRDHAPYITRySNDEDAIA 284
Cdd:pfam08282 229 GNASPEVKAAADYVTD-SNNEDGVA 252
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 20-287 1.50e-44

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: 151.59  E-value: 1.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRaSPTGVRVAETYL 99
Cdd:cd07516    2 IALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVY-DPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 100 SPNAVAAVLDSGKKSGFdpilhvdhyeeGVDILAESPITDPKFHNYSGGDLKRSRVVKNCLDYGSDRILVACFLSQQKEH 179
Cdd:cd07516   81 SKEDVKELEEFLRKLGI-----------GINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 180 LVELESNllsLPESVQFRTVITRihGVAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAM 259
Cdd:cd07516  150 LDELIAK---LPEEFFDDLSVVR--SAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAM 224

                        250       260
                 ....*....|....*....|....*...
gi 498254215 260 KNAISYLRDHAPYITRySNDEDAIAMTL 287
Cdd:cd07516  225 GNAIDEVKEAADYVTL-TNNEDGVAKAI 251
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 17-284 2.95e-37

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: 131.03  E-value: 2.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  17 IHTIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRaSPTGVRVAE 96
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIY-DPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  97 TYLSPNAVAAVLDSGKKSGFDPILHVdhyeegvdilaespitdpkfhnYSGGdlkrsrvvkncldygsdrilvacflsqq 176
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQVVV----------------------RSGP---------------------------- 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 177 kehlvelesnllslpesvqfrtvitrihgvaYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFG 256
Cdd:COG0561  111 -------------------------------GFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLG 159

                        250       260
                 ....*....|....*....|....*...
gi 498254215 257 FAMKNAISYLRDHAPYITRySNDEDAIA 284
Cdd:COG0561  160 VAMGNAPPEVKAAADYVTG-SNDEDGVA 186
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 20-284 4.21e-36

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: 129.70  E-value: 4.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRASPTGVrVAETYL 99
Cdd:TIGR00099   2 IFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI-LYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  100 SPNAVAAVLDSGKKSGFDPIL-----------HVDHYEEGVDILAESPITDPKFHNYSGGDLKrsrVVKNCLDYgsdril 168
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILygddsiyasknDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK---ILLLFLDP------ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  169 VACFLSQQKEHLVELESNLlslpeSVQFRTvitrihgvAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWE 248
Cdd:TIGR00099 152 EDLDLLIEALNKLELEENV-----SVVSSG--------PYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIE 218

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 498254215  249 MISHAGFGFAMKNAISYLRDHAPYITRySNDEDAIA 284
Cdd:TIGR00099 219 MLEAAGYGVAMGNADEELKALADYVTD-SNNEDGVA 253
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 17-285 2.21e-21

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 90.91  E-value: 2.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  17 IHTIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPF----ALEFSGDlFVVSNNGQVLRASPTGV 92
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYlkelHMEQPGD-YCITNNGALVQKAADGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  93 RVAETYLSpnavaavldsgkksgFDPILHVDHY--EEGV---------------DI----LAESPITdpkfhnysGGDLK 151
Cdd:PRK10513  82 TVAQTALS---------------YDDYLYLEKLsrEVGVhfhaldrntlytanrDIsyytVHESFLT--------GIPLV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 152 RSRVVKncLDYGSDRILVACFlsqqkEHLVELESNLLSLPESVQFRTVITRihGVAYCLEVLEKNVSKWSAIDTFLRANQ 231
Cdd:PRK10513 139 FREVEK--MDPNLQFPKVMMI-----DEPEILDAAIARIPAEVKERYTVLK--SAPYFLEILDKRVNKGTGVKSLAEHLG 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 498254215 232 LDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRySNDEDAIAM 285
Cdd:PRK10513 210 IKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTK-SNLEDGVAF 262
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 23-291 5.57e-19

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: 83.04  E-value: 5.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  23 DLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDlFVVSNNGQvlrasptgvrvaetylspn 102
Cdd:cd07517    6 DIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGID-SYVSYNGQ------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 103 avaavldsgkksgfdpilHVdHYEEGVdiLAESPITDPKFHnysggdlkrsRVVKNCLDYGSDRILVACFLSQQKEHLVE 182
Cdd:cd07517   66 ------------------YV-FFEGEV--IYKNPLPQELVE----------RLTEFAKEQGHPVSFYGQLLLFEDEEEEQ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 183 LesnLLSLPESVQFrtviTRIHGVAYclEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAMKNA 262
Cdd:cd07517  115 K---YEELRPELRF----VRWHPLST--DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNA 185

                        250       260
                 ....*....|....*....|....*....
gi 498254215 263 ISYLRDHAPYITRySNDEDAIAMTLLELG 291
Cdd:cd07517  186 HEELKEIADYVTK-DVDEDGILKALKHFG 213
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 20-287 6.46e-16

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: 74.16  E-value: 6.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRG-CISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRASPTgvrvaety 98
Cdd:cd07518    3 IATDMDGTFLNDDKtYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVYFKFT-------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  99 lspnavaavldsgkksgfdpilhVDHYEEgvdilaESPITDPKFHNYSGGDLkrsrvvkncldygsdrilvacflsqqke 178
Cdd:cd07518   75 -----------------------LNVPDE------AAPDIIDELNQKFGGIL---------------------------- 97

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 179 hlvelesnllslpesvqfrTVITRIHGVaycLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFA 258
Cdd:cd07518   98 -------------------RAVTSGFGS---IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYA 155

                        250       260
                 ....*....|....*....|....*....
gi 498254215 259 MKNAISYLRDHAPYITRySNDEDAIAMTL 287
Cdd:cd07518  156 MENAPEEVKAAAKYVAP-SNNENGVLQVI 183
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 20-287 3.41e-14

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 70.82  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRGCI--SSLNhyVLNAALSQGIRLIIATGRRFSSTLPF--ALEFsgDLFVVSNNG---------QVLR 86
Cdd:PRK10530   6 IALDLDGTLLTPKKTIlpESLE--ALARAREAGYKVIIVTGRHHVAIHPFyqALAL--DTPAICCNGtylydyqakKVLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  87 ASPtgvrvaetyLSPNAVAAVLDSGKKSGFDPILHVDH---YEEGVDIL------AES--PITDPKFhnysggdlkrsRV 155
Cdd:PRK10530  82 ADP---------LPVQQALQVIEMLDEHQIHGLMYVDDamlYEHPTGHVirtlnwAQTlpPEQRPTF-----------TQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 156 VKNcldygsdrilvacfLSQQKEHLVELESNLLSLPESVQFRTVITRIH---GVAyC-------LEVLEKNVSKWSAIDT 225
Cdd:PRK10530 142 VDS--------------LAQAARQVNAIWKFALTHEDLPQLQHFAKHVEhelGLE-CewswhdqVDIARKGNSKGKRLTQ 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498254215 226 FLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRySNDEDAIAMTL 287
Cdd:PRK10530 207 WVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIG-DNTTPSIAEFI 267
PRK15126 PRK15126
HMP-PP phosphatase;
21-273 1.10e-11

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 63.94  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  21 AMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRaSPTGVRVAETYLS 100
Cdd:PRK15126   6 AFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVH-SLEGELLHRQDLP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 101 PNAVAAVL--------------DSGKKSGFD-PILHVDHYEEGvdilaespitdpkFHnYSGGDLKR---SRVVKNCLDY 162
Cdd:PRK15126  85 ADVAELVLhqqwdtrasmhvfnDDGWFTGKEiPALLQAHVYSG-------------FR-YQLIDLKRlpaHGVTKICFCG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 163 GSDRIlvaCFLSQQ-KEHLVELESNLLSLPEsvqfrtvitrihgvayCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFG 241
Cdd:PRK15126 151 DHDDL---TRLQIQlNEALGERAHLCFSATD----------------CLEVLPVGCNKGAALAVLSQHLGLSLADCMAFG 211

                        250       260       270
                 ....*....|....*....|....*....|..
gi 498254215 242 DEKNDWEMISHAGFGFAMKNAISYLRDHAPYI 273
Cdd:PRK15126 212 DAMNDREMLGSVGRGFIMGNAMPQLRAELPHL 243
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 20-259 1.37e-10

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: 59.70  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   20 IAMDLDGTLLNSRgcisslNHYV-------LNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQVLRASPTGV 92
Cdd:TIGR01484   2 LFFDLDGTLLDPN------AHELspetieaLERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215   93 -----RVAETYLSPNAVAAVLDSgkksgfdpilhvdhyEEGVDILAESPITDPKFH-NYSGGDLKRSRVVKncldygsdr 166
Cdd:TIGR01484  76 yiepsDVFEEILGIKFEEIGAEL---------------KSLSEHYVGTFIEDKAIAvAIHYVGAELGQELD--------- 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  167 ilvacflsqqKEHLVELESNLLSLPEsVQFRTVItrihgvAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKND 246
Cdd:TIGR01484 132 ----------SKMRERLEKIGRNDLE-LEAIYSG------KTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGND 194

                         250
                  ....*....|...
gi 498254215  247 WEMISHAGFGFAM 259
Cdd:TIGR01484 195 EEMFEVAGLAVAV 207
PRK10976 PRK10976
putative hydrolase; Provisional
 18-290 2.44e-09

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 56.98  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  18 HTIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPFALEFSGDLFVVSNNGQvlRASPT-GVRVAE 96
Cdd:PRK10976   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGA--RVHDTdGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  97 TYLSPNaVAAVLDSGKKSGFDPILHV---------DHYEEGVDILAESpitDPKFHNYSGGDLKRSRVVKncldygsdri 167
Cdd:PRK10976  81 HNLDRD-IASDLFGVVHDNPDIITNVyrddewfmnRHRPEEMRFFKEA---VFKYQLYEPGLLEPDGVSK---------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 168 lvACFLSQQKEHLVELESNLL-----SLPESVQFRTvitrihgvayCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGD 242
Cdd:PRK10976 147 --VFFTCDSHEKLLPLEQAINarwgdRVNVSFSTLT----------CLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGD 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 498254215 243 EKNDWEMISHAGFGFAMKNAISYLRDHAPYITRY-SNDEDAIAMTLLEL 290
Cdd:PRK10976 215 GMNDAEMLSMAGKGCIMGNAHQRLKDLLPELEVIgSNADDAVPHYLRKL 263
PLN02887 PLN02887
hydrolase family protein
 20-289 1.44e-06

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 49.49  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRRFSSTLPF--ALEFSGDLFVVSNNG--------------- 82
Cdd:PLN02887 311 IFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDIlkMVDLAGKDGIISESSpgvflqgllvygrqg 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  83 -QVLRAS--PTGVRVAETYLSPNAVAAVLDSGKK--SGFD-PI---LHVDHYEEGVDI-------LAESPITDPKFHNYS 146
Cdd:PLN02887 391 rEIYRSNldQEVCREACLYSLEHKIPLIAFSQDRclTLFDhPLvdsLHTIYHEPKAEImssvdqlLAAADIQKVIFLDTA 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 147 GGdlkrsrVVKNCLDYGSDRIlvacflsQQKEHLVELESNLlslpesvqfrtvitrihgvaycLEVLEKNVSKWSAIDTF 226
Cdd:PLN02887 471 EG------VSSVLRPYWSEAT-------GDRANVVQAQPDM----------------------LEIVPPGTSKGNGVKML 515

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498254215 227 LRANQLDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITrYSNDEDAIAMTLLE 289
Cdd:PLN02887 516 LNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIG-VSNDEDGVADAIYR 577
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 208-280 2.96e-06

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 47.28  E-value: 2.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498254215 208 YCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRYSNDE 280
Cdd:PRK01158 147 FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGE 219
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 217-280 5.74e-06

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: 45.27  E-value: 5.74e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498254215 217 VSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRYSNDE 280
Cdd:cd07514   66 VDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGD 129
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 19-110 2.73e-05

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: 42.96  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  19 TIAMDLDGTLLNSRGCISSLNHYVLNAALSQGIRLIIATGRrfssTLPFA------LEFSGDlfVVSNNGQVLRAspTGV 92
Cdd:cd07514    1 LIAVDIDGTLTDRRRSIDLRAIEAIRKLEKAGIPVVLVTGN----SLPVAralakyLGLSGP--VVAENGGVDKG--TGL 72

                         90       100
                 ....*....|....*....|
gi 498254215  93 R-VAETY-LSPNAVAAVLDS 110
Cdd:cd07514   73 EkLAERLgIDPEEVLAIGDS 92
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 232-284 1.31e-04

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: 41.36  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 498254215  232 LDSAGVVAFGDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRYSNDEDAIA 284
Cdd:TIGR01670  90 LAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVR 142
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 219-283 9.16e-04

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: 38.66  E-value: 9.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498254215 219 KWSAIDtFLRANQLDSAGVVAF-GDEKNDWEMISHAGFGFAMKNAISYLRDHAPYITRYSNDEDAI 283
Cdd:cd01630   77 KLEALE-ELLEKLGLSDEEVAYmGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAV 141
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 20-276 1.92e-03

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: 38.87  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  20 IAMDLDGTLLNSRGCISSLNH---YVLNAALSQGIRLIIATGRRFSSTLpfalefsgDLFvvsnnGQVLRASP----TGV 92
Cdd:cd02605    2 LVSDLDETLVGHDTNLQALERlqdLLEQLTADNDVILVYATGRSPESVL--------ELI-----KEVMLPKPdfiiSDV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  93 RVAETYlsPNAVAAVLDSGKKSGFDPILHVDHYEEGVDILAESPITDPkfhnYSGGDLKRSRVVKNCLDygsdrilvacf 172
Cdd:cd02605   69 GTEIYY--GESGYLEPDTYWNEVLSEGWERFLFEAIADLFKQLKPQSE----LEQNPHKISFYLDPQND----------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215 173 lsqqKEHLVELESNLLSLpesvQFRTVITRIHGVAYCLEVLEKNVSKWSAIDTFLRANQLDSAGVVAFGDEKNDWEMISH 252
Cdd:cd02605  132 ----AAVIEQLEEMLLKA----GLTVRIIYSSGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLST 203

                        250       260
                 ....*....|....*....|....
gi 498254215 253 AGFGFAMKNAISYLRDHAPYITRY 276
Cdd:cd02605  204 GTRGVIVGNAQPELLKWADRVTRS 227
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 23-110 4.46e-03

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 36.22  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498254215  23 DLDGTLLNsrgcisslnHYVLNAALSQGIRLIIATGRRFSSTLPFA----LEFSGDLFVVSNNGQVLRASPTGVRVA--E 96
Cdd:cd01427    5 DLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALRALLeklgLGDLFDGIIGSDGGGTPKPKPKPLLLLllK 75

                         90
                 ....*....|....
gi 498254215  97 TYLSPNAVAAVLDS 110
Cdd:cd01427   76 LGVDPEEVLFVGDS 89
 
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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