NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446207493|ref|WP_000285348|]
View 

MULTISPECIES: sugar/pyridoxal phosphate phosphatase YigL [Shigella]

Protein Classification

HAD family hydrolase( domain architecture ID 11485135)

The HAD (haloacid dehalogenase) family of hydrolase includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10976 PRK10976
putative hydrolase; Provisional
 1-265 0e+00

putative hydrolase; Provisional


:

Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASDLFGVVNDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFTCDSHEQLLPL 160
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLEPDGVSKVFFTCDSHEKLLPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:PRK10976 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLKD 240

                        250       260
                 ....*....|....*....|....*
gi 446207493 241 LHPELEVIGTNADDAVPHYLRKLYL 265
Cdd:PRK10976 241 LLPELEVIGSNADDAVPHYLRKLYL 265
 
Name Accession Description Interval E-value
PRK10976 PRK10976
putative hydrolase; Provisional
 1-265 0e+00

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASDLFGVVNDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFTCDSHEQLLPL 160
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLEPDGVSKVFFTCDSHEKLLPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:PRK10976 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLKD 240

                        250       260
                 ....*....|....*....|....*
gi 446207493 241 LHPELEVIGTNADDAVPHYLRKLYL 265
Cdd:PRK10976 241 LLPELEVIGSNADDAVPHYLRKLYL 265
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-260 4.73e-90

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: 267.21  E-value: 4.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    4 VVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   84 DRDIASDLFGVVNDNpDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYALY-EPGLLEPEGISKVFFTCDSHEQLLPLEQ 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKH-GLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEvVDIQYLPDDILKILLLFLDPEDLDLLIE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  163 AINA-RWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDL 241
Cdd:TIGR00099 160 ALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKAL 239

                         250
                  ....*....|....*....
gi 446207493  242 HPelEVIGTNADDAVPHYL 260
Cdd:TIGR00099 240 AD--YVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-260 2.16e-78

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 237.52  E-value: 2.16e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    5 VASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNLD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   85 RDIASDLFGVVNDNpDIITNVYRDDEWFM---NRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFtCDSHEQLLPLE 161
Cdd:pfam08282  81 KEAVKEIIEYLKEN-NLEILLYTDDGVYIlndNELEKILKELNYTKSFVPEIDDFELLEDEDINKILI-LLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  162 QAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDL 241
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*....
gi 446207493  242 HPelEVIGTNADDAVPHYL 260
Cdd:pfam08282 239 AD--YVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-262 3.54e-77

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 234.41  E-value: 3.54e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNL 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  84 DRDIASDLFGVVNDNPDIItNVYRDDEW---FMNRHRPEEMRFFKEAvfkyaLYEPGLLEPEGISKVFFtCDSHEQLLPL 160
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGI-NIYTNDDWadtIYEENEDDEIIKPAEI-----LDDLLLPPDEDITKILF-VGEDEELDEL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:cd07516  154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKE 233

                        250       260
                 ....*....|....*....|..
gi 446207493 241 LHPelEVIGTNADDAVPHYLRK 262
Cdd:cd07516  234 AAD--YVTLTNNEDGVAKAIEK 253
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-263 4.66e-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: 201.13  E-value: 4.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASDLfgvvndnpdiitnvyrddewfmnrhrpeeMRFFKEAVFKYALyepgllepegiskvfftcdsheqllpl 160
Cdd:COG0561   81 RPLDPEDVREI-----------------------------LELLREHGLHLQV--------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 eqainarwgdrvnVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:COG0561  105 -------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                        250       260
                 ....*....|....*....|...
gi 446207493 241 LHpeLEVIGTNADDAVPHYLRKL 263
Cdd:COG0561  172 AA--DYVTGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
PRK10976 PRK10976
putative hydrolase; Provisional
 1-265 0e+00

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASDLFGVVNDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFTCDSHEQLLPL 160
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDNPDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLEPDGVSKVFFTCDSHEKLLPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:PRK10976 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQRLKD 240

                        250       260
                 ....*....|....*....|....*
gi 446207493 241 LHPELEVIGTNADDAVPHYLRKLYL 265
Cdd:PRK10976 241 LLPELEVIGSNADDAVPHYLRKLYL 265
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-260 4.73e-90

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: 267.21  E-value: 4.73e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    4 VVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNL 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   84 DRDIASDLFGVVNDNpDIITNVYRDDEWFMNRHRPEEMRFFKEAVFKYALY-EPGLLEPEGISKVFFTCDSHEQLLPLEQ 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKH-GLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEvVDIQYLPDDILKILLLFLDPEDLDLLIE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  163 AINA-RWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDL 241
Cdd:TIGR00099 160 ALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKAL 239

                         250
                  ....*....|....*....
gi 446207493  242 HPelEVIGTNADDAVPHYL 260
Cdd:TIGR00099 240 AD--YVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-260 2.16e-78

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 237.52  E-value: 2.16e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    5 VASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNLD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   85 RDIASDLFGVVNDNpDIITNVYRDDEWFM---NRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFtCDSHEQLLPLE 161
Cdd:pfam08282  81 KEAVKEIIEYLKEN-NLEILLYTDDGVYIlndNELEKILKELNYTKSFVPEIDDFELLEDEDINKILI-LLDEEDLDELE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  162 QAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDL 241
Cdd:pfam08282 159 KELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAA 238

                         250
                  ....*....|....*....
gi 446207493  242 HPelEVIGTNADDAVPHYL 260
Cdd:pfam08282 239 AD--YVTDSNNEDGVAKAL 255
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-262 3.54e-77

phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 234.41  E-value: 3.54e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHNL 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  84 DRDIASDLFGVVNDNPDIItNVYRDDEW---FMNRHRPEEMRFFKEAvfkyaLYEPGLLEPEGISKVFFtCDSHEQLLPL 160
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGI-NIYTNDDWadtIYEENEDDEIIKPAEI-----LDDLLLPPDEDITKILF-VGEDEELDEL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 EQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:cd07516  154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKE 233

                        250       260
                 ....*....|....*....|..
gi 446207493 241 LHPelEVIGTNADDAVPHYLRK 262
Cdd:cd07516  234 AAD--YVTLTNNEDGVAKAIEK 253
PRK15126 PRK15126
HMP-PP phosphatase;
1-260 1.34e-75

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 231.12  E-value: 1.34e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASD-LFGVVNDNPDIitNVYRDDEWFMNRHRPEEMRFFKEAVFKYALYEPGLLEPEGISKVFFtCDSHEQLLP 159
Cdd:PRK15126  81 QDLPADVAELvLHQQWDTRASM--HVFNDDGWFTGKEIPALLQAHVYSGFRYQLIDLKRLPAHGVTKICF-CGDHDDLTR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 160 LEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLK 239
Cdd:PRK15126 158 LQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNAMPQLR 237

                        250       260
                 ....*....|....*....|.
gi 446207493 240 DLHPELEVIGTNADDAVPHYL 260
Cdd:PRK15126 238 AELPHLPVIGHCRNQAVSHYL 258
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-263 4.66e-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: 201.13  E-value: 4.66e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFA 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  81 HNLDRDIASDLfgvvndnpdiitnvyrddewfmnrhrpeeMRFFKEAVFKYALyepgllepegiskvfftcdsheqllpl 160
Cdd:COG0561   81 RPLDPEDVREI-----------------------------LELLREHGLHLQV--------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 161 eqainarwgdrvnVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:COG0561  105 -------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                        250       260
                 ....*....|....*....|...
gi 446207493 241 LHpeLEVIGTNADDAVPHYLRKL 263
Cdd:COG0561  172 AA--DYVTGSNDEDGVAEALEKL 192
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 8-241 5.73e-26

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: 101.15  E-value: 5.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   8 DLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYmITSNGARVHDlDGNLIFAHNLDRDI 87
Cdd:cd07517    6 DIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSY-VSYNGQYVFF-EGEVIYKNPLPQEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  88 asdlfgvvndnpdiitnVYRDDEWFMNRHRPeemrffkeavfkYALYepgllepegiSKVFFTCDSHEQLLPLEQAIN-- 165
Cdd:cd07517   84 -----------------VERLTEFAKEQGHP------------VSFY----------GQLLLFEDEEEEQKYEELRPElr 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446207493 166 -ARWGDrvnvsFSTltclEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDL 241
Cdd:cd07517  125 fVRWHP-----LST----DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEI 192
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-262 2.61e-23

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 95.48  E-value: 2.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   2 YQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAH 81
Cdd:PRK10530   3 YRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVLEA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  82 N-LDRDIASDLFGVVnDNPDIITNVYRDDEWFMNR---H--R--------PEEMR--FFK-----------EAVFKYALY 134
Cdd:PRK10530  83 DpLPVQQALQVIEML-DEHQIHGLMYVDDAMLYEHptgHviRtlnwaqtlPPEQRptFTQvdslaqaarqvNAIWKFALT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 135 EPGLLEPEGISKvfftcdSHEQLLPLEqaINARWGDRVNVSfstltclevmAGGVSKGHALEAVAKKLGYSLKDCIAFGD 214
Cdd:PRK10530 162 HEDLPQLQHFAK------HVEHELGLE--CEWSWHDQVDIA----------RKGNSKGKRLTQWVEAQGWSMKNVVAFGD 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446207493 215 GMNDAEMLSMAGKGCIMGSAHQRLKDlHPELeVIGTNADDAVPHYLRK 262
Cdd:PRK10530 224 NFNDISMLEAAGLGVAMGNADDAVKA-RADL-VIGDNTTPSIAEFIYS 269
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-231 1.08e-22

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: 92.44  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    4 VVASDLDGTLLSP-DHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDlDGNLIFAHN 82
Cdd:TIGR01484   1 LLFFDLDGTLLDPnAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFY-PGEILYIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   83 LD--RDIASDLFGVVNDnpdiITNVYRDDEWFMNRHRPEEMRffkeavfkyaLYEPGLLEPEgiskvfftcdshEQLLPL 160
Cdd:TIGR01484  80 SDvfEEILGIKFEEIGA----ELKSLSEHYVGTFIEDKAIAV----------AIHYVGAELG------------QELDSK 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446207493  161 EQAINARWGDR---VNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIM 231
Cdd:TIGR01484 134 MRERLEKIGRNdleLEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 3-265 1.01e-20

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 88.60  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKS---YMITSNGARV-HDLDGNLI 78
Cdd:PRK10513   4 KLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQpgdYCITNNGALVqKAADGETV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  79 FAHNLD-----------RDI-----ASDLFGVVNDNPDIitNVYRDDEWFMN----RHRP-EEM----RFFKEAVFKyal 133
Cdd:PRK10513  84 AQTALSyddylyleklsREVgvhfhALDRNTLYTANRDI--SYYTVHESFLTgiplVFREvEKMdpnlQFPKVMMID--- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 134 yEPGLLEpEGISKvfftcdsheqlLPLEQAinarwgDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFG 213
Cdd:PRK10513 159 -EPEILD-AAIAR-----------IPAEVK------ERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIG 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446207493 214 DGMNDAEMLSMAGKGCIMGSAHQRLKDLHPelEVIGTNADDAVPHYLRKLYL 265
Cdd:PRK10513 220 DQENDIAMIEYAGVGVAMGNAIPSVKEVAQ--FVTKSNLEDGVAFAIEKYVL 269
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-256 1.48e-19

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: 83.40  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLSPDHTL-SPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVhdldgnlifahn 82
Cdd:cd07518    2 LIATDMDGTFLNDDKTYdHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAVV------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  83 ldrdiasdlfgvvndnpdiitnvyrddewfmnrhrpeemrffkeaVFKYALYEPGLLEPEgiskvfftcdsheqllpLEQ 162
Cdd:cd07518   70 ---------------------------------------------YFKFTLNVPDEAAPD-----------------IID 87

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 163 AINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKDLh 242
Cdd:cd07518   88 ELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAA- 166

                        250
                 ....*....|....
gi 446207493 243 pELEVIGTNADDAV 256
Cdd:cd07518  167 -AKYVAPSNNENGV 179
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 4-245 2.75e-16

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: 75.85  E-value: 2.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLsPDHTLSPYAKETLKLL----TARGINFVFATGRHHVDVGQIRD--NLEIKSYMITSNGARVH------ 71
Cdd:cd02605    1 LLVSDLDETLV-GHDTNLQALERLQDLLeqltADNDVILVYATGRSPESVLELIKevMLPKPDFIISDVGTEIYygesgy 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  72 ---DLDGNLIFAHNLDRDIASDLFGVVNdnpdiitnvyrddewfmnrHRPEEmRFFKEAVFKYALYepglLEPEGISKVf 148
Cdd:cd02605   80 lepDTYWNEVLSEGWERFLFEAIADLFK-------------------QLKPQ-SELEQNPHKISFY----LDPQNDAAV- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 149 ftcdsheqLLPLEQAINArWGDRVNVSFST-----LTCLEVMAGgvsKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLS 223
Cdd:cd02605  135 --------IEQLEEMLLK-AGLTVRIIYSSglaydLDILPLGAG---KGEALRYLQEKWNFPPERTLVCGDSGNDIALLS 202

                        250       260
                 ....*....|....*....|..
gi 446207493 224 MAGKGCIMGSAHQRLKDLHPEL 245
Cdd:cd02605  203 TGTRGVIVGNAQPELLKWADRV 224
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 5-239 3.98e-13

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: 66.72  E-value: 3.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    5 VASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDldgnlifahnld 84
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGGEISY------------ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   85 rdiasdlfgvvNDNPDIITNVYRDDEWFMNRhRPEEMRFFKEAVFKYALyEPGLLepegisKVFFTCDSHEqllpLEQAI 164
Cdd:TIGR01482  69 -----------NEGLDDIFLAYLEEEWFLDI-VIAKTFPFSRLKVQYPR-RASLV------KMRYGIDVDT----VREII 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446207493  165 NARwGDRVNVSFSTLTcLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLK 239
Cdd:TIGR01482 126 KEL-GLNLVAVDSGFD-IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELK 198
PLN02887 PLN02887
hydrolase family protein
 8-256 4.53e-13

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 68.75  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   8 DLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEI--KSYMITS-------NGARVHDLDGNLI 78
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLagKDGIISEsspgvflQGLLVYGRQGREI 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  79 FAHNLDRDIASD--LFGVVNDNPDIItnvyrddewFMNRHRpeeMRFFKEAV---FKYALYEPG---------LLEPEGI 144
Cdd:PLN02887 394 YRSNLDQEVCREacLYSLEHKIPLIA---------FSQDRC---LTLFDHPLvdsLHTIYHEPKaeimssvdqLLAAADI 461

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 145 SKVFFTcDSHEQLlplEQAINARW----GDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAE 220
Cdd:PLN02887 462 QKVIFL-DTAEGV---SSVLRPYWseatGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIE 537

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446207493 221 MLSMAGKGCIMGSAHQRLKDLhpeLEVIG-TNADDAV 256
Cdd:PLN02887 538 MLQLASLGVALSNGAEKTKAV---ADVIGvSNDEDGV 571
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 4-244 3.86e-12

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: 64.21  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    4 VVASDLDGTLLSPD--HTLSPYAketlkLLTARGIN--FVFATGRHHVDVGQIRD--NLEIKSYMITSNGARVHDLDGNL 77
Cdd:pfam05116   4 LLVSDLDNTLVDGDneALARLNQ-----LLEAYRPDvgLVFATGRSLDSAKELLKekPLPTPDYLITSVGTEIYYGPSLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   78 ifahnLDRDIASDLfgvvndnpdiitnvyrDDEWFMNRHRpEEMRFFkeavfkyalyePGL-LEPE---GISKVFFTCDS 153
Cdd:pfam05116  79 -----PDQSWQEHL----------------DYHWDRQAVV-EALAKF-----------PGLtLQPEeeqRPHKVSYFLDP 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  154 H---EQLLPLEQAINARwGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCI 230
Cdd:pfam05116 126 EaaaAVLAELEQLLRKR-GLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVV 204

                         250
                  ....*....|....
gi 446207493  231 MGSAHQRLKDLHPE 244
Cdd:pfam05116 205 VGNAQPELLQWYLE 218
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 5-240 6.76e-12

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 63.22  E-value: 6.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    5 VASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRhhvdVGQIRDNLEIksyMITSNGARVHDlDGNLIFAHNLD 84
Cdd:TIGR01487   4 VAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGN----TVPFARALAV---LIGTSGPVVAE-NGGVIFYNKED 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   85 RDIASdlfgvvndnpdiitnvyRDDEWFMNRhrpEEMRFFKEAVFKYALYEPGLlepegiskvFFTCDSHEqllpLEQAI 164
Cdd:TIGR01487  76 IFLAN-----------------MEEEWFLDE---EKKKRFPRDRLSNEYPRASL---------VIMREGKD----VDEVR 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446207493  165 NARWGDRVNVSFSTLTcLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLKD 240
Cdd:TIGR01487 123 EIIKERGLNLVASGFA-IHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKE 197
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 4-249 2.00e-10

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 59.57  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLL-SPDHTLSPyAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGnlIFAHN 82
Cdd:PRK00192   6 LVFTDLDGTLLdHHTYSYEP-AKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIYIPKN--YFPFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  83 LDRDIASDLFGVVNDNPDIitnvyrdDEW--FMNRHRPEEMRFFK-------EAVFK----------------YAlyEPG 137
Cdd:PRK00192  83 PDGERLKGDYWVIELGPPY-------EELreILDEISDELGYPLKgfgdlsaEEVAEltglsgesarlakdreFS--EPF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 138 LLEPEGISKvfftcdshEQLLPLEQAINARW--GDRvnvsFSTLTclevmaGGVSKGHALEAVAKKLG--YSLKdCIAFG 213
Cdd:PRK00192 154 LWNGSEAAK--------ERFEEALKRLGLKVtrGGR----FLHLL------GGGDKGKAVRWLKELYRrqDGVE-TIALG 214

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446207493 214 DGMNDAEMLSMAGKGCIMGSAHQRLKDLHPELEVIG 249
Cdd:PRK00192 215 DSPNDLPMLEAADIAVVVPGPDGPNPPLLPGIADGE 250
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-239 2.84e-10

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 58.83  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGrhhvdvgqirdN-----------LEIKSYMITSNGAR 69
Cdd:PRK01158   2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATG-----------NvlcfaraaaklIGTSGPVIAENGGV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  70 V-HDLDGNLIFAHNLD-----RDIASDLFGVVNDNPDIITNVYRDDEWFMNRHRP-EEMRffkeavfkyalyepGLLEPE 142
Cdd:PRK01158  71 IsVGFDGKRIFLGDIEecekaYSELKKRFPEASTSLTKLDPDYRKTEVALRRTVPvEEVR--------------ELLEEL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 143 GISKVFFtcDSheqllpleqainarwgdrvnvSFStltcLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEML 222
Cdd:PRK01158 137 GLDLEIV--DS---------------------GFA----IHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMF 189

                        250
                 ....*....|....*..
gi 446207493 223 SMAGKGCIMGSAHQRLK 239
Cdd:PRK01158 190 EVAGFGVAVANADEELK 206
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 187-239 1.06e-09

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: 55.29  E-value: 1.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446207493 187 GGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGSAHQRLK 239
Cdd:cd07514   64 GGVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELK 116
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 4-246 6.58e-09

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 55.22  E-value: 6.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLSPdHTlspY----AKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHdLDGNLIF 79
Cdd:COG3769    5 LVFTDLDGTLLDH-DT---YswaaALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGAAIF-IPKGYFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  80 AHNLDRDIasdlfgvvnDNPDIITNVYRDDEW--FMNRHRPEEMRFFK-------------------EAvfkyAL----- 133
Cdd:COG3769   80 FPSGTADI---------DGYWVIELGKPYAEIraVLEQLREELGFKFTgfgdmsaeevaeltglsleQA----ALakqre 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 134 Y-EPGLLEpegiskvfftcDSHEQLLPLEQAI-----NARWGDRvnvsFSTLTclevmaGGVSKGHALEAVAKKlgYSLK 207
Cdd:COG3769  147 FsEPLLWL-----------GSDEALERFIAALaalglTVLRGGR----FLHLM------GGADKGKAVRWLVEQ--YRQR 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 446207493 208 DC-----IAFGDGMNDAEMLSMAGKGCIMGSAHqrlkDLHPELE 246
Cdd:COG3769  204 FGknvvtIALGDSPNDIPMLEAADIAVVIRSPH----GAPPELE 243
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 182-229 1.30e-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: 53.69  E-value: 1.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446207493 182 LEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGC 229
Cdd:COG0560  147 VGPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPV 194
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 4-244 3.88e-07

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


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 49.71  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    4 VVASDLDGTLLSPDHT-LSPyAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHdldgnlifahn 82
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYdWGP-AKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIY----------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   83 LDRdiasdLFGVVNDNPDIITNVyrddEWFMNRHRPEEMRffKEAVFKYALY---------EPGLLEPEGI--------S 145
Cdd:TIGR01486  69 GPR-----GWRPEPEYPVIALGI----PYEKIRARLRELS--EELGFKFRGLgdltdeeiaELTGLSRELArlaqrreyS 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  146 KVFFTCDSHEQLlpLEQAINAR-----WGDRvnvsFSTltcleVMAGGVSKGHALEAVAKKlgYSLKDC----IAFGDGM 216
Cdd:TIGR01486 138 ETILWSEERRER--FTEALVAVglevtHGGR----FYH-----VLGAGSDKGKAVNALKAF--YNQPGGaikvVGLGDSP 204

                         250       260
                  ....*....|....*....|....*...
gi 446207493  217 NDAEMLSMAGKGCIMGSAHQRLKDLHPE 244
Cdd:TIGR01486 205 NDLPLLEVVDLAVVVPGPNGPNVSLKPG 232
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 4-222 8.05e-07

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 48.90  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   4 VVASDLDGTLLSP-DHTLSPyAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGArvhdldgnLIFahn 82
Cdd:cd07507    1 VIFTDLDGTLLDHhTYSFDP-ARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGG--------AIF--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493  83 LDRD-IASDLFGVVNDNPDIITnvyrddewFMNRHRpeEMRFFKEAV---FKYALYEPGLLEPEGISKvfFTCdsheqlL 158
Cdd:cd07507   69 IPRGyFKFPGRCKSEGGYEVIE--------LGKPYR--EIRAALEKIreeTGFKITGFGDLTEEEIAE--LTG------L 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493 159 PLEQAINAR---------WGDRVN--VSFSTLTC---LEVMAGG---------VSKGHALEAVAK--KLGYSLKDCIAFG 213
Cdd:cd07507  131 PRERAALAKereysetiiLRSDEEedEKVLEALEergLKITKGGrfyhvlgagADKGKAVAILAAlyRQLYEAIVTVGLG 210


                 ....*....
gi 446207493 214 DGMNDAEML 222
Cdd:cd07507  211 DSPNDLPML 219
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 2-226 4.73e-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: 46.04  E-value: 4.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493    2 YQVVASDLDGTLLSPdhtlSPYAKETLKLLTAR---GINFVFATGRHHVDVGQIRDNLEIKSYmitsngarvhDLDGNLI 78
Cdd:pfam00702   1 IKAVVFDLDGTLTDG----EPVVTEAIAELASEhplAKAIVAAAEDLPIPVEDFTARLLLGKR----------DWLEELD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   79 FAHNLDRDIASDLFGVVNDNPDIITNVYrdDEWFmnrHRPEEMRFFKEavfkyalyepglLEPEGISKVFFTCDSHEQLL 158
Cdd:pfam00702  67 ILRGLVETLEAEGLTVVLVELLGVIALA--DELK---LYPGAAEALKA------------LKERGIKVAILTGDNPEAAE 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446207493  159 PLEQAINarwgdrVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAG 226
Cdd:pfam00702 130 ALLRLLG------LDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 3-85 1.73e-05

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


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 45.69  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446207493   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDLDGNLIFAHN 82
Cdd:PRK14502 417 KIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIFIPKDYFRLPFA 496


                 ...
gi 446207493  83 LDR 85
Cdd:PRK14502 497 YDR 499
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 4-75 6.05e-05

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: 41.23  E-value: 6.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446207493   4 VVASDLDGTLLspdhtlspyAKETLKLLTARGINFVFATGRHHVDVGQIRDNLEIKSYM---ITSNGARVHDLDG 75
Cdd:cd01427    1 AVLFDLDGTLL---------AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFdgiIGSDGGGTPKPKP 66
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 187-228 7.21e-05

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 42.53  E-value: 7.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446207493 187 GGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKG 228
Cdd:cd07500  134 DAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLG 175
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 188-226 9.41e-05

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 42.33  E-value: 9.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446207493  188 GVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAG 226
Cdd:TIGR01490 153 GEGKVHALAELLAEEQIDLKDSYAYGDSISDLPLLSLVG 191
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 190-226 5.58e-04

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 39.98  E-value: 5.58e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446207493 190 SKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAG 226
Cdd:cd02612  151 GKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVG 187
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 5-42 6.64e-04

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 38.22  E-value: 6.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446207493    5 VASDLDGTLLSpDHTLSPYAKETLKLLTARGINFVFAT 42
Cdd:pfam13344   1 FLFDIDGVLWR-GGEPIPGAAEALRALRAAGKPVVFVT 37
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
190-232 1.77e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 37.83  E-value: 1.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446207493 190 SKGHALE--AVAKKLGysLKDCIAFGDGMNDAEMLSMAGKG-CIMG 232
Cdd:COG4087   75 SGDQAEEklEFVEKLG--AETTVAIGNGRNDVLMLKEAALGiAVIG 118
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-42 3.24e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 38.17  E-value: 3.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446207493   1 MYQVVASDLDGTLLSpDHTLSPYAKETLKLLTARGINFVFAT 42
Cdd:COG0647    7 RYDAFLLDLDGVLYR-GDEPIPGAVEALARLRAAGKPVLFLT 47
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 191-230 5.94e-03

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 35.45  E-value: 5.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446207493 191 KGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCI 230
Cdd:cd01427   65 KPKPLLLLLLKLGVDPEEVLFVGDSENDIEAARAAGGRTV 104
PLN02382 PLN02382
probable sucrose-phosphatase
 182-244 7.51e-03

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 37.27  E-value: 7.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446207493 182 LEVMAGGVSKGHALEAVAKKL---GYSLKDCIAFGDGMNDAEMLSMAG-KGCIMGSAHQRLKDLHPE 244
Cdd:PLN02382 167 LDVLPQGAGKGQALAYLLKKLkaeGKAPVNTLVCGDSGNDAELFSVPDvYGVMVSNAQEELLQWYAE 233
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH