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Conserved domains on  [gi|495624344|ref|WP_008348923|]
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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 3.27e-70

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: 217.46  E-value: 3.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   5 LLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIpTSTLVTHSGAFIADKLDEPLhvkk 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL-DSPLITFNGALVYDPTGKEI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  85 LTEEKTFNLVQILESFDCNVRLLHEKFSIGNRKKTqsqlmgktlIHPSDPIFYPVQFVESLSDMLMDEPVSTPVIEVYST 164
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIGINIYTNDDWADT---------IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 165 AA-LQPEIHTTIQQAFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGN 243
Cdd:cd07516  147 DEeLDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGN 226

                        250       260
                 ....*....|....*....|....*..
gi 495624344 244 APHSVKRKADWVTRSHDEQGVAYMIKE 270
Cdd:cd07516  227 AIDEVKEAADYVTLTNNEDGVAKAIEK 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 3.27e-70

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: 217.46  E-value: 3.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   5 LLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIpTSTLVTHSGAFIADKLDEPLhvkk 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL-DSPLITFNGALVYDPTGKEI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  85 LTEEKTFNLVQILESFDCNVRLLHEKFSIGNRKKTqsqlmgktlIHPSDPIFYPVQFVESLSDMLMDEPVSTPVIEVYST 164
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIGINIYTNDDWADT---------IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 165 AA-LQPEIHTTIQQAFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGN 243
Cdd:cd07516  147 DEeLDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGN 226

                        250       260
                 ....*....|....*....|....*..
gi 495624344 244 APHSVKRKADWVTRSHDEQGVAYMIKE 270
Cdd:cd07516  227 AIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-268 8.69e-53

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 172.81  E-value: 8.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    6 LALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTsTLVTHSGAFIADKLDEPLHVKKL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD-PVICYNGALIYDENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   86 TEEKTFNLVQILESFDCNVRLLHEKFSIGNrKKTQSQLMGKTLIHPSDPIFYPVqfvesLSDMLMDEPVSTpvIEVYSTA 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYIL-NDNELEKILKELNYTKSFVPEID-----DFELLEDEDINK--ILILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  166 ALQPEIHTTIQQAFPSVDLIKISDEK-MNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNA 244
Cdd:pfam08282 152 EDLDELEKELKELFGSLITITSSGPGyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 495624344  245 PHSVKRKADWVTRSHDEQGVAYMI 268
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-271 4.05e-52

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: 168.78  E-value: 4.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   2 SKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTsTLVTHSGAFIADKLDEPLH 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-PLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  82 VKKLTEEKTFNLVQILESFDCnvrllhekfsignrkktqsqlmgktlihpsdpifyPVQFVESLSDMLMDepvstpviev 161
Cdd:COG0561   80 ERPLDPEDVREILELLREHGL-----------------------------------HLQVVVRSGPGFLE---------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 162 ystaalqpeihttiqqafpsvdlikisdekmnIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAM 241
Cdd:COG0561  115 --------------------------------ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162

                        250       260       270
                 ....*....|....*....|....*....|
gi 495624344 242 GNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:COG0561  163 GNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-268 4.12e-45

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: 153.19  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    5 LLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTStLVTHSGAFIADKLDEPLHVKK 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTP-FITANGAAVIDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   85 LTEEKTFNLVQILESFDCNVRL-----------LHEKFSIGNRKKTQSQLMGKTLIHPSDPIFYPVQFVESLSDMlmdep 153
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILygddsiyasknDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDL----- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  154 vsTPVIEVYSTAALQPEIHTTIQqAFPSVDLIKisdekmnivcKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLE 233
Cdd:TIGR00099 155 --DLLIEALNKLELEENVSVVSS-GPYSIEITA----------KGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLE 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 495624344  234 LAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMI 268
Cdd:TIGR00099 222 AAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-271 3.37e-27

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 106.70  E-value: 3.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   1 MSKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKI--PTSTLVTHSGAFIADKLD- 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMeqPGDYCITNNGALVQKAADg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  78 EPLHVKKLTEEKTFNLVQILESFDCNVRLLHEkfsigNRKKTQSQLMGKTLIHPSDPIFYPVQF--VESLSD-------M 148
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVHFHALDR-----NTLYTANRDISYYTVHESFLTGIPLVFreVEKMDPnlqfpkvM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 149 LMDEPvstpviEVYSTAalqpeIHTTIQQAFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDD 228
Cdd:PRK10513 156 MIDEP------EILDAA-----IARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQEND 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 495624344 229 IPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:PRK10513 225 IAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-270 3.27e-70

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: 217.46  E-value: 3.27e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   5 LLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIpTSTLVTHSGAFIADKLDEPLhvkk 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL-DSPLITFNGALVYDPTGKEI---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  85 LTEEKTFNLVQILESFDCNVRLLHEKFSIGNRKKTqsqlmgktlIHPSDPIFYPVQFVESLSDMLMDEPVSTPVIEVYST 164
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIGINIYTNDDWADT---------IYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 165 AA-LQPEIHTTIQQAFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGN 243
Cdd:cd07516  147 DEeLDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGN 226

                        250       260
                 ....*....|....*....|....*..
gi 495624344 244 APHSVKRKADWVTRSHDEQGVAYMIKE 270
Cdd:cd07516  227 AIDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-268 8.69e-53

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 172.81  E-value: 8.69e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    6 LALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTsTLVTHSGAFIADKLDEPLHVKKL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD-PVICYNGALIYDENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   86 TEEKTFNLVQILESFDCNVRLLHEKFSIGNrKKTQSQLMGKTLIHPSDPIFYPVqfvesLSDMLMDEPVSTpvIEVYSTA 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYIL-NDNELEKILKELNYTKSFVPEID-----DFELLEDEDINK--ILILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  166 ALQPEIHTTIQQAFPSVDLIKISDEK-MNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNA 244
Cdd:pfam08282 152 EDLDELEKELKELFGSLITITSSGPGyLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 495624344  245 PHSVKRKADWVTRSHDEQGVAYMI 268
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-271 4.05e-52

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: 168.78  E-value: 4.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   2 SKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTsTLVTHSGAFIADKLDEPLH 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-PLITSNGALIYDPDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  82 VKKLTEEKTFNLVQILESFDCnvrllhekfsignrkktqsqlmgktlihpsdpifyPVQFVESLSDMLMDepvstpviev 161
Cdd:COG0561   80 ERPLDPEDVREILELLREHGL-----------------------------------HLQVVVRSGPGFLE---------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 162 ystaalqpeihttiqqafpsvdlikisdekmnIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAM 241
Cdd:COG0561  115 --------------------------------ILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAM 162

                        250       260       270
                 ....*....|....*....|....*....|
gi 495624344 242 GNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:COG0561  163 GNAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-268 4.12e-45

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: 153.19  E-value: 4.12e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    5 LLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTStLVTHSGAFIADKLDEPLHVKK 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTP-FITANGAAVIDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   85 LTEEKTFNLVQILESFDCNVRL-----------LHEKFSIGNRKKTQSQLMGKTLIHPSDPIFYPVQFVESLSDMlmdep 153
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILygddsiyasknDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDL----- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  154 vsTPVIEVYSTAALQPEIHTTIQqAFPSVDLIKisdekmnivcKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLE 233
Cdd:TIGR00099 155 --DLLIEALNKLELEENVSVVSS-GPYSIEITA----------KGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLE 221

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 495624344  234 LAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMI 268
Cdd:TIGR00099 222 AAGYGVAMGNADEELKALADYVTDSNNEDGVALAL 256
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-271 1.79e-27

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: 105.77  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   4 KLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIptSTLVTHSGAFIADKlDEPLHVK 83
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGI--DSYVSYNGQYVFFE-GEVIYKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  84 KLTEEKTFNLVQILESFDcnvrllhekfsignrkktqsqlmgktlihpsdpifYPVQFVESLSDMLMDEPVSTPVIEvys 163
Cdd:cd07517   78 PLPQELVERLTEFAKEQG-----------------------------------HPVSFYGQLLLFEDEEEEQKYEEL--- 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 164 taalqpeihttiqqaFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGN 243
Cdd:cd07517  120 ---------------RPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                        250       260
                 ....*....|....*....|....*...
gi 495624344 244 APHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:cd07517  185 AHEELKEIADYVTKDVDEDGILKALKHF 212
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-271 3.37e-27

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 106.70  E-value: 3.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   1 MSKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKI--PTSTLVTHSGAFIADKLD- 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMeqPGDYCITNNGALVQKAADg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  78 EPLHVKKLTEEKTFNLVQILESFDCNVRLLHEkfsigNRKKTQSQLMGKTLIHPSDPIFYPVQF--VESLSD-------M 148
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVHFHALDR-----NTLYTANRDISYYTVHESFLTGIPLVFreVEKMDPnlqfpkvM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 149 LMDEPvstpviEVYSTAalqpeIHTTIQQAFPSVDLIKISDEKMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDD 228
Cdd:PRK10513 156 MIDEP------EILDAA-----IARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQEND 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 495624344 229 IPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:PRK10513 225 IAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-271 3.50e-20

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 87.77  E-value: 3.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   1 MSKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTSTLVThSGAFIAD-KLDEP 79
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICC-NGTYLYDyQAKKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  80 LHVKKLTEEKTFNLVQILESFDCNvRLLH------EKFSIGNRKKTQSqlMGKTLIHPSDPIFypvQFVESLSDMLMDep 153
Cdd:PRK10530  80 LEADPLPVQQALQVIEMLDEHQIH-GLMYvddamlYEHPTGHVIRTLN--WAQTLPPEQRPTF---TQVDSLAQAARQ-- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 154 vstpVIEVYSTAALQPEIhTTIQQAFPSVDlikisdEKMNIVC------------KGVSKEAGLSLLTSALGFTLEDTVV 221
Cdd:PRK10530 152 ----VNAIWKFALTHEDL-PQLQHFAKHVE------HELGLECewswhdqvdiarKGNSKGKRLTQWVEAQGWSMKNVVA 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 495624344 222 IGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:PRK10530 221 FGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSH 270
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 192-269 1.98e-19

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: 83.40  E-value: 1.98e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495624344 192 MNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIK 269
Cdd:cd07518  107 IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 198-272 1.31e-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: 69.16  E-value: 1.31e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495624344 198 GVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIKEYF 272
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-265 1.74e-14

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 71.16  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   1 MSKKLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNR--HFRSAqkiakalkipTSTLVTHSGAFIADklde 78
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNvlCFARA----------AAKLIGTSGPVIAE---- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  79 plhvkklteektfNLVQILESFDCNVRLLHEK------FSIgNRKKTQSQLMGKTLIHP----SDPIFYPVQFVESLSDM 148
Cdd:PRK01158  67 -------------NGGVISVGFDGKRIFLGDIeecekaYSE-LKKRFPEASTSLTKLDPdyrkTEVALRRTVPVEEVREL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 149 LMDEPvstPVIEVYSTaalQPEIHttiqqafpsvdlikisdekmnIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDD 228
Cdd:PRK01158 133 LEELG---LDLEIVDS---GFAIH---------------------IKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSEND 185

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 495624344 229 IPMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVA 265
Cdd:PRK01158 186 LEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGVA 222
PLN02887 PLN02887
hydrolase family protein
 9-271 7.63e-13

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 68.36  E-value: 7.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   9 NIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTST-LVTHS--GAFIadkldEPLHVKKL 85
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDgIISESspGVFL-----QGLLVYGR 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  86 TEEKTF--NLVQILESFDCNVRLLHEKFSIGNRKKTQSQLMGKTLI--------HPSDPIFYPVQFVESLSD----MLMD 151
Cdd:PLN02887 389 QGREIYrsNLDQEVCREACLYSLEHKIPLIAFSQDRCLTLFDHPLVdslhtiyhEPKAEIMSSVDQLLAAADiqkvIFLD 468

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 152 --EPVSTpVIEVYSTAALQPEIHttIQQAFPSVdlikisdekMNIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDI 229
Cdd:PLN02887 469 taEGVSS-VLRPYWSEATGDRAN--VVQAQPDM---------LEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDI 536

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 495624344 230 PMLELAGLGVAMGNAPHSVKRKADWVTRSHDEQGVAYMIKEY 271
Cdd:PLN02887 537 EMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-241 5.59e-12

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: 63.55  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    5 LLALNIDGTLLRSN-GKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPtSTLVTHSGAFIadkldeplHVK 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNaHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLP-LPLIAENGALI--------FYP 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   84 KLTEEKTFNLVQILesfdcnvrLLHEKFSIgnrkktqsqlMGKTLIHPSDpiFYPVQFVESLSDMLMDEPVSTPVievys 163
Cdd:TIGR01484  72 GEILYIEPSDVFEE--------ILGIKFEE----------IGAELKSLSE--HYVGTFIEDKAIAVAIHYVGAEL----- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  164 TAALQPEIhttiqqaFPSVDLIKISDEKMNIVC----------KGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLE 233
Cdd:TIGR01484 127 GQELDSKM-------RERLEKIGRNDLELEAIYsgktdlevlpAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFE 199


                  ....*...
gi 495624344  234 LAGLGVAM 241
Cdd:TIGR01484 200 VAGLAVAV 207
PRK10976 PRK10976
putative hydrolase; Provisional
 7-249 3.56e-10

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 59.29  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   7 ALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIpTSTLVTHSGAFIADKLDEPLHVKKLT 86
Cdd:PRK10976   6 ASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEI-KSYMITSNGARVHDTDGNLIFSHNLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  87 EEKTFNLVQIlESFDCNVrllhekfsIGNRKKTQSQLMGKtliHPSDPIFYpvqFVESLSDMLMDEPVSTP---VIEVYS 163
Cdd:PRK10976  85 RDIASDLFGV-VHDNPDI--------ITNVYRDDEWFMNR---HRPEEMRF---FKEAVFKYQLYEPGLLEpdgVSKVFF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 164 TAAlQPEIHTTIQQAFPSV--DLIKISDEKMN---IVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLG 238
Cdd:PRK10976 150 TCD-SHEKLLPLEQAINARwgDRVNVSFSTLTcleVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKG 228

                        250
                 ....*....|.
gi 495624344 239 VAMGNAPHSVK 249
Cdd:PRK10976 229 CIMGNAHQRLK 239
PRK15126 PRK15126
HMP-PP phosphatase;
4-244 7.58e-07

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 49.31  E-value: 7.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   4 KLLALNIDGTLLRSNGKIHSATKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIpTSTLVTHSGAFIADKLDEPLHVK 83
Cdd:PRK15126   3 RLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSL-DAYLITGNGTRVHSLEGELLHRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344  84 KLTEE----------------KTFNLVQILESFDCNVRLLHEKFSIGNRKKTQSQLMGKTLIHPsdpifypVQFVESLSD 147
Cdd:PRK15126  82 DLPADvaelvlhqqwdtrasmHVFNDDGWFTGKEIPALLQAHVYSGFRYQLIDLKRLPAHGVTK-------ICFCGDHDD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 148 MLMdepvstpvIEVYSTAALQPEIHTTiqqaFPSVDLIKIsdekmniVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTD 227
Cdd:PRK15126 155 LTR--------LQIQLNEALGERAHLC----FSATDCLEV-------LPVGCNKGAALAVLSQHLGLSLADCMAFGDAMN 215

                        250
                 ....*....|....*..
gi 495624344 228 DIPMLELAGLGVAMGNA 244
Cdd:PRK15126 216 DREMLGSVGRGFIMGNA 232
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 193-253 9.91e-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: 48.68  E-value: 9.91e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495624344 193 NIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMgNAPHSVKRKAD 253
Cdd:COG0560  148 GPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 190-257 1.10e-06

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: 47.74  E-value: 1.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495624344 190 EKMNI--VCKGVS-KEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTR 257
Cdd:COG1778   70 EELGIthVYQGVKdKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTT 140
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 151-263 1.61e-06

sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3.1.3.24) catalyzes the dephosphorylation of sucrose-6(F)-phosphate (Suc6P)-the final step in the pathway of sucrose biosynthesis in plants and cyanobacteria. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 48.11  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344 151 DEPVSTPVIEVYSTAALQPEIHTTIQQafpSVDLIKISDekmnIVCKGVSKEAGLSLLTSALGFTLEDTVVIGHGTDDIP 230
Cdd:cd02605  127 DPQNDAAVIEQLEEMLLKAGLTVRIIY---SSGLAYDLD----ILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIA 199

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495624344 231 MLELAGLGVAMGNAPHSVKRKADWVTRSHDEQG 263
Cdd:cd02605  200 LLSTGTRGVIVGNAQPELLKWADRVTRSRLAKG 232
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 200-240 3.45e-06

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 46.39  E-value: 3.45e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495624344 200 SKEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVA 240
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 201-259 6.00e-06

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: 45.21  E-value: 6.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495624344 201 KEAGLSLLTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTRSH 259
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRAR 135
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 6-84 5.53e-05

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 41.30  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344    6 LALNIDGTLLRSNGKIHSAtKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALK-----IPTSTLVThSGAFIADKLDEPL 80
Cdd:pfam13344   1 FLFDIDGVLWRGGEPIPGA-AEALRALRAAGKPVVFVTNNSSRSREEYAEKLRklgfdIDEDEIIT-SGTAAADYLKERK 78


                  ....
gi 495624344   81 HVKK 84
Cdd:pfam13344  79 FGKK 82
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-87 1.07e-04

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 40.84  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495624344   5 LLALNIDGTLLrsngkihsaTKEAVEYVKKKGVYVTIVTNRHFRSAQKIAKALKIPTS--TLVTHSGAFIADKLDEPLHV 82
Cdd:cd01427    1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLfdGIIGSDGGGTPKPKPKPLLL 71


                 ....*
gi 495624344  83 KKLTE 87
Cdd:cd01427   72 LLLKL 76
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
208-257 2.14e-03

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 38.37  E-value: 2.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 495624344 208 LTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPHSVKRKADWVTR 257
Cdd:PRK09484 104 LLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTR 153
serB PRK11133
phosphoserine phosphatase; Provisional
 208-264 6.91e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 37.62  E-value: 6.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495624344 208 LTSALGFTLEDTVVIGHGTDDIPMLELAGLGVAMGNAPhSVKRKADWVTRSHDEQGV 264
Cdd:PRK11133 256 LAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKP-KVNEQAQVTIRHADLMGV 311
 
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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