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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Bacillus]

Protein Classification

Cof-type HAD-IIB family hydrolase( domain architecture ID 11576297)

Cof-type HAD-IIB family hydrolase, part of the HAD (haloacid dehalogenase) family that includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-265 2.10e-92

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: 272.93  E-value: 2.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldskwgTHHS 85
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDP------TGKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRACFDFGVKNiyaEVMDDVYVREIDEDKKHIFEFGSPKIFTGDLLNTLNDHPT-----CLLIDAHDEHS 160
Cdd:cd07516    75 ILERLISKEDVKELEEFLRKL---GIGINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDeditkILFVGEDEELD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 161 SAIRQHLTDMHaevIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAI 240
Cdd:cd07516   152 ELIAKLPEEFF---DDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAI 228

                         250       260
                  ....*....|....*....|....*
gi 1104394684 241 PELKSLANHTTLTNEEDGIALYLEE 265
Cdd:cd07516   229 DEVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-265 2.10e-92

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: 272.93  E-value: 2.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldskwgTHHS 85
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDP------TGKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRACFDFGVKNiyaEVMDDVYVREIDEDKKHIFEFGSPKIFTGDLLNTLNDHPT-----CLLIDAHDEHS 160
Cdd:cd07516    75 ILERLISKEDVKELEEFLRKL---GIGINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDeditkILFVGEDEELD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 161 SAIRQHLTDMHaevIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAI 240
Cdd:cd07516   152 ELIAKLPEEFF---DDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAI 228

                         250       260
                  ....*....|....*....|....*
gi 1104394684 241 PELKSLANHTTLTNEEDGIALYLEE 265
Cdd:cd07516   229 DEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-263 4.93e-78

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 236.75  E-value: 4.93e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   7 IALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldSKWGTHHSP 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE--NGKILYSNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  87 LELATAQEIVRACFDFGVkNIYAEVMDDVYVREIDEDKKHIFEFGSPKIF---TGDLLNTLNDHPTCLLIDAHDEHSSAI 163
Cdd:pfam08282  79 ISKEAVKEIIEYLKENNL-EILLYTDDGVYILNDNELEKILKELNYTKSFvpeIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 164 RQHLTdmHAEVIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPEL 243
Cdd:pfam08282 158 EKELK--ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 1104394684 244 KSLANHTTLTNEEDGIALYL 263
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-265 2.72e-64

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: 199.21  E-value: 2.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   3 KQHLIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgT 82
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEV--L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  83 HHSPLELATAQEIVRACFDFGVkniyaevmddvyvreidedkkhifefgspkiftgdllntlndhptcllidahdehssa 162
Cdd:COG0561    79 YERPLDPEDVREILELLREHGL---------------------------------------------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 163 irqhltdmHAEVIDHrkWGAPWpiIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPE 242
Cdd:COG0561   101 --------HLQVVVR--SGPGF--LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|...
gi 1104394684 243 LKSLANHTTLTNEEDGIALYLEE 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEK 191
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-263 5.17e-63

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: 198.26  E-value: 5.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgTHHS 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI--LYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRACFDFGVkNIYAEVMDDVYVREIDEDKKHIFE--FGSPKIFTGDLLNTLNDHPTCLLIDAHDEHSSAI 163
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGL-DVILYGDDSIYASKNDPEYFTIFKkfLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 164 RQHLtdMHAEVIDHRKWGAPWP-IIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPE 242
Cdd:TIGR00099 158 IEAL--NKLELEENVSVVSSGPySIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1104394684 243 LKSLANHTTLTNEEDGIALYL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 6-264 1.71e-37

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 132.89  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTP----IVNfNGAYVHHpldskwg 81
Cdd:PRK10513    5 LIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdycITN-NGALVQK------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  82 thhspleLATAQEIVRACFDFGvKNIYAEVMD---DVYVREIDEDK-----KHIFEF--------GSPKIFTG--DLLNT 143
Cdd:PRK10513   77 -------AADGETVAQTALSYD-DYLYLEKLSrevGVHFHALDRNTlytanRDISYYtvhesfltGIPLVFREveKMDPN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 144 LNdHPTCLLIDAHDEHSSAI-------RQHLTDMHAevidhrkwgAPWpIIEIVKSGLNKAVGLQKISSHYNIPQERIIA 216
Cdd:PRK10513  149 LQ-FPKVMMIDEPEILDAAIaripaevKERYTVLKS---------APY-FLEILDKRVNKGTGVKSLAEHLGIKPEEVMA 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1104394684 217 FGDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTNEEDGIALYLE 264
Cdd:PRK10513  218 IGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-265 2.10e-92

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: 272.93  E-value: 2.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldskwgTHHS 85
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDP------TGKE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRACFDFGVKNiyaEVMDDVYVREIDEDKKHIFEFGSPKIFTGDLLNTLNDHPT-----CLLIDAHDEHS 160
Cdd:cd07516    75 ILERLISKEDVKELEEFLRKL---GIGINIYTNDDWADTIYEENEDDEIIKPAEILDDLLLPPDeditkILFVGEDEELD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 161 SAIRQHLTDMHaevIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAI 240
Cdd:cd07516   152 ELIAKLPEEFF---DDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAI 228

                         250       260
                  ....*....|....*....|....*
gi 1104394684 241 PELKSLANHTTLTNEEDGIALYLEE 265
Cdd:cd07516   229 DEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-263 4.93e-78

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 236.75  E-value: 4.93e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   7 IALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldSKWGTHHSP 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE--NGKILYSNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  87 LELATAQEIVRACFDFGVkNIYAEVMDDVYVREIDEDKKHIFEFGSPKIF---TGDLLNTLNDHPTCLLIDAHDEHSSAI 163
Cdd:pfam08282  79 ISKEAVKEIIEYLKENNL-EILLYTDDGVYILNDNELEKILKELNYTKSFvpeIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 164 RQHLTdmHAEVIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPEL 243
Cdd:pfam08282 158 EKELK--ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV 235

                         250       260
                  ....*....|....*....|
gi 1104394684 244 KSLANHTTLTNEEDGIALYL 263
Cdd:pfam08282 236 KAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-265 2.72e-64

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: 199.21  E-value: 2.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   3 KQHLIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgT 82
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEV--L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  83 HHSPLELATAQEIVRACFDFGVkniyaevmddvyvreidedkkhifefgspkiftgdllntlndhptcllidahdehssa 162
Cdd:COG0561    79 YERPLDPEDVREILELLREHGL---------------------------------------------------------- 100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 163 irqhltdmHAEVIDHrkWGAPWpiIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPE 242
Cdd:COG0561   101 --------HLQVVVR--SGPGF--LEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|...
gi 1104394684 243 LKSLANHTTLTNEEDGIALYLEE 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEK 191
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-263 5.17e-63

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: 198.26  E-value: 5.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgTHHS 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEI--LYKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRACFDFGVkNIYAEVMDDVYVREIDEDKKHIFE--FGSPKIFTGDLLNTLNDHPTCLLIDAHDEHSSAI 163
Cdd:TIGR00099  79 PLDLDLVEEILNFLKKHGL-DVILYGDDSIYASKNDPEYFTIFKkfLGEPKLEVVDIQYLPDDILKILLLFLDPEDLDLL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 164 RQHLtdMHAEVIDHRKWGAPWP-IIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPE 242
Cdd:TIGR00099 158 IEAL--NKLELEENVSVVSSGPySIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1104394684 243 LKSLANHTTLTNEEDGIALYL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 9-265 2.02e-38

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: 133.89  E-value: 2.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   9 LDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTpIVNFNGAYVHhpldskwgthhsple 88
Cdd:cd07517     5 FDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVF--------------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  89 lataqeivracfdFGVKNIYAEVMDDVYVREIdedKKHIFEFGSPKIFTGDLLNTLNDHPTCLLIDAHDEHssairqHLT 168
Cdd:cd07517    69 -------------FEGEVIYKNPLPQELVERL---TEFAKEQGHPVSFYGQLLLFEDEEEEQKYEELRPEL------RFV 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 169 DMHAEVIDhrkwgapwpiieIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELKSLAN 248
Cdd:cd07517   127 RWHPLSTD------------VIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIAD 194

                         250
                  ....*....|....*..
gi 1104394684 249 HTTLTNEEDGIALYLEE 265
Cdd:cd07517   195 YVTKDVDEDGILKALKH 211
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 6-264 1.71e-37

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 132.89  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTP----IVNfNGAYVHHpldskwg 81
Cdd:PRK10513    5 LIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPgdycITN-NGALVQK------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  82 thhspleLATAQEIVRACFDFGvKNIYAEVMD---DVYVREIDEDK-----KHIFEF--------GSPKIFTG--DLLNT 143
Cdd:PRK10513   77 -------AADGETVAQTALSYD-DYLYLEKLSrevGVHFHALDRNTlytanRDISYYtvhesfltGIPLVFREveKMDPN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 144 LNdHPTCLLIDAHDEHSSAI-------RQHLTDMHAevidhrkwgAPWpIIEIVKSGLNKAVGLQKISSHYNIPQERIIA 216
Cdd:PRK10513  149 LQ-FPKVMMIDEPEILDAAIaripaevKERYTVLKS---------APY-FLEILDKRVNKGTGVKSLAEHLGIKPEEVMA 217

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1104394684 217 FGDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTNEEDGIALYLE 264
Cdd:PRK10513  218 IGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIE 265
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 6-260 4.82e-25

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 100.10  E-value: 4.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgTHHS 85
Cdd:PRK10530    5 VIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKK--VLEA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 -PLELATAQEIVRACFDFGVKNIyaevmddVYVreideDKKHIFEFGspkifTGDLLNTLN--------DHPTCL----L 152
Cdd:PRK10530   83 dPLPVQQALQVIEMLDEHQIHGL-------MYV-----DDAMLYEHP-----TGHVIRTLNwaqtlppeQRPTFTqvdsL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 153 IDA------------HDEHSSAIRQHLTDMHAEVIDHRKWGapW-PIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGD 219
Cdd:PRK10530  146 AQAarqvnaiwkfalTHEDLPQLQHFAKHVEHELGLECEWS--WhDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGD 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1104394684 220 EDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTNEEDGIA 260
Cdd:PRK10530  224 NFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIA 264
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 6-264 8.43e-25

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 97.27  E-value: 8.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKI-ISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVhhpldskwgthh 84
Cdd:cd07518     2 LIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV------------ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  85 splelataqeivracfdfgvkniyaevmddvyvreidedkkhIFEFgspkiftgdllnTLNDHPtclliDAHDEHSSAIR 164
Cdd:cd07518    70 ------------------------------------------YFKF------------TLNVPD-----EAAPDIIDELN 90

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 165 QHLTDMHAEVIDHRKWgapwpiIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELK 244
Cdd:cd07518    91 QKFGGILRAVTSGFGS------IDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVK 164

                         250       260
                  ....*....|....*....|
gi 1104394684 245 SLANHTTLTNEEDGIALYLE 264
Cdd:cd07518   165 AAAKYVAPSNNENGVLQVIE 184
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 6-236 6.00e-24

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: 95.91  E-value: 6.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKI-ISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKWGTHh 84
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHeLSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  85 spleLATAQEIvrACFDFGVKNIYAEVMDDVYVREIDEDKKHIFEFgspkIFTGDLLNTLNDHptcLLIDAHDEHSSAIR 164
Cdd:TIGR01484  80 ----SDVFEEI--LGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAI----HYVGAELGQELDS---KMRERLEKIGRNDL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1104394684 165 QHLTDMHAEVIdhrkwgapwpiIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAM 236
Cdd:TIGR01484 147 ELEAIYSGKTD-----------LEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-251 1.35e-17

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: 79.04  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   7 IALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPldskwgthhsp 86
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISYN----------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  87 lelataqeivracfdFGVKNIYAEVMDDVYVREIDEDKKHIFEFGSPKIFTGDLLNTLNDHptcllIDAhdEHSSAIRQH 166
Cdd:TIGR01482  70 ---------------EGLDDIFLAYLEEEWFLDIVIAKTFPFSRLKVQYPRRASLVKMRYG-----IDV--DTVREIIKE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 167 LTdmhaEVIDHRKWGAPWpiiEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELKSL 246
Cdd:TIGR01482 128 LG----LNLVAVDSGFDI---HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEW 200


                  ....*
gi 1104394684 247 ANHTT 251
Cdd:TIGR01482 201 ADYVT 205
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 6-260 9.03e-16

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 74.24  E-value: 9.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKwgthhs 85
Cdd:PRK01158    5 AIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGGVISVGFDGK------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 PLELATAQEIVRAcFDFgVKNIYAEVMDDVYVREIDEDKKHI-FEFGSPKIFTGDLLNTLNdhptcLLIDAHDehsSAIR 164
Cdd:PRK01158   79 RIFLGDIEECEKA-YSE-LKKRFPEASTSLTKLDPDYRKTEVaLRRTVPVEEVRELLEELG-----LDLEIVD---SGFA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 165 QHLTDmhaevidhrkwgaPWpiieivksgLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELK 244
Cdd:PRK01158  149 IHIKS-------------PG---------VNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELK 206

                         250
                  ....*....|....*.
gi 1104394684 245 SLANHTTLTNEEDGIA 260
Cdd:PRK01158  207 EAADYVTEKSYGEGVA 222
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 6-251 1.75e-15

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: 73.24  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVhhpldskwgthhs 85
Cdd:TIGR01487   3 LVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVI------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 plelataqeivracFDFGVKNIYAEVMDDVYVREIDEdkkhifefgspKIFTGDLLNtlNDHP-TCLLIDAHDEHSSAIR 164
Cdd:TIGR01487  70 --------------FYNKEDIFLANMEEEWFLDEEKK-----------KRFPRDRLS--NEYPrASLVIMREGKDVDEVR 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 165 QHLTDMHAEVIDHRKwgapwpIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELK 244
Cdd:TIGR01487 123 EIIKERGLNLVASGF------AIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLK 196


                  ....*..
gi 1104394684 245 SLANHTT 251
Cdd:TIGR01487 197 EIADYVT 203
PRK15126 PRK15126
HMP-PP phosphatase;
6-263 2.83e-14

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 70.88  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDskwgthhs 85
Cdd:PRK15126    4 LAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEG-------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  86 plELATAQEIVracfdfgvkniyAEVMDDVYVREIDEDkkhifefGSPKIFTGDLLNTLNDHPTclLIDAHdeHSSAIRQ 165
Cdd:PRK15126   76 --ELLHRQDLP------------ADVAELVLHQQWDTR-------ASMHVFNDDGWFTGKEIPA--LLQAH--VYSGFRY 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 166 HLTDM----------------HAEVIDHR-----KWGAPWPI-------IEIVKSGLNKAVGLQKISSHYNIPQERIIAF 217
Cdd:PRK15126  131 QLIDLkrlpahgvtkicfcgdHDDLTRLQiqlneALGERAHLcfsatdcLEVLPVGCNKGAALAVLSQHLGLSLADCMAF 210

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1104394684 218 GDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTN--EEDGIALYL 263
Cdd:PRK15126  211 GDAMNDREMLGSVGRGFIMGNAMPQLRAELPHLPVIGhcRNQAVSHYL 258
PLN02887 PLN02887
hydrolase family protein
 7-260 4.38e-12

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 65.67  E-value: 4.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   7 IALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLN---------TPIVNFNGAYVH---- 73
Cdd:PLN02887  311 IFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYgrqg 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  74 -----HPLDSK---------WgTHHSPLeLATAQEIVRACFDFGVkniyAEVMDDVYvreiDEDKKHIFefgsPKIftgD 139
Cdd:PLN02887  391 reiyrSNLDQEvcreaclysL-EHKIPL-IAFSQDRCLTLFDHPL----VDSLHTIY----HEPKAEIM----SSV---D 453

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 140 LLNTLNDHPTCLLIDAHDEHSSAIRQH---LTDMHAEVIDhrkwgAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIA 216
Cdd:PLN02887  454 QLLAAADIQKVIFLDTAEGVSSVLRPYwseATGDRANVVQ-----AQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMA 528

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1104394684 217 FGDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTNEEDGIA 260
Cdd:PLN02887  529 IGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVA 572
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 193-267 9.27e-12

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: 61.07  E-value: 9.27e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1104394684 193 GLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTTLTNEEDGIALYLEEVL 267
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-265 2.05e-11

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


Pssm-ID: 319792 [Multi-domain]  Cd Length: 245  Bit Score: 62.37  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTR---TKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTP--IVNFNGAYVHHPLDSKW 80
Cdd:cd02605     1 LLVSDLDETLVGHDTNLQALerlQDLLEQLTADNDVILVYATGRSPESVLELIKEVMLPKPdfIISDVGTEIYYGESGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  81 GTHHSplelataqeivracfdfgvkniYAEVMDDVYVREIDEDKKHIFEFGSPKiftgdllNTLNDHPTCLLIDAHDEHS 160
Cdd:cd02605    81 EPDTY----------------------WNEVLSEGWERFLFEAIADLFKQLKPQ-------SELEQNPHKISFYLDPQND 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 161 SAIRQHLTDMHaevidhRKWGAPWPII---------EIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAG 231
Cdd:cd02605   132 AAVIEQLEEML------LKAGLTVRIIyssglaydlDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGT 205

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1104394684 232 HGIAMGNAIPELKSLANHTTLT-----NEEDGIALYLEE 265
Cdd:cd02605   206 RGVIVGNAQPELLKWADRVTRSrlakgPYAGGILEGLAH 244
PRK10976 PRK10976
putative hydrolase; Provisional
 5-265 7.57e-11

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 60.83  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   5 HLIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTPIVNFNGAYVHHPLDSKWGTHH 84
Cdd:PRK10976    3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFSHN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  85 splelaTAQEIVRACFdfGVKNIYAEVMDDVYV-------REIDEDKKHIFEFGSP-KIFTGDLLNTlndHPTCLLIDAH 156
Cdd:PRK10976   83 ------LDRDIASDLF--GVVHDNPDIITNVYRddewfmnRHRPEEMRFFKEAVFKyQLYEPGLLEP---DGVSKVFFTC 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 157 DEHssairQHLTDMHaEVIDHRkWGAPWPI-------IEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEF 229
Cdd:PRK10976  152 DSH-----EKLLPLE-QAINAR-WGDRVNVsfstltcLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSM 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1104394684 230 AGHGIAMGNAIPELKSLanHTTL----TNEEDGIALYLEE 265
Cdd:PRK10976  225 AGKGCIMGNAHQRLKDL--LPELevigSNADDAVPHYLRK 262
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-256 1.07e-07

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 51.87  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   1 MNKQHLIALDLDGTLLTDNKIISTRTKHTIAKAKEQGhIVVISTGRPFRASFDYY-KELGLNTP-IVNfNGAYVHHPlds 78
Cdd:PRK00192    1 DMMKLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKG-IPVIPCTSKTAAEVEVLrKELGLEDPfIVE-NGAAIYIP--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  79 kwgTHHSPLELATAqeivRACFDFGVKniyaevmddvyvreidedkkhifEFGSPKIFTGDLLntlndhptcllidahDE 158
Cdd:PRK00192   76 ---KNYFPFQPDGE----RLKGDYWVI-----------------------ELGPPYEELREIL---------------DE 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 159 HSSAIRQHLT---DMHAEVIDH--------------RKWGAP--WP--------IIEIVKS-GLN--------------- 195
Cdd:PRK00192  111 ISDELGYPLKgfgDLSAEEVAEltglsgesarlakdREFSEPflWNgseaakerFEEALKRlGLKvtrggrflhllgggd 190

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1104394684 196 KAVGLQKISSHYNIPQER-IIAFGDEDNDFEMIEFAGHGIAMGNA----IPELKSLAN-HTTLTNEE 256
Cdd:PRK00192  191 KGKAVRWLKELYRRQDGVeTIALGDSPNDLPMLEAADIAVVVPGPdgpnPPLLPGIADgEFILASAP 257
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 196-247 2.75e-07

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 49.84  E-value: 2.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1104394684 196 KAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMgNAIPELKSLA 247
Cdd:COG0560   156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAA 206
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 6-243 1.45e-06

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: 48.03  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLT-DNKiiSTRTKHTIAKAKEQGHIVVISTGRPFRASFDYYKELGLNTP--IVNFNGAYVHHP----LDS 78
Cdd:pfam05116   4 LLVSDLDNTLVDgDNE--ALARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPTPdyLITSVGTEIYYGpslvPDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  79 KWgthhsplelataQEIVRACFDfgvKNIYAEVMDDVYVREIDEDKKhifefgspkiftgdllntLNDHPTCLLIDAHDE 158
Cdd:pfam05116  82 SW------------QEHLDYHWD---RQAVVEALAKFPGLTLQPEEE------------------QRPHKVSYFLDPEAA 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 159 HSS--AIRQHL--TDMHAEVIdhRKWGApwpIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGI 234
Cdd:pfam05116 129 AAVlaELEQLLrkRGLDVKVI--YSSGR---DLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGV 203


                  ....*....
gi 1104394684 235 AMGNAIPEL 243
Cdd:pfam05116 204 VVGNAQPEL 212
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 188-235 2.13e-05

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: 44.08  E-value: 2.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1104394684 188 EIVkSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIA 235
Cdd:cd07500   131 PIV-DAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 6-247 8.38e-05

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. 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: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 42.66  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLT-----DNKIISTRTKHTIAK-AKEQGHIVVISTGRPFRASFDYYKELGLntPIVNFNGAYVHHPLDSK 79
Cdd:cd01627     1 LLFLDYDGTLAPivpdpDAAVPSPELLEALKKlAADPKNAVAIVSGRDLDDLDKWLGLPGI--GLAGEHGAEIRLPGGGE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684  80 WgTHHSPLELATAQEIVRACFdfgvkNIYAEVMDDVYVreidEDKKHIFEFgspkiftgdllntlndHptclLIDAHDEH 159
Cdd:cd01627    79 W-VTLAPKADLEWKEEVEAIF-----KYFTERTPGSLV----EDKGASLAW----------------H----YRNADPEG 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684 160 SSAIRQHLTDMHAEVIDHRKWGAPWPIIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNA 239
Cdd:cd01627   129 ARAALELALHLASDLLKALEVVPGKKVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRALNGEGGFSVK 208


                  ....*...
gi 1104394684 240 IPELKSLA 247
Cdd:cd01627   209 VGEGPTAA 216
serB PRK11133
phosphoserine phosphatase; Provisional
 196-235 2.17e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 41.86  E-value: 2.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1104394684 196 KAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIA 235
Cdd:PRK11133  249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 186-251 6.19e-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: 39.04  E-value: 6.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1104394684 186 IIEIVKSGLNKAVGLQKISSHYNIPQERIIAFGDEDNDFEMIEFAGHGIAMGNAIPELKSLANHTT 251
Cdd:cd01630    67 IEDLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 6-98 7.53e-04

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


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 40.08  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104394684   6 LIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTGRPfRASFDYY-KELGLNTPIVNFNGAYVHhpLDSKWGTHH 84
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKT-AAEVEYLrKELGLEDPFIVENGGAIY--GPRGWRPEP 77

                          90
                  ....*....|....*.
gi 1104394684  85 SP--LELATAQEIVRA 98
Cdd:TIGR01486  78 EYpvIALGIPYEKIRA 93
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-54 4.26e-03

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 37.62  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1104394684   1 MNKQHLIALDLDGTLLTDNKIISTRTKHTIAKAKEQGHIVVISTG-----------RPFRASFDY 54
Cdd:PTZ00174    2 EMKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGsdypkikeqlgEDVLEDFDY 66
 
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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