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Conserved domains on  [gi|489080678|ref|WP_002990612|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Streptococcus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-266 1.27e-78

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 238.26  E-value: 1.27e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   5 ILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDK 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDS---PLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  85 SSLSFDQVCQIQQALEAVGLPTDIISggdvysipSKDGRHSQY--HLANPLLTFIEVTSVAELPKDITYNKIVTVTDPDF 162
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYT--------NDDWADTIYeeNEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 163 LDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVS 242
Cdd:cd07516  150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                        250       260
                 ....*....|....*....|....
gi 489080678 243 GAKAVADAVtTLTNDESGVAEAVK 266
Cdd:cd07516  230 EVKEAADYV-TLTNNEDGVAKAIE 252
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-266 1.27e-78

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 238.26  E-value: 1.27e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   5 ILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDK 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDS---PLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  85 SSLSFDQVCQIQQALEAVGLPTDIISggdvysipSKDGRHSQY--HLANPLLTFIEVTSVAELPKDITYNKIVTVTDPDF 162
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYT--------NDDWADTIYeeNEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 163 LDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVS 242
Cdd:cd07516  150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                        250       260
                 ....*....|....*....|....
gi 489080678 243 GAKAVADAVtTLTNDESGVAEAVK 266
Cdd:cd07516  230 EVKEAADYV-TLTNNEDGVAKAIE 252
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-270 2.43e-64

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 202.62  E-value: 2.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   1 MNIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDHDDYSITFNGGLVQR-NTG 79
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKaADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  80 EVLDKSSLSFDQVCQIQQALEAVGLPTDIISGGDVYSiPSKDgrHSQYHLANPLLTFIEVT--SVAELPKDITYNKIVTV 157
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT-ANRD--ISYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 158 TDPDFLDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAM 237
Cdd:PRK10513 158 DEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAM 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489080678 238 ANGVSGAKAVADAVTTlTNDESGVAEAVKTFIL 270
Cdd:PRK10513 238 GNAIPSVKEVAQFVTK-SNLEDGVAFAIEKYVL 269
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-264 8.38e-63

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 197.85  E-value: 8.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    6 LALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDKS 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   86 SLSFDQVCQIQQALEAVGLPTDIISGGDVYsIPSKDGRHSQYHLANPLLTFIEVTSVAELPKDITYNKIVTVTDPDFLDQ 165
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVY-ILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  166 QIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAK 245
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 489080678  246 AVADAVTTlTNDESGVAEA 264
Cdd:pfam08282 237 AAADYVTD-SNNEDGVAKA 254
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-264 8.76e-55

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: 177.46  E-value: 8.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    5 ILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDK 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   85 SSLSFDQVCQIQQALEAVGLPTDIISGGDVYsIPSKDGRHSQYHLANPLLTFIEVTSVAELPKDItYNKIVTVTDPDFLD 164
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIY-ASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  165 QQIIKL-SPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSG 243
Cdd:TIGR00099 156 LLIEALnKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489080678  244 AKAVADaVTTLTNDESGVAEA 264
Cdd:TIGR00099 236 LKALAD-YVTDSNNEDGVALA 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-268 1.08e-54

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: 174.94  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   2 NIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIgnlLEELDLLDHDDYSITFNGGLVQRNTGEV 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSA---LPLLEELGLDDPLITSNGALIYDPDGEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  82 LDKSSLSFDQVCQIQQALEAVGLPTDIIsggdvysipskdgrhsqyhlanplltfievtsvaelpkditynkivtvtdpd 161
Cdd:COG0561   78 LYERPLDPEDVREILELLREHGLHLQVV---------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 162 fldqqiiklspslfedfeaFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGV 241
Cdd:COG0561  106 -------------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAP 166

                        250       260
                 ....*....|....*....|....*..
gi 489080678 242 SGAKAVADAVtTLTNDESGVAEAVKTF 268
Cdd:COG0561  167 PEVKAAADYV-TGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-266 1.27e-78

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 238.26  E-value: 1.27e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   5 ILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDK 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDS---PLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  85 SSLSFDQVCQIQQALEAVGLPTDIISggdvysipSKDGRHSQY--HLANPLLTFIEVTSVAELPKDITYNKIVTVTDPDF 162
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYT--------NDDWADTIYeeNEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 163 LDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVS 242
Cdd:cd07516  150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                        250       260
                 ....*....|....*....|....
gi 489080678 243 GAKAVADAVtTLTNDESGVAEAVK 266
Cdd:cd07516  230 EVKEAADYV-TLTNNEDGVAKAIE 252
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-270 2.43e-64

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 202.62  E-value: 2.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   1 MNIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDHDDYSITFNGGLVQR-NTG 79
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKaADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  80 EVLDKSSLSFDQVCQIQQALEAVGLPTDIISGGDVYSiPSKDgrHSQYHLANPLLTFIEVT--SVAELPKDITYNKIVTV 157
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT-ANRD--ISYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 158 TDPDFLDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAM 237
Cdd:PRK10513 158 DEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAM 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489080678 238 ANGVSGAKAVADAVTTlTNDESGVAEAVKTFIL 270
Cdd:PRK10513 238 GNAIPSVKEVAQFVTK-SNLEDGVAFAIEKYVL 269
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-264 8.38e-63

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 197.85  E-value: 8.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    6 LALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDKS 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD---PVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   86 SLSFDQVCQIQQALEAVGLPTDIISGGDVYsIPSKDGRHSQYHLANPLLTFIEVTSVAELPKDITYNKIVTVTDPDFLDQ 165
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVY-ILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  166 QIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAK 245
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*....
gi 489080678  246 AVADAVTTlTNDESGVAEA 264
Cdd:pfam08282 237 AAADYVTD-SNNEDGVAKA 254
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-264 8.76e-55

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: 177.46  E-value: 8.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    5 ILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLDK 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   85 SSLSFDQVCQIQQALEAVGLPTDIISGGDVYsIPSKDGRHSQYHLANPLLTFIEVTSVAELPKDItYNKIVTVTDPDFLD 164
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIY-ASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  165 QQIIKL-SPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSG 243
Cdd:TIGR00099 156 LLIEALnKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489080678  244 AKAVADaVTTLTNDESGVAEA 264
Cdd:TIGR00099 236 LKALAD-YVTDSNNEDGVALA 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-268 1.08e-54

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: 174.94  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   2 NIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIgnlLEELDLLDHDDYSITFNGGLVQRNTGEV 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSA---LPLLEELGLDDPLITSNGALIYDPDGEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  82 LDKSSLSFDQVCQIQQALEAVGLPTDIIsggdvysipskdgrhsqyhlanplltfievtsvaelpkditynkivtvtdpd 161
Cdd:COG0561   78 LYERPLDPEDVREILELLREHGLHLQVV---------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 162 fldqqiiklspslfedfeaFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGV 241
Cdd:COG0561  106 -------------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAP 166

                        250       260
                 ....*....|....*....|....*..
gi 489080678 242 SGAKAVADAVtTLTNDESGVAEAVKTF 268
Cdd:COG0561  167 PEVKAAADYV-TGSNDEDGVAEALEKL 192
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-268 6.49e-30

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: 111.93  E-value: 6.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   4 RILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIgnllEELDLLDHDDYSITFNGGLVQrNTGEVLD 83
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEI----QPIVKALGIDSYVSYNGQYVF-FEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  84 KSSLSfdqvcqiQQALEAVglptdiisggdvysIPSKDGRHSQYHLANPLLTFievtsvaelpkditynkivtvtdpdFL 163
Cdd:cd07517   76 KNPLP-------QELVERL--------------TEFAKEQGHPVSFYGQLLLF-------------------------ED 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 164 DQQIIKLSPsLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSG 243
Cdd:cd07517  110 EEEEQKYEE-LRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEE 188

                        250       260
                 ....*....|....*....|....*
gi 489080678 244 AKAVADAVTTlTNDESGVAEAVKTF 268
Cdd:cd07517  189 LKEIADYVTK-DVDEDGILKALKHF 212
PLN02887 PLN02887
hydrolase family protein
 9-265 2.78e-24

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 101.87  E-value: 2.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   9 DLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTG--RP-----LKAIgNLLEELDLLDHDDYSITFNGGLVQRNTGEV 81
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGkaRPavidiLKMV-DLAGKDGIISESSPGVFLQGLLVYGRQGRE 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  82 LDKSSLSFDqVCQ--IQQALEAvGLPTDIISGGDVYSI---PSKDGRHSQYHLANPLLtfieVTSVAELPKDITYNKIVT 156
Cdd:PLN02887 393 IYRSNLDQE-VCReaCLYSLEH-KIPLIAFSQDRCLTLfdhPLVDSLHTIYHEPKAEI----MSSVDQLLAAADIQKVIF 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 157 VTDPDFLDQQIIKLSPSLFED-FEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGV 235
Cdd:PLN02887 467 LDTAEGVSSVLRPYWSEATGDrANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGV 546

                        250       260       270
                 ....*....|....*....|....*....|
gi 489080678 236 AMANGVSGAKAVADaVTTLTNDESGVAEAV 265
Cdd:PLN02887 547 ALSNGAEKTKAVAD-VIGVSNDEDGVADAI 575
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-270 3.05e-21

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 90.08  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   1 MNIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIgnlleeldlldHDDY--------SITFNGG 72
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAI-----------HPFYqalaldtpAICCNGT 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  73 -LVQRNTGEVLDKSSLSFDQVCQIQQALEAvglpTDI-----ISGGDVYSIPSkdG---RHSQYHLANPLL---TFIEVT 140
Cdd:PRK10530  70 yLYDYQAKKVLEADPLPVQQALQVIEMLDE----HQIhglmyVDDAMLYEHPT--GhviRTLNWAQTLPPEqrpTFTQVD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 141 SVAELPKDItyNKI--VTVTDPDfldqqIIKLspslfEDFEAFKSRDIIFE----------IMPKGIDKAFGLNLLCQHL 208
Cdd:PRK10530 144 SLAQAARQV--NAIwkFALTHED-----LPQL-----QHFAKHVEHELGLEcewswhdqvdIARKGNSKGKRLTQWVEAQ 211

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489080678 209 GLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAKAVADAVtTLTNDESGVAEAVKTFIL 270
Cdd:PRK10530 212 GWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLV-IGDNTTPSIAEFIYSHVL 272
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-270 8.18e-21

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 88.11  E-value: 8.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   1 MNIRILALDLDGTL-YNTEKIVTDAnKKALAAAREKGVKVVITTGRPL-------KAIGnlleeldlldhddysitFNGG 72
Cdd:PRK01158   1 MKIKAIAIDIDGTItDKDRRLSLKA-VEAIRKAEKLGIPVILATGNVLcfaraaaKLIG-----------------TSGP 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  73 LVQRNTGEVLDKSSLsfdqvcqiqqaleavglpTDIISGgdvysipSKDGRHSQYHLanpLLTFIEVTSVAELPKDITYN 152
Cdd:PRK01158  63 VIAENGGVISVGFDG------------------KRIFLG-------DIEECEKAYSE---LKKRFPEASTSLTKLDPDYR 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 153 KIVTVTDPDFLDQQIIKLSPSLFEDFEAFKSRDIIfEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAG 232
Cdd:PRK01158 115 KTEVALRRTVPVEEVRELLEELGLDLEIVDSGFAI-HIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAG 193

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489080678 233 LGVAMANGVSGAKAVADAVTTLTNDEsGVAEAVKTFIL 270
Cdd:PRK01158 194 FGVAVANADEELKEAADYVTEKSYGE-GVAEAIEHLLL 230
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 151-266 1.24e-20

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: 86.48  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 151 YNKIVTVTDPDFLDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEW 230
Cdd:cd07518   70 YFKFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKY 149

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489080678 231 AGLGVAMANGVSGAKAVADAvTTLTNDESGVAEAVK 266
Cdd:cd07518  150 AGYSYAMENAPEEVKAAAKY-VAPSNNENGVLQVIE 184
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-237 3.96e-20

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: 85.90  E-value: 3.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    5 ILALDLDGTLYN-TEKIVTDANKKALAAAREKGVKVVITTGRPLKAIgnlLEELDLLDHDDYSITFNGGLVQRNTGEVLD 83
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEI---KELLKQLNLPLPLIAENGALIFYPGEILYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   84 KSSLSFDQVCQIQQALeaVGLPTDIISGgdvysipskdgrhsqyHLANPLLTFIEVTSVAELPKDITYnkivTVTDPDFL 163
Cdd:TIGR01484  78 EPSDVFEEILGIKFEE--IGAELKSLSE----------------HYVGTFIEDKAIAVAIHYVGAELG----QELDSKMR 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489080678  164 DqqIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAM 237
Cdd:TIGR01484 136 E--RLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 194-268 8.25e-15

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: 69.54  E-value: 8.25e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489080678 194 GIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAKAVADAVTTLTNDEsGVAEAVKTF 268
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGD-GVLEAIDKL 138
PRK15126 PRK15126
HMP-PP phosphatase;
4-246 1.63e-12

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 65.87  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   4 RILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRP-------LKAIGnlleeldlldHDDYSITFNGGLVQR 76
Cdd:PRK15126   3 RLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHvlemqhiLGALS----------LDAYLITGNGTRVHS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  77 NTGEVLDKSSLSfdqvcqiQQALEAVgLPTDIISGGDVYsIPSKDGRHSQYHLANPLLTFI------EVTSVAELPKDiT 150
Cdd:PRK15126  73 LEGELLHRQDLP-------ADVAELV-LHQQWDTRASMH-VFNDDGWFTGKEIPALLQAHVysgfryQLIDLKRLPAH-G 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 151 YNKIVTVTDPDFLDQQIIKLSpslfedfEAFKSR-DIIF------EIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEAN 223
Cdd:PRK15126 143 VTKICFCGDHDDLTRLQIQLN-------EALGERaHLCFsatdclEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMN 215

                        250       260
                 ....*....|....*....|...
gi 489080678 224 DFAMLEWAGLGVAMANGVSGAKA 246
Cdd:PRK15126 216 DREMLGSVGRGFIMGNAMPQLRA 238
PRK10976 PRK10976
putative hydrolase; Provisional
 4-239 9.83e-08

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 51.97  E-value: 9.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   4 RILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAIGNLLEELDLLDhddYSITFNGGLVQRNTGEVLD 83
Cdd:PRK10976   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKS---YMITSNGARVHDTDGNLIF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  84 KSSLSFD---QVCQIQQAleavglPTDIISggDVY---------SIPSKD----GRHSQYHLANPlltfievtsvAELPK 147
Cdd:PRK10976  80 SHNLDRDiasDLFGVVHD------NPDIIT--NVYrddewfmnrHRPEEMrffkEAVFKYQLYEP----------GLLEP 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 148 DITYNKIVTVTDPDFLdqqiIKLSpslfedfEAFKSR-----DIIF------EIMPKGIDKAFGLNLLCQHLGLDARHVM 216
Cdd:PRK10976 142 DGVSKVFFTCDSHEKL----LPLE-------QAINARwgdrvNVSFstltclEVMAGGVSKGHALEAVAKKLGYSLKDCI 210

                        250       260
                 ....*....|....*....|...
gi 489080678 217 AMGDEANDFAMLEWAGLGVAMAN 239
Cdd:PRK10976 211 AFGDGMNDAEMLSMAGKGCIMGN 233
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 197-236 1.48e-07

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: 50.24  E-value: 1.48e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489080678 197 KAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVA 236
Cdd:cd07500  138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 197-236 2.02e-07

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: 50.61  E-value: 2.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489080678 197 KAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVA 236
Cdd:COG0560  156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVA 195
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 196-265 2.13e-07

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: 49.06  E-value: 2.13e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 196 DKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAKAVADAVTTLTNDESGVAEAV 265
Cdd:cd01630   76 DKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVC 145
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 190-268 3.01e-07

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: 50.04  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 190 IMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMANGVSGAKAVADAVTTLTNDES----GVAEAV 265
Cdd:cd02605  163 ILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKGpyagGILEGL 242


                 ...
gi 489080678 266 KTF 268
Cdd:cd02605  243 AHF 245
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 183-239 2.02e-05

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: 44.95  E-value: 2.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489080678  183 SRDIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVAMAN 239
Cdd:pfam05116 151 SSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGN 207
serB PRK11133
phosphoserine phosphatase; Provisional
 197-236 9.13e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.93  E-value: 9.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489080678 197 KAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAGLGVA 236
Cdd:PRK11133 249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-43 1.51e-03

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 39.32  E-value: 1.51e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489080678   1 MNIRILALDLDGTLYNTEKIVTDAnKKALAAAREKGVKVVITT 43
Cdd:COG0647    6 DRYDAFLLDLDGVLYRGDEPIPGA-VEALARLRAAGKPVLFLT 47
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-232 1.89e-03

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 38.34  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678    3 IRILALDLDGTLYNTEKIVTDANKKAlaaarekgvkvviTTGRPLKAIGNLLEELDLLDHDDYSITFNGGLVQRntgevl 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAEL-------------ASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDW------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678   83 dksslsFDQVCQIQQALEAVGLPTDIISGGDVYSIpskdgrhsqYHLANPLLTFIEVTSVAELPKDITYnKIVTVTDPDF 162
Cdd:pfam00702  62 ------LEELDILRGLVETLEAEGLTVVLVELLGV---------IALADELKLYPGAAEALKALKERGI-KVAILTGDNP 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678  163 LDQQIIKLSPSLFEDFEAFKSRDIIFEIMPKGIDKafglNLLCQHLGLDARHVMAMGDEANDFAMLEWAG 232
Cdd:pfam00702 126 EAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIY----LAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 8-50 2.10e-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: 36.99  E-value: 2.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489080678   8 LDLDGTLYNTEkivtdankkALAAAREKGVKVVITTGRPLKAI 50
Cdd:cd01427    4 FDLDGTLLAVE---------LLKRLRAAGIKLAIVTNRSREAL 37
P-type_ATPase cd07539
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ...
 211-253 4.46e-03

uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319840 [Multi-domain]  Cd Length: 634  Bit Score: 38.17  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489080678 211 DARHVMAM-GDEANDFAMLEWAGLGVAMAN-GVSGAKAVADAVTT 253
Cdd:cd07539  516 AAGRVVAMtGDGANDAAAIRAADVGIGVGArGSDAAREAADLVLT 560
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-50 7.39e-03

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 36.85  E-value: 7.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489080678   1 MNIRILALDLDGTLYNTEKIVTDANKKALAAAREKGVKVVITTGRPLKAI 50
Cdd:PTZ00174   3 MKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKI 52
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 154-237 7.78e-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: 35.45  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489080678 154 IVTVTDPDFLDQQIIKLSPSLFEDFEafksrdIIFEIMPKGIDKAFGLNLLCQHLGLDARHVMAMGDEANDFAMLEWAG- 232
Cdd:cd01427   28 IVTNRSREALRALLEKLGLGDLFDGI------IGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGg 101


                 ....*
gi 489080678 233 LGVAM 237
Cdd:cd01427  102 RTVAV 106
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
210-257 8.32e-03

Soluble P-type ATPase [General function prediction only];


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 35.91  E-value: 8.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489080678 210 LDARHVMAMGDEANDFAMLEWAGLGVA--MANGVSG-AKAVADAVTTLTND 257
Cdd:COG4087   89 LGAETTVAIGNGRNDVLMLKEAALGIAviGPEGASVkALLAADIVVKSILD 139
 
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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