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Conserved domains on  [gi|124802833|ref|XP_001347609|]
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haloacid dehalogenase-like hydrolase [Plasmodium falciparum 3D7]

Protein Classification

HAD family hydrolase( domain architecture ID 12089052)

HAD (haloacid dehalogenase) family hydrolase, part of the HAD 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.-.-.-|3.1.3.-
Gene Ontology:  GO:0016787
PubMed:  16889794
SCOP:  3001890

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 24-282 1.97e-72

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


:

Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 223.27  E-value: 1.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   24 IFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNrislLPGIYMNGCVTFDEKGSRVI 103
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVI-KELGLD----DPVICYNGALIYDENGKILY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  104 DRIMNNDLKMEIHEFSKQINIskYAIWFCLEKTYCFEIN---DCIREYMEVEALNPDVIEDNMLEGLTVYKVLFSLPENI 180
Cdd:pfam08282  76 SNPISKEAVKEIIEYLKENNL--EILLYTDDGVYILNDNeleKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:pfam08282 154 LDELEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250       260
                  ....*....|....*....|..
gi 124802833  261 KVKNSAAYVGPSNNEHAISHVL 282
Cdd:pfam08282 234 EVKAAADYVTDSNNEDGVAKAL 255
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 24-282 1.97e-72

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 223.27  E-value: 1.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   24 IFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNrislLPGIYMNGCVTFDEKGSRVI 103
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVI-KELGLD----DPVICYNGALIYDENGKILY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  104 DRIMNNDLKMEIHEFSKQINIskYAIWFCLEKTYCFEIN---DCIREYMEVEALNPDVIEDNMLEGLTVYKVLFSLPENI 180
Cdd:pfam08282  76 SNPISKEAVKEIIEYLKENNL--EILLYTDDGVYILNDNeleKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:pfam08282 154 LDELEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250       260
                  ....*....|....*....|..
gi 124802833  261 KVKNSAAYVGPSNNEHAISHVL 282
Cdd:pfam08282 234 EVKAAADYVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 23-283 2.18e-48

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: 161.22  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNrislLPGIYMNGCVTFDEKGSRV 102
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYL-EELGLD----SPLITFNGALVYDPTGKEI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 103 IDRIMNNDLKMEIHEFSKQINISkYAIWfclektycFEINDCIREYMEVEALNPDVI-----EDNMLEGLTVYKVLF-SL 176
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIG-INIY--------TNDDWADTIYEENEDDEIIKPaeildDLLLPPDEDITKILFvGE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 177 PENILENTLKLCREKFSHrINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVH 256
Cdd:cd07516  147 DEELDELIAKLPEEFFDD-LSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMG 225

                        250       260
                 ....*....|....*....|....*..
gi 124802833 257 NASEKVKNSAAYVGPSNNEHAISHVLK 283
Cdd:cd07516  226 NAIDEVKEAADYVTLTNNEDGVAKAIE 252
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 21-285 3.82e-47

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: 156.06  E-value: 3.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGEHvkKNRISLlpgIYMNGCVTFDEKGS 100
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEEL--GLDDPL---ITSNGALIYDPDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 101 RVIDRimnndlkmeihefskqiniskyaiwfclektycfeindcireymevealnpdviednmlegltvykvlfSLPENI 180
Cdd:COG0561   77 VLYER---------------------------------------------------------------------PLDPED 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:COG0561   88 VREILELLREHGLHLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                        250       260
                 ....*....|....*....|....*
gi 124802833 261 KVKNSAAYVGPSNNEHAISHVLKTF 285
Cdd:COG0561  168 EVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 23-282 1.12e-46

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: 157.04  E-value: 1.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGEhvKKNRISLlpgIYMNGCVTFDEKGSRV 102
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKE--LGLDTPF---ITANGAAVIDDQGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  103 IDRIMNNDLKMEIHEFSKQINISkyAIWFCLEKTY-CFEINDCIREYMEVEALNPDVIEDNMLEGLTVYKVLFSLPEnil 181
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLD--VILYGDDSIYaSKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLD--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  182 ENTLKLCREKFSH-----RINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVH 256
Cdd:TIGR00099 151 PEDLDLLIEALNKleleeNVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|....*.
gi 124802833  257 NASEKVKNSAAYVGPSNNEHAISHVL 282
Cdd:TIGR00099 231 NADEELKALADYVTDSNNEDGVALAL 256
PLN02887 PLN02887
hydrolase family protein
 22-279 3.90e-26

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 107.65  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRS------IFSVENVIGehvKKNRIS-LLPGIYMNGCVT 94
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKArpavidILKMVDLAG---KDGIISeSSPGVFLQGLLV 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  95 FDEKGSRVIDRIMNNDLKMEIHEFSKQINISKYAiwFCLEKTYC-FE--INDCIRE-YMEVEA-LNPDVieDNMLEGLTV 169
Cdd:PLN02887 386 YGRQGREIYRSNLDQEVCREACLYSLEHKIPLIA--FSQDRCLTlFDhpLVDSLHTiYHEPKAeIMSSV--DQLLAAADI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 170 YKVLF-SLPENILENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSG 248
Cdd:PLN02887 462 QKVIFlDTAEGVSSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQL 541

                        250       260       270
                 ....*....|....*....|....*....|.
gi 124802833 249 LTHSVGVHNASEKVKNSAAYVGPSNNEHAIS 279
Cdd:PLN02887 542 ASLGVALSNGAEKTKAVADVIGVSNDEDGVA 572
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 24-282 1.97e-72

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 223.27  E-value: 1.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   24 IFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNrislLPGIYMNGCVTFDEKGSRVI 103
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVI-KELGLD----DPVICYNGALIYDENGKILY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  104 DRIMNNDLKMEIHEFSKQINIskYAIWFCLEKTYCFEIN---DCIREYMEVEALNPDVIEDNMLEGLTVYKVLFSLPENI 180
Cdd:pfam08282  76 SNPISKEAVKEIIEYLKENNL--EILLYTDDGVYILNDNeleKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:pfam08282 154 LDELEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASP 233

                         250       260
                  ....*....|....*....|..
gi 124802833  261 KVKNSAAYVGPSNNEHAISHVL 282
Cdd:pfam08282 234 EVKAAADYVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 23-283 2.18e-48

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: 161.22  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNrislLPGIYMNGCVTFDEKGSRV 102
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYL-EELGLD----SPLITFNGALVYDPTGKEI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 103 IDRIMNNDLKMEIHEFSKQINISkYAIWfclektycFEINDCIREYMEVEALNPDVI-----EDNMLEGLTVYKVLF-SL 176
Cdd:cd07516   76 LERLISKEDVKELEEFLRKLGIG-INIY--------TNDDWADTIYEENEDDEIIKPaeildDLLLPPDEDITKILFvGE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 177 PENILENTLKLCREKFSHrINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVH 256
Cdd:cd07516  147 DEELDELIAKLPEEFFDD-LSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMG 225

                        250       260
                 ....*....|....*....|....*..
gi 124802833 257 NASEKVKNSAAYVGPSNNEHAISHVLK 283
Cdd:cd07516  226 NAIDEVKEAADYVTLTNNEDGVAKAIE 252
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 21-285 3.82e-47

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: 156.06  E-value: 3.82e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGEHvkKNRISLlpgIYMNGCVTFDEKGS 100
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEEL--GLDDPL---ITSNGALIYDPDGE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 101 RVIDRimnndlkmeihefskqiniskyaiwfclektycfeindcireymevealnpdviednmlegltvykvlfSLPENI 180
Cdd:COG0561   77 VLYER---------------------------------------------------------------------PLDPED 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:COG0561   88 VREILELLREHGLHLQVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                        250       260
                 ....*....|....*....|....*
gi 124802833 261 KVKNSAAYVGPSNNEHAISHVLKTF 285
Cdd:COG0561  168 EVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 23-282 1.12e-46

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: 157.04  E-value: 1.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGEhvKKNRISLlpgIYMNGCVTFDEKGSRV 102
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKE--LGLDTPF---ITANGAAVIDDQGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  103 IDRIMNNDLKMEIHEFSKQINISkyAIWFCLEKTY-CFEINDCIREYMEVEALNPDVIEDNMLEGLTVYKVLFSLPEnil 181
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLD--VILYGDDSIYaSKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLD--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  182 ENTLKLCREKFSH-----RINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVH 256
Cdd:TIGR00099 151 PEDLDLLIEALNKleleeNVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMG 230

                         250       260
                  ....*....|....*....|....*.
gi 124802833  257 NASEKVKNSAAYVGPSNNEHAISHVL 282
Cdd:TIGR00099 231 NADEELKALADYVTDSNNEDGVALAL 256
PLN02887 PLN02887
hydrolase family protein
 22-279 3.90e-26

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 107.65  E-value: 3.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRS------IFSVENVIGehvKKNRIS-LLPGIYMNGCVT 94
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKArpavidILKMVDLAG---KDGIISeSSPGVFLQGLLV 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  95 FDEKGSRVIDRIMNNDLKMEIHEFSKQINISKYAiwFCLEKTYC-FE--INDCIRE-YMEVEA-LNPDVieDNMLEGLTV 169
Cdd:PLN02887 386 YGRQGREIYRSNLDQEVCREACLYSLEHKIPLIA--FSQDRCLTlFDhpLVDSLHTiYHEPKAeIMSSV--DQLLAAADI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 170 YKVLF-SLPENILENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSG 248
Cdd:PLN02887 462 QKVIFlDTAEGVSSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQL 541

                        250       260       270
                 ....*....|....*....|....*....|.
gi 124802833 249 LTHSVGVHNASEKVKNSAAYVGPSNNEHAIS 279
Cdd:PLN02887 542 ASLGVALSNGAEKTKAVADVIGVSNDEDGVA 572
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 22-283 4.78e-25

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: 98.42  E-value: 4.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLI-RAQEKGIKVVIATGRSIFSVenvigehvkknrISLLPGIymngcvtfdekgs 100
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILdQLLKKGIKFVVASGRQYYQL------------ISFFPEI------------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 101 rvidrimnndlkmeihefskqinisKYAIWFclektycfeindcireymevealnpdvIEDNmlEGLTVYKVLFSLPENI 180
Cdd:cd07518   56 -------------------------KDEMSF---------------------------VAEN--GAVVYFKFTLNVPDEA 81

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 181 LENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:cd07518   82 APDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPE 161

                        250       260
                 ....*....|....*....|...
gi 124802833 261 KVKNSAAYVGPSNNEHAISHVLK 283
Cdd:cd07518  162 EVKAAAKYVAPSNNENGVLQVIE 184
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 22-285 4.62e-24

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: 96.52  E-value: 4.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgEHVKKNRIsllpgIYMNGCVTFDEKGsr 101
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIV-KALGIDSY-----VSYNGQYVFFEGE-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 102 VI-DRIMNNDLKMEIHEFSKQINISkyaiwfclektYCFEINDCIREYMEVEALnpdviednmlegltvYKVLFSlpeni 180
Cdd:cd07517   73 VIyKNPLPQELVERLTEFAKEQGHP-----------VSFYGQLLLFEDEEEEQK---------------YEELRP----- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 181 lenTLKLCRekfSHRInvantfqsYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:cd07517  122 ---ELRFVR---WHPL--------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHE 187

                        250       260
                 ....*....|....*....|....*
gi 124802833 261 KVKNSAAYVGPSNNEHAISHVLKTF 285
Cdd:cd07517  188 ELKEIADYVTKDVDEDGILKALKHF 212
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 21-285 4.94e-23

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 95.14  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGE-HVKKnrisllPGIYmngCVTFD--- 96
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKElHMEQ------PGDY---CITNNgal 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  97 ----EKGSRVIDRIMNNDLKMEIHEFSKQINISKYAiwfcLEKTYCFEINDCIREYMEVEA------LNPDVIEDnMLEG 166
Cdd:PRK10513  74 vqkaADGETVAQTALSYDDYLYLEKLSREVGVHFHA----LDRNTLYTANRDISYYTVHESfltgipLVFREVEK-MDPN 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 167 LTVYKVLFSLPENILENTLKLCREKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEML 246
Cdd:PRK10513 149 LQFPKVMMIDEPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMI 228

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 124802833 247 SGLTHSVGVHNASEKVKNSAAYVGPSNNEHAISHVLKTF 285
Cdd:PRK10513 229 EYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 23-255 9.92e-19

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: 82.43  E-value: 9.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   23 IIFTDLDGTLLNSEN-KVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIgehvkKNRISLLPGIYMNGCVTFDEKGS- 100
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELL-----KQLNLPLPLIAENGALIFYPGEIl 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  101 --------RVIDRIMNNDLKMEIHEFSkqiniskyAIWFCLEktycFEINDCIREYMEVEALNPDVIEDNMLEGLTVYKV 172
Cdd:TIGR01484  76 yiepsdvfEEILGIKFEEIGAELKSLS--------EHYVGTF----IEDKAIAVAIHYVGAELGQELDSKMRERLEKIGR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  173 LFslpenilentlklcrekfsHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHS 252
Cdd:TIGR01484 144 ND-------------------LELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLA 204


                  ...
gi 124802833  253 VGV 255
Cdd:TIGR01484 205 VAV 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 21-269 5.68e-16

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 75.01  E-value: 5.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVigehvkknriSLLPGIymNGCVtFDEKGS 100
Cdd:PRK01158   3 IKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAA----------AKLIGT--SGPV-IAENGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 101 RVIDRIMNNDLKMEihefskqiNISKYaiwfclEKTYCFeindcIREYMEvEALNPDVIEDNMLEgltvyKVLFSLPENI 180
Cdd:PRK01158  70 VISVGFDGKRIFLG--------DIEEC------EKAYSE-----LKKRFP-EASTSLTKLDPDYR-----KTEVALRRTV 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 181 LENTLKLCREKFSHRINVANTFQSYvELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASE 260
Cdd:PRK01158 125 PVEEVRELLEELGLDLEIVDSGFAI-HIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADE 203


                 ....*....
gi 124802833 261 KVKNSAAYV 269
Cdd:PRK01158 204 ELKEAADYV 212
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 24-285 1.43e-15

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: 74.04  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   24 IFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENV---IGEhvkknrisllPGIYM--NGCVTFDEK 98
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALaklIGT----------PDPVIaeNGGEISYNE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   99 GSrviDRIMNNDLKMEIHEFSKQINISKYAIwfcLEKTYCFEIND-CIREYMEVEALnPDVIEdnmlegltvykvlfSLP 177
Cdd:TIGR01482  71 GL---DDIFLAYLEEEWFLDIVIAKTFPFSR---LKVQYPRRASLvKMRYGIDVDTV-REIIK--------------ELG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  178 ENilentLKLCREKFShrinvantfqsyVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHN 257
Cdd:TIGR01482 130 LN-----LVAVDSGFD------------IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVAN 192

                         250       260       270
                  ....*....|....*....|....*....|..
gi 124802833  258 ASEKVKNSAAYVGPS----NNEHAISHVLKTF 285
Cdd:TIGR01482 193 AQPELKEWADYVTESpygeGGAEAIGEILQAI 224
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 23-273 6.16e-11

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: 61.21  E-value: 6.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  23 IIFTDLDGTLL-NSENKVSEQNLESLI--RAQEKGIKVVIATGRSIFSVENVIGEHVkknriSLLPGiymngcVTFDEKG 99
Cdd:cd02605    1 LLVSDLDETLVgHDTNLQALERLQDLLeqLTADNDVILVYATGRSPESVLELIKEVM-----LPKPD------FIISDVG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 100 SRVIDRimnNDLKMEIHEFSKQInISKYAIWFCLEKtycfeINDCIREYMEVEAL--NPdviednmlegltvYKVLFSLP 177
Cdd:cd02605   70 TEIYYG---ESGYLEPDTYWNEV-LSEGWERFLFEA-----IADLFKQLKPQSELeqNP-------------HKISFYLD 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 178 ENILENTLKLCRE-----KFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHS 252
Cdd:cd02605  128 PQNDAAVIEQLEEmllkaGLTVRIIYSSGLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRG 207

                        250       260
                 ....*....|....*....|.
gi 124802833 253 VGVHNASEKVKNSAAYVGPSN 273
Cdd:cd02605  208 VIVGNAQPELLKWADRVTRSR 228
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 21-282 1.19e-10

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: 59.75  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVEnvigehvkknriSLLPGIYMNGCVtFDEKGS 100
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFAR------------ALAVLIGTSGPV-VAENGG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  101 RVIDRimnndlkmeihefskqinisKYAIWFCLEKTyCFEINDCIREYMEVEALN---PDVIEDNMLEGltvyKVLFSLP 177
Cdd:TIGR01487  68 VIFYN--------------------KEDIFLANMEE-EWFLDEEKKKRFPRDRLSneyPRASLVIMREG----KDVDEVR 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  178 ENILENTLKLCREKFShrinvantfqsyVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHN 257
Cdd:TIGR01487 123 EIIKERGLNLVASGFA------------IHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVAN 190

                         250       260
                  ....*....|....*....|....*
gi 124802833  258 ASEKVKNSAAYVGPSNNEHAISHVL 282
Cdd:TIGR01487 191 ADDQLKEIADYVTSNPYGEGVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 214-269 1.55e-10

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: 57.98  E-value: 1.55e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124802833 214 NKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVHNASEKVKNSAAYV 269
Cdd:cd07514   67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYV 122
PRK10976 PRK10976
putative hydrolase; Provisional
 23-283 1.70e-09

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 57.37  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVigehvkknRISLLPGIYM---NGCVTFDEKG 99
Cdd:PRK10976   4 VVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQI--------RDNLEIKSYMitsNGARVHDTDG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 100 SRV----IDRIMNNDLKMEIHEFSKQI-NISKYAIWFCleKTYCFEINDCIREYMeveaLNPDVIEDNMLEGLTVYKVLF 174
Cdd:PRK10976  76 NLIfshnLDRDIASDLFGVVHDNPDIItNVYRDDEWFM--NRHRPEEMRFFKEAV----FKYQLYEPGLLEPDGVSKVFF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 175 S-------LPeniLENTLKlcrEKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLS 247
Cdd:PRK10976 150 TcdsheklLP---LEQAIN---ARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLS 223

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 124802833 248 GLTHSVGVHNASEKVKNSAAY--VGPSNNEHAISHVLK 283
Cdd:PRK10976 224 MAGKGCIMGNAHQRLKDLLPEleVIGSNADDAVPHYLR 261
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 22-261 2.32e-09

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: 56.50  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   22 KIIFTDLDGTLLNSENKVSEQnLESLIRAQEKGIKVVIATGRSIFSVENVIGEhvkKNrislLP---------G--IYMN 90
Cdd:pfam05116   3 LLLVSDLDNTLVDGDNEALAR-LNQLLEAYRPDVGLVFATGRSLDSAKELLKE---KP----LPtpdylitsvGteIYYG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   91 GCVTFDekgsrvidrimnndlkmeiHEFSKQINiskyAIWfclektycfeindcireymevealNPDVIEDNM--LEGLT 168
Cdd:pfam05116  75 PSLVPD-------------------QSWQEHLD----YHW------------------------DRQAVVEALakFPGLT 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  169 V--------YKVLFSLPENILENTLKLCR---EKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMG 237
Cdd:pfam05116 108 LqpeeeqrpHKVSYFLDPEAAAAVLAELEqllRKRGLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCG 187

                         250       260
                  ....*....|....*....|....
gi 124802833  238 DGENDIEMLSGLTHSVGVHNASEK 261
Cdd:pfam05116 188 DSGNDEELFIGGTRGVVVGNAQPE 211
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 22-63 1.48e-08

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 54.64  E-value: 1.48e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGR 63
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGR 45
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 23-120 1.37e-07

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


Pssm-ID: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 51.60  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVEnvigEHVKKNRISlLPGIYMNGCVTFDEKGSRV 102
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVE----YLRKELGIE-DPFIVENGGAIFIPRGYFK 75

                         90
                 ....*....|....*...
gi 124802833 103 IDRIMNNDLKMEIHEFSK 120
Cdd:cd07507   76 FPGRCKSEGGYEVIELGK 93
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 23-246 2.05e-07

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 50.86  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833   23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVigehvkknRISL---LPGIYMNGCVTFDEKG 99
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYL--------RKELgleDPFIVENGGAIYGPRG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  100 SRVIDR-------IMNNDLKMEIHEFSKQINISKYAiwfcLEKTYCFEINdcireymEVEALNPDVIEDNMLEGltvYKV 172
Cdd:TIGR01486  73 WRPEPEypvialgIPYEKIRARLRELSEELGFKFRG----LGDLTDEEIA-------ELTGLSRELARLAQRRE---YSE 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  173 LFSLPENILENTLKLCRE---------KFSHRINVantfqsyvelfhqHTNKFEGVKEICKYYNISLNN--ALAMGDGEN 241
Cdd:TIGR01486 139 TILWSEERRERFTEALVAvglevthggRFYHVLGA-------------GSDKGKAVNALKAFYNQPGGAikVVGLGDSPN 205


                  ....*
gi 124802833  242 DIEML 246
Cdd:TIGR01486 206 DLPLL 210
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 24-99 4.55e-06

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: 44.69  E-value: 4.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124802833  24 IFTDLDGTLLNsenkvseqnLESLIRAQEKGIKVVIATGRSIFSVENVIGEHVKKNRISLLpgIYMNGCVTFDEKG 99
Cdd:cd01427    2 VLFDLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGI--IGSDGGGTPKPKP 66
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 21-61 1.03e-05

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 46.09  E-value: 1.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 124802833  21 IKIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIAT 61
Cdd:PRK00192   4 KLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCT 44
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 22-261 2.25e-05

bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; Provisional


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 45.69  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  22 KIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGEHVKKNrisllPGIYMNGCVTFDEKG-- 99
Cdd:PRK14502 417 KIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKD-----PFITENGGAIFIPKDyf 491

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 100 --SRVIDRIMNNDLKMEIHEFSKQI-NISKYAIwfcleKTYCFEI-------NDCIREY--MEVEalnpdviEDNMLEGL 167
Cdd:PRK14502 492 rlPFAYDRVAGNYLVIELGMAYKDIrHILKKAL-----AEACTEIensekagNIFITSFgdMSVE-------DVSRLTDL 559

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 168 TVYKVLFSLPENILEnTLKLCREKFSHRINVANTFQSYVEL-----FHQHT---NKFEGVKEICKYYNISLNNAL--AMG 237
Cdd:PRK14502 560 NLKQAELAKQREYSE-TVHIEGDKRSTNIVLNHIQQSGLEYsfggrFYEVTggnDKGKAIKILNELFRLNFGNIHtfGLG 638

                        250       260
                 ....*....|....*....|....
gi 124802833 238 DGENDIEMLSGLTHSVGVHNASEK 261
Cdd:PRK14502 639 DSENDYSMLETVDSPILVQRPGNK 662
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 23-61 2.74e-05

Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 44.43  E-value: 2.74e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 124802833  23 IIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIAT 61
Cdd:COG3769    5 LVFTDLDGTLLDHDTYSWAAALPALARLKARGIPVILNT 43
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 217-266 7.66e-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: 42.90  E-value: 7.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 124802833 217 EGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGVhNASEKVKNSA 266
Cdd:COG0560  158 EALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAA 206
PRK15126 PRK15126
HMP-PP phosphatase;
27-282 8.07e-05

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 43.14  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833  27 DLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIATGRSIFSVENVIGehvkknRISL---LpgIYMNGCVTFDEKGsrvi 103
Cdd:PRK15126   8 DMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILG------ALSLdayL--ITGNGTRVHSLEG---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 104 DRIMNNDLKMEIHEFskqiniSKYAIWFCLEKTYCFEINDCIREYMEVEALNPDV--------IEDNMLEGLTVYKVLFS 175
Cdd:PRK15126  76 ELLHRQDLPADVAEL------VLHQQWDTRASMHVFNDDGWFTGKEIPALLQAHVysgfryqlIDLKRLPAHGVTKICFC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124802833 176 LP-ENILENTLKLCrEKFSHRINVANTFQSYVELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVG 254
Cdd:PRK15126 150 GDhDDLTRLQIQLN-EALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFI 228

                        250       260       270
                 ....*....|....*....|....*....|.
gi 124802833 255 VHNASEKVKNSAAY---VGPSNNEhAISHVL 282
Cdd:PRK15126 229 MGNAMPQLRAELPHlpvIGHCRNQ-AVSHYL 258
osmo_MPG_phos TIGR02461
mannosyl-3-phosphoglycerate phosphatase; Members of this family are ...
 23-69 1.75e-04

mannosyl-3-phosphoglycerate phosphatase; Members of this family are mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70). It acts sequentially after mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles.


Pssm-ID: 131514  Cd Length: 225  Bit Score: 42.07  E-value: 1.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 124802833   23 IIFTDLDGTLLNSENKVSEQnLESLIRAQEKGIKVVIATGRSIFSVE 69
Cdd:TIGR02461   1 VIFTDLDGTLLDPGYEPGPA-REALEELKDLGFPIVFVSSKTRAEQE 46
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 207-269 1.90e-04

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 40.97  E-value: 1.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124802833 207 ELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLS--GLthSVGVHNASEKVKNSAAYV 269
Cdd:cd01630   69 DLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKrvGL--SVAPADAHPEVREAADYV 131
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 214-246 5.86e-04

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: 39.84  E-value: 5.86e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 124802833 214 NKFEGVKEICKYYNISLNNALAMGDGENDIEML 246
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPML 169
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 215-266 1.86e-03

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 38.88  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 124802833  215 KFEGVKEICKYYNISLNNALAMGDGENDIEMLSGLTHSVGvHNASEKVKNSA 266
Cdd:TIGR00338 153 KGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIA-FNAKPKLQQKA 203
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 207-255 3.10e-03

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 36.60  E-value: 3.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 124802833 207 ELFHQHTNKFEGVKEICKYYNISLNNALAMGDGENDIEMLS-GLTHSVGV 255
Cdd:cd01427   57 DGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARaAGGRTVAV 106
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
16-61 4.89e-03

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 37.69  E-value: 4.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 124802833  16 NLNDEIkIIFTDLDGTLLNSENKVSEQNLESLIRAQEKGIKVVIAT 61
Cdd:PRK03669   3 SLQDPL-LIFTDLDGTLLDSHTYDWQPAAPWLTRLREAQVPVILCS 47
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 22-64 7.56e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 35.84  E-value: 7.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124802833   22 KIIFTDLDGTLLNSENKVSEQNLESLIR--------AQEKGIKVVIATGRS 64
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDERILYPevpdalaeLKEAGYKVVIVTNQS 51
 
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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