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Conserved domains on  [gi|985629529|ref|WP_060855615|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Citrobacter]

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 6.26e-86

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: 254.05  E-value: 6.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   4 KVIVTDMDGTFLDDAKQYDRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFehgkqlfhge 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  84 ltrhesrivigellkdkqlnfvacglqsayvsenapesfvglmskhyhrlkpvkdyqdiddvlFKFSLNLPDQQIPLVID 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 164 HLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIA 243
Cdd:cd07518   88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                        250
                 ....*....|....*..
gi 985629529 244 RYQTDDNNHQGALNVIQ 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 6.26e-86

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: 254.05  E-value: 6.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   4 KVIVTDMDGTFLDDAKQYDRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFehgkqlfhge 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  84 ltrhesrivigellkdkqlnfvacglqsayvsenapesfvglmskhyhrlkpvkdyqdiddvlFKFSLNLPDQQIPLVID 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 164 HLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIA 243
Cdd:cd07518   88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                        250
                 ....*....|....*..
gi 985629529 244 RYQTDDNNHQGALNVIQ 260
Cdd:cd07518  168 KYVAPSNNENGVLQVIE 184
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-259 5.15e-74

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: 226.38  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    5 VIVTDMDGTFLDDAKQYdRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALV-FEHGKQLFHGE 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTI-SPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAViDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   84 LTRHESRIVIGELLKDKqLNFVACGLQSAYVSENAPESFVGLMSKHYHRLKPVKDYQD-IDDVLFKFSLNLPDQQIPLVI 162
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHG-LDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYlPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  163 DHLHSA-LDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKA 241
Cdd:TIGR00099 159 EALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 985629529  242 IARYQTDDNNHQGALNVI 259
Cdd:TIGR00099 239 LADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-259 3.71e-57

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 183.59  E-value: 3.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    6 IVTDMDGTFLDDAKQYDRaRFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALV-FEHGKQLFHGEL 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISE-KTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIyDENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   85 TRhESRIVIGELLKDKQLNFVACGLQSAYVSENAPESFVGLMSKHYHRLKPVKDYQDI--DDVLFKFSLNLPDQQIPLVI 162
Cdd:pfam08282  80 SK-EAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELleDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  163 DHLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAI 242
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*..
gi 985629529  243 ARYQTDDNNHQGALNVI 259
Cdd:pfam08282 239 ADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-260 9.03e-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: 167.62  E-value: 9.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   2 TIKVIVTDMDGTFLDDAKQYDRaRFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFE-HGKQLF 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISP-RTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDpDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  81 HGELTRHESRIVIgELLKDKQLNFVACglqsayvsenapesfvglmskhyhrlkpvkdyqdiddvlfkfslnlpdqqipl 160
Cdd:COG0561   80 ERPLDPEDVREIL-ELLREHGLHLQVV----------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 161 vidhlhsaldgimkpVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIK 240
Cdd:COG0561  106 ---------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVK 170

                        250       260
                 ....*....|....*....|
gi 985629529 241 AIARYQTDDNNHQGALNVIQ 260
Cdd:COG0561  171 AAADYVTGSNDEDGVAEALE 190
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-260 5.01e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 83.10  E-value: 5.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   1 MTIKVIVTDMDGTFLDDakqyDRA---RFLAQYQELKKRDIEFVVASGNqyyqLISFFPQLKDEISFvaeNGALVFEHGK 77
Cdd:PRK01158   1 MKIKAIAIDIDGTITDK----DRRlslKAVEAIRKAEKLGIPVILATGN----VLCFARAAAKLIGT---SGPVIAENGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  78 QLFHGELTRhesRIVIGELLKdkqlnfvaCglQSAY--VSENAPESFVGLMSKH-YHRLKPVKDYQDID-----DVLFKF 149
Cdd:PRK01158  70 VISVGFDGK---RIFLGDIEE--------C--EKAYseLKKRFPEASTSLTKLDpDYRKTEVALRRTVPveevrELLEEL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 150 SLNLpdqqipLVIDhlhsaldgimkpvtSGFGfIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYS 229
Cdd:PRK01158 137 GLDL------EIVD--------------SGFA-IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFG 195

                        250       260       270
                 ....*....|....*....|....*....|.
gi 985629529 230 FAMANAAESIKAIARYQTDDNNHQGALNVIQ 260
Cdd:PRK01158 196 VAVANADEELKEAADYVTEKSYGEGVAEAIE 226
 
Name Accession Description Interval E-value
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-260 6.26e-86

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: 254.05  E-value: 6.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   4 KVIVTDMDGTFLDDAKQYDRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFehgkqlfhge 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVVY---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  84 ltrhesrivigellkdkqlnfvacglqsayvsenapesfvglmskhyhrlkpvkdyqdiddvlFKFSLNLPDQQIPLVID 163
Cdd:cd07518   71 ---------------------------------------------------------------FKFTLNVPDEAAPDIID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 164 HLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIA 243
Cdd:cd07518   88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                        250
                 ....*....|....*..
gi 985629529 244 RYQTDDNNHQGALNVIQ 260
Cdd:cd07518  168 KYVAPSNNENGVLQVIE 184
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-259 5.15e-74

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: 226.38  E-value: 5.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    5 VIVTDMDGTFLDDAKQYdRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALV-FEHGKQLFHGE 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTI-SPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAViDDQGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   84 LTRHESRIVIGELLKDKqLNFVACGLQSAYVSENAPESFVGLMSKHYHRLKPVKDYQD-IDDVLFKFSLNLPDQQIPLVI 162
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHG-LDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYlPDDILKILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  163 DHLHSA-LDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKA 241
Cdd:TIGR00099 159 EALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 985629529  242 IARYQTDDNNHQGALNVI 259
Cdd:TIGR00099 239 LADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-259 3.71e-57

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 183.59  E-value: 3.71e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    6 IVTDMDGTFLDDAKQYDRaRFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALV-FEHGKQLFHGEL 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISE-KTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIyDENGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   85 TRhESRIVIGELLKDKQLNFVACGLQSAYVSENAPESFVGLMSKHYHRLKPVKDYQDI--DDVLFKFSLNLPDQQIPLVI 162
Cdd:pfam08282  80 SK-EAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELleDEDINKILILLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  163 DHLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAI 242
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*..
gi 985629529  243 ARYQTDDNNHQGALNVI 259
Cdd:pfam08282 239 ADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-260 9.03e-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: 167.62  E-value: 9.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   2 TIKVIVTDMDGTFLDDAKQYDRaRFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFE-HGKQLF 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISP-RTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDpDGEVLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  81 HGELTRHESRIVIgELLKDKQLNFVACglqsayvsenapesfvglmskhyhrlkpvkdyqdiddvlfkfslnlpdqqipl 160
Cdd:COG0561   80 ERPLDPEDVREIL-ELLREHGLHLQVV----------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 161 vidhlhsaldgimkpVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIK 240
Cdd:COG0561  106 ---------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVK 170

                        250       260
                 ....*....|....*....|
gi 985629529 241 AIARYQTDDNNHQGALNVIQ 260
Cdd:COG0561  171 AAADYVTGSNDEDGVAEALE 190
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-254 7.46e-34

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: 123.09  E-value: 7.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   5 VIVTDMDGTFLDDAKQydrarfLAQY-----QELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFE-HGKQ 78
Cdd:cd07516    1 LIALDLDGTLLNSDKE------ISPRtkeaiKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDpTGKE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  79 LFHgeltRHESRIVIGELLKDKQLNFVACGLqsaYVSENAPESFVGLMSKHYHRLKP---VKDYQDIDDVLFKFSLNLPD 155
Cdd:cd07516   75 ILE----RLISKEDVKELEEFLRKLGIGINI---YTNDDWADTIYEENEDDEIIKPAeilDDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 156 QQIPLVIDHLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANA 235
Cdd:cd07516  148 EELDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250
                 ....*....|....*....
gi 985629529 236 AESIKAIARYQTDDNNHQG 254
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDG 246
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-257 5.45e-23

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 93.44  E-value: 5.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   4 KVIVTDMDGTFLDDAKQYdRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEiSFVAENGALVFEHGKQLFHGE 83
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTI-PESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGID-SYVSYNGQYVFFEGEVIYKNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  84 LTRHESRIVIgELLKDKQLNFVACGLQSAYVSENAPESFVGLMSKhyhrlkpvkdyqdiddvlFKFSLNLPDqqiplvid 163
Cdd:cd07517   79 LPQELVERLT-EFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPE------------------LRFVRWHPL-------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 164 hlhsaldgimkpvtsgfgFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIA 243
Cdd:cd07517  132 ------------------STDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIA 193

                        250
                 ....*....|....
gi 985629529 244 RYQTDDNNHQGALN 257
Cdd:cd07517  194 DYVTKDVDEDGILK 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-260 5.01e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 83.10  E-value: 5.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   1 MTIKVIVTDMDGTFLDDakqyDRA---RFLAQYQELKKRDIEFVVASGNqyyqLISFFPQLKDEISFvaeNGALVFEHGK 77
Cdd:PRK01158   1 MKIKAIAIDIDGTITDK----DRRlslKAVEAIRKAEKLGIPVILATGN----VLCFARAAAKLIGT---SGPVIAENGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  78 QLFHGELTRhesRIVIGELLKdkqlnfvaCglQSAY--VSENAPESFVGLMSKH-YHRLKPVKDYQDID-----DVLFKF 149
Cdd:PRK01158  70 VISVGFDGK---RIFLGDIEE--------C--EKAYseLKKRFPEASTSLTKLDpDYRKTEVALRRTVPveevrELLEEL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 150 SLNLpdqqipLVIDhlhsaldgimkpvtSGFGfIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYS 229
Cdd:PRK01158 137 GLDL------EIVD--------------SGFA-IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFG 195

                        250       260       270
                 ....*....|....*....|....*....|.
gi 985629529 230 FAMANAAESIKAIARYQTDDNNHQGALNVIQ 260
Cdd:PRK01158 196 VAVANADEELKEAADYVTEKSYGEGVAEAIE 226
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-232 3.73e-18

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: 80.50  E-value: 3.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    5 VIVTDMDGTFLDDAKQYDRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFEHGKQLFHGEL 84
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   85 TRhesriviGELLKDKQLNFVACGLQSAyvSENAPESFVGLMSkhyhrlkpvkdyqdiDDVLFKFSLNLPDQQIplvIDH 164
Cdd:TIGR01484  81 DV-------FEEILGIKFEEIGAELKSL--SEHYVGTFIEDKA---------------IAVAIHYVGAELGQEL---DSK 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985629529  165 LHSALDGI------MKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAM 232
Cdd:TIGR01484 134 MRERLEKIgrndleLEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-264 1.25e-16

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: 76.73  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    6 IVTDMDGTFLDDakqyDRARFLAQYQELKKRD---IEFVVASGNQYyqlisffpQLKDEIS-FVAENGALVFEHGKQLFH 81
Cdd:TIGR01482   1 IASDIDGTLTDP----NRAINESALEAIRKAEskgIPVVLVTGNSV--------QFARALAkLIGTPDPVIAENGGEISY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   82 GELTRhesRIVIGELLKDKQLNFVacglqSAYVSENAPESFvglmsKHYHRLKPVKDYQDIDDvlfkfslnlpdQQIPLV 161
Cdd:TIGR01482  69 NEGLD---DIFLAYLEEEWFLDIV-----IAKTFPFSRLKV-----QYPRRASLVKMRYGIDV-----------DTVREI 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  162 IDHLhsaldGIM-KPVTSGFGfIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIK 240
Cdd:TIGR01482 125 IKEL-----GLNlVAVDSGFD-IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELK 198

                         250       260
                  ....*....|....*....|....
gi 985629529  241 AIARYQTDDNNHQGALNVIQAVLD 264
Cdd:TIGR01482 199 EWADYVTESPYGEGGAEAIGEILQ 222
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 189-263 2.88e-16

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: 73.39  E-value: 2.88e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985629529 189 GLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIARYQTDDNNHQGALNVIQAVL 263
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-260 6.72e-16

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 75.50  E-value: 6.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   1 MTIKVIVTDMDGTFLDDAKQYDrARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQL---KDEISFVAENGALV--FEH 75
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTIS-PAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELhmeQPGDYCITNNGALVqkAAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  76 GKQLFHGELTrHESRIVIGELLKDKQLNFVACGLQSAY-----VSE-NAPESFVGLMSKHYHRLkpvkdyQDIDdvlfkf 149
Cdd:PRK10513  80 GETVAQTALS-YDDYLYLEKLSREVGVHFHALDRNTLYtanrdISYyTVHESFLTGIPLVFREV------EKMD------ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 150 slnlPDQQIPLV--IDH---LHSALDGIMKPVTSGFG-------FIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSG 217
Cdd:PRK10513 147 ----PNLQFPKVmmIDEpeiLDAAIARIPAEVKERYTvlksapyFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQE 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 985629529 218 NDAEMLKMAHYSFAMANAAESIKAIARYQTDDNNHQGALNVIQ 260
Cdd:PRK10513 223 NDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-262 2.04e-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: 70.84  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   5 VIVTDMDGTFL-DDAKQYDRARFLAQYQEL-KKRDIEFVVASGNQ---YYQLISFFPQLKDEISFvaenGALvfehGKQL 79
Cdd:cd02605    1 LLVSDLDETLVgHDTNLQALERLQDLLEQLtADNDVILVYATGRSpesVLELIKEVMLPKPDFII----SDV----GTEI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  80 FHGEltrheSRIVIGELLKDKQLNfvacglqsayvSENAPESFVGLMSKHYHRLKPVKDYQDiddvLFKFSLNLPDQQIP 159
Cdd:cd02605   73 YYGE-----SGYLEPDTYWNEVLS-----------EGWERFLFEAIADLFKQLKPQSELEQN----PHKISFYLDPQNDA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 160 LVIDHL--HSALDGI-MKPVTSGFGFIDL-IIP-GLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMAN 234
Cdd:cd02605  133 AVIEQLeeMLLKAGLtVRIIYSSGLAYDLdILPlGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGN 212

                        250       260       270
                 ....*....|....*....|....*....|
gi 985629529 235 AAESIKAIARYQTDDNNHQG--ALNVIQAV 262
Cdd:cd02605  213 AQPELLKWADRVTRSRLAKGpyAGGILEGL 242
PLN02887 PLN02887
hydrolase family protein
 4-259 8.28e-13

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 67.98  E-value: 8.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   4 KVIVTDMDGTFLDDAKQYDRARFLAqYQELKKRDIEFVVASGNQYYQLISFFP--QLKDEISFVAE-------NGALVF- 73
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKA-LKEALSRGVKVVIATGKARPAVIDILKmvDLAGKDGIISEsspgvflQGLLVYg 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  74 EHGKQLFHGELTRHESRIVIGELLKDKqLNFVACGLQSAYVSENAPesFVGLMSKHYHRLK----PVKDY----QDIDDV 145
Cdd:PLN02887 388 RQGREIYRSNLDQEVCREACLYSLEHK-IPLIAFSQDRCLTLFDHP--LVDSLHTIYHEPKaeimSSVDQllaaADIQKV 464

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 146 LFkfsLNLPDQQIPLVIDHLHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKM 225
Cdd:PLN02887 465 IF---LDTAEGVSSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQL 541

                        250       260       270
                 ....*....|....*....|....*....|....
gi 985629529 226 AHYSFAMANAAESIKAIARYQTDDNNHQGALNVI 259
Cdd:PLN02887 542 ASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 3-259 2.16e-12

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: 64.76  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    3 IKVIVTDMDGTFLDDAKQYDrARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFehgkqlfhg 82
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMIS-ERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIF--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   83 eltrhesrivigelLKDKQLNFVACGLQSAYVSEnapesfvglMSKHYHRLKPVKDYQDIDDVLFKFSLNLpDQQIPLvi 162
Cdd:TIGR01487  71 --------------YNKEDIFLANMEEEWFLDEE---------KKKRFPRDRLSNEYPRASLVIMREGKDV-DEVREI-- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  163 dhlhsALDGIMKPVTSGFGfIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAI 242
Cdd:TIGR01487 125 -----IKERGLNLVASGFA-IHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEI 198

                         250
                  ....*....|....*..
gi 985629529  243 ARYQTDDNNHQGALNVI 259
Cdd:TIGR01487 199 ADYVTSNPYGEGVVEVL 215
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 4-252 1.05e-11

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: 63.05  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    4 KVIVTDMDGTFLDDAKQyDRARFLaQYQELKKRDIEFVVASGNQYyqlisffpqlkdeisfvaengalvfehgkqlfhgE 83
Cdd:pfam05116   3 LLLVSDLDNTLVDGDNE-ALARLN-QLLEAYRPDVGLVFATGRSL----------------------------------D 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   84 LTRhesrivigELLKDKQLnfvacgLQSAYVSenapeSFVGLMSKHYHRLKPVKDYQDIDDVL----------------- 146
Cdd:pfam05116  47 SAK--------ELLKEKPL------PTPDYLI-----TSVGTEIYYGPSLVPDQSWQEHLDYHwdrqavvealakfpglt 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  147 ---------FKFSLNLPDQQIPLVID----HLHSA-LDgiMKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVA 212
Cdd:pfam05116 108 lqpeeeqrpHKVSYFLDPEAAAAVLAeleqLLRKRgLD--VKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLV 185

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 985629529  213 IGDSGNDAEMLKMAHYSFAMANAAESIKAIARYQTDDNNH 252
Cdd:pfam05116 186 CGDSGNDEELFIGGTRGVVVGNAQPELLQWYLENARDNPR 225
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-259 7.58e-10

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 58.11  E-value: 7.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   1 MTIKVIVTDMDGTFLDDAKQYDRARfLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVFE-HGKQL 79
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPES-LEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDyQAKKV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  80 FHGE-LTRHESRIVIgELLKDKQLNfvacglqsayvsenapesfvGLMskhyhrlkpvkdYQDiDDVLFKF--------- 149
Cdd:PRK10530  80 LEADpLPVQQALQVI-EMLDEHQIH--------------------GLM------------YVD-DAMLYEHptghvirtl 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 150 --SLNLPDQQIPLV--IDHLHSALDG---IMKpvtsgFGFIDLIIPGLH--------------------------KANGI 196
Cdd:PRK10530 126 nwAQTLPPEQRPTFtqVDSLAQAARQvnaIWK-----FALTHEDLPQLQhfakhvehelglecewswhdqvdiarKGNSK 200

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 985629529 197 SRLLKRW----NLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIARYQTDDNNHQGALNVI 259
Cdd:PRK10530 201 GKRLTQWveaqGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFI 267
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-230 8.09e-10

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 58.03  E-value: 8.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   1 MTIKVIVTDMDGTFLdDAKQYDRARFLAQYQELKKRDIEFVVASGNQYYQLISFFPQLKDEISFVAENGALVF---EHGK 77
Cdd:PRK00192   2 MMKLLVFTDLDGTLL-DHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIYipkNYFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  78 QLFHGELTRHESRIV--------IGELLKD--KQLNFVACGLQSayVSENAPESFVGLmskHYHRLKPVKDYQdiddvlf 147
Cdd:PRK00192  81 FQPDGERLKGDYWVIelgppyeeLREILDEisDELGYPLKGFGD--LSAEEVAELTGL---SGESARLAKDRE------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 148 kFS----LNLPDQQIPLVIDHLHSalDGIMkpVTSGFGFIDLIIPGlHKANGISRLLKRWN-LSPQNVVAIGDSGNDAEM 222
Cdd:PRK00192 149 -FSepflWNGSEAAKERFEEALKR--LGLK--VTRGGRFLHLLGGG-DKGKAVRWLKELYRrQDGVETIALGDSPNDLPM 222


                 ....*...
gi 985629529 223 LKMAHYSF 230
Cdd:PRK00192 223 LEAADIAV 230
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 5-222 2.81e-07

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: 50.20  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    5 VIVTDMDGTFLD--DAKQYDRARFLAQYQELKKRDIEFVVASGNQYyqliSFFPQLKDEISFVaENGALVFEHGKQLFHG 82
Cdd:TIGR01485   3 LLVSDLDNTLVDhtDGDNQALLRLNALLEDHRGEDSLLVYSTGRSP----HSYKELQKQKPLL-TPDIWVTSVGSEIYYG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   83 ELTRHESRivigellkdkqlnfvacglQSAYVSENAPESFVGLMSKHYHRLKPVKDYQDIDdvlFKFSLNLPDQQIPLVI 162
Cdd:TIGR01485  78 GAEVPDQH-------------------WAEYLSEKWQRDIVVAITDKFEELKPQPDLEQRP---HKVSFFLDPEAAPEVI 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985629529  163 DHLHSALD--GI-MKPVTSGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEM 222
Cdd:TIGR01485 136 KQLTEMLKetGLdVKLIYSSGKDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIEL 198
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 192-244 3.11e-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: 3.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 985629529 192 KANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMaNAAESIKAIAR 244
Cdd:COG0560  156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-227 1.85e-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: 44.50  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529    3 IKVIVTDMDGTFLDDAKQYDRArflaqyqelkkrdiefvvasgnqYYQLISFFPQLKDEISFVAENGALVFEHGKQLFHG 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEA-----------------------IAELASEHPLAKAIVAAAEDLPIPVEDFTARLLLG 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   83 ELTRhesrivIGELLKDKQLNfvacglqsayvsENAPESFVGLMSKHYHRLKPVKDYQDIDDVLFKFSLNLPDQQIPLVI 162
Cdd:pfam00702  58 KRDW------LEELDILRGLV------------ETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAI 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985629529  163 ---DHLHSALD-----GIMKPVTSGFGFIDLIIPGLHKAnGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAH 227
Cdd:pfam00702 120 ltgDNPEAAEAllrllGLDDYFDVVISGDDVGVGKPKPE-IYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 181-255 2.43e-05

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: 43.28  E-value: 2.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985629529 181 GFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKAIARYQTDDNNHQGA 255
Cdd:cd01630   66 GIEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGA 140
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-230 7.59e-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: 43.12  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   5 VIVTDMDGTFLD-DAKQYDRAR-FLAqyqELKKRDIEFVVASG-----NQYYQLisffpQLKDEISFVAENGALVF---- 73
Cdd:cd07507    1 VIFTDLDGTLLDhHTYSFDPARpALE---RLKERGIPVVPCTSktraeVEYLRK-----ELGIEDPFIVENGGAIFiprg 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  74 ---EHGKQLFHGELTRHESRIVIGEL---LKDKQLNFVACGLQSAYVSENAPESFVGLmSKHYHRLKPVKDYqdiDDVLF 147
Cdd:cd07507   73 yfkFPGRCKSEGGYEVIELGKPYREIraaLEKIREETGFKITGFGDLTEEEIAELTGL-PRERAALAKEREY---SETII 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 148 KFSLNLPDQQIplvidhlHSALDGIMKPVTSGFGFIDLIIPGLHKANGISRLLKRWN--LSPQNVVAIGDSGNDAEMLKM 225
Cdd:cd07507  149 LRSDEEEDEKV-------LEALEERGLKITKGGRFYHVLGAGADKGKAVAILAALYRqlYEAIVTVGLGDSPNDLPMLEA 221


                 ....*
gi 985629529 226 AHYSF 230
Cdd:cd07507  222 VDIAF 226
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 186-243 1.90e-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: 41.57  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 985629529  186 IIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMaNAAESIKAIA 243
Cdd:TIGR00338 147 IVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKA 203
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 141-226 3.25e-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: 39.30  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 141 DIDDVLF--KFSLNLPDQQIPLVI---DHLHsALDGIMKPVTSGFGFIDLIIPGLH-----KANGISRLLKRWNLSPQNV 210
Cdd:cd01427    5 DLDGTLLavELLKRLRAAGIKLAIvtnRSRE-ALRALLEKLGLGDLFDGIIGSDGGgtpkpKPKPLLLLLLKLGVDPEEV 83

                         90
                 ....*....|....*.
gi 985629529 211 VAIGDSGNDAEMLKMA 226
Cdd:cd01427   84 LFVGDSENDIEAARAA 99
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 5-234 3.34e-04

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 41.35  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529   5 VIVTDMDGTFLD-DAKQYDRAR-FLAqyqELKKRDIEFVVASGNQYYQLIsffpQLKDEIS----FVAENGALVFehgkq 78
Cdd:COG3769    5 LVFTDLDGTLLDhDTYSWAAALpALA---RLKARGIPVILNTSKTAAEVE----PLRQELGlsdpFIVENGAAIF----- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529  79 LFHGELTRHESRIVIGEllkdkqlnfvacglqsayvsenapesfvglmskhYHRLKPVKDYQDIDDVL--------FKFS 150
Cdd:COG3769   73 IPKGYFAFPSGTADIDG----------------------------------YWVIELGKPYAEIRAVLeqlreelgFKFT 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 151 L--NLPDQQI---------------------PLVIDHLHSALD---------GIMkpVTSGFGFIdLIIPGLHKANGISR 198
Cdd:COG3769  119 GfgDMSAEEVaeltglsleqaalakqrefsePLLWLGSDEALErfiaalaalGLT--VLRGGRFL-HLMGGADKGKAVRW 195

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 985629529 199 LLKRWNLSPQN---VVAIGDSGNDAEMLKMAHYSFAMAN 234
Cdd:COG3769  196 LVEQYRQRFGKnvvTIALGDSPNDIPMLEAADIAVVIRS 234
serB PRK11133
phosphoserine phosphatase; Provisional
 186-226 6.01e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 40.70  E-value: 6.01e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 985629529 186 IIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMA 226
Cdd:PRK11133 243 IVDAQYKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAA 283
PRK15126 PRK15126
HMP-PP phosphatase;
178-241 6.38e-04

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 40.45  E-value: 6.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985629529 178 SGFGFIDLIIPGLHKANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAHYSFAMANAAESIKA 241
Cdd:PRK15126 175 SATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLRA 238
PTP_tensin-1 cd14560
protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin ...
 145-248 1.74e-03

protein tyrosine phosphatase-like domain of tensin-1; Tensin-1 (TNS1) is part of the tensin family of intracellular proteins (tensin-1, -2, -3 and -4), which act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility. It plays an essential role in TGF-beta-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. It also positively regulates RhoA activity through its interaction with DLC1, a RhoGAP-containing tumor suppressor; the tensin-1-DLC1-RhoA signaling axis is critical in regulating cellular functions that lead to angiogenesis. Tensin-1 contains an N-terminal region with a protein tyrosine phosphatase (PTP)-like domain followed by a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains.


Pssm-ID: 350408 [Multi-domain]  Cd Length: 159  Bit Score: 38.04  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 145 VLFKFSLNLPDqqiplvIDHLHS-ALDgimkpvtsgFGFIDLIIPGLHKANGISRLLKRW-NLSPQNVVAIGDSGNDAE- 221
Cdd:cd14560   43 LLFNLSERRHD------ISKLHPkVLD---------FGWPDLHAPALEKICSICKAMDTWlNADPHNVVVIHNKGNRGRt 107

                         90       100       110
                 ....*....|....*....|....*....|..
gi 985629529 222 ---MLKMAHYSFAMANAAESIK--AIARYQTD 248
Cdd:cd14560  108 gvvIAAYMHYSNISASADQALDrfAMKRFYED 139
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 192-227 2.08e-03

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 38.30  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 985629529 192 KANGISRLLKRWNLSPQNVVAIGDSGNDAEMLKMAH 227
Cdd:cd07500  138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAG 173
PLN02382 PLN02382
probable sucrose-phosphatase
 148-222 9.22e-03

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 37.27  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985629529 148 KFSLNLPDQQIPLVIDHLHSALD--GI-MKPVTSGFGFIDLIIPGLHKANGISRLLKRWNL---SPQNVVAIGDSGNDAE 221
Cdd:PLN02382 129 KVSFYVDKKKAQEVIKELSERLEkrGLdVKIIYSGGIDLDVLPQGAGKGQALAYLLKKLKAegkAPVNTLVCGDSGNDAE 208


                 .
gi 985629529 222 M 222
Cdd:PLN02382 209 L 209
 
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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