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Conserved domains on  [gi|446563088|ref|WP_000640434|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Bacillus]

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 ...
 5-270 8.63e-72

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: 221.32  E-value: 8.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   5 LLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRL 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  85 SEEktfnIVQVLEHFDCNVRISHERFSignRERNTPNLIARTVLSSadplfyPVQFVDSLGDALRDHPVAAPKIDVVFHS 164
Cdd:cd07516   81 SKE----DVKELEEFLRKLGIGINIYT---NDDWADTIYEENEDDE------IIKPAEILDDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 165 KGEKERGLTTLRKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNA 244
Cdd:cd07516  148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 446563088 245 PVELKQAADWITRSNSENGVEYMIKE 270
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 8.63e-72

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: 221.32  E-value: 8.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   5 LLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRL 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  85 SEEktfnIVQVLEHFDCNVRISHERFSignRERNTPNLIARTVLSSadplfyPVQFVDSLGDALRDHPVAAPKIDVVFHS 164
Cdd:cd07516   81 SKE----DVKELEEFLRKLGIGINIYT---NDDWADTIYEENEDDE------IIKPAEILDDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 165 KGEKERGLTTLRKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNA 244
Cdd:cd07516  148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 446563088 245 PVELKQAADWITRSNSENGVEYMIKE 270
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-268 8.24e-51

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 167.80  E-value: 8.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    6 LALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRLS 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   86 EEKTFNIVQVLEHFDCNVRISHERFSIGNRERNTpnliartvLSSADPLFYPVQFVDSLGDALRDHPVAAPKIdVVFHSK 165
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNEL--------EKILKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  166 GEKERglttLRKAFQDIEYVECDAKR-----IEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVA 240
Cdd:pfam08282 152 EDLDE----LEKELKELFGSLITITSsgpgyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227

                         250       260
                  ....*....|....*....|....*...
gi 446563088  241 MGNAPVELKQAADWITRSNSENGVEYMI 268
Cdd:pfam08282 228 MGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-271 2.47e-49

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: 161.84  E-value: 2.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   3 YRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQR 82
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  83 RLSEEKTFNIVQVLEHFDCNvrisherfsignrerntpnliartvlssadplfypvqfvdslgdalrdhpvaapkIDVVF 162
Cdd:COG0561   82 PLDPEDVREILELLREHGLH-------------------------------------------------------LQVVV 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 163 HSKGEkerglttlrkafqdieyvecdakRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMG 242
Cdd:COG0561  107 RSGPG-----------------------FLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 446563088 243 NAPVELKQAADWITRSNSENGVEYMIKEH 271
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-264 2.09e-31

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: 117.37  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    5 LLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRL 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   85 SEEKTFNIVQVLEHFDCNV-----------RISHERFSIGNRERNTPNLIARTVLSSADPLFYPVQFVDSLGDAlrdhpv 153
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVilygddsiyasKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDL------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  154 aaPKIDVVFHSKGEKErGLTTLRKAfqdieyvecdAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIE 233
Cdd:TIGR00099 155 --DLLIEALNKLELEE-NVSVVSSG----------PYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLE 221

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446563088  234 NVGLGVAMGNAPVELKQAADWITRSNSENGV 264
Cdd:TIGR00099 222 AAGYGVAMGNADEELKALADYVTDSNNEDGV 252
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-269 1.80e-25

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 102.08  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   1 MIYRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDS---ILVTHGGAFVSATLDK 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQpgdYCITNNGALVQKAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  78 PYVqrrLSEEKTFNIVQVLEHFDCNVRISHERFSigNRERNTPN--LIARTVLSS---ADPLFY-PVQFVDSlgdALR-- 149
Cdd:PRK10513  81 ETV---AQTALSYDDYLYLEKLSREVGVHFHALD--RNTLYTANrdISYYTVHESfltGIPLVFrEVEKMDP---NLQfp 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 150 -----DHPvaapkiDVVfhskgekERGLTTL-RKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIG 223
Cdd:PRK10513 153 kvmmiDEP------EIL-------DAAIARIpAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIG 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446563088 224 DSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGVEYMIK 269
Cdd:PRK10513 220 DQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 8.63e-72

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: 221.32  E-value: 8.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   5 LLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRL 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  85 SEEktfnIVQVLEHFDCNVRISHERFSignRERNTPNLIARTVLSSadplfyPVQFVDSLGDALRDHPVAAPKIDVVFHS 164
Cdd:cd07516   81 SKE----DVKELEEFLRKLGIGINIYT---NDDWADTIYEENEDDE------IIKPAEILDDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 165 KGEKERGLTTLRKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNA 244
Cdd:cd07516  148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 446563088 245 PVELKQAADWITRSNSENGVEYMIKE 270
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-268 8.24e-51

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 167.80  E-value: 8.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    6 LALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRLS 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   86 EEKTFNIVQVLEHFDCNVRISHERFSIGNRERNTpnliartvLSSADPLFYPVQFVDSLGDALRDHPVAAPKIdVVFHSK 165
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNEL--------EKILKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  166 GEKERglttLRKAFQDIEYVECDAKR-----IEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVA 240
Cdd:pfam08282 152 EDLDE----LEKELKELFGSLITITSsgpgyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVA 227

                         250       260
                  ....*....|....*....|....*...
gi 446563088  241 MGNAPVELKQAADWITRSNSENGVEYMI 268
Cdd:pfam08282 228 MGNASPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-271 2.47e-49

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: 161.84  E-value: 2.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   3 YRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQR 82
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  83 RLSEEKTFNIVQVLEHFDCNvrisherfsignrerntpnliartvlssadplfypvqfvdslgdalrdhpvaapkIDVVF 162
Cdd:COG0561   82 PLDPEDVREILELLREHGLH-------------------------------------------------------LQVVV 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 163 HSKGEkerglttlrkafqdieyvecdakRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMG 242
Cdd:COG0561  107 RSGPG-----------------------FLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 446563088 243 NAPVELKQAADWITRSNSENGVEYMIKEH 271
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-264 2.09e-31

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: 117.37  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    5 LLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQRRL 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   85 SEEKTFNIVQVLEHFDCNV-----------RISHERFSIGNRERNTPNLIARTVLSSADPLFYPVQFVDSLGDAlrdhpv 153
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVilygddsiyasKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDL------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  154 aaPKIDVVFHSKGEKErGLTTLRKAfqdieyvecdAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIE 233
Cdd:TIGR00099 155 --DLLIEALNKLELEE-NVSVVSSG----------PYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLE 221

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446563088  234 NVGLGVAMGNAPVELKQAADWITRSNSENGV 264
Cdd:TIGR00099 222 AAGYGVAMGNADEELKALADYVTDSNNEDGV 252
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-269 1.80e-25

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 102.08  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   1 MIYRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDS---ILVTHGGAFVSATLDK 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQpgdYCITNNGALVQKAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  78 PYVqrrLSEEKTFNIVQVLEHFDCNVRISHERFSigNRERNTPN--LIARTVLSS---ADPLFY-PVQFVDSlgdALR-- 149
Cdd:PRK10513  81 ETV---AQTALSYDDYLYLEKLSREVGVHFHALD--RNTLYTANrdISYYTVHESfltGIPLVFrEVEKMDP---NLQfp 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 150 -----DHPvaapkiDVVfhskgekERGLTTL-RKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIG 223
Cdd:PRK10513 153 kvmmiDEP------EIL-------DAAIARIpAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIG 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446563088 224 DSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGVEYMIK 269
Cdd:PRK10513 220 DQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-271 1.11e-23

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: 95.75  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   4 RLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSIlVTHGGAFVsATLDKPYVQRR 83
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSY-VSYNGQYV-FFEGEVIYKNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  84 LSEEKtfnIVQVLEHFDcnvRISHErFSIGNrerntpnliARTVLSSADPLFYPVQFVDSLgDALRDHPVAApkidvvfh 163
Cdd:cd07517   79 LPQEL---VERLTEFAK---EQGHP-VSFYG---------QLLLFEDEEEEQKYEELRPEL-RFVRWHPLST-------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 164 skgekerglttlrkafqdieyvecdakriEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGN 243
Cdd:cd07517  134 -----------------------------DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                        250       260
                 ....*....|....*....|....*...
gi 446563088 244 APVELKQAADWITRSNSENGVEYMIKEH 271
Cdd:cd07517  185 AHEELKEIADYVTKDVDEDGILKALKHF 212
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 192-269 3.85e-21

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: 88.02  E-value: 3.85e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446563088 192 IEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGVEYMIK 269
Cdd:cd07518  107 IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-271 3.52e-17

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 79.30  E-value: 3.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   1 MIYRLLALNIDGTLLYNNGKIakgLRETIEFVKR---KDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVsatLDk 77
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTI---LPESLEALARareAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYL---YD- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  78 pYVQRR------LSEEKTFNIVQVLEHFDcnvrISH---------ERFSIGNRERnTPNLiARTVLSSADPLFypvQFVD 142
Cdd:PRK10530  74 -YQAKKvleadpLPVQQALQVIEMLDEHQ----IHGlmyvddamlYEHPTGHVIR-TLNW-AQTLPPEQRPTF---TQVD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 143 SLGDALRD------HPVAAPKIDVV--FHSKGEKERGLttlrkafqdieyvECD---AKRIEILPQNVSKLRGLQLLGEH 211
Cdd:PRK10530 144 SLAQAARQvnaiwkFALTHEDLPQLqhFAKHVEHELGL-------------ECEwswHDQVDIARKGNSKGKRLTQWVEA 210

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 212 LNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGVEYMIKEH 271
Cdd:PRK10530 211 QGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSH 270
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-272 3.70e-15

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 73.08  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   1 MIYRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPyv 80
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVGFDGK-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  81 qrrlseektfNIVqvlehfdcnvrisherfsIGNRERNTpnlIARTVLSSadplFYPVQFV--DSLGDALRdhpvaapKI 158
Cdd:PRK01158  79 ----------RIF------------------LGDIEECE---KAYSELKK----RFPEASTslTKLDPDYR-------KT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 159 DVVFHSKGEKERGLTTLRKAFQDIEYVecDAK-RIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGL 237
Cdd:PRK01158 117 EVALRRTVPVEEVRELLEELGLDLEIV--DSGfAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGF 194

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446563088 238 GVAMGNAPVELKQAADWIT-RSNSENGVEYMikEHF 272
Cdd:PRK01158 195 GVAVANADEELKEAADYVTeKSYGEGVAEAI--EHL 228
PRK15126 PRK15126
HMP-PP phosphatase;
2-251 1.30e-14

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 72.03  E-value: 1.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   2 IYRLLALNIDGTLLYNNGKIAkglRETIEFVKR---KDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKP 78
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLG---EKTLSTLARlreRDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  79 YVQRRLSEEktfnIVQVLEHFDCNVRISHERFSIGN--RERNTPNLIARTVLSSadplfYPVQFVDslgdaLRDHPV-AA 155
Cdd:PRK15126  78 LHRQDLPAD----VAELVLHQQWDTRASMHVFNDDGwfTGKEIPALLQAHVYSG-----FRYQLID-----LKRLPAhGV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 156 PKIdvVFHSKGEKERGL-TTLRKAFQD-----IEYVECdakrIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDL 229
Cdd:PRK15126 144 TKI--CFCGDHDDLTRLqIQLNEALGErahlcFSATDC----LEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDR 217

                        250       260
                 ....*....|....*....|..
gi 446563088 230 EVIENVGLGVAMGNAPVELKQA 251
Cdd:PRK15126 218 EMLGSVGRGFIMGNAMPQLRAE 239
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-241 2.55e-14

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: 70.10  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    5 LLALNIDGTLL-YNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVsatldkpyvqrR 83
Cdd:TIGR01484   1 LLFFDLDGTLLdPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALI-----------F 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   84 LSEEKTFNivqvlehfdcnvrisherfsignrernTPNLIARTVLSSADPLfypvqfVDSLGDALRDHPVAA----PKID 159
Cdd:TIGR01484  70 YPGEILYI---------------------------EPSDVFEEILGIKFEE------IGAELKSLSEHYVGTfiedKAIA 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  160 VVFHSKG-EKERGLTTLRKA--------FQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLE 230
Cdd:TIGR01484 117 VAIHYVGaELGQELDSKMRErlekigrnDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEE 196

                         250
                  ....*....|.
gi 446563088  231 VIENVGLGVAM 241
Cdd:TIGR01484 197 MFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 199-264 3.48e-14

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: 68.00  E-value: 3.48e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446563088 199 VSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGV 264
Cdd:cd07514   66 VDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGV 131
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-264 3.67e-14

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: 69.77  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    4 RLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGafvSATLDKPYVQRR 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENG---GVIFYNKEDIFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   84 LSEEKTFNIVQVLEHFDCNVRISHERFSIGnrerntpnliartvlssadplfypvQFVDslgdalrdhpvaAPKIDVVFH 163
Cdd:TIGR01487  79 ANMEEEWFLDEEKKKRFPRDRLSNEYPRAS-------------------------LVIM------------REGKDVDEV 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  164 SKGEKERGLttlrkafqdieYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGN 243
Cdd:TIGR01487 122 REIIKERGL-----------NLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVAN 190

                         250       260
                  ....*....|....*....|.
gi 446563088  244 APVELKQAADWITRSNSENGV 264
Cdd:TIGR01487 191 ADDQLKEIADYVTSNPYGEGV 211
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-274 5.72e-14

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: 69.41  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088    6 LALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVsaTLDKPYVQRRLS 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEI--SYNEGLDDIFLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   86 EEKtfnivqvlEHFDCNVRIS-HERFSignRERNTPNLIARTVlssadplfypvqfVDSLGdalrdhpvaapkIDVVFHS 164
Cdd:TIGR01482  79 YLE--------EEWFLDIVIAkTFPFS---RLKVQYPRRASLV-------------KMRYG------------IDVDTVR 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  165 KGEKERGLttlrkafqdiEYVECDA-KRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGN 243
Cdd:TIGR01482 123 EIIKELGL----------NLVAVDSgFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVAN 192

                         250       260       270
                  ....*....|....*....|....*....|.
gi 446563088  244 APVELKQAADWITRSNSENGVEYMIKEHFRK 274
Cdd:TIGR01482 193 AQPELKEWADYVTESPYGEGGAEAIGEILQA 223
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 192-274 9.45e-12

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: 63.52  E-value: 9.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 192 IEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGVEYM-IKE 270
Cdd:cd02605  161 LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKGPYAGgILE 240


                 ....
gi 446563088 271 HFRK 274
Cdd:cd02605  241 GLAH 244
PLN02887 PLN02887
hydrolase family protein
 185-271 1.86e-11

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 64.13  E-value: 1.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 185 VECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENGV 264
Cdd:PLN02887 492 VQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGV 571


                 ....*..
gi 446563088 265 EYMIKEH 271
Cdd:PLN02887 572 ADAIYRY 578
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 192-259 8.38e-11

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


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 59.29  E-value: 8.38e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446563088 192 IEILPQNVS-KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSN 259
Cdd:COG1778   74 ITHVYQGVKdKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKP 142
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 192-263 1.29e-09

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: 55.61  E-value: 1.29e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446563088 192 IEILPQNVS-KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENG 263
Cdd:cd01630   67 IEDLFQGVKdKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRG 139
PRK10976 PRK10976
putative hydrolase; Provisional
 2-273 1.02e-07

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 51.97  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088   2 IYRLLALNIDGTLLYNNGKIAKGLRETIEFVKRKDVYVTLFTSRNFQSAHKVAKALKLDSILVTHGGAFVSATLDKPYVQ 81
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088  82 RRLSEE---KTFNIVQVLEHFDCNVRISHERFSigNRERNTPNLIARTVLSSADpLFYPVQFvdslgdalrdhpvAAPKI 158
Cdd:PRK10976  81 HNLDRDiasDLFGVVHDNPDIITNVYRDDEWFM--NRHRPEEMRFFKEAVFKYQ-LYEPGLL-------------EPDGV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 159 DVVFHSKGEKERgLTTLRKAFQ---------DIEYVECdakrIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDL 229
Cdd:PRK10976 145 SKVFFTCDSHEK-LLPLEQAINarwgdrvnvSFSTLTC----LEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDA 219

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446563088 230 EVIENVGLGVAMGNAPVELKQAADW--ITRSNSENGVEYMIKEHFR 273
Cdd:PRK10976 220 EMLSMAGKGCIMGNAHQRLKDLLPEleVIGSNADDAVPHYLRKLYL 265
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
174-257 1.68e-07

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 50.32  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446563088 174 TLRKAfQDIEYvECDAKRIEILPQNVS-KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAA 252
Cdd:PRK09484  71 TGRKS-KLVED-RMTTLGITHLYQGQSnKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRA 148


                 ....*
gi 446563088 253 DWITR 257
Cdd:PRK09484 149 DYVTR 153
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 192-263 5.80e-07

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: 48.29  E-value: 5.80e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446563088  192 IEILPQNVS-KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQAADWITRSNSENG 263
Cdd:TIGR01670  67 ITHLYQGQSnKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRG 139
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 201-253 1.41e-05

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: 45.21  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446563088 201 KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMgNAPVELKQAAD 253
Cdd:COG0560  156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 174-250 4.89e-04

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: 40.71  E-value: 4.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446563088  174 TLRKAFQDIEYVECDAKRIEILPQNVSKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVAMGNAPVELKQ 250
Cdd:pfam05116 138 LLRKRGLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPELLQ 214
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 200-240 2.02e-03

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: 38.30  E-value: 2.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446563088 200 SKLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVA 240
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
serB PRK11133
phosphoserine phosphatase; Provisional
 201-240 5.20e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.01  E-value: 5.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446563088 201 KLRGLQLLGEHLNISLNEMVAIGDSMEDLEVIENVGLGVA 240
Cdd:PRK11133 249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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