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Conserved domains on  [gi|15830153|ref|NP_308926|]
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sugar-phosphatase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576316)

Cof-type haloacid dehalogenase (HAD)-IIB family hydrolase uses a nucleophilic aspartate in the phosphoryl transfer reaction and may function as a phosphatase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

CATH:  3.30.1240.10
EC:  3.1.3.-|3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  16889794|15337123|33940035|37786806
SCOP:  3001890

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-260 4.71e-90

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: 264.83  E-value: 4.71e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   4 KVIVTDMDGTFLNDVKTYNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYehgkqlfhge 83
Cdd:cd07518   1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  84 ltrhesrivigellkdkqlnfvacglqsayvsenapeafvalmakhyhrlkpvkdyqeiddvlFKFSLNLPDEQIPLVID 163
Cdd:cd07518  71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 164 KLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIA 243
Cdd:cd07518  88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                       250
                ....*....|....*..
gi 15830153 244 RYATDDNNHEGALNVIQ 260
Cdd:cd07518 168 KYVAPSNNENGVLQVIE 184
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-260 4.71e-90

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: 264.83  E-value: 4.71e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   4 KVIVTDMDGTFLNDVKTYNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYehgkqlfhge 83
Cdd:cd07518   1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  84 ltrhesrivigellkdkqlnfvacglqsayvsenapeafvalmakhyhrlkpvkdyqeiddvlFKFSLNLPDEQIPLVID 163
Cdd:cd07518  71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 164 KLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIA 243
Cdd:cd07518  88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                       250
                ....*....|....*..
gi 15830153 244 RYATDDNNHEGALNVIQ 260
Cdd:cd07518 168 KYVAPSNNENGVLQVIE 184
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-259 6.65e-80

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: 241.40  E-value: 6.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     5 VIVTDMDGTFLNDVKTyNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALV-YEHGKQLFHGE 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHT-ISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAViDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    84 LTRHESRIVIGELLKDKqLNFVACGLQSAYVSENAPEAFVALMAKHYHRLKPVKDYQE-IDDVLFKFSLNLPDEQIPLVI 162
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHG-LDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYlPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   163 DKLH-IALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQ 241
Cdd:TIGR00099 159 EALNkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 15830153   242 IARYATDDNNHEGALNVI 259
Cdd:TIGR00099 239 LADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-259 4.13e-57

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 183.21  E-value: 4.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     6 IVTDMDGTFLNDVKTYNqPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVY-EHGKQLFHGEL 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKIS-EKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYdENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    85 TRhESRIVIGELLKDKQLNFVACGLQSAYVSENAPEAFVALMAKHYHRLKPVKDYQEI--DDVLFKFSLNLPDEQIPLVI 162
Cdd:pfam08282  80 SK-EAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELleDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   163 DKLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQI 242
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*..
gi 15830153   243 ARYATDDNNHEGALNVI 259
Cdd:pfam08282 239 ADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-260 2.57e-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: 2.57e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   2 SVKVIVTDMDGTFLNDVKTYNqPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYEHGkqlfh 81
Cdd:COG0561   1 MIKLIALDLDGTLLNDDGEIS-PRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPD----- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  82 geltrhesriviGELLKDKQLnfvacglqsayvsenapeafvalmakhyhrlkPVKDYQEIDDVLFKFslnlpdeqiplv 161
Cdd:COG0561  75 ------------GEVLYERPL--------------------------------DPEDVREILELLREH------------ 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 162 idKLHIALdgimkPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQ 241
Cdd:COG0561  99 --GLHLQV-----VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                       250
                ....*....|....*....
gi 15830153 242 IARYATDDNNHEGALNVIQ 260
Cdd:COG0561 172 AADYVTGSNDEDGVAEALE 190
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-260 2.50e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 83.87  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFlndvkTYNQPRF----MAQYQELKKRGIEFVVASGNqyyqLISFFPELKDEISFvaeNGALVYEHG 76
Cdd:PRK01158   1 MKIKAIAIDIDGTI-----TDKDRRLslkaVEAIRKAEKLGIPVILATGN----VLCFARAAAKLIGT---SGPVIAENG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   77 KQLFHGELTRhesRIVIGELLKdkqlnfvaCglQSAY--VSENAPEAFVALMAKHyhrlkpvKDYQEIDDVLFKfslNLP 154
Cdd:PRK01158  69 GVISVGFDGK---RIFLGDIEE--------C--EKAYseLKKRFPEASTSLTKLD-------PDYRKTEVALRR---TVP 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  155 DEQIPLVIDKLHIALDgimkPVTSGFGfIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGN 234
Cdd:PRK01158 126 VEEVRELLEELGLDLE----IVDSGFA-IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVAN 200

                        250       260
                 ....*....|....*....|....*.
gi 15830153  235 AAENIKQIARYATDDNNHEGALNVIQ 260
Cdd:PRK01158 201 ADEELKEAADYVTEKSYGEGVAEAIE 226
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-260 4.71e-90

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: 264.83  E-value: 4.71e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   4 KVIVTDMDGTFLNDVKTYNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYehgkqlfhge 83
Cdd:cd07518   1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  84 ltrhesrivigellkdkqlnfvacglqsayvsenapeafvalmakhyhrlkpvkdyqeiddvlFKFSLNLPDEQIPLVID 163
Cdd:cd07518  71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 164 KLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIA 243
Cdd:cd07518  88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                       250
                ....*....|....*..
gi 15830153 244 RYATDDNNHEGALNVIQ 260
Cdd:cd07518 168 KYVAPSNNENGVLQVIE 184
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-259 6.65e-80

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: 241.40  E-value: 6.65e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     5 VIVTDMDGTFLNDVKTyNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALV-YEHGKQLFHGE 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHT-ISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAViDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    84 LTRHESRIVIGELLKDKqLNFVACGLQSAYVSENAPEAFVALMAKHYHRLKPVKDYQE-IDDVLFKFSLNLPDEQIPLVI 162
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHG-LDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYlPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   163 DKLH-IALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQ 241
Cdd:TIGR00099 159 EALNkLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 15830153   242 IARYATDDNNHEGALNVI 259
Cdd:TIGR00099 239 LADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-259 4.13e-57

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 183.21  E-value: 4.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     6 IVTDMDGTFLNDVKTYNqPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVY-EHGKQLFHGEL 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKIS-EKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYdENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    85 TRhESRIVIGELLKDKQLNFVACGLQSAYVSENAPEAFVALMAKHYHRLKPVKDYQEI--DDVLFKFSLNLPDEQIPLVI 162
Cdd:pfam08282  80 SK-EAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELleDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   163 DKLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQI 242
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*..
gi 15830153   243 ARYATDDNNHEGALNVI 259
Cdd:pfam08282 239 ADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-260 2.57e-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: 2.57e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   2 SVKVIVTDMDGTFLNDVKTYNqPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYEHGkqlfh 81
Cdd:COG0561   1 MIKLIALDLDGTLLNDDGEIS-PRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPD----- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  82 geltrhesriviGELLKDKQLnfvacglqsayvsenapeafvalmakhyhrlkPVKDYQEIDDVLFKFslnlpdeqiplv 161
Cdd:COG0561  75 ------------GEVLYERPL--------------------------------DPEDVREILELLREH------------ 98

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 162 idKLHIALdgimkPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQ 241
Cdd:COG0561  99 --GLHLQV-----VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                       250
                ....*....|....*....
gi 15830153 242 IARYATDDNNHEGALNVIQ 260
Cdd:COG0561 172 AADYVTGSNDEDGVAEALE 190
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-254 4.93e-36

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: 128.87  E-value: 4.93e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   5 VIVTDMDGTFLNDVKTYNQPRFMAqYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYE-HGKQLFHge 83
Cdd:cd07516   1 LIALDLDGTLLNSDKEISPRTKEA-IKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDpTGKEILE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  84 ltRHESRIVIGELLKDKQLNFVACGLqsaYVSENAP----EAFVALMAKHYHRLKPVKDyQEIDDVLFKFSLNLPDEQIP 159
Cdd:cd07516  78 --RLISKEDVKELEEFLRKLGIGINI---YTNDDWAdtiyEENEDDEIIKPAEILDDLL-LPPDEDITKILFVGEDEELD 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 160 LVIDKLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENI 239
Cdd:cd07516 152 ELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEV 231

                       250
                ....*....|....*
gi 15830153 240 KQIARYATDDNNHEG 254
Cdd:cd07516 232 KEAADYVTLTNNEDG 246
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-257 5.34e-25

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: 98.83  E-value: 5.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   4 KVIVTDMDGTFLNDVKTYNQPRFMAqYQELKKRGIEFVVASGNQYYQLISFFPELKDEiSFVAENGALVYEHGKQLFHGE 83
Cdd:cd07517   1 KIVFFDIDGTLLDEDTTIPESTKEA-IAALKEKGILVVIATGRAPFEIQPIVKALGID-SYVSYNGQYVFFEGEVIYKNP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  84 LTRHESRIVIgELLKDKQlnfvacglqSAYVSENAPEAFVALMAKHYhrlkPVKDYQEiddvlFKFSLNLPDeqiplvid 163
Cdd:cd07517  79 LPQELVERLT-EFAKEQG---------HPVSFYGQLLLFEDEEEEQK----YEELRPE-----LRFVRWHPL-------- 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 164 klhialdgimkpvtsgfgFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIA 243
Cdd:cd07517 132 ------------------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIA 193

                       250
                ....*....|....
gi 15830153 244 RYATDDNNHEGALN 257
Cdd:cd07517 194 DYVTKDVDEDGILK 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-260 2.50e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 83.87  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFlndvkTYNQPRF----MAQYQELKKRGIEFVVASGNqyyqLISFFPELKDEISFvaeNGALVYEHG 76
Cdd:PRK01158   1 MKIKAIAIDIDGTI-----TDKDRRLslkaVEAIRKAEKLGIPVILATGN----VLCFARAAAKLIGT---SGPVIAENG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   77 KQLFHGELTRhesRIVIGELLKdkqlnfvaCglQSAY--VSENAPEAFVALMAKHyhrlkpvKDYQEIDDVLFKfslNLP 154
Cdd:PRK01158  69 GVISVGFDGK---RIFLGDIEE--------C--EKAYseLKKRFPEASTSLTKLD-------PDYRKTEVALRR---TVP 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  155 DEQIPLVIDKLHIALDgimkPVTSGFGfIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGN 234
Cdd:PRK01158 126 VEEVRELLEELGLDLE----IVDSGFA-IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVAN 200

                        250       260
                 ....*....|....*....|....*.
gi 15830153  235 AAENIKQIARYATDDNNHEGALNVIQ 260
Cdd:PRK01158 201 ADEELKEAADYVTEKSYGEGVAEAIE 226
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-264 5.65e-18

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: 80.20  E-value: 5.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     6 IVTDMDGTFLNDVKTYNQPRFMAQYQELKKrGIEFVVASGNQYyqliSFFPELKDEIsfvAENGALVYEHGKQLFHGELT 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESK-GIPVVLVTGNSV----QFARALAKLI---GTPDPVIAENGGEISYNEGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    86 RhesRIVIGELLKDKQLNFVacglqSAYVSENApeafvALMAKHYHRLKPVKDYQEIDdvlfkfslnlPDEqIPLVIDKL 165
Cdd:TIGR01482  73 D---DIFLAYLEEEWFLDIV-----IAKTFPFS-----RLKVQYPRRASLVKMRYGID----------VDT-VREIIKEL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   166 HIALDgimkPVTSGFGfIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIARY 245
Cdd:TIGR01482 129 GLNLV----AVDSGFD-IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADY 203

                         250
                  ....*....|....*....
gi 15830153   246 ATDDNNHEGALNVIQAVLD 264
Cdd:TIGR01482 204 VTESPYGEGGAEAIGEILQ 222
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-260 9.66e-18

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 80.51  E-value: 9.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFLNDVKTYNqPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPEL---KDEISFVAENGALVY--EH 75
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTIS-PAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELhmeQPGDYCITNNGALVQkaAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   76 GKQLFHGELTrHESRIVIGELLKDKQLNFVACGLQSAY-----VSE-NAPEAFVALMAKHYHRLkpvkdyQEIDDVLFKF 149
Cdd:PRK10513  80 GETVAQTALS-YDDYLYLEKLSREVGVHFHALDRNTLYtanrdISYyTVHESFLTGIPLVFREV------EKMDPNLQFP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  150 SLNLPDEqiPLVIDKlhiALDGIMKPVTSGFG-------FIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEM 222
Cdd:PRK10513 153 KVMMIDE--PEILDA---AIARIPAEVKERYTvlksapyFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAM 227

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15830153  223 LKMARYSFAMGNAAENIKQIARYATDDNNHEGALNVIQ 260
Cdd:PRK10513 228 IEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-232 1.14e-17

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: 78.96  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     5 VIVTDMDGTFLNDVKTYNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYEHGKQLFHGEL 84
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    85 TRhesriviGELLKDKQLNFVACGLQSAyvSENAPEAFVALMAkhyhrlkpvkdyqeiDDVLFKF-SLNLPDEQIPLVID 163
Cdd:TIGR01484  81 DV-------FEEILGIKFEEIGAELKSL--SEHYVGTFIEDKA---------------IAVAIHYvGAELGQELDSKMRE 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15830153   164 KL--HIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAM 232
Cdd:TIGR01484 137 RLekIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 189-263 5.59e-17

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: 75.32  E-value: 5.59e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830153 189 GLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIARYATDDNNHEGALNVIQAVL 263
Cdd:cd07514  65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-262 2.75e-14

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: 70.46  E-value: 2.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   5 VIVTDMDGTFLNDVKTYNQPRFMAQYQEL--KKRGIEFVVASGNQ---YYQLISFFPELKDEISFvaenGALvyehGKQL 79
Cdd:cd02605   1 LLVSDLDETLVGHDTNLQALERLQDLLEQltADNDVILVYATGRSpesVLELIKEVMLPKPDFII----SDV----GTEI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  80 FHGEltrheSRIVIGELLKDKQLNfvacglqsayvSENAPEAFVALmAKHYHRLKPVKDYQEIDdvlFKFSLNLPDEQIP 159
Cdd:cd02605  73 YYGE-----SGYLEPDTYWNEVLS-----------EGWERFLFEAI-ADLFKQLKPQSELEQNP---HKISFYLDPQNDA 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 160 LVIDKL--HIALDGI-MKPVTSGFGFIDL-IIP-GLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGN 234
Cdd:cd02605 133 AVIEQLeeMLLKAGLtVRIIYSSGLAYDLdILPlGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGN 212

                       250       260       270
                ....*....|....*....|....*....|
gi 15830153 235 AAENIKQIARYATDDNNHEG--ALNVIQAV 262
Cdd:cd02605 213 AQPELLKWADRVTRSRLAKGpyAGGILEGL 242
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-259 5.10e-14

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 70.05  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFLNDVKTYnQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYE-HGKQL 79
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTI-LPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDyQAKKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   80 FHGE-LTRHESRIVIgELLKDKQLNfvacGLqsAYVSEnapeafvALMakhyhrlkpvkdYQEIDDVL---FKFSLNLPD 155
Cdd:PRK10530  80 LEADpLPVQQALQVI-EMLDEHQIH----GL--MYVDD-------AML------------YEHPTGHVirtLNWAQTLPP 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  156 EQIPLV--IDKLHIALDG---IMKpvtsgFGFIDLIIPGLH--------------------------KANGISRLLKRW- 203
Cdd:PRK10530 134 EQRPTFtqVDSLAQAARQvnaIWK-----FALTHEDLPQLQhfakhvehelglecewswhdqvdiarKGNSKGKRLTQWv 208

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15830153  204 ---DLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIARYATDDNNHEGALNVI 259
Cdd:PRK10530 209 eaqGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFI 267
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 147-252 2.82e-12

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: 64.59  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   147 FKFSLNLPDEQIPLVIDKLHIALD--GI-MKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEML 223
Cdd:pfam05116 117 HKVSYFLDPEAAAAVLAELEQLLRkrGLdVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF 196

                          90       100
                  ....*....|....*....|....*....
gi 15830153   224 KMARYSFAMGNAAENIKQIARYATDDNNH 252
Cdd:pfam05116 197 IGGTRGVVVGNAQPELLQWYLENARDNPR 225
PLN02887 PLN02887
hydrolase family protein
 4-259 7.58e-12

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 64.90  E-value: 7.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    4 KVIVTDMDGTFLNDvKTYNQPRFMAQYQELKKRGIEFVVASGNQYYQLISFFP--ELKDEISFVAE-------NGALVY- 73
Cdd:PLN02887 309 SYIFCDMDGTLLNS-KSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKmvDLAGKDGIISEsspgvflQGLLVYg 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   74 EHGKQLFHGELTRH----------ESRIVIGELLKDKQLNFVACGL-QSAYVSENAPEAfvALMAKHYHRLKPVkdyqEI 142
Cdd:PLN02887 388 RQGREIYRSNLDQEvcreaclyslEHKIPLIAFSQDRCLTLFDHPLvDSLHTIYHEPKA--EIMSSVDQLLAAA----DI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  143 DDVLFkfsLNLPDEQIPLVIDKLHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEM 222
Cdd:PLN02887 462 QKVIF---LDTAEGVSSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEM 538

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15830153  223 LKMARYSFAMGNAAENIKQIARYATDDNNHEGALNVI 259
Cdd:PLN02887 539 LQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-263 1.04e-08

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 54.56  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFLnDVKTYN-QPrfmAQ--YQELKKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVY---E 74
Cdd:PRK00192   2 MMKLLVFTDLDGTLL-DHHTYSyEP---AKpaLKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIYipkN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   75 HGKQLFHGELTRHESRIV--------IGELLKD--KQLNFVACGLqsayvSENAPEAFVALMAKHYHRLKPVKD--YQEi 142
Cdd:PRK00192  78 YFPFQPDGERLKGDYWVIelgppyeeLREILDEisDELGYPLKGF-----GDLSAEEVAELTGLSGESARLAKDreFSE- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  143 ddvlfKFSLNLPDEQIPLVIDKLHiaLDGIMkpVTSGFGFIDLIIPGlHKANGISRLLKRW-DLSPQNVVAIGDSGNDAE 221
Cdd:PRK00192 152 -----PFLWNGSEAAKERFEEALK--RLGLK--VTRGGRFLHLLGGG-DKGKAVRWLKELYrRQDGVETIALGDSPNDLP 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15830153  222 MLKMARYSFAMGNA----AENIKQIAR---YATDDNNHEGALNVIQAVL 263
Cdd:PRK00192 222 MLEAADIAVVVPGPdgpnPPLLPGIADgefILASAPGPEGWAEAINKLL 270
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 5-241 3.75e-08

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 52.89  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     5 VIVTDMDGTFLNDVKTYNQ--PRFMAQYQELKKRGIEFVVASGNQYyqliSFFPELKDEISFVaENGALVYEHGKQLFHG 82
Cdd:TIGR01485   3 LLVSDLDNTLVDHTDGDNQalLRLNALLEDHRGEDSLLVYSTGRSP----HSYKELQKQKPLL-TPDIWVTSVGSEIYYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    83 ELTRHESRivigellkdkqlnfvacglQSAYVSENAPEAFVALMAKHYHRLKPVKDYQEIDdvlFKFSLNLPDEQIPLVI 162
Cdd:TIGR01485  78 GAEVPDQH-------------------WAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRP---HKVSFFLDPEAAPEVI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   163 DKLHIALD--GI-MKPVTSGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMAR-YSFAMGNAAEN 238
Cdd:TIGR01485 136 KQLTEMLKetGLdVKLIYSSGKDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEIGSvRGVIVSNAQEE 215


                  ...
gi 15830153   239 IKQ 241
Cdd:TIGR01485 216 LLQ 218
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 192-231 3.97e-06

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 46.75  E-value: 3.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15830153 192 KANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFA 231
Cdd:COG0560 156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVA 195
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-234 1.84e-05

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: 45.05  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   5 VIVTDMDGTFLnDVKTYNQPRFMAQYQELKKRGIEFVVASG-----NQYYQLisffpELKDEISFVAENGALVY------ 73
Cdd:cd07507   1 VIFTDLDGTLL-DHHTYSFDPARPALERLKERGIPVVPCTSktraeVEYLRK-----ELGIEDPFIVENGGAIFiprgyf 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  74 -EHGKQLFHGELTRHESRIVIGEL------LKDKqlnfvaCGLQSAYVSENAPEAFVALMAKHYHRLKPVKDyQEIDDVL 146
Cdd:cd07507  75 kFPGRCKSEGGYEVIELGKPYREIraalekIREE------TGFKITGFGDLTEEEIAELTGLPRERAALAKE-REYSETI 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 147 FKFSLNLPDEQIplvidklHIALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRW-DLSPQ-NVVAIGDSGNDAEMLK 224
Cdd:cd07507 148 ILRSDEEEDEKV-------LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYrQLYEAiVTVGLGDSPNDLPMLE 220

                       250
                ....*....|
gi 15830153 225 MARYSFAMGN 234
Cdd:cd07507 221 AVDIAFVVKS 230
PRK15126 PRK15126
HMP-PP phosphatase;
178-241 7.10e-05

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 43.14  E-value: 7.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830153  178 SGFGFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQ 241
Cdd:PRK15126 175 SATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLRA 238
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-226 9.26e-05

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 42.19  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153     3 VKVIVTDMDGTFLNDvktynqprfmaqyqelkKRGIEFVVASGNQYYQLISFFPELKDEISFVAENGALVYEHGKQLFHG 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDG-----------------EPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    83 ELTRHESRIVigellkdkqlnfvacGLQSAYVSENAPEAFVALMAKHYHRLKPvkdyqEIDDVLfkfsLNLPDEQIPLVI 162
Cdd:pfam00702  64 ELDILRGLVE---------------TLEAEGLTVVLVELLGVIALADELKLYP-----GAAEAL----KALKERGIKVAI 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830153   163 ---DKLHIALD-----GIMKPVTSGFGFIDLIIPGLHKAnGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMA 226
Cdd:pfam00702 120 ltgDNPEAAEAllrllGLDDYFDVVISGDDVGVGKPKPE-IYLAALERLGVKPEEVLMVGDGVNDIPAAKAA 190
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 5-226 1.97e-04

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 41.74  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   5 VIVTDMDGTFLnDVKTYN-QPrfmAQY--QELKKRGIEFVVASGNQYYQLIsffpELKDEIS----FVAENGALVYehgk 77
Cdd:COG3769   5 LVFTDLDGTLL-DHDTYSwAA---ALPalARLKARGIPVILNTSKTAAEVE----PLRQELGlsdpFIVENGAAIF---- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153  78 qLFHGELTRHESRIVIGEllkdkqlnfvacglqsayvsenapeafvalmakhYHRLKPVKDYQEIDDVL--------FKF 149
Cdd:COG3769  73 -IPKGYFAFPSGTADIDG----------------------------------YWVIELGKPYAEIRAVLeqlreelgFKF 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153 150 SL--NLPDEQI---------------------PLVID---------KLHIALDGIMkpVTSGFGFIdLIIPGLHKANGIS 197
Cdd:COG3769 118 TGfgDMSAEEVaeltglsleqaalakqrefsePLLWLgsdealerfIAALAALGLT--VLRGGRFL-HLMGGADKGKAVR 194

                       250       260       270
                ....*....|....*....|....*....|..
gi 15830153 198 RLLKRWDLSPQN---VVAIGDSGNDAEMLKMA 226
Cdd:COG3769 195 WLVEQYRQRFGKnvvTIALGDSPNDIPMLEAA 226
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 181-255 3.33e-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: 39.81  E-value: 3.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830153 181 GFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQIARYATDDNNHEGA 255
Cdd:cd01630  66 GIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGA 140
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 186-243 4.05e-04

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


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 40.80  E-value: 4.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15830153   186 IIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMgNAAENIKQIA 243
Cdd:TIGR00338 147 IVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKA 203
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 158-226 4.44e-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: 38.92  E-value: 4.44e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15830153 158 IPLVI--DKLHIALDGIMKPVTSGFGFIDLIIPGLH-----KANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMA 226
Cdd:cd01427  24 IKLAIvtNRSREALRALLEKLGLGDLFDGIIGSDGGgtpkpKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAA 99
serB PRK11133
phosphoserine phosphatase; Provisional
 186-226 4.71e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 41.09  E-value: 4.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15830153  186 IIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMA 226
Cdd:PRK11133 243 IVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAA 283
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-105 3.08e-03

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 38.01  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153    1 MSVKVIVTDMDGTFL-------NDVKTYnqprfmaqYQELKKRGIEFVVASGNQYYQLISffpELKDEIS----FV-AEN 68
Cdd:PTZ00174   3 MKKTILLFDVDGTLTkprnpitQEMKDT--------LAKLKSKGFKIGVVGGSDYPKIKE---QLGEDVLedfdYVfSEN 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15830153   69 GALVYEHGKQLFHGELTRHesrivIGELLKDKQLNFV 105
Cdd:PTZ00174  72 GLVAYKDGELFHSQSILKF-----LGEEKLKKFINFC 103
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
205-231 3.70e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 37.06  E-value: 3.70e-03
                        10        20
                ....*....|....*....|....*..
gi 15830153 205 LSPQNVVAIGDSGNDAEMLKMARYSFA 231
Cdd:COG4087  89 LGAETTVAIGNGRNDVLMLKEAALGIA 115
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-64 4.24e-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: 36.22  E-value: 4.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830153   5 VIVTDMDGTFLndvktynqprFMAQYQELKKRGIEFVVASGNQYYQLISFFPELKDEISF 64
Cdd:cd01427   1 AVLFDLDGTLL----------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLF 50
PRK10976 PRK10976
putative hydrolase; Provisional
 189-242 4.89e-03

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 37.72  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15830153  189 GLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIKQI 242
Cdd:PRK10976 188 GVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLKDL 241
 
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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