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Conserved domains on  [gi|489156077|ref|WP_003065757|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Streptococcus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 3.54e-88

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: 262.53  E-value: 3.54e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDK 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  86 SELTRAQLKRLHSTLDPLALPFDVLSDGIVYSlasqgnqSLYPQ--ANPKLKFVELTSFDDIPENIIYNKVVSVTNPEFL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDDWAD-------TIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 164 DKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 489156077 244 AKETADAVtTRTNDESGVAEAVEK 267
Cdd:cd07516  231 VKEAADYV-TLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 3.54e-88

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: 262.53  E-value: 3.54e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDK 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  86 SELTRAQLKRLHSTLDPLALPFDVLSDGIVYSlasqgnqSLYPQ--ANPKLKFVELTSFDDIPENIIYNKVVSVTNPEFL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDDWAD-------TIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 164 DKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 489156077 244 AKETADAVtTRTNDESGVAEAVEK 267
Cdd:cd07516  231 VKEAADYV-TLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-264 1.80e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 225.19  E-value: 1.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    7 LALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDKS 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGL---DDPVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   87 ELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNQSLYPQANPKLKFVELTSFDDIPENIIYNKVVSVTNPEFLDKQ 166
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  167 ILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKE 246
Cdd:pfam08282 158 EKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKA 237

                         250
                  ....*....|....*...
gi 489156077  247 TADAVTTrTNDESGVAEA 264
Cdd:pfam08282 238 AADYVTD-SNNEDGVAKA 254
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 4-271 2.42e-66

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 207.62  E-value: 2.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   4 IKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLISDEDYIITFNGGLVQKT-NGDI 82
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAaDGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  83 LDKSELTRAQLKRLHSTLDPLALPFDVLSDGIVYSlasqGNQ--SLYPQANPKLKFVELT--SFDDIPENIIYNKVVSVT 158
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT----ANRdiSYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMID 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 159 NPEFLDKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMA 238
Cdd:PRK10513 159 EPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMG 238

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489156077 239 NGVAIAKETADAVtTRTNDESGVAEAVEKYILN 271
Cdd:PRK10513 239 NAIPSVKEVAQFV-TKSNLEDGVAFAIEKYVLN 270
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-268 3.46e-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: 201.90  E-value: 3.46e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   3 DIKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDI 82
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIYDPDGEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  83 LDKSELTRAQLKRLHSTLDPLALPFDVlsdgivyslasqgnqslypqanpklkfveltsfddipeniiynkvvsvtnpef 162
Cdd:COG0561   78 LYERPLDPEDVREILELLREHGLHLQV----------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 163 ldkqilqfpkelynefeIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVA 242
Cdd:COG0561  105 -----------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                        250       260
                 ....*....|....*....|....*.
gi 489156077 243 IAKETADAVtTRTNDESGVAEAVEKY 268
Cdd:COG0561  168 EVKAAADYV-TGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-264 1.18e-55

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: 179.77  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    6 LLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDK 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGL---DTPFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   86 SELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNqsLYPQANPKLKFVELTSFD-DIPENIIYNKVVSVTNPEFLD 164
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPE--YFTIFKKFLGEPKLEVVDiQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  165 KQILQFPK-ELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:TIGR00099 156 LLIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489156077  244 AKETADAVTTrTNDESGVAEA 264
Cdd:TIGR00099 236 LKALADYVTD-SNNEDGVALA 255
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 3.54e-88

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: 262.53  E-value: 3.54e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDK 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  86 SELTRAQLKRLHSTLDPLALPFDVLSDGIVYSlasqgnqSLYPQ--ANPKLKFVELTSFDDIPENIIYNKVVSVTNPEFL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDDWAD-------TIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 164 DKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 489156077 244 AKETADAVtTRTNDESGVAEAVEK 267
Cdd:cd07516  231 VKEAADYV-TLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-264 1.80e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 225.19  E-value: 1.80e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    7 LALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDKS 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGL---DDPVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   87 ELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNQSLYPQANPKLKFVELTSFDDIPENIIYNKVVSVTNPEFLDKQ 166
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  167 ILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKE 246
Cdd:pfam08282 158 EKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKA 237

                         250
                  ....*....|....*...
gi 489156077  247 TADAVTTrTNDESGVAEA 264
Cdd:pfam08282 238 AADYVTD-SNNEDGVAKA 254
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 4-271 2.42e-66

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 207.62  E-value: 2.42e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   4 IKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLISDEDYIITFNGGLVQKT-NGDI 82
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAaDGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  83 LDKSELTRAQLKRLHSTLDPLALPFDVLSDGIVYSlasqGNQ--SLYPQANPKLKFVELT--SFDDIPENIIYNKVVSVT 158
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT----ANRdiSYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMID 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 159 NPEFLDKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMA 238
Cdd:PRK10513 159 EPEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMG 238

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489156077 239 NGVAIAKETADAVtTRTNDESGVAEAVEKYILN 271
Cdd:PRK10513 239 NAIPSVKEVAQFV-TKSNLEDGVAFAIEKYVLN 270
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 3-268 3.46e-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: 201.90  E-value: 3.46e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   3 DIKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDI 82
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIYDPDGEV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  83 LDKSELTRAQLKRLHSTLDPLALPFDVlsdgivyslasqgnqslypqanpklkfveltsfddipeniiynkvvsvtnpef 162
Cdd:COG0561   78 LYERPLDPEDVREILELLREHGLHLQV----------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 163 ldkqilqfpkelynefeIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVA 242
Cdd:COG0561  105 -----------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPP 167

                        250       260
                 ....*....|....*....|....*.
gi 489156077 243 IAKETADAVtTRTNDESGVAEAVEKY 268
Cdd:COG0561  168 EVKAAADYV-TGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-264 1.18e-55

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: 179.77  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    6 LLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDK 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGL---DTPFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   86 SELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNqsLYPQANPKLKFVELTSFD-DIPENIIYNKVVSVTNPEFLD 164
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPE--YFTIFKKFLGEPKLEVVDiQYLPDDILKILLLFLDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  165 KQILQFPK-ELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:TIGR00099 156 LLIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|.
gi 489156077  244 AKETADAVTTrTNDESGVAEA 264
Cdd:TIGR00099 236 LKALADYVTD-SNNEDGVALA 255
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 5-268 4.23e-43

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: 145.83  E-value: 4.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   5 KLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdeDYIITFNGGLVQkTNGDILD 84
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGI----DSYVSYNGQYVF-FEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  85 KSELTRAQLKRLHSTLDplalpfdvlSDGIVYSLASQgnqslypqanpklkfveLTSFDDIPEniiynkvvsvtnpefld 164
Cdd:cd07517   76 KNPLPQELVERLTEFAK---------EQGHPVSFYGQ-----------------LLLFEDEEE----------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 165 kqiLQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIA 244
Cdd:cd07517  113 ---EQKYEELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEEL 189

                        250       260
                 ....*....|....*....|....
gi 489156077 245 KETADAVTTrTNDESGVAEAVEKY 268
Cdd:cd07517  190 KEIADYVTK-DVDEDGILKALKHF 212
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 5-266 3.34e-28

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: 106.51  E-value: 3.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   5 KLLALDLDGTLFNSQKVVSPEN-KKALRAARDKGIKVVITTGRPLkaiSGLLEELDLISDEDYIITFNGGLVqktngdil 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERfFAILDQLLKKGIKFVVASGRQY---YQLISFFPEIKDEMSFVAENGAVV-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  84 dkseltraqlkrlhstldplalpfdvlsdgivyslasqgnqslypqanpKLKFVeLTSFDDIPENIIYNkvvsvtnpefl 163
Cdd:cd07518   70 -------------------------------------------------YFKFT-LNVPDEAAPDIIDE----------- 88

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 164 dkqilqFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAI 243
Cdd:cd07518   89 ------LNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEE 162

                        250       260
                 ....*....|....*....|...
gi 489156077 244 AKETADAVTTrTNDESGVAEAVE 266
Cdd:cd07518  163 VKAAAKYVAP-SNNENGVLQVIE 184
PLN02887 PLN02887
hydrolase family protein
 10-268 1.90e-27

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 110.73  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  10 DLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLISDEDYIITFNGG------LVQKTNGDIL 83
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDGIISESSPGvflqglLVYGRQGREI 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  84 DKSELTR-----AQLKRLHSTLDPLALPFD----VLSDGIVYSLasqgnQSLYPQanPKLKFVelTSFDDIPENIIYNKV 154
Cdd:PLN02887 394 YRSNLDQevcreACLYSLEHKIPLIAFSQDrcltLFDHPLVDSL-----HTIYHE--PKAEIM--SSVDQLLAAADIQKV 464

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 155 VSVTNPEFLDKQILQF-PKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGL 233
Cdd:PLN02887 465 IFLDTAEGVSSVLRPYwSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASL 544

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489156077 234 GVAMANGVAIAKETADAVTTrTNDESGVAEAVEKY 268
Cdd:PLN02887 545 GVALSNGAEKTKAVADVIGV-SNDEDGVADAIYRY 578
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 5-270 4.79e-27

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 105.88  E-value: 4.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   5 KLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGG-LVQKTNGDIL 83
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALAL---DTPAICCNGTyLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  84 DKSELTRAQLKRLHSTLDPL----------ALPFDVLSDGIVYSLAsqGNQSLYPQANPKLKFVEltSFDDIPE--NIIY 151
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHqihglmyvddAMLYEHPTGHVIRTLN--WAQTLPPEQRPTFTQVD--SLAQAARqvNAIW 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 152 NKVVSVTNPEFLDKQILQFPKE--LYNEFEIFKSRDIilemMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLK 229
Cdd:PRK10530 157 KFALTHEDLPQLQHFAKHVEHElgLECEWSWHDQVDI----ARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLE 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489156077 230 WAGLGVAMANGVAIAKETADAVtTRTNDESGVAEAVEKYIL 270
Cdd:PRK10530 233 AAGLGVAMGNADDAVKARADLV-IGDNTTPSIAEFIYSHVL 272
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 4-270 8.92e-27

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 103.90  E-value: 8.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   4 IKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEeldLISDEDYIITFNGGLVQK---TNG 80
Cdd:PRK01158   3 IKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAK---LIGTSGPVIAENGGVISVgfdGKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  81 DIL-DKSELTRAqlkrlhstldplalpFDVLSDgivyslasqgnqsLYPQAnpKLKFVELTSFDDIPENIIYNKVvsvtN 159
Cdd:PRK01158  80 IFLgDIEECEKA---------------YSELKK-------------RFPEA--STSLTKLDPDYRKTEVALRRTV----P 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 160 PEFLDKQIlqfpKELYNEFEIFKSRdIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMAN 239
Cdd:PRK01158 126 VEEVRELL----EELGLDLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVAN 200

                        250       260       270
                 ....*....|....*....|....*....|.
gi 489156077 240 GVAIAKETADAVTTRTNDEsGVAEAVEKYIL 270
Cdd:PRK01158 201 ADEELKEAADYVTEKSYGE-GVAEAIEHLLL 230
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 6-237 8.31e-24

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 95.53  E-value: 8.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    6 LLALDLDGTLFNSQK-VVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILD 84
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNL---PLPLIAENGALIFYPGEILYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   85 KSELTRAQLKRLHSTLDPLALpfdvlsdgivYSLASQGNQslypqanpklKFVELTSFDDipeNIIYnkvVSVTNPEFLD 164
Cdd:TIGR01484  78 EPSDVFEEILGIKFEEIGAEL----------KSLSEHYVG----------TFIEDKAIAV---AIHY---VGAELGQELD 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489156077  165 KQI---LQFPKELYNEFEIFKSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAM 237
Cdd:TIGR01484 132 SKMrerLEKIGRNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-265 9.27e-18

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: 79.40  E-value: 9.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    4 IKLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLleeldlisdeDYIITFNGGLVQKTNGDIL 83
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARAL----------AVLIGTSGPVVAENGGVIF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   84 DKSEltraqlkrlhstldplalpfdvlsdgiVYSLASQGNQSLYPQANPKLKFVELTSFDdipeniiYNKVVSVTnpeFL 163
Cdd:TIGR01487  71 YNKE---------------------------DIFLANMEEEWFLDEEKKKRFPRDRLSNE-------YPRASLVI---MR 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  164 DKQILQFPKELYNE--FEIFKSRDIIlEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGV 241
Cdd:TIGR01487 114 EGKDVDEVREIIKErgLNLVASGFAI-HIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANAD 192

                         250       260
                  ....*....|....*....|....
gi 489156077  242 AIAKETADAVTTRTNDEsGVAEAV 265
Cdd:TIGR01487 193 DQLKEIADYVTSNPYGE-GVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 194-268 2.15e-17

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 76.47  E-value: 2.15e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489156077 194 GVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRTNDEsGVAEAVEKY 268
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGD-GVLEAIDKL 138
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-266 5.00e-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: 77.89  E-value: 5.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    7 LALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRplkaISGLLEELD-LISDEDYIITFNGGLVqkTNGDILDK 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGN----SVQFARALAkLIGTPDPVIAENGGEI--SYNEGLDD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   86 SELTraqLKRLHSTLDPL---ALPFDVLSdgivysLASQGNQSLYpqanpklkfveltsfddipeniiynkVVSvtnpEF 162
Cdd:TIGR01482  75 IFLA---YLEEEWFLDIViakTFPFSRLK------VQYPRRASLV--------------------------KMR----YG 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  163 LDKQILQfpkelynefEIFKSRDIIL---------EMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGL 233
Cdd:TIGR01482 116 IDVDTVR---------EIIKELGLNLvavdsgfdiHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGF 186

                         250       260       270
                  ....*....|....*....|....*....|...
gi 489156077  234 GVAMANGVAIAKETADAVTTRTNDESGVAEAVE 266
Cdd:TIGR01482 187 GVAVANAQPELKEWADYVTESPYGEGGAEAIGE 219
PRK15126 PRK15126
HMP-PP phosphatase;
5-239 6.09e-15

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 72.80  E-value: 6.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   5 KLLALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILD 84
Cdd:PRK15126   3 RLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSL---DAYLITGNGTRVHSLEGELLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  85 KSELTrAQLKR--LHSTLDPLAlPFDVLSDGIVYSlASQGNQSLYPQANPKLKFvELTSFDDIPENIIyNKVVSVTNPEF 162
Cdd:PRK15126  80 RQDLP-ADVAElvLHQQWDTRA-SMHVFNDDGWFT-GKEIPALLQAHVYSGFRY-QLIDLKRLPAHGV-TKICFCGDHDD 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489156077 163 LDKQILQFPKELYNEFEI-FKSRDIiLEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMAN 239
Cdd:PRK15126 155 LTRLQIQLNEALGERAHLcFSATDC-LEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGN 231
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 194-272 2.29e-12

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 63.53  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 194 GVH-KAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRTNDESGVAEAVEkYILNA 272
Cdd:COG1778   80 GVKdKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCE-LILKA 158
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 5-239 2.30e-10

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: 59.20  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    5 KLLALDLDGTLfnsqkvVSPENK-----KALRAARDKGIKVVITTGRPLKAISGLLEELDLISdEDYIITFNGGLVQKTN 79
Cdd:pfam05116   3 LLLVSDLDNTL------VDGDNEalarlNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPT-PDYLITSVGTEIYYGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   80 GDILDKSelTRAQLK------RLHSTLDplALPFDVLSD-------GIVYSLASQGNQSLYPQANPKLKFVELTSfddip 146
Cdd:pfam05116  76 SLVPDQS--WQEHLDyhwdrqAVVEALA--KFPGLTLQPeeeqrphKVSYFLDPEAAAAVLAELEQLLRKRGLDV----- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  147 eNIIYNkvvsvtNPEFLDkqILqfpkelynefeifksrdiilemmPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLS 226
Cdd:pfam05116 147 -KVIYS------SGRDLD--IL-----------------------PLRASKGEALRYLALKLGLPLENTLVCGDSGNDEE 194

                         250
                  ....*....|...
gi 489156077  227 MLKWAGLGVAMAN 239
Cdd:pfam05116 195 LFIGGTRGVVVGN 207
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 197-266 5.35e-10

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: 56.38  E-value: 5.35e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 197 KAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRTNDESGVAEAVE 266
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 6-83 2.17e-09

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: 53.94  E-value: 2.17e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489156077   6 LLALDLDGTLFNsqkvvspenKKALRAARDKGIKVVITTGRPLKAISGLLEELDLISDEDYIITFNGGLVQKTNGDIL 83
Cdd:cd01427    1 AVLFDLDGTLLA---------VELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPL 69
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 197-236 2.13e-08

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: 52.55  E-value: 2.13e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489156077 197 KAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVA 236
Cdd:cd07500  138 KAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 187-236 8.17e-08

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: 51.76  E-value: 8.17e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489156077 187 ILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVA 236
Cdd:COG0560  146 VVGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVA 195
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-69 3.42e-07

Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 50.11  E-value: 3.42e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489156077   1 MEDIKLLALDLDGTLFNSQKVVsPENKKALRAARDKGIKVVI---TTGRPLKAISGLLEELDLISDEDYIIT 69
Cdd:COG0647    5 ADRYDAFLLDLDGVLYRGDEPI-PGAVEALARLRAAGKPVLFltnNSSRTPEDVAEKLRRLGIPVAEDEIVT 75
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-268 1.08e-06

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: 48.50  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQkvVSPENKKALRA-----ARDKGIKVVITTGRPLKAISGLLEELDLISdEDYIITFNGGLVQKTNG 80
Cdd:cd02605    1 LLVSDLDETLVGHD--TNLQALERLQDlleqlTADNDVILVYATGRSPESVLELIKEVMLPK-PDFIISDVGTEIYYGES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  81 DILDKSELTRAQLKRLhstldplALPFDVLS-DGIVYSLASQG---------NQSLYPQANPK-LKFVELTSFD-DIPEN 148
Cdd:cd02605   78 GYLEPDTYWNEVLSEG-------WERFLFEAiADLFKQLKPQSeleqnphkiSFYLDPQNDAAvIEQLEEMLLKaGLTVR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 149 IIYNkvvsvtNPEFLDKQILqfpkelynefeifksrdiilemmPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSML 228
Cdd:cd02605  151 IIYS------SGLAYDLDIL-----------------------PLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALL 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489156077 229 KWAGLGVAMANGVAIAKETADAVT----TRTNDESGVAEAVEKY 268
Cdd:cd02605  202 STGTRGVIVGNAQPELLKWADRVTrsrlAKGPYAGGILEGLAHF 245
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-79 1.39e-06

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 48.41  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   1 MEDIKLLAL-DLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEElDLISDEDYIITFNGGLVQKTN 79
Cdd:PTZ00174   1 MEMKKTILLfDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKIKEQLGE-DVLEDFDYVFSENGLVAYKDG 79
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 7-69 2.51e-06

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 45.15  E-value: 2.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489156077    7 LALDLDGTLFNSQKVVsPENKKALRAARDKGIKVVITT---GRPLKAISGLLEELDLISDEDYIIT 69
Cdd:pfam13344   1 FLFDIDGVLWRGGEPI-PGAAEALRALRAAGKPVVFVTnnsSRSREEYAEKLRKLGFDIDEDEIIT 65
HAD_PMM cd02585
phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis ...
 6-208 2.92e-06

phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM; PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. 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: 319784  Cd Length: 238  Bit Score: 47.27  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQKVVSPENKKALRAARDKgIKVVITTGRPLKAISGLLEELDLISDEDYIITFNgGLVQKTNGDILDK 85
Cdd:cd02585    1 LLLFDVDGTLTPPRQPITPEMAEFLAELRQK-VKIGVVGGSDYDKIKEQLGDNVPLLDFDYVFPEN-GLVAYRDGELLSR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  86 SELTRA----QLKRL-HSTLDPLA-LPFDVLSDGIVYSLASQGNQSlyP-----QANPKLKFVELTSfddipENIIYNKV 154
Cdd:cd02585   79 QSIIRAlgeeKLQALiNFCLRYIAdLDLPKKRGTFIEFRNGMINIS--PigrncSQEERIEFEELDK-----KHKIREKF 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489156077 155 VSVTNPEFLDKQiLQFPKELYNEFEIFksrdiilemmPKGVHKAAGLNQLIQHL 208
Cdd:cd02585  152 VSALKEEFADKG-LTFSIGGQISFDVF----------PKGWDKTYCLRHLEEDL 194
PRK10976 PRK10976
putative hydrolase; Provisional
 8-239 5.62e-06

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 46.58  E-value: 5.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   8 ALDLDGTLFNSQKVVSPENKKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLVQKTNGDILDKSE 87
Cdd:PRK10976   6 ASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEI---KSYMITSNGARVHDTDGNLIFSHN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  88 LTR---AQLKRLHSTlDPlalpfDVLS---------------DGIVYSLASQGNQSLYPQANPKLKFVELTSFD-DIPEN 148
Cdd:PRK10976  83 LDRdiaSDLFGVVHD-NP-----DIITnvyrddewfmnrhrpEEMRFFKEAVFKYQLYEPGLLEPDGVSKVFFTcDSHEK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 149 IIynKVVSVTNPEFLDKQILQFpkelynefeifkSRDIILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSML 228
Cdd:PRK10976 157 LL--PLEQAINARWGDRVNVSF------------STLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEML 222

                        250
                 ....*....|.
gi 489156077 229 KWAGLGVAMAN 239
Cdd:PRK10976 223 SMAGKGCIMGN 233
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-232 6.93e-06

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: 45.65  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077    4 IKLLALDLDGTLFNSQKVVSpenkKALRAArdkgikvviTTGRPLKAISGLLEELDLISDEDYIITFNGGlvqktngdil 83
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVT----EAIAEL---------ASEHPLAKAIVAAAEDLPIPVEDFTARLLLG---------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   84 dKSELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNQSLYPQANPKLKfvELTSfddipENIiynKVVSVTNPEfl 163
Cdd:pfam00702  58 -KRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALK--ALKE-----RGI---KVAILTGDN-- 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489156077  164 dkqiLQFPKELYNEFEIFKSRDIILEMMPKGVHK--AAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAG 232
Cdd:pfam00702 125 ----PEAAEALLRLLGLDDYFDVVISGDDVGVGKpkPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
P-type_ATPase_Pb_Zn_Cd2-like cd07546
P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective ...
 198-266 1.17e-05

P-type heavy metal-transporting ATPase, similar to Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+); Escherichia coli ZntA mediates resistance to toxic levels of selected divalent metal ions. ZntA has the highest selectivity for Pb(2+), followed by Zn(2+) and Cd(2+); it also shows low levels of activity with Cu(2+), Ni(2+), and Co(2+). It is upregulated by the transcription factor ZntR at high zinc concentrations. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319846 [Multi-domain]  Cd Length: 597  Bit Score: 46.24  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 198 AAGLNqLIQHLNLLPEN-------------VMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEA 264
Cdd:cd07546  459 AAELG-LDFRAGLLPEDkvkavrelaqhgpVAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTH-NRLGGVAAM 536


                 ..
gi 489156077 265 VE 266
Cdd:cd07546  537 IE 538
serB PRK11133
phosphoserine phosphatase; Provisional
 197-236 2.62e-05

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 44.94  E-value: 2.62e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 489156077 197 KAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVA 236
Cdd:PRK11133 249 KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
6-245 3.04e-05

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 44.03  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTL--FNS---QKVVSPENKKALRA-ARDKGIKVVITTGRPLKAISGLLEELDLisdeDYI------ITFNGG 73
Cdd:COG1877    5 LLFLDFDGTLapIVPdpdAARPPPELRELLRRlAARPGGAVAIVSGRDLADLDRLLGPLGL----PLAgshgaeRRLPGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  74 LVQktngdILDKSELTRAQLKRLHSTLDPLALPFdvlsDGIV-----YSLAsqgnqsL-YPQANPKLKfveltsfddipe 147
Cdd:COG1877   81 EWE-----VLPLAAEAPEWLDALRAALEALAART----PGVLvedkgASLA------LhYRQAPPEEA------------ 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 148 niiynkvvsvtnpEFLDKQILQFPKELYNEFEIFKSRDIIlEMMPKGVHKAAGLNQLIQHLNlLPENVMAMGDEENDLSM 227
Cdd:COG1877  134 -------------EELRAALRELAARLGPGLEVLPGKKVV-ELRPAGVDKGRAVRALLAELP-FGRAPVFIGDDVTDEDA 198

                        250       260
                 ....*....|....*....|.
gi 489156077 228 LKWA---GLGVAMANGVAIAK 245
Cdd:COG1877  199 FAALpagGLGIKVGSGPTAAR 219
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
197-253 3.61e-05

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 43.38  E-value: 3.61e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489156077 197 KAAGLNQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTT 253
Cdd:PRK09484  97 KLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTR 153
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 6-245 3.65e-05

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 43.82  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   6 LLALDLDGTLFNSQK-----VVSPENKKALR--AARDKGIkVVITTGRPLKAISGLLEELDLisdedYIITFNGGLVQKT 78
Cdd:cd01627    1 LLFLDYDGTLAPIVPdpdaaVPSPELLEALKklAADPKNA-VAIVSGRDLDDLDKWLGLPGI-----GLAGEHGAEIRLP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  79 NGDILDksELTRAQLKRLHSTLDPLALPFDVLSDGIvyslasqgnqslypqanpklkFVEltsfddipeniiyNKVVSVT 158
Cdd:cd01627   75 GGGEWV--TLAPKADLEWKEEVEAIFKYFTERTPGS---------------------LVE-------------DKGASLA 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 159 -----NPEFLDKQILQFPKELynEFEIFKSRDI-----ILEMMPKGVHKAAGLNQLIQHLNLLPENVMAMGDEENDLSML 228
Cdd:cd01627  119 whyrnADPEGARAALELALHL--ASDLLKALEVvpgkkVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAF 196

                        250       260
                 ....*....|....*....|.
gi 489156077 229 KWA----GLGVAMANGVAIAK 245
Cdd:cd01627  197 RALngegGFSVKVGEGPTAAK 217
PLN02423 PLN02423
phosphomannomutase
 5-96 8.25e-05

phosphomannomutase


Pssm-ID: 178043 [Multi-domain]  Cd Length: 245  Bit Score: 42.78  E-value: 8.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   5 KLLAL-DLDGTLFNSQKVVSPENKKALRAARDKgIKVVITTGRPLKAISGLLEElDLISDEDYIITFNgGLVQKTNGDIL 83
Cdd:PLN02423   7 GVIALfDVDGTLTAPRKEATPEMLEFMKELRKV-VTVGVVGGSDLSKISEQLGK-TVINDYDYVFSEN-GLVAHKDGKLI 83

                         90
                 ....*....|....*..
gi 489156077  84 D----KSELTRAQLKRL 96
Cdd:PLN02423  84 GtqslKSFLGEDKLKEF 100
P-type_ATPase_HM cd02079
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ...
 197-267 1.28e-04

P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319774 [Multi-domain]  Cd Length: 617  Bit Score: 42.97  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 197 KAAGLNQLiqHLNLLPE--------------NVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVA 262
Cdd:cd02079  483 KELGIDEV--HAGLLPEdklaivkalqaeggPVAMVGDGINDAPALAQADVGIAMGSGTDVAIETADIVLLS-NDLSKLP 559


                 ....*
gi 489156077 263 EAVEK 267
Cdd:cd02079  560 DAIRL 564
copA PRK10671
copper-exporting P-type ATPase CopA;
186-266 1.71e-04

copper-exporting P-type ATPase CopA;


Pssm-ID: 182635 [Multi-domain]  Cd Length: 834  Bit Score: 42.81  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 186 IILEMMPKGvhKAAGlnqlIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETAdAVTTRTNDESGVAEAV 265
Cdd:PRK10671 692 VIAGVLPDG--KAEA----IKRLQSQGRQVAMVGDGINDAPALAQADVGIAMGGGSDVAIETA-AITLMRHSLMGVADAL 764


                 .
gi 489156077 266 E 266
Cdd:PRK10671 765 A 765
ATPase_P-type TIGR01494
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ...
 185-267 2.18e-04

ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily.


Pssm-ID: 273656 [Multi-domain]  Cd Length: 545  Bit Score: 42.30  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  185 DIILEMMPKgvHKAaglnQLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGvAIAKETADAVTTRtNDESGVAEA 264
Cdd:TIGR01494 427 DVFARVKPE--EKA----AIVEALQEKGRTVAMTGDGVNDAPALKKADVGIAMGSG-DVAKAAADIVLLD-DDLSTIVEA 498


                  ...
gi 489156077  265 VEK 267
Cdd:TIGR01494 499 VKE 501
P-type_ATPase_SERCA cd02083
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ...
 196-266 2.22e-04

sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319778 [Multi-domain]  Cd Length: 979  Bit Score: 42.28  E-value: 2.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489156077 196 HKAAgLNQLIQHLNLlpenVMAM-GDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRTNDESGVAeAVE 266
Cdd:cd02083  673 HKSK-IVELLQSQGE----ITAMtGDGVNDAPALKKAEIGIAMGSGTAVAKSASDMVLADDNFATIVA-AVE 738
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 9-269 4.31e-04

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 40.69  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077   9 LDLDGTLFNSQKVvSPEN-KKALRAARDKGIKVVITTGRPLKAISGLLEELDLisdEDYIITFNGGLV--------QKTN 79
Cdd:PRK00192   9 TDLDGTLLDHHTY-SYEPaKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGL---EDPFIVENGAAIyipknyfpFQPD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  80 GDILDKS----------ELTRAQLKRLHSTLDPLALPFDVLSDGIVYSLASQGNQSLyPQANpKLKFVE---LTSFDDIP 146
Cdd:PRK00192  85 GERLKGDywvielgppyEELREILDEISDELGYPLKGFGDLSAEEVAELTGLSGESA-RLAK-DREFSEpflWNGSEAAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 147 ENIIynkvvsvtnpefldkQILQFpkelyNEFEIFK-SRdiILEMMpKGVHKAAGLNQLIQHLNLLPE-NVMAMGDEEND 224
Cdd:PRK00192 163 ERFE---------------EALKR-----LGLKVTRgGR--FLHLL-GGGDKGKAVRWLKELYRRQDGvETIALGDSPND 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489156077 225 LSMLKWAGLGVAMANGV----AIAKETADAVTTRTNDE--SGVAEAVEKYI 269
Cdd:PRK00192 220 LPMLEAADIAVVVPGPDgpnpPLLPGIADGEFILASAPgpEGWAEAINKLL 270
zntA PRK11033
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
 210-266 5.40e-04

zinc/cadmium/mercury/lead-transporting ATPase; Provisional


Pssm-ID: 236827 [Multi-domain]  Cd Length: 741  Bit Score: 41.13  E-value: 5.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 210 LLPEN-------------VMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEAVE 266
Cdd:PRK11033 613 LLPEDkvkavtelnqhapLAMVGDGINDAPAMKAASIGIAMGSGTDVALETADAALTH-NRLRGLAQMIE 681
P-type_ATPase_Cu-like cd07552
P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+) ...
 38-266 5.77e-04

P-type heavy metal-transporting ATPase, similar to Archaeoglobus fulgidus CopB, a Cu(2+)-ATPase; Archaeoglobus fulgidus CopB transports Cu(2+) from the cytoplasm to the exterior of the cell using ATP as energy source, it transports preferentially Cu(2+) over Cu(+), it is activated by Cu(2+) with high affinity and partially by Cu(+) and Ag(+). This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319850 [Multi-domain]  Cd Length: 632  Bit Score: 41.14  E-value: 5.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077  38 IKVVITTGRPLKAISGLL----EELDLISDEDYIItfngglvqktngdiLDKS-ELTRAQLKRLHSTldplalPFDVLSD 112
Cdd:cd07552  292 IPLVVARSTSIAAKNGLLirnrEALERARDIDVVL--------------FDKTgTLTEGKFGVTDVI------TFDEYDE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 113 GIVYSL-ASQGNQSLYP-------QANPK-LKFVELTSFDDIP----ENIIYNKVVSVTNPEFLDKQILQFPKEL----- 174
Cdd:cd07552  352 DEILSLaAALEAGSEHPlaqaivsAAKEKgIRPVEVENFENIPgvgvEGTVNGKRYQVVSPKYLKELGLKYDEELvkrla 431

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 175 -----------------------------YNEFEIFKSRDIILEMM-------PKGVHKAAGLNQLiqHLNLLPEN---- 214
Cdd:cd07552  432 qqgntvsfliqdgevigaialgdeikpesKEAIRALKAQGITPVMLtgdneevAQAVAEELGIDEY--FAEVLPEDkakk 509

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489156077 215 ----------VMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEAVE 266
Cdd:cd07552  510 vkelqaegkkVAMVGDGVNDAPALAQADVGIAIGAGTDVAIESADVVLVK-SDPRDIVDFLE 570
HAD-SF-IIA TIGR01460
Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural ...
 8-58 6.48e-04

Haloacid Dehalogenase Superfamily Class (subfamily) IIA; This model represents one structural subclass of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The classes are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Class I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Class II consists of sequences in which the capping domain is found between the second and third motifs. Class III sequences have no capping domain in iether of these positions. The Class IIA capping domain is predicted by PSI-PRED to consist of a mixed alpha-beta fold with the basic pattern: Helix-Helix-Helix-Sheet-Helix-Loop-Sheet-Helix-Sheet-Helix. Presently, this subfamily encompasses a single equivalog model (TIGR01452) for the eukaryotic phosphoglycolate phosphatase, as well as four hypothetical equivalogs covering closely related sequences (TIGR01456 and TIGR01458 in eukaryotes, TIGR01457 in gram positive bacteria and TIGR01459 in gram negative bacteria). The Escherishia coli NagD gene and the Bacillus subtilus AraL gene are members of this subfamily but are not members of the any of the presently defined equivalogs within it. NagD is part of the NAG operon responsible for N-acetylglucosamine metabolism. The function of this gene is unknown. Genes from several organisms have been annotated as NagD, or NagD-like. However, without data on the presence of other members of this pathway, (such as in the case of Yersinia pestis) these assignments should not be given great weight. The AraL gene is similar: it is part of the L-arabinose operon, but the function is unknown. A gene from Halobacterium has been annotated as AraL, but no other Ara operon genes have been annotated. Many of the genes in this subfamily have been annotated as "pNPPase" "4-nitrophenyl phosphatase" or "NPPase". These all refer to the same activity versus a common lab test compound used to determine phosphatase activity. There is no evidence that this activity is physiologically relevant. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273637 [Multi-domain]  Cd Length: 236  Bit Score: 40.00  E-value: 6.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489156077    8 ALDLDGTLFNSQKVVsPENKKALRAARDKGIKVVITTGRPLKAISGLLEEL 58
Cdd:TIGR01460   2 LFDIDGVLWLGHKPI-PGAAEALNRLRAKGKPVVFLTNNSSRSEEDYAEKL 51
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 153-237 6.78e-04

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 38.15  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 153 KVVSVTN--PEFLDKQILQFPKELYNEFEIFKSRDIILEMMPKGVHKAAglnqliQHLNLLPENVMAMGDEENDLSMLKW 230
Cdd:cd01427   25 KLAIVTNrsREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLL------LKLGVDPEEVLFVGDSENDIEAARA 98


                 ....*...
gi 489156077 231 AG-LGVAM 237
Cdd:cd01427   99 AGgRTVAV 106
P-type_ATPase_Cu-like cd02094
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ...
 185-266 2.08e-03

P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319783 [Multi-domain]  Cd Length: 647  Bit Score: 39.38  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 185 DIILEMMPKGvhKAAglnqLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEA 264
Cdd:cd02094  509 EVIAEVLPED--KAE----KVKKLQAQGKKVAMVGDGINDAPALAQADVGIAIGSGTDVAIESADIVLMR-GDLRGVVTA 581


                 ..
gi 489156077 265 VE 266
Cdd:cd02094  582 ID 583
P-type_ATPases cd01431
ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ...
 213-266 2.88e-03

ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319764 [Multi-domain]  Cd Length: 319  Bit Score: 38.59  E-value: 2.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489156077 213 ENVMAMGDEENDLSMLKWAGLGVAMA-NGVAIAKETADAVTTRTNDESGVAEAVE 266
Cdd:cd01431  207 EVVAMTGDGVNDAPALKQADVGIAMGsTGTDVAKEAADIVLLDDNFATIVEAVEE 261
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 189-266 3.32e-03

P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 38.79  E-value: 3.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489156077 189 EMMPKgvHKAAglnqLIQHLNLLPENVMAMGDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEAVE 266
Cdd:cd07550  467 EALPE--DKAE----IVEKLQAEGRTVAFVGDGINDSPALSYADVGISMRGGTDIARETADVVLLE-DDLRGLAEAIE 537
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
209-257 3.52e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 37.06  E-value: 3.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489156077 209 NLLPENVMAMGDEENDLSMLKWAGLGVAM-----ANGVAIAKetADAVTTRTND 257
Cdd:COG4087   88 KLGAETTVAIGNGRNDVLMLKEAALGIAVigpegASVKALLA--ADIVVKSILD 139
ZntA COG2217
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
209-266 4.04e-03

Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];


Pssm-ID: 441819 [Multi-domain]  Cd Length: 717  Bit Score: 38.59  E-value: 4.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489156077 209 NLLPE-------------NVMAM-GDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESGVAEAVE 266
Cdd:COG2217  586 EVLPEdkaaavrelqaqgKKVAMvGDGINDAPALAAADVGIAMGSGTDVAIEAADIVLMR-DDLRGVPDAIR 656
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 5-45 5.52e-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: 36.23  E-value: 5.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489156077    5 KLLALDLDGTLFNSQKVVSPEN--------KKALRAARDKGIKVVITTG 45
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDerilypevPDALAELKEAGYKVVIVTN 49
P-type_ATPase_HM_ZosA_PfeT-like cd07551
P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which ...
 195-265 8.88e-03

P-type heavy metal-transporting ATPase, similar to Bacillus subtilis ZosA/PfeT which transports copper, and perhaps zinc under oxidative stress, and perhaps ferrous iron; Bacillus subtilis ZosA/PfeT (previously known as YkvW) transports copper, it may also transport zinc under oxidative stress and may also be involved in ferrous iron efflux. ZosA/PfeT is expressed under the regulation of the peroxide-sensing repressor PerR. It is involved in competence development. Disruption of the zosA/pfeT gene results in low transformability. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.


Pssm-ID: 319849 [Multi-domain]  Cd Length: 611  Bit Score: 37.23  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489156077 195 VHKAAGLNQLIQhlNLLPE-------------NVMAM-GDEENDLSMLKWAGLGVAMANGVAIAKETADAVTTRtNDESG 260
Cdd:cd07551  473 VAKELGIDEVVA--NLLPEdkvaiirelqqeyGTVAMvGDGINDAPALANADVGIAMGAGTDVALETADVVLMK-DDLSK 549


                 ....*
gi 489156077 261 VAEAV 265
Cdd:cd07551  550 LPYAI 554
 
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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