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Conserved domains on  [gi|1176233983|gb|OQY43006|]
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hypothetical protein B6227_00380 [Fusobacteriia bacterium 4572_74]

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 ...
 7-258 4.77e-77

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: 233.64  E-value: 4.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE--KEYPVKE 84
Cdd:cd07516     4 LDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEilERLISKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  85 KsLKILIEIAREYKTHLNIYQHEIW----YSENItNKETEIYKDISGLEPVKKDFDrldemfSTKVLYIGEHENLLKIEK 160
Cdd:cd07516    84 D-VKELEEFLRKLGIGINIYTNDDWadtiYEENE-DDEIIKPAEILDDLLLPPDED------ITKILFVGEDEELDELIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 161 DIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVA 240
Cdd:cd07516   156 KLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAA 235

                         250
                  ....*....|....*...
gi 1176233983 241 DHVTISNNESGVGEFLKK 258
Cdd:cd07516   236 DYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-258 4.77e-77

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: 233.64  E-value: 4.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE--KEYPVKE 84
Cdd:cd07516     4 LDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEilERLISKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  85 KsLKILIEIAREYKTHLNIYQHEIW----YSENItNKETEIYKDISGLEPVKKDFDrldemfSTKVLYIGEHENLLKIEK 160
Cdd:cd07516    84 D-VKELEEFLRKLGIGINIYTNDDWadtiYEENE-DDEIIKPAEILDDLLLPPDED------ITKILFVGEDEELDELIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 161 DIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVA 240
Cdd:cd07516   156 KLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAA 235

                         250
                  ....*....|....*...
gi 1176233983 241 DHVTISNNESGVGEFLKK 258
Cdd:cd07516   236 DYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-256 1.01e-76

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 232.90  E-value: 1.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KEYPVKEK 85
Cdd:pfam08282   3 SDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKIlYSNPISKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  86 SLKILIEIAREYKTHLNIYQHEIWYSENITNKETEI--YKDISGLEPVKKDFDRLDEMFSTKVLYIGEHENLLKIEKDIK 163
Cdd:pfam08282  83 AVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILkeLNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDELEKELK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 164 DRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHV 243
Cdd:pfam08282 163 ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYV 242

                         250
                  ....*....|...
gi 1176233983 244 TISNNESGVGEFL 256
Cdd:pfam08282 243 TDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 7-256 6.38e-66

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: 205.58  E-value: 6.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KEYPVKEK 85
Cdd:TIGR00099   4 IDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEIlYKKPLDLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  86 SLKILIEIAREYKTHLNIYQHEIWYSENITNKETEIYKDISGLEPVKKDFDRLDEMF-STKVLYIGEHENLLKIEKDIKD 164
Cdd:TIGR00099  84 LVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDiLKILLLFLDPEDLDLLIEALNK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 165 -RLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHV 243
Cdd:TIGR00099 164 lELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYV 243

                         250
                  ....*....|...
gi 1176233983 244 TISNNESGVGEFL 256
Cdd:TIGR00099 244 TDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-259 1.70e-65

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: 202.29  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KE 79
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVlYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  80 YPVKEKSLKILIEIAREYKTHLNIYqheiwysenitnketeiykdisglepvkkdfdrldemfstkvlyigehenllkie 159
Cdd:COG0561    81 RPLDPEDVREILELLREHGLHLQVV------------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 160 kdikdrlgdgihtTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQV 239
Cdd:COG0561   106 -------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAA 172

                         250       260
                  ....*....|....*....|
gi 1176233983 240 ADHVTISNNESGVGEFLKKY 259
Cdd:COG0561   173 ADYVTGSNDEDGVAEALEKL 192
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-259 3.45e-43

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 147.53  E-value: 3.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   2 IKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPA---ICYNGAKIIHHNGSE- 77
Cdd:PRK10513    3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGdycITNNGALVQKAADGEt 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  78 -KEYPVKEKSLKILIEIAREYKTHLNIYQHEIWYSENitnketeiyKDISGLE---------PVKkdFDRLDEMFST--- 144
Cdd:PRK10513   83 vAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYTAN---------RDISYYTvhesfltgiPLV--FREVEKMDPNlqf 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 145 -KVLYIGEHENL----LKIEKDIKDRlgdgiHTTF-SKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKE 218
Cdd:PRK10513  152 pKVMMIDEPEILdaaiARIPAEVKER-----YTVLkSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIA 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1176233983 219 MLETAGVGVAMDGAFEELKQVADHVTISNNESGVGEFLKKY 259
Cdd:PRK10513  227 MIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 7-258 4.77e-77

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: 233.64  E-value: 4.77e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE--KEYPVKE 84
Cdd:cd07516     4 LDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEilERLISKE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  85 KsLKILIEIAREYKTHLNIYQHEIW----YSENItNKETEIYKDISGLEPVKKDFDrldemfSTKVLYIGEHENLLKIEK 160
Cdd:cd07516    84 D-VKELEEFLRKLGIGINIYTNDDWadtiYEENE-DDEIIKPAEILDDLLLPPDED------ITKILFVGEDEELDELIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 161 DIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVA 240
Cdd:cd07516   156 KLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAA 235

                         250
                  ....*....|....*...
gi 1176233983 241 DHVTISNNESGVGEFLKK 258
Cdd:cd07516   236 DYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-256 1.01e-76

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 232.90  E-value: 1.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KEYPVKEK 85
Cdd:pfam08282   3 SDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKIlYSNPISKE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  86 SLKILIEIAREYKTHLNIYQHEIWYSENITNKETEI--YKDISGLEPVKKDFDRLDEMFSTKVLYIGEHENLLKIEKDIK 163
Cdd:pfam08282  83 AVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILkeLNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDELEKELK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 164 DRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHV 243
Cdd:pfam08282 163 ELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYV 242

                         250
                  ....*....|...
gi 1176233983 244 TISNNESGVGEFL 256
Cdd:pfam08282 243 TDSNNEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 7-256 6.38e-66

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: 205.58  E-value: 6.38e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KEYPVKEK 85
Cdd:TIGR00099   4 IDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEIlYKKPLDLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  86 SLKILIEIAREYKTHLNIYQHEIWYSENITNKETEIYKDISGLEPVKKDFDRLDEMF-STKVLYIGEHENLLKIEKDIKD 164
Cdd:TIGR00099  84 LVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDiLKILLLFLDPEDLDLLIEALNK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 165 -RLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHV 243
Cdd:TIGR00099 164 lELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYV 243

                         250
                  ....*....|...
gi 1176233983 244 TISNNESGVGEFL 256
Cdd:TIGR00099 244 TDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-259 1.70e-65

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: 202.29  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSE-KE 79
Cdd:COG0561     1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVlYE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  80 YPVKEKSLKILIEIAREYKTHLNIYqheiwysenitnketeiykdisglepvkkdfdrldemfstkvlyigehenllkie 159
Cdd:COG0561    81 RPLDPEDVREILELLREHGLHLQVV------------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 160 kdikdrlgdgihtTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQV 239
Cdd:COG0561   106 -------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAA 172

                         250       260
                  ....*....|....*....|
gi 1176233983 240 ADHVTISNNESGVGEFLKKY 259
Cdd:COG0561   173 ADYVTGSNDEDGVAEALEKL 192
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 2-259 3.45e-43

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 147.53  E-value: 3.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   2 IKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPA---ICYNGAKIIHHNGSE- 77
Cdd:PRK10513    3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGdycITNNGALVQKAADGEt 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  78 -KEYPVKEKSLKILIEIAREYKTHLNIYQHEIWYSENitnketeiyKDISGLE---------PVKkdFDRLDEMFST--- 144
Cdd:PRK10513   83 vAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYTAN---------RDISYYTvhesfltgiPLV--FREVEKMDPNlqf 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 145 -KVLYIGEHENL----LKIEKDIKDRlgdgiHTTF-SKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKE 218
Cdd:PRK10513  152 pKVMMIDEPEILdaaiARIPAEVKER-----YTVLkSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIA 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1176233983 219 MLETAGVGVAMDGAFEELKQVADHVTISNNESGVGEFLKKY 259
Cdd:PRK10513  227 MIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 3-259 4.47e-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: 132.73  E-value: 4.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   3 KAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTpAICYNGAKIIHHNGSEKEYPV 82
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFFEGEVIYKNPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  83 KEKSLKILIEIAREYkthlniyQHEIWYSENITNKETEIYKDisglepvkkdfdrldemfstkvLYIGEHENLlkiekdi 162
Cdd:cd07517    80 PQELVERLTEFAKEQ-------GHPVSFYGQLLLFEDEEEEQ----------------------KYEELRPEL------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 163 kdrlgdgiHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADH 242
Cdd:cd07517   124 --------RFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADY 195

                         250
                  ....*....|....*..
gi 1176233983 243 VTISNNESGVGEFLKKY 259
Cdd:cd07517   196 VTKDVDEDGILKALKHF 212
PRK10976 PRK10976
putative hydrolase; Provisional
 1-258 1.39e-31

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 117.07  E-value: 1.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIihHNGSEKey 80
Cdd:PRK10976    1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARV--HDTDGN-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  81 pvkekslkiLI-------EIARE------YKTHL--NIYQHEIWYSENITNKETEIYK----DISGLEPvkkdfDRLDEM 141
Cdd:PRK10976   77 ---------LIfshnldrDIASDlfgvvhDNPDIitNVYRDDEWFMNRHRPEEMRFFKeavfKYQLYEP-----GLLEPD 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 142 FSTKVLYIGE-HENLLKIEKDIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEML 220
Cdd:PRK10976  143 GVSKVFFTCDsHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEML 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1176233983 221 ETAGVGVAMDGAFEELKQVADHVTI--SNNESGVGEFLKK 258
Cdd:PRK10976  223 SMAGKGCIMGNAHQRLKDLLPELEVigSNADDAVPHYLRK 262
PRK15126 PRK15126
HMP-PP phosphatase;
1-260 1.04e-28

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 109.78  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSEKEy 80
Cdd:PRK15126    1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLH- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  81 pvkekSLKILIEIARE-YKTH------LNIYQHEIWYSEnitnketeiyKDI---------SGLEPVKKDFDRLDEMFST 144
Cdd:PRK15126   80 -----RQDLPADVAELvLHQQwdtrasMHVFNDDGWFTG----------KEIpallqahvySGFRYQLIDLKRLPAHGVT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 145 KVLYIGEHENLLKIEKDIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAG 224
Cdd:PRK15126  145 KICFCGDHDDLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVG 224

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1176233983 225 VGVAMDGAFEELKQVADHVTISNN--ESGVGEFLKKYL 260
Cdd:PRK15126  225 RGFIMGNAMPQLRAELPHLPVIGHcrNQAVSHYLTHWL 262
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-260 9.37e-28

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 106.21  E-value: 9.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAkIIHHNGSEKEY 80
Cdd:PRK01158    2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIGTSGPVIAENGG-VISVGFDGKRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  81 PVKEKSlkilieiareykthlniyqheiwysenitnKETEIYKDISGLEPVKK-DFDRLDEMFSTKVLYIGEHENLLKIE 159
Cdd:PRK01158   81 FLGDIE------------------------------ECEKAYSELKKRFPEAStSLTKLDPDYRKTEVALRRTVPVEEVR 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 160 KDIKDrLGDGIHTTFSKpFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQV 239
Cdd:PRK01158  131 ELLEE-LGLDLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEA 208

                         250       260
                  ....*....|....*....|.
gi 1176233983 240 ADHVTISNNESGVGEFLKKYL 260
Cdd:PRK01158  209 ADYVTEKSYGEGVAEAIEHLL 229
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-229 1.60e-27

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: 105.16  E-value: 1.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   4 AVMLDLDGTLLD-NLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIihHNGSEKEYPV 82
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALI--FYPGEILYIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  83 KEKSLKILIEIAREYKTHLNIYQHEIWYSENITNKETEIYKDISGLEPvkkdfdrldemfstkvlyigEHENLLKIEKDI 162
Cdd:TIGR01484  79 PSDVFEEILGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHYVGAEL--------------------GQELDSKMRERL 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176233983 163 K--DRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAM 229
Cdd:TIGR01484 139 EkiGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 7-260 2.08e-27

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 106.26  E-value: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   7 LDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGA--------KIIHHNgsek 78
Cdd:PRK10530    8 LDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTylydyqakKVLEAD---- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  79 eyPVKEKSLKILIEIAREYKTH-------LNIYQHE-------IWYSENITNKETEIYKDISGLEPVKKDFDRLDEmFST 144
Cdd:PRK10530   84 --PLPVQQALQVIEMLDEHQIHglmyvddAMLYEHPtghvirtLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWK-FAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 145 KvlyigeHENLLK-------IEKDIkdrlgdGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDK 217
Cdd:PRK10530  161 T------HEDLPQlqhfakhVEHEL------GLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDI 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1176233983 218 EMLETAGVGVAMDGAFEELKQVADHVTISNNESGVGEFLKKYL 260
Cdd:PRK10530  229 SMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHV 271
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 3-252 8.96e-27

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: 102.28  E-value: 8.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   3 KAVMLDLDGTLLDNLHK-ISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEElnlttpaicyngakiihhngsekeyp 81
Cdd:cd07518     1 KLIATDMDGTFLNDDKTyDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPE-------------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  82 vkekslkilieiareykthlniYQHEIWY-SENitnkETEIYKDISGLEPVKKDFDrldemfstkvlyigehenllkIEK 160
Cdd:cd07518    55 ----------------------IKDEMSFvAEN----GAVVYFKFTLNVPDEAAPD---------------------IID 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 161 DIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVA 240
Cdd:cd07518    88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAA 167

                         250
                  ....*....|..
gi 1176233983 241 DHVTISNNESGV 252
Cdd:cd07518   168 KYVAPSNNENGV 179
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-251 9.39e-21

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: 87.79  E-value: 9.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   5 VMLDLDGTLLDNLHKISDTN--KEILKKL-EDKGIKIFLATGRSYESMRSYHEELNLTTPAIcyngakIIHHNGSEkeyp 81
Cdd:cd02605     2 LVSDLDETLVGHDTNLQALErlQDLLEQLtADNDVILVYATGRSPESVLELIKEVMLPKPDF------IISDVGTE---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  82 vkekslkILieiareYKTHLNIYQHEIWYSENITNKETEIYKDISGLEPVKKdFDRLDEMFSTKVLYIGEHENLLKIEKD 161
Cdd:cd02605    72 -------IY------YGESGYLEPDTYWNEVLSEGWERFLFEAIADLFKQLK-PQSELEQNPHKISFYLDPQNDAAVIEQ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 162 IKDRLGD-GIHTTFS----KPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEEL 236
Cdd:cd02605   138 LEEMLLKaGLTVRIIyssgLAYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPEL 217

                         250
                  ....*....|....*
gi 1176233983 237 KQVADHVTISNNESG 251
Cdd:cd02605   218 LKWADRVTRSRLAKG 232
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-258 7.12e-20

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: 85.21  E-value: 7.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   5 VMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSEKEYPVKE 84
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISYNEGLDDIFLAYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  85 KSlkilieiareyKTHLNIYQHEIWYSENITNK---ETEIYKDISGLEPvkkdfdrldemfstkvlyigehENLLKIEKD 161
Cdd:TIGR01482  81 EE-----------EWFLDIVIAKTFPFSRLKVQyprRASLVKMRYGIDV----------------------DTVREIIKE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 162 IKDRLgdgihTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVAD 241
Cdd:TIGR01482 128 LGLNL-----VAVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWAD 202

                         250       260
                  ....*....|....*....|.
gi 1176233983 242 HVTIS----NNESGVGEFLKK 258
Cdd:TIGR01482 203 YVTESpygeGGAEAIGEILQA 223
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 2-256 4.79e-19

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: 82.87  E-value: 4.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   2 IKAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAkIIHHNGSEKEYP 81
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGG-VIFYNKEDIFLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  82 VKEKSlkilieiareykthlniyqheiWYSENITNKETEIykdisglepvkkdfDRLDEMFSTKVLYI-GEHENLLKIEK 160
Cdd:TIGR01487  80 NMEEE----------------------WFLDEEKKKRFPR--------------DRLSNEYPRASLVImREGKDVDEVRE 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 161 DIKDRlgdGIHTTFSKpFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVA 240
Cdd:TIGR01487 124 IIKER---GLNLVASG-FAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIA 199

                         250
                  ....*....|....*.
gi 1176233983 241 DHVTISNNESGVGEFL 256
Cdd:TIGR01487 200 DYVTSNPYGEGVVEVL 215
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-227 9.46e-19

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 83.07  E-value: 9.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   1 MIKAVMLDLDGTLLDNlHKISDTN-KEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKI-IHHNG--- 75
Cdd:PRK00192    3 MKLLVFTDLDGTLLDH-HTYSYEPaKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIyIPKNYfpf 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  76 ------SEKEYPVKEKSLK------ILIEIAREYKTHLNIYqheiwysENITNKETEiykDISGLEP--VKKDFDRldeM 141
Cdd:PRK00192   82 qpdgerLKGDYWVIELGPPyeelreILDEISDELGYPLKGF-------GDLSAEEVA---ELTGLSGesARLAKDR---E 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 142 FSTKVLYIGEHENLLKIEKDIKDRlgdGIHTT----FSKpffleiLDRNVNKGTAMKNIMEE-ENISLSQVIAFGDGLND 216
Cdd:PRK00192  149 FSEPFLWNGSEAAKERFEEALKRL---GLKVTrggrFLH------LLGGGDKGKAVRWLKELyRRQDGVETIALGDSPND 219

                         250
                  ....*....|.
gi 1176233983 217 KEMLETAGVGV 227
Cdd:PRK00192  220 LPMLEAADIAV 230
PLN02887 PLN02887
hydrolase family protein
 3-259 1.90e-18

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 84.16  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   3 KAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLT---------TPAICYNGAKIIHH 73
Cdd:PLN02887  309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYGR 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  74 NGSEkeypVKEKSLKIliEIAREykTHLNIYQHEI------------WYSENITNKETEIYKdisglEPVKKDFDRLDEM 141
Cdd:PLN02887  389 QGRE----IYRSNLDQ--EVCRE--ACLYSLEHKIpliafsqdrcltLFDHPLVDSLHTIYH-----EPKAEIMSSVDQL 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 142 FST----KVLYIGEHENL-LKIEKDIKDRLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLND 216
Cdd:PLN02887  456 LAAadiqKVIFLDTAEGVsSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGEND 535

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1176233983 217 KEMLETAGVGVAMDGAFEELKQVADHVTISNNESGVGEFLKKY 259
Cdd:PLN02887  536 IEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 174-260 2.11e-15

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: 71.08  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 174 FSKPFFLEilDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHVTISNNESGVG 253
Cdd:cd07514    55 LSGPVVAE--NGGVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVL 132


                  ....*..
gi 1176233983 254 EFLKKYL 260
Cdd:cd07514   133 EAIDKLL 139
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 5-232 2.88e-14

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: 70.51  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   5 VMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGS--EKEYPV 82
Cdd:TIGR01486   2 IFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIYGPRGWrpEPEYPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  83 KE--KSLKI----LIEIAREYKTHLNIYqheiwysENITNKETEiykDISGLEPVKKDFDRLDEMFSTKVLYIGEHENLL 156
Cdd:TIGR01486  82 IAlgIPYEKirarLRELSEELGFKFRGL-------GDLTDEEIA---ELTGLSRELARLAQRREYSETILWSEERRERFT 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176233983 157 KIEKDIkdrlgdGIHTTFSKPFFlEILDRNVNKGTAMKNIMEEENISLSQ--VIAFGDGLNDKEMLETAGVGVAMDGA 232
Cdd:TIGR01486 152 EALVAV------GLEVTHGGRFY-HVLGAGSDKGKAVNALKAFYNQPGGAikVVGLGDSPNDLPLLEVVDLAVVVPGP 222
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 8-227 5.70e-13

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 66.77  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   8 DLDGTLLDnlHkisDT-----NKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKI-IHHNG------ 75
Cdd:COG3769     9 DLDGTLLD--H---DTyswaaALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGAAIfIPKGYfafpsg 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  76 --SEKEYPVKEKS------LKILIEIAREYKTHLniyqheIWYSEnITnkETEIyKDISGLEPvkkdfdrlDE------- 140
Cdd:COG3769    84 taDIDGYWVIELGkpyaeiRAVLEQLREELGFKF------TGFGD-MS--AEEV-AELTGLSL--------EQaalakqr 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 141 MFSTKVLYIGEHENLLKIEKDIKDRlgdGIHTTFSkPFFLEILDrNVNKGTAM---KNIMEEENISLSQVIAFGDGLNDK 217
Cdd:COG3769   146 EFSEPLLWLGSDEALERFIAALAAL---GLTVLRG-GRFLHLMG-GADKGKAVrwlVEQYRQRFGKNVVTIALGDSPNDI 220

                         250
                  ....*....|
gi 1176233983 218 EMLETAGVGV 227
Cdd:COG3769   221 PMLEAADIAV 230
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 181-241 4.23e-10

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: 57.92  E-value: 4.23e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1176233983 181 EILDRNvNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDgAFEELKQVAD 241
Cdd:COG0560   149 PIVDGE-GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN-PDPALREAAD 207
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-233 4.97e-10

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: 58.14  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   5 VMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIHHNGSEKE----- 79
Cdd:cd07507     2 IFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIFIPRGYFKFpgrck 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  80 ----YPVKE-----KSLKILIEIAREyKTHLNIYQheiwyseNITNKETEIYKdISGLEPVKKDFDRLDEMfsTKVLYIG 150
Cdd:cd07507    82 seggYEVIElgkpyREIRAALEKIRE-ETGFKITG-------FGDLTEEEIAE-LTGLPRERAALAKEREY--SETIILR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 151 EHENllKIEKDIKDrLGDGIHTTFSKPFFLEILDRNVNKGTAMKNIME--EENISLSQVIAFGDGLNDKEMLEtagvgvA 228
Cdd:cd07507   151 SDEE--EDEKVLEA-LEERGLKITKGGRFYHVLGAGADKGKAVAILAAlyRQLYEAIVTVGLGDSPNDLPMLE------A 221


                  ....*
gi 1176233983 229 MDGAF 233
Cdd:cd07507   222 VDIAF 226
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 181-228 8.54e-10

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: 56.40  E-value: 8.54e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1176233983 181 EILDRNVnKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVA 228
Cdd:cd07500   131 PIVDAQR-KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 3-238 3.82e-08

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: 52.65  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   3 KAVMLDLDGTLL--DNLHKisdtnKEILKKLEDKGIKIFL--ATGRSYESMRSYHEELNLTTP--AICYNGAKIIHHNGS 76
Cdd:pfam05116   3 LLLVSDLDNTLVdgDNEAL-----ARLNQLLEAYRPDVGLvfATGRSLDSAKELLKEKPLPTPdyLITSVGTEIYYGPSL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  77 EKEypvkekslkilieiaREYKTHLNiyqhEIWYSENITnketEIYKDISGLEPVKKDFDRldemfSTKVLYIGEHENLL 156
Cdd:pfam05116  78 VPD---------------QSWQEHLD----YHWDRQAVV----EALAKFPGLTLQPEEEQR-----PHKVSYFLDPEAAA 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 157 KIEKDIKDRL---GDGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAF 233
Cdd:pfam05116 130 AVLAELEQLLrkrGLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQ 209


                  ....*
gi 1176233983 234 EELKQ 238
Cdd:pfam05116 210 PELLQ 214
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 4-95 2.31e-07

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: 48.16  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   4 AVMLDLDGTLLdnlhkisdtNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLT---TPAICYNGakiiHHNGSEKEY 80
Cdd:cd01427     1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGdlfDGIIGSDG----GGTPKPKPK 67

                          90
                  ....*....|....*
gi 1176233983  81 PVKEKSLKILIEIAR 95
Cdd:cd01427    68 PLLLLLLKLGVDPEE 82
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 188-244 8.50e-07

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: 47.52  E-value: 8.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176233983 188 NKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHVT 244
Cdd:cd01630    76 DKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 3-222 1.28e-04

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


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 42.99  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   3 KAVMLDLDGTLLDNLHKISDTNKEILKKLEDKGIKIFLATGRSYESMRSYHEELNLTTPAICYNGAKIIhhngSEKEYPV 82
Cdd:PRK14502  417 KIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIF----IPKDYFR 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  83 KEKSLK------ILIEIAREYK--TH-----LNIYQHEIWYSENITNKETEIYKDISgLEPVKKDFD---RLDEMFSTKv 146
Cdd:PRK14502  493 LPFAYDrvagnyLVIELGMAYKdiRHilkkaLAEACTEIENSEKAGNIFITSFGDMS-VEDVSRLTDlnlKQAELAKQR- 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983 147 lyigEHENLLKIEKD-------IKDRLGDGIHTTFSKPFFlEILDRNvNKGTAMKNIMEEENISLSQVIAF--GDGLNDK 217
Cdd:PRK14502  571 ----EYSETVHIEGDkrstnivLNHIQQSGLEYSFGGRFY-EVTGGN-DKGKAIKILNELFRLNFGNIHTFglGDSENDY 644


                  ....*
gi 1176233983 218 EMLET 222
Cdd:PRK14502  645 SMLET 649
serB PRK11133
phosphoserine phosphatase; Provisional
 189-228 1.88e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 41.86  E-value: 1.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1176233983 189 KGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGVGVA 228
Cdd:PRK11133  249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-224 4.79e-04

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: 40.26  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983   2 IKAVMLDLDGTLLDNLHKISDTNKEILKkledkGIKIFLATGRSYESMRsyhEELNLTTPAICYNGAKIIHHNGSEKEYP 81
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELAS-----EHPLAKAIVAAAEDLP---IPVEDFTARLLLGKRDWLEELDILRGLV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176233983  82 VKEKSLKILIEIAREYkthlniyqHEIWYSENITNKEteiykdisGLEPVkkdFDRLDEM-FSTKVLYIGEHENLLKIEK 160
Cdd:pfam00702  73 ETLEAEGLTVVLVELL--------GVIALADELKLYP--------GAAEA---LKALKERgIKVAILTGDNPEAAEALLR 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1176233983 161 DIkdrlgdGIHTTFSKPFFLEILDRNVNKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAG 224
Cdd:pfam00702 134 LL------GLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
200-244 5.62e-04

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 39.37  E-value: 5.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1176233983 200 ENISLSQVIAFGDGLNDKEMLETAGVGVAM---DGAFEELKQVADHVT 244
Cdd:COG4087    87 EKLGAETTVAIGNGRNDVLMLKEAALGIAVigpEGASVKALLAADIVV 134
ATPase-IB2_Cd TIGR01512
heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ...
 195-258 6.78e-04

heavy metal-(Cd/Co/Hg/Pb/Zn)-translocating P-type ATPase; This model describes the P-type ATPase primarily responsible for translocating cadmium ions (and other closely-related divalent heavy metals such as cobalt, mercury, lead and zinc) across biological membranes. These transporters are found in prokaryotes and plants. Experimentally characterized members of the seed alignment include: SP|P37617 from E. coli, SP|Q10866 from Mycobacterium tuberculosis and SP|Q59998 from Synechocystis PCC6803. The cadmium P-type ATPases have been characterized as Type IB based on a phylogenetic analysis which combines the copper-translocating ATPases with the cadmium-translocating species. This model and that describing the copper-ATPases (TIGR01511) are well separated, and thus we further type the copper-ATPases as IB1 and the cadmium-ATPases as IB2. Several sequences which have not been characterized experimentally fall just below trusted cutoff for both of these models (SP|Q9CCL1 from Mycobacterium leprae, GP|13816263 from Sulfolobus solfataricus, OMNI|NTL01CJ01098 from Campylobacter jejuni, OMNI|NTL01HS01687 from Halobacterium sp., GP|6899169 from Ureaplasma urealyticum and OMNI|HP1503 from Helicobacter pylori). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273665 [Multi-domain]  Cd Length: 550  Bit Score: 40.77  E-value: 6.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176233983 195 NIMEEENISLSQVIAFGDGLNDKEMLETAGVGVAMDGAFEEL-KQVADHVTISNNESGVGEFLKK 258
Cdd:TIGR01512 430 EIVKELREKAGPVAMVGDGINDAPALAAADVGIAMGASGSDVaLETADVVLLNDDLSRLPQAIRL 494
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
 206-258 1.03e-03

heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the copper and cadmium-type heavy metal transporting P-type ATPases (TIGR01511 and TIGR01512) as well as those species which score ambiguously between both models. For more comments and references, see the files on TIGR01511 and 01512.


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 39.92  E-value: 1.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1176233983 206 QVIAFGDGLNDKEMLETAGVGVAMDGAFEELKQVADHVTISNNESGVGEFLKK 258
Cdd:TIGR01525 452 PVAMVGDGINDAPALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAIDL 504
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 2-59 2.45e-03

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: 37.50  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176233983   2 IKAVMLDLDGTLLDNLHKISDTNKEI----------LKKLEDKGIKIFLATGRSYESMRSYHEELNLT 59
Cdd:cd01630     1 IKLLVLDVDGVLTDGRIYYDSNGEELksfnvrdglgIKLLQKSGIEVAIITGRQSEAVRRRAKELGIE 68
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-46 5.50e-03

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 36.61  E-value: 5.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176233983   1 MIKAVMLDLDGTLLDNLHKISDTNK--------EILKKLEDKGIKIFLAT-----GRSY 46
Cdd:COG0241     2 MKKAVFLDRDGTINEDVGYVKSPEEfeflpgvlEALARLNEAGYRLVVVTnqsgiGRGL 60
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 3-57 6.34e-03

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


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 35.84  E-value: 6.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176233983   3 KAVMLDLDGTLLDNLHKISDTN--------KEILKKLEDKGIKIFLATGRSYESMRSYHEELN 57
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDerilypevPDALAELKEAGYKVVIVTNQSGIGRGYFSRSFS 63
HAD_PPase cd07509
inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic ...
 3-57 9.02e-03

inorganic pyrophosphatase similar to a human phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP); LHPP hydrolyzes nitrogen-phosphorus bonds in phospholysine, phosphohistidine and imidodiphosphate as well as oxygen-phosphorus bonds in inorganic pyrophosphate in vitro. This family also includes human haloacid dehalogenase like hydrolase domain containing 2 protine (HDHD2) a phosphatase which may be involved in polygenic hypertension. 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: 319812 [Multi-domain]  Cd Length: 248  Bit Score: 36.49  E-value: 9.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1176233983   3 KAVMLDLDGTLLDNLHKISDTnKEILKKLEDKGIKIFLATGRSYESMRSYHEELN 57
Cdd:cd07509     1 KAVLLDLSGTLYISGAAIPGA-AEALKRLRHAGLKVRFLTNTTKESRRTLAERLQ 54
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 188-229 9.57e-03

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 35.06  E-value: 9.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1176233983 188 NKGTAMKNIMEEENISLSQVIAFGDGLNDKEMLETAGV-GVAM 229
Cdd:cd01427    64 PKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGrTVAV 106
 
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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