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Conserved domains on  [gi|489821682|ref|WP_003725481|]
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sugar-phosphatase [Listeria monocytogenes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10513 super family cl32525
sugar phosphate phosphatase; Provisional
 3-269 2.90e-100

sugar phosphate phosphatase; Provisional


The actual alignment was detected with superfamily member PRK10513:

Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 293.91  E-value: 2.90e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   3 KIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLLDEGDYAITFNGAVVLETASEKTL 82
Cdd:PRK10513   4 KLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADGETV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  83 ADITLNKteleEIYAFCH--AENVNVTY--FDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDS 158
Cdd:PRK10513  84 AQTALSY----DDYLYLEklSREVGVHFhaLDRNTLYTANRDISYYTVHESFLTGIPLVFREVEKMDPNLQFPKVMMIDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 PEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGN 238
Cdd:PRK10513 160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489821682 239 ATEHIKEIANYTTTTNNEDGVAQAIQMLILD 269
Cdd:PRK10513 240 AIPSVKEVAQFVTKSNLEDGVAFAIEKYVLN 270
 
Name Accession Description Interval E-value
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 3-269 2.90e-100

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 293.91  E-value: 2.90e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   3 KIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLLDEGDYAITFNGAVVLETASEKTL 82
Cdd:PRK10513   4 KLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADGETV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  83 ADITLNKteleEIYAFCH--AENVNVTY--FDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDS 158
Cdd:PRK10513  84 AQTALSY----DDYLYLEklSREVGVHFhaLDRNTLYTANRDISYYTVHESFLTGIPLVFREVEKMDPNLQFPKVMMIDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 PEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGN 238
Cdd:PRK10513 160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489821682 239 ATEHIKEIANYTTTTNNEDGVAQAIQMLILD 269
Cdd:PRK10513 240 AIPSVKEVAQFVTKSNLEDGVAFAIEKYVLN 270
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-265 3.28e-97

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: 285.26  E-value: 3.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   4 IIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVLETaSEKTLA 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDP-TGKEIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  84 DITLNKTELEEIYAFCHAENVNVTYFDGKNMyvpsrKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDSPEKIT 163
Cdd:cd07516   77 ERLISKEDVKELEEFLRKLGIGINIYTNDDW-----ADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 164 DVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHI 243
Cdd:cd07516  152 ELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEV 231

                        250       260
                 ....*....|....*....|..
gi 489821682 244 KEIANYTTTTNNEDGVAQAIQM 265
Cdd:cd07516  232 KEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-263 7.67e-84

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: 251.42  E-value: 7.67e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    4 IIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLielDLLDEGDYAITFNGAVVLETASEkTLA 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNIL---KELGLDTPFITANGAAVIDDQGE-ILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   84 DITLNKTELEEIYAFCHAENVNVTYFDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIhVSKVMLLDSPEKIT 163
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  164 DVIKKLP-ESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEH 242
Cdd:TIGR00099 156 LLIEALNkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489821682  243 IKEIANYTTTTNNEDGVAQAI 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-263 6.84e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 223.65  E-value: 6.84e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    5 IAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKsliELDLLDEGDYAITFNGAVVLEtASEKTLAD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILP---VIKELGLDDPVICYNGALIYD-ENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   85 ITLNKTELEEIYAFCHAENVNVTYFDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDSPEKITD 164
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  165 VIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIK 244
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 489821682  245 EIANYTTTTNNEDGVAQAI 263
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-266 2.25e-68

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: 209.99  E-value: 2.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVLeTASEK 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIY-DPDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  81 TLADITLNKTELEEIYAFCHAENVNVtyfdgknmyvpsrkiteitcqdslllgtplyhlpveeapesihvskvmlldspe 160
Cdd:COG0561   77 VLYERPLDPEDVREILELLREHGLHL------------------------------------------------------ 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 161 kitdvikklpesikekFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNAT 240
Cdd:COG0561  103 ----------------QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAP 166

                        250       260
                 ....*....|....*....|....*.
gi 489821682 241 EHIKEIANYTTTTNNEDGVAQAIQML 266
Cdd:COG0561  167 PEVKAAADYVTGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 3-269 2.90e-100

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 293.91  E-value: 2.90e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   3 KIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLLDEGDYAITFNGAVVLETASEKTL 82
Cdd:PRK10513   4 KLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADGETV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  83 ADITLNKteleEIYAFCH--AENVNVTY--FDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDS 158
Cdd:PRK10513  84 AQTALSY----DDYLYLEklSREVGVHFhaLDRNTLYTANRDISYYTVHESFLTGIPLVFREVEKMDPNLQFPKVMMIDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 PEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGN 238
Cdd:PRK10513 160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489821682 239 ATEHIKEIANYTTTTNNEDGVAQAIQMLILD 269
Cdd:PRK10513 240 AIPSVKEVAQFVTKSNLEDGVAFAIEKYVLN 270
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-265 3.28e-97

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: 285.26  E-value: 3.28e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   4 IIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVLETaSEKTLA 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDP-TGKEIL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  84 DITLNKTELEEIYAFCHAENVNVTYFDGKNMyvpsrKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDSPEKIT 163
Cdd:cd07516   77 ERLISKEDVKELEEFLRKLGIGINIYTNDDW-----ADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 164 DVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHI 243
Cdd:cd07516  152 ELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEV 231

                        250       260
                 ....*....|....*....|..
gi 489821682 244 KEIANYTTTTNNEDGVAQAIQM 265
Cdd:cd07516  232 KEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-263 7.67e-84

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: 251.42  E-value: 7.67e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    4 IIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLielDLLDEGDYAITFNGAVVLETASEkTLA 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNIL---KELGLDTPFITANGAAVIDDQGE-ILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   84 DITLNKTELEEIYAFCHAENVNVTYFDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIhVSKVMLLDSPEKIT 163
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  164 DVIKKLP-ESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEH 242
Cdd:TIGR00099 156 LLIEALNkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489821682  243 IKEIANYTTTTNNEDGVAQAI 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-263 6.84e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 223.65  E-value: 6.84e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    5 IAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKsliELDLLDEGDYAITFNGAVVLEtASEKTLAD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILP---VIKELGLDDPVICYNGALIYD-ENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   85 ITLNKTELEEIYAFCHAENVNVTYFDGKNMYVPSRKITEITCQDSLLLGTPLYHLPVEEAPESIHVSKVMLLDSPEKITD 164
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  165 VIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIK 244
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 489821682  245 EIANYTTTTNNEDGVAQAI 263
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-266 2.25e-68

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: 209.99  E-value: 2.25e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVLeTASEK 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIY-DPDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  81 TLADITLNKTELEEIYAFCHAENVNVtyfdgknmyvpsrkiteitcqdslllgtplyhlpveeapesihvskvmlldspe 160
Cdd:COG0561   77 VLYERPLDPEDVREILELLREHGLHL------------------------------------------------------ 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 161 kitdvikklpesikekFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNAT 240
Cdd:COG0561  103 ----------------QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAP 166

                        250       260
                 ....*....|....*....|....*.
gi 489821682 241 EHIKEIANYTTTTNNEDGVAQAIQML 266
Cdd:COG0561  167 PEVKAAADYVTGSNDEDGVAEALEKL 192
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 3-264 1.80e-47

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: 157.00  E-value: 1.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   3 KIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldegDYAITFNGA-VVLEtasEKT 81
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGI----DSYVSYNGQyVFFE---GEV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  82 LADITLNKTELEEIYAFCHAENVNVTYFDgknmyvpsrkITEITCQDSLLlgtplyHLPVEEAPEsihvskvmlldspek 161
Cdd:cd07517   74 IYKNPLPQELVERLTEFAKEQGHPVSFYG----------QLLLFEDEEEE------QKYEELRPE--------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 162 itdvikklpesikekFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATE 241
Cdd:cd07517  123 ---------------LRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHE 187

                        250       260
                 ....*....|....*....|...
gi 489821682 242 HIKEIANYTTTTNNEDGVAQAIQ 264
Cdd:cd07517  188 ELKEIADYVTKDVDEDGILKALK 210
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 3-264 4.70e-37

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: 129.24  E-value: 4.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   3 KIIAIDIDGTLLNDAHE-ITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKkslielDLLDEGDYAITF---NGAVVletas 78
Cdd:cd07518    1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLI------SFFPEIKDEMSFvaeNGAVV----- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  79 ektladitlnkteleeiyafchaenvnvtyfdgknmyvpsrkiteitcqdslllgtplyhlpveeapesihVSKVMLLDS 158
Cdd:cd07518   70 -----------------------------------------------------------------------YFKFTLNVP 78

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 PEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGN 238
Cdd:cd07518   79 DEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMEN 158

                        250       260
                 ....*....|....*....|....*.
gi 489821682 239 ATEHIKEIANYTTTTNNEDGVAQAIQ 264
Cdd:cd07518  159 APEEVKAAAKYVAPSNNENGVLQVIE 184
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-268 3.57e-33

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 120.85  E-value: 3.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPL--AGIKKSLIELDlldegDYAITFNGAVVLEtas 78
Cdd:PRK01158   2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLcfARAAAKLIGTS-----GPVIAENGGVISV--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  79 EKTLADITLNKTELEEIyAFCHAENVNVTYFDGKNMYVPSRKITEITCQDSLllgtplyhlPVEEApesihvskvmllds 158
Cdd:PRK01158  74 GFDGKRIFLGDIEECEK-AYSELKKRFPEASTSLTKLDPDYRKTEVALRRTV---------PVEEV-------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 pekitdviKKLPESIKEKFYVVRSvPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGN 238
Cdd:PRK01158 130 --------RELLEELGLDLEIVDS-GFAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVAN 200

                        250       260       270
                 ....*....|....*....|....*....|
gi 489821682 239 ATEHIKEIANYTTTTNNEDGVAQAIQMLIL 268
Cdd:PRK01158 201 ADEELKEAADYVTEKSYGEGVAEAIEHLLL 230
PLN02887 PLN02887
hydrolase family protein
 2-263 3.59e-32

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 124.22  E-value: 3.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   2 YKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldegdyaiTFNGAVVLETASEKT 81
Cdd:PLN02887 308 FSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDL--------AGKDGIISESSPGVF 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  82 LADITLNKTELEEIYAfchaENVNVTYFDGKNMYVPSRKITEIT-CQDSL--LLGTPL-------YHLP-------VEEA 144
Cdd:PLN02887 380 LQGLLVYGRQGREIYR----SNLDQEVCREACLYSLEHKIPLIAfSQDRCltLFDHPLvdslhtiYHEPkaeimssVDQL 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 145 PESIHVSKVMLLDSPEKITDVIKKL-PESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQEND 223
Cdd:PLN02887 456 LAAADIQKVIFLDTAEGVSSVLRPYwSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGEND 535

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 489821682 224 ITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDGVAQAI 263
Cdd:PLN02887 536 IEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-268 5.95e-26

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 102.79  E-value: 5.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   2 YKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldegDY-AITFNGAVVLETASEK 80
Cdd:PRK10530   3 YRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALAL----DTpAICCNGTYLYDYQAKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  81 TLADITLNKTEleeiyafchAENVnVTYFDGKN----MYVpsrkiteitcQDSLLLGTPLYH----------LPVEEAPE 146
Cdd:PRK10530  79 VLEADPLPVQQ---------ALQV-IEMLDEHQihglMYV----------DDAMLYEHPTGHvirtlnwaqtLPPEQRPT 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 147 SIHVSKvmLLDSPEKITDVIK---------KLPESIKEkfyVVRSVPYNLEF--------LQKGVNKGSALASLAEKLGV 209
Cdd:PRK10530 139 FTQVDS--LAQAARQVNAIWKfalthedlpQLQHFAKH---VEHELGLECEWswhdqvdiARKGNSKGKRLTQWVEAQGW 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489821682 210 SQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDGVAQAIQMLIL 268
Cdd:PRK10530 214 SMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHVL 272
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-263 4.19e-25

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: 99.46  E-value: 4.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    5 IAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIeldLLDEGDYAITFNGAVVLETASEKTLAD 84
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAK---LIGTPDPVIAENGGEISYNEGLDDIFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   85 ITLNKT-----ELEEIYAFchaENVNVTYFDGKNMYVPSrkiteitcqdslllgtplYHLPVEEAPEsihvskvmlldsp 159
Cdd:TIGR01482  78 AYLEEEwfldiVIAKTFPF---SRLKVQYPRRASLVKMR------------------YGIDVDTVRE------------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  160 ekitdVIKKLPESIKEKfyvvrSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNA 239
Cdd:TIGR01482 124 -----IIKELGLNLVAV-----DSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANA 193

                         250       260
                  ....*....|....*....|....
gi 489821682  240 TEHIKEIANYTTTTNNEDGVAQAI 263
Cdd:TIGR01482 194 QPELKEWADYVTESPYGEGGAEAI 217
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 3-263 1.97e-23

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: 94.81  E-value: 1.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    3 KIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGR--PLAGIKKSLIELDlldegDYAITFNGAVVLETASEK 80
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNtvPFARALAVLIGTS-----GPVVAENGGVIFYNKEDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   81 TLADITLNKTELEEIYAFCHAENVNVTYfdgknmyvpSRKITEItcqdslllgtplyhlpveeapesihvskvmllDSPE 160
Cdd:TIGR01487  77 FLANMEEEWFLDEEKKKRFPRDRLSNEY---------PRASLVI--------------------------------MREG 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  161 KITDVIKKLpesIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNAT 240
Cdd:TIGR01487 116 KDVDEVREI---IKERGLNLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANAD 192

                         250       260
                  ....*....|....*....|...
gi 489821682  241 EHIKEIANYTTTTNNEDGVAQAI 263
Cdd:TIGR01487 193 DQLKEIADYVTSNPYGEGVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 193-266 3.11e-23

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: 91.88  E-value: 3.11e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821682 193 GVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDGVAQAIQML 266
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
PRK10976 PRK10976
putative hydrolase; Provisional
 1-246 2.60e-21

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 90.11  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGR---PLAGIKKSLiELDlldegDYAITFNGAVVLETA 77
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRhhvDVGQIRDNL-EIK-----SYMITSNGARVHDTD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  78 SEKtladITLNKTELEEIYAFCHAENVNvtyfdgknmyvpSRKITEITCQDSLLLGTPL-------------YHL--PVE 142
Cdd:PRK10976  75 GNL----IFSHNLDRDIASDLFGVVHDN------------PDIITNVYRDDEWFMNRHRpeemrffkeavfkYQLyePGL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 143 EAPESihVSKVMLL-DSPEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQE 221
Cdd:PRK10976 139 LEPDG--VSKVFFTcDSHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGM 216

                        250       260
                 ....*....|....*....|....*
gi 489821682 222 NDITMIEYAGMGVAMGNATEHIKEI 246
Cdd:PRK10976 217 NDAEMLSMAGKGCIMGNAHQRLKDL 241
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-236 6.01e-21

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: 87.82  E-value: 6.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    4 IIAIDIDGTLLN-DAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVlETASEKTL 82
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNL---PLPLIAENGALI-FYPGEILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   83 A-DITLNKTELEEIYA-FCHAENVNVTYFDGKNMYVPSRKITeitcqdslllgtplYHLPVEEAPEsihvskVMLLDSPE 160
Cdd:TIGR01484  77 IePSDVFEEILGIKFEeIGAELKSLSEHYVGTFIEDKAIAVA--------------IHYVGAELGQ------ELDSKMRE 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821682  161 KItDVIKklpeSIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAM 236
Cdd:TIGR01484 137 RL-EKIG----RNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK15126 PRK15126
HMP-PP phosphatase;
1-239 5.45e-15

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 72.80  E-value: 5.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldEGdYAITFNGAVVLETASEK 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSL--DA-YLITGNGTRVHSLEGEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  81 TLADiTLNKTELEEIY-------AFCHAENVNvTYFDGKNmyVPSRKITEITCQDSLLLgTPLYHLPVEeapesiHVSKV 153
Cdd:PRK15126  78 LHRQ-DLPADVAELVLhqqwdtrASMHVFNDD-GWFTGKE--IPALLQAHVYSGFRYQL-IDLKRLPAH------GVTKI 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 154 MLLDSPEKITDVIKKLPESIKEKFYVVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMG 233
Cdd:PRK15126 147 CFCGDHDDLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRG 226


                 ....*.
gi 489821682 234 VAMGNA 239
Cdd:PRK15126 227 FIMGNA 232
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 159-264 1.99e-10

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: 59.28  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 159 PEKITDVIKKLPESIKEKFY---VVRSVP--YNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMG 233
Cdd:cd02605  128 PQNDAAVIEQLEEMLLKAGLtvrIIYSSGlaYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRG 207

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489821682 234 VAMGNATEHIK----EIANYTTTTNNE-DGVAQAIQ 264
Cdd:cd02605  208 VIVGNAQPELLkwadRVTRSRLAKGPYaGGILEGLA 243
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 188-260 1.05e-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: 52.91  E-value: 1.05e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821682 188 EFLQKGV-NKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDGVA 260
Cdd:cd01630   68 EDLFQGVkDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAV 141
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-73 5.24e-08

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: 50.09  E-value: 5.24e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489821682   5 IAIDIDGTLLndaheitlaVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLLDEGDYAITFNGAVV 73
Cdd:cd01427    2 VLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT 61
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-267 7.18e-08

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 52.25  E-value: 7.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAIDIDGTLLnDAHEITL-AVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLldeGDYAITFNGAVVLETASE 79
Cdd:PRK00192   3 MKLLVFTDLDGTLL-DHHTYSYePAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGL---EDPFIVENGAAIYIPKNY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  80 KTLADITLNKTELEEIYAFChaenvnvtyfdgknmyVPSRKITEITCQDSLLLG---TPLYHLPVEEA-------PESI- 148
Cdd:PRK00192  79 FPFQPDGERLKGDYWVIELG----------------PPYEELREILDEISDELGyplKGFGDLSAEEVaeltglsGESAr 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 149 -----HVSKVMLLDSPEKITDVIKKLPESikekfyvvrsvpYNLEFLQ--------KGVNKGSALASLAEKLGVSQS-EV 214
Cdd:PRK00192 143 lakdrEFSEPFLWNGSEAAKERFEEALKR------------LGLKVTRggrflhllGGGDKGKAVRWLKELYRRQDGvET 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 215 MSIGDQENDITMIEYAGMGVAMGNAT----EHIKEIAN---YTTTTNNEDGVAQAIQMLI 267
Cdd:PRK00192 211 IALGDSPNDLPMLEAADIAVVVPGPDgpnpPLLPGIADgefILASAPGPEGWAEAINKLL 270
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 3-241 1.91e-07

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 50.73  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    3 KIIAIDIDGTLLnDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIELDLLdEGDYAIT-------FNGAVVLE 75
Cdd:pfam05116   3 LLLVSDLDNTLV-DGDNEALARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLP-TPDYLITsvgteiyYGPSLVPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   76 TASEKTLaDITLNKTELEEIyafchaenvnvtyfdgknmyvpSRKITEITCQDSLLLGtPL---YHLPVEEAPESIHVSK 152
Cdd:pfam05116  81 QSWQEHL-DYHWDRQAVVEA----------------------LAKFPGLTLQPEEEQR-PHkvsYFLDPEAAAAVLAELE 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  153 VMLLDSpekitdvikKLPESIkekfyvVRSVPYNLEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGM 232
Cdd:pfam05116 137 QLLRKR---------GLDVKV------IYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTR 201


                  ....*....
gi 489821682  233 GVAMGNATE 241
Cdd:pfam05116 202 GVVVGNAQP 210
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 195-235 4.82e-06

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 46.00  E-value: 4.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489821682 195 NKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVA 235
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 193-247 5.94e-06

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: 45.98  E-value: 5.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489821682 193 GVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMgNATEHIKEIA 247
Cdd:COG0560  153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAA 206
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 4-228 7.55e-06

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 46.20  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   4 IIAIDIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGrplagikKSLIEL----DLLDEGDYAITFNGAVV------ 73
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTS-------KTRAEVeylrKELGIEDPFIVENGGAIfiprgy 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  74 ----LETASEKTLADITLNKT------ELEEIYAFCHAenVNVTYFDgknmyVPSRKITEITcqdslllgtplyHLPVEE 143
Cdd:cd07507   74 fkfpGRCKSEGGYEVIELGKPyreiraALEKIREETGF--KITGFGD-----LTEEEIAELT------------GLPRER 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 144 AP--------ESIhvskvMLLDSPEKITDVIKKLPESIKEkfYVVRSVPYNLefLQKGVNKGSALASLAE--KLGVSQSE 213
Cdd:cd07507  135 AAlakereysETI-----ILRSDEEEDEKVLEALEERGLK--ITKGGRFYHV--LGAGADKGKAVAILAAlyRQLYEAIV 205

                        250
                 ....*....|....*
gi 489821682 214 VMSIGDQENDITMIE 228
Cdd:cd07507  206 TVGLGDSPNDLPMLE 220
PLN02382 PLN02382
probable sucrose-phosphatase
 147-241 3.84e-05

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 44.59  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682 147 SIHVSKvmlldspEKITDVIKKLPESIKEK---FYVVRSVPYNLEFLQKGVNKGSALASLAEKL---GVSQSEVMSIGDQ 220
Cdd:PLN02382 131 SFYVDK-------KKAQEVIKELSERLEKRgldVKIIYSGGIDLDVLPQGAGKGQALAYLLKKLkaeGKAPVNTLVCGDS 203

                         90       100
                 ....*....|....*....|..
gi 489821682 221 ENDITMIEYAGM-GVAMGNATE 241
Cdd:PLN02382 204 GNDAELFSVPDVyGVMVSNAQE 225
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-231 4.72e-05

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: 42.96  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682    2 YKIIAIDIDGTLLNDAHEITLAVRDsikaakakgvkvvLCTGRPLA-GIKKSLIELDLLDEGDYAITFNGAVVLETASEK 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAE-------------LASEHPLAkAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDI 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   81 TLADITLNKTELEEIYAfchaenvnvtyfdgknmyvpSRKITEITCQDSLLLgtplyHLPVEEAPESIH---VSKVMLLD 157
Cdd:pfam00702  68 LRGLVETLEAEGLTVVL--------------------VELLGVIALADELKL-----YPGAAEALKALKergIKVAILTG 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821682  158 SPEKITDVIKKLPESIKEKFYVVRSvpynlEFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAG 231
Cdd:pfam00702 123 DNPEAAEALLRLLGLDDYFDVVISG-----DDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 188-268 7.76e-05

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: 42.13  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682  188 EFLQKGVNKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDG-VAQAIQML 266
Cdd:TIGR01670  69 HLYQGQSNKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGaVREVCELL 148


                  ..
gi 489821682  267 IL 268
Cdd:TIGR01670 149 LL 150
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-79 1.04e-04

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 42.63  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821682   1 MYKIIAI-DIDGTLLNDAHEITLAVRDSIKAAKAKGVKVVLCTGRPLAGIKKSLIElDLLDEGDYAITFNGAVVLETASE 79
Cdd:PTZ00174   3 MKKTILLfDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKIKEQLGE-DVLEDFDYVFSENGLVAYKDGEL 81
serB PRK11133
phosphoserine phosphatase; Provisional
 196-235 1.17e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 42.63  E-value: 1.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489821682 196 KGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVA 235
Cdd:PRK11133 249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 196-247 1.31e-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: 41.96  E-value: 1.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489821682  196 KGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMgNATEHIKEIA 247
Cdd:TIGR00338 153 KGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKA 203
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 5-58 6.57e-04

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 38.22  E-value: 6.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489821682    5 IAIDIDGTLLNDAHEITLAVrDSIKAAKAKGVKVVLCT---GRPLAGIKKSLIELDL 58
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGAA-EALRALRAAGKPVVFVTnnsSRSREEYAEKLRKLGF 56
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
195-268 1.11e-03

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 39.14  E-value: 1.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489821682 195 NKGSALASLAEKLGVSQSEVMSIGDQENDITMIEYAGMGVAMGNATEHIKEIANYTTTTNNEDGVAQAIQMLIL 268
Cdd:PRK09484  96 NKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLL 169
 
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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