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Conserved domains on  [gi|1468674136|ref|WP_117548031|]
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Cof-type HAD-IIB family hydrolase [Longicatena caecimuris]

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 ...
 5-265 1.22e-82

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: 248.28  E-value: 1.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYreaKILEMDRFKGYLLSYNGAHVCDyPNQQVIY 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQ---PYLEELGLDSPLITFNGALVYD-PTGKEIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  85 NKTIDKKYILPIINNAKALNLGImvnkgeYVVVDDPHTYQLeYEAHATNMKTMVV---DDLRTFVDFEPNKFLISAPPEY 161
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGI------NIYTNDDWADTI-YEENEDDEIIKPAeilDDLLLPPDEDITKILFVGEDEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 162 LKMQFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVK 241
Cdd:cd07516   150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250       260
                  ....*....|....*....|....
gi 1468674136 242 PIKLIANEITASNDEDGIAKSLYK 265
Cdd:cd07516   230 EVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-265 1.22e-82

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: 248.28  E-value: 1.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYreaKILEMDRFKGYLLSYNGAHVCDyPNQQVIY 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQ---PYLEELGLDSPLITFNGALVYD-PTGKEIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  85 NKTIDKKYILPIINNAKALNLGImvnkgeYVVVDDPHTYQLeYEAHATNMKTMVV---DDLRTFVDFEPNKFLISAPPEY 161
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGI------NIYTNDDWADTI-YEENEDDEIIKPAeilDDLLLPPDEDITKILFVGEDEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 162 LKMQFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVK 241
Cdd:cd07516   150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250       260
                  ....*....|....*....|....
gi 1468674136 242 PIKLIANEITASNDEDGIAKSLYK 265
Cdd:cd07516   230 EVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-261 8.22e-71

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 218.26  E-value: 8.22e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   6 IVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEmdrFKGYLLSYNGAHVCDYpNQQVIYN 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELG---LDDPVICYNGALIYDE-NGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  86 KTIDKKYILPIINNAKALNLGIMVNKGEYVVVDDPH-TYQLEYEAHATNMKTMVVDDLRTFVDFEPNKFLISAPPEYLKM 164
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNeLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 165 QFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIK 244
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*..
gi 1468674136 245 LIANEITASNDEDGIAK 261
Cdd:pfam08282 237 AAADYVTDSNNEDGVAK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-263 1.75e-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: 199.80  E-value: 1.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPtpglYREAK-ILEMDRFKGYLLSYNGAHVCDYpNQQVI 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRP----YKEVKnILKELGLDTPFITANGAAVIDD-QGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  84 YNKTIDKKYILPIINNAKALNLGIMVNKGEYVVVDDPHTYQLEYEAHATNMKTMVVDDLRTFVDFEPNKFLISAPPEYLK 163
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 164 MQFEDFKLP-FGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:TIGR00099 156 LLIEALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1468674136 243 IKLIANEITASNDEDGIAKSL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-265 1.12e-61

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: 193.04  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDrfkGYLLSYNGAHVCDyPNQQV 82
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYD-PDGEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  83 IYNKTIDKKYILPIINNAKALNLGIMVnkgeyvvvddphtyqleyeahatnmktmvvddlrtfvdfepnkflisappeyl 162
Cdd:COG0561    78 LYERPLDPEDVREILELLREHGLHLQV----------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 163 kmqfedfklpfgdrlsIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:COG0561   105 ----------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|...
gi 1468674136 243 IKLIANEITASNDEDGIAKSLYK 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEK 191
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-265 3.02e-49

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 163.71  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   1 MGYKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFKGYLLSYNGAHVCDYPNQ 80
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  81 QVIYNKTI---DKKYIlpiinNAKALNLGIMVNKGEYVVVDDPHTYQLEYEAHATNMKTMVVDdLRTFVDFEPN----KF 153
Cdd:PRK10513   81 ETVAQTALsydDYLYL-----EKLSREVGVHFHALDRNTLYTANRDISYYTVHESFLTGIPLV-FREVEKMDPNlqfpKV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 154 LISAPPEYL-----KMQFEDFKlpfgdRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQ 228
Cdd:PRK10513  155 MMIDEPEILdaaiaRIPAEVKE-----RYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIE 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1468674136 229 YAGHGVAMGNAVKPIKLIANEITASNDEDGIAKSLYK 265
Cdd:PRK10513  230 YAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-265 1.22e-82

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: 248.28  E-value: 1.22e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYreaKILEMDRFKGYLLSYNGAHVCDyPNQQVIY 84
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQ---PYLEELGLDSPLITFNGALVYD-PTGKEIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  85 NKTIDKKYILPIINNAKALNLGImvnkgeYVVVDDPHTYQLeYEAHATNMKTMVV---DDLRTFVDFEPNKFLISAPPEY 161
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGI------NIYTNDDWADTI-YEENEDDEIIKPAeilDDLLLPPDEDITKILFVGEDEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 162 LKMQFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVK 241
Cdd:cd07516   150 LDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAID 229

                         250       260
                  ....*....|....*....|....
gi 1468674136 242 PIKLIANEITASNDEDGIAKSLYK 265
Cdd:cd07516   230 EVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-261 8.22e-71

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 218.26  E-value: 8.22e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   6 IVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEmdrFKGYLLSYNGAHVCDYpNQQVIYN 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELG---LDDPVICYNGALIYDE-NGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  86 KTIDKKYILPIINNAKALNLGIMVNKGEYVVVDDPH-TYQLEYEAHATNMKTMVVDDLRTFVDFEPNKFLISAPPEYLKM 164
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNeLEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 165 QFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIK 244
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*..
gi 1468674136 245 LIANEITASNDEDGIAK 261
Cdd:pfam08282 237 AAADYVTDSNNEDGVAK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-263 1.75e-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: 199.80  E-value: 1.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPtpglYREAK-ILEMDRFKGYLLSYNGAHVCDYpNQQVI 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRP----YKEVKnILKELGLDTPFITANGAAVIDD-QGEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  84 YNKTIDKKYILPIINNAKALNLGIMVNKGEYVVVDDPHTYQLEYEAHATNMKTMVVDDLRTFVDFEPNKFLISAPPEYLK 163
Cdd:TIGR00099  76 YKKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 164 MQFEDFKLP-FGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:TIGR00099 156 LLIEALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 1468674136 243 IKLIANEITASNDEDGIAKSL 263
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALAL 256
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-265 1.12e-61

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: 193.04  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDrfkGYLLSYNGAHVCDyPNQQV 82
Cdd:COG0561     2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLD---DPLITSNGALIYD-PDGEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  83 IYNKTIDKKYILPIINNAKALNLGIMVnkgeyvvvddphtyqleyeahatnmktmvvddlrtfvdfepnkflisappeyl 162
Cdd:COG0561    78 LYERPLDPEDVREILELLREHGLHLQV----------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 163 kmqfedfklpfgdrlsIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:COG0561   105 ----------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                         250       260
                  ....*....|....*....|...
gi 1468674136 243 IKLIANEITASNDEDGIAKSLYK 265
Cdd:COG0561   169 VKAAADYVTGSNDEDGVAEALEK 191
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-265 3.02e-49

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 163.71  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   1 MGYKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFKGYLLSYNGAHVCDYPNQ 80
Cdd:PRK10513    1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  81 QVIYNKTI---DKKYIlpiinNAKALNLGIMVNKGEYVVVDDPHTYQLEYEAHATNMKTMVVDdLRTFVDFEPN----KF 153
Cdd:PRK10513   81 ETVAQTALsydDYLYL-----EKLSREVGVHFHALDRNTLYTANRDISYYTVHESFLTGIPLV-FREVEKMDPNlqfpKV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 154 LISAPPEYL-----KMQFEDFKlpfgdRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQ 228
Cdd:PRK10513  155 MMIDEPEILdaaiaRIPAEVKE-----RYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIE 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1468674136 229 YAGHGVAMGNAVKPIKLIANEITASNDEDGIAKSLYK 265
Cdd:PRK10513  230 YAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-263 3.17e-41

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: 141.21  E-value: 3.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   4 KLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFkgylLSYNGAHVCDypNQQVI 83
Cdd:cd07517     1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSY----VSYNGQYVFF--EGEVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  84 YNKTIDKKYILPIINNAKalnlgimvnKGEYVVVddphtyqleyeahatnmktmVVDDLRTFVDFEPNKFLISAPPEylk 163
Cdd:cd07517    75 YKNPLPQELVERLTEFAK---------EQGHPVS--------------------FYGQLLLFEDEEEEQKYEELRPE--- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 164 mqfedfklpfgdrLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPI 243
Cdd:cd07517   123 -------------LRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEEL 189

                         250       260
                  ....*....|....*....|
gi 1468674136 244 KLIANEITASNDEDGIAKSL 263
Cdd:cd07517   190 KEIADYVTKDVDEDGILKAL 209
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-263 9.64e-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: 102.66  E-value: 9.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   4 KLIVMDMDGTLTNSKKEISEETRTALIEA-QKLGASIVLASGRPtpgLYREAKILEMDRFKGYLLSYNGAhvcdypnqqV 82
Cdd:cd07518     1 KLIATDMDGTFLNDDKTYDHERFFAILDQlLKKGIKFVVASGRQ---YYQLISFFPEIKDEMSFVAENGA---------V 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  83 IYNKtidkkyilpiinnakalnlgIMVNkgeyvvVDDPHTYQLEYEAHATnmktmvvddlrtfvdfepnkflisappeyl 162
Cdd:cd07518    69 VYFK--------------------FTLN------VPDEAAPDIIDELNQK------------------------------ 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 163 kmqfedfklpFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:cd07518    93 ----------FGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEE 162

                         250       260
                  ....*....|....*....|.
gi 1468674136 243 IKLIANEITASNDEDGIAKSL 263
Cdd:cd07518   163 VKAAAKYVAPSNNENGVLQVI 183
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-265 1.67e-26

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 104.34  E-value: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   1 MGYKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRfkgYLLSYNGAHVCDYPNQ 80
Cdd:PRK10530    1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDT---PAICCNGTYLYDYQAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  81 QVIYNKTidkkyiLPIinnAKALNLGIMVNKGE---YVVVDDPHTYQleyEAHATNMKTMV---------------VDDL 142
Cdd:PRK10530   78 KVLEADP------LPV---QQALQVIEMLDEHQihgLMYVDDAMLYE---HPTGHVIRTLNwaqtlppeqrptftqVDSL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 143 RTFVDfEPN---KFLISAPpEYLKMQfeDFKLPFGDRLSIYTSAPFY--IEVVSNGIDKGKALAGIAERLGIQREEIIAF 217
Cdd:PRK10530  146 AQAAR-QVNaiwKFALTHE-DLPQLQ--HFAKHVEHELGLECEWSWHdqVDIARKGNSKGKRLTQWVEAQGWSMKNVVAF 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1468674136 218 GDEMNDLTMLQYAGHGVAMGNAVKPIKLIANEITASNDEDGIAKSLYK 265
Cdd:PRK10530  222 GDNFNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-265 2.76e-25

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 100.05  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   1 MGYKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEmdrFKGYLLSYNGAHVCDYPNQ 80
Cdd:PRK01158    1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLIG---TSGPVIAENGGVISVGFDG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  81 QVIYNKTIDKKYIlpiinnAKALNLGIMVNKGEYVVVDDPhtyqlEYEahatnmKTMVVddLRTFVDFEPNKFLISAppe 160
Cdd:PRK01158   78 KRIFLGDIEECEK------AYSELKKRFPEASTSLTKLDP-----DYR------KTEVA--LRRTVPVEEVRELLEE--- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 161 ylkmqfedfklpFGDRLSIYTSApFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAV 240
Cdd:PRK01158  136 ------------LGLDLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANAD 202

                         250       260
                  ....*....|....*....|....*
gi 1468674136 241 KPIKLIANEITASNDEDGIAKSLYK 265
Cdd:PRK01158  203 EELKEAADYVTEKSYGEGVAEAIEH 227
PLN02887 PLN02887
hydrolase family protein
 3-267 6.08e-25

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 103.80  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFKGYLLSYN------GAHVCD 76
Cdd:PLN02887  308 FSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDGIISESSpgvflqGLLVYG 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  77 YPNQQvIYNKTIDK-----------KYILPII--NNAKALNLGimvnkgEYVVVDDPHTyqLEYEAHATNMKTmvVDDLR 143
Cdd:PLN02887  388 RQGRE-IYRSNLDQevcreaclyslEHKIPLIafSQDRCLTLF------DHPLVDSLHT--IYHEPKAEIMSS--VDQLL 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 144 TFVDFEPNKFLISapPEYLKMQFEDF-KLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMN 222
Cdd:PLN02887  457 AAADIQKVIFLDT--AEGVSSVLRPYwSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGEN 534

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1468674136 223 DLTMLQYAGHGVAMGNAVKPIKLIANEITASNDEDGIAKSLYK-AF 267
Cdd:PLN02887  535 DIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRyAF 580
PRK15126 PRK15126
HMP-PP phosphatase;
3-239 1.67e-21

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 90.91  E-value: 1.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRptpglyreaKILEMDR------FKGYLLSYNGAHVCD 76
Cdd:PRK15126    2 ARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGR---------HVLEMQHilgalsLDAYLITGNGTRVHS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  77 yPNQQVIYNKTIDKKYILPIINNAKALNLGIMV--NKGEYVVVDDPHTYQleyeAHATNMKTMVVDDLRTFVDFEPNKFL 154
Cdd:PRK15126   73 -LEGELLHRQDLPADVAELVLHQQWDTRASMHVfnDDGWFTGKEIPALLQ----AHVYSGFRYQLIDLKRLPAHGVTKIC 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 155 ISAPPE---YLKMQFEDFklpFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAG 231
Cdd:PRK15126  148 FCGDHDdltRLQIQLNEA---LGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVG 224


                  ....*...
gi 1468674136 232 HGVAMGNA 239
Cdd:PRK15126  225 RGFIMGNA 232
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-236 1.92e-21

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: 89.36  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   5 LIVMDMDGTLTNSKK-EISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRfkgYLLSYNGAHVCDYPNQQVI 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPL---PLIAENGALIFYPGEILYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  84 YNKTiDKKYILPIINNakalnlgiMVNKGEYVVVDdpHTYQLEYEAHAtnmktmvVDDLRTFVDFEPNKFLISAPPEYLk 163
Cdd:TIGR01484  78 EPSD-VFEEILGIKFE--------EIGAELKSLSE--HYVGTFIEDKA-------IAVAIHYVGAELGQELDSKMRERL- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468674136 164 mqfEDFKLPFGDrLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAM 236
Cdd:TIGR01484 139 ---EKIGRNDLE-LEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10976 PRK10976
putative hydrolase; Provisional
 3-267 6.72e-18

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 80.86  E-value: 6.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLyreAKILEMDRFKGYLLSYNGAHVCDyPNQQV 82
Cdd:PRK10976    2 YQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDV---GQIRDNLEIKSYMITSNGARVHD-TDGNL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  83 IYNKTIDKKYilpiinnakALNLGIMVNkgeyvvvDDPHTYQLEYEAHATNMKTMVVDDLRTFVD-------FEPNK--- 152
Cdd:PRK10976   78 IFSHNLDRDI---------ASDLFGVVH-------DNPDIITNVYRDDEWFMNRHRPEEMRFFKEavfkyqlYEPGLlep 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 153 ------FLISAPPEYLKMQFEDFKLPFGDRLSIYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTM 226
Cdd:PRK10976  142 dgvskvFFTCDSHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEM 221

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1468674136 227 LQYAGHGVAMGNAVKPIK--LIANEITASNDEDGIAKSLYKAF 267
Cdd:PRK10976  222 LSMAGKGCIMGNAHQRLKdlLPELEVIGSNADDAVPHYLRKLY 264
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-263 1.67e-17

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: 78.63  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   4 KLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKilemdrfkgyLLSYNGAHVCDypNQQVI 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAV----------LIGTSGPVVAE--NGGVI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  84 YNKTIDKkyilpiinnakalnlgIMVNKGEYVVVDD--PHTYQLEYEAHATNMKTMVVDDLRTFVDFepnkflISAPPEY 161
Cdd:TIGR01487  70 FYNKEDI----------------FLANMEEEWFLDEekKKRFPRDRLSNEYPRASLVIMREGKDVDE------VREIIKE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 162 LkmqfedfklpfgdRLSIYTSApFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVK 241
Cdd:TIGR01487 128 R-------------GLNLVASG-FAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADD 193

                         250       260
                  ....*....|....*....|..
gi 1468674136 242 PIKLIANEITASNDEDGIAKSL 263
Cdd:TIGR01487 194 QLKEIADYVTSNPYGEGVVEVL 215
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-270 9.51e-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: 77.12  E-value: 9.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   6 IVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRpTPGLYREAKILemdrfkgylLSYNGAHVCDypNQQVI-Y 84
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGN-SVQFARALAKL---------IGTPDPVIAE--NGGEIsY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  85 NKTIDKKYIlpiINNAKALNLGIMVNKGEYVvvdDPHTYQLEYEAHATNMktmvvddlRTFVDFEPNKFLISAPPEYLKm 164
Cdd:TIGR01482  69 NEGLDDIFL---AYLEEEWFLDIVIAKTFPF---SRLKVQYPRRASLVKM--------RYGIDVDTVREIIKELGLNLV- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 165 qfedfklpfgdrlsiYTSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIK 244
Cdd:TIGR01482 134 ---------------AVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELK 198

                         250       260
                  ....*....|....*....|....*.
gi 1468674136 245 LIANEITASNDEDGIAKSLYKAFPEI 270
Cdd:TIGR01482 199 EWADYVTESPYGEGGAEAIGEILQAI 224
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 193-265 2.85e-14

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: 68.00  E-value: 2.85e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468674136 193 GIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIKLIANEITASNDEDGIAKSLYK 265
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDK 137
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 165-258 8.31e-10

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: 57.74  E-value: 8.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136 165 QFEDFKLPFGDRLSIYTSAPFYIEV--VSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:cd02605   137 QLEEMLLKAGLTVRIIYSSGLAYDLdiLPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPE 216

                          90
                  ....*....|....*.
gi 1468674136 243 IKLIANEITASNDEDG 258
Cdd:cd02605   217 LLKWADRVTRSRLAKG 232
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 187-235 7.40e-09

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: 54.46  E-value: 7.40e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1468674136 187 IEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVA 235
Cdd:COG0560   147 VGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVA 195
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 190-250 1.63e-06

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 48.40  E-value: 1.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468674136 190 VSNGIDKGKALAGIAERLGIQRE-EIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIKLIANEI 250
Cdd:PRK00192  185 LLGGGDKGKAVRWLKELYRRQDGvETIALGDSPNDLPMLEAADIAVVVPGPDGPNPPLLPGI 246
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 196-235 1.99e-06

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: 47.16  E-value: 1.99e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1468674136 196 KGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVA 235
Cdd:cd07500   138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 187-254 6.37e-06

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: 44.82  E-value: 6.37e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468674136 187 IEVVSNGI-DKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNAVKPIKLIANEITASN 254
Cdd:cd01630    67 IEDLFQGVkDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRAR 135
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 179-239 9.30e-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: 45.72  E-value: 9.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468674136 179 IYtSAPFYIEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVAMGNA 239
Cdd:pfam05116 149 IY-SSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNA 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-231 3.15e-05

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 43.73  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   3 YKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKIL--EMDRFKGYLLSYNGAHVCDYPNQ 80
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAELASEHPLAKAIVAAAEDLPIPVEDFTARLLlgKRDWLEELDILRGLVETLEAEGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136  81 QVIYNKtidkkyilpiinnakalNLGIMVNKGEYVVVDDphTYQLEYEAHATNMKTMVV-DDLRTFVDfepnkflisapp 159
Cdd:pfam00702  81 TVVLVE-----------------LLGVIALADELKLYPG--AAEALKALKERGIKVAILtGDNPEAAE------------ 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468674136 160 eylkmqfedfklPFGDRLSIYTSAPFYIEVVSNGIDK--GKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAG 231
Cdd:pfam00702 130 ------------ALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-93 1.20e-04

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 42.25  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468674136   1 MGYKLIVMDMDGTLTNSKKEISEETRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFKgYLLSYNGAHVcdYPNQ 80
Cdd:PTZ00174    3 MKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKIKEQLGEDVLEDFD-YVFSENGLVA--YKDG 79

                          90
                  ....*....|...
gi 1468674136  81 QVIYNKTIdKKYI 93
Cdd:PTZ00174   80 ELFHSQSI-LKFL 91
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 187-228 1.98e-04

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 41.19  E-value: 1.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1468674136 187 IEVVSNGIDKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQ 228
Cdd:TIGR01488 134 GQVNPEGECKGKVLKELLEESKITLKKIIAVGDSVNDLPMLK 175
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 195-236 3.07e-04

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 39.30  E-value: 3.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1468674136 195 DKGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAG-HGVAM 236
Cdd:cd01427    64 PKPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGgRTVAV 106
serB PRK11133
phosphoserine phosphatase; Provisional
 196-235 8.51e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 40.32  E-value: 8.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1468674136 196 KGKALAGIAERLGIQREEIIAFGDEMNDLTMLQYAGHGVA 235
Cdd:PRK11133  249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 190-242 1.23e-03

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 39.43  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1468674136 190 VSNGIDKGKALAGIAERLGIQREE---IIAFGDEMNDLTMLQYAGHGVAMGNAVKP 242
Cdd:COG3769   183 LMGGADKGKAVRWLVEQYRQRFGKnvvTIALGDSPNDIPMLEAADIAVVIRSPHGA 238
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-75 3.39e-03

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 36.22  E-value: 3.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468674136   5 LIVMDMDGTLTnskkeiseeTRTALIEAQKLGASIVLASGRPTPGLYREAKILEMDRFKGYLLSYNGAHVC 75
Cdd:cd01427     1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTP 62
HAD pfam12710
haloacid dehalogenase-like hydrolase;
173-228 8.29e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 36.36  E-value: 8.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1468674136 173 FGDRLSIYTSAPFYIEVVSNGIDKGKALAG--IAERLGIQREEIIAFGDEMNDLTMLQ 228
Cdd:pfam12710 131 LEVDDGRFTGELRLIGPPCAGEGKVRRLRAwlAARGLGLDLADSVAYGDSPSDLPMLR 188
 
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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