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Conserved domains on  [gi|446516899|ref|WP_000594245|]
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MULTISPECIES: Cof-type HAD-IIB family hydrolase [Bacillus]

Protein Classification

HAD family hydrolase( domain architecture ID 12089052)

HAD (haloacid dehalogenase) family hydrolase, part of the HAD 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.-.-.-|3.1.3.-
Gene Ontology:  GO:0016787
PubMed:  16889794
SCOP:  3001890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-258 3.52e-52

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


:

Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 170.50  E-value: 3.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    5 FVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATFD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   85 SSILPDLL-AMTNEDPYFRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLqKIDDTIFPNKISVGGTKESLQLLQK 163
Cdd:pfam08282  81 KEAVKEIIeYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDF-ELLEDEDINKILILLDEEDLDELEK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  164 KIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHA 243
Cdd:pfam08282 160 ELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAA 239

                         250
                  ....*....|....*.
gi 446516899  244 HYVVNHV-KDAVNHVI 258
Cdd:pfam08282 240 DYVTDSNnEDGVAKAL 255
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-258 3.52e-52

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 170.50  E-value: 3.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    5 FVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATFD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   85 SSILPDLL-AMTNEDPYFRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLqKIDDTIFPNKISVGGTKESLQLLQK 163
Cdd:pfam08282  81 KEAVKEIIeYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDF-ELLEDEDINKILILLDEEDLDELEK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  164 KIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHA 243
Cdd:pfam08282 160 ELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAA 239

                         250
                  ....*....|....*.
gi 446516899  244 HYVVNHV-KDAVNHVI 258
Cdd:pfam08282 240 DYVTDSNnEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-258 2.64e-45

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: 152.81  E-value: 2.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    4 MFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATF 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   84 DSSILPDLLAMTNEDPY-FRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLQKIDDTIFpnKISVGGTKESLQLLQ 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLdVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK--ILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  163 KKIDEK-FHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKN 241
Cdd:TIGR00099 159 EALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 446516899  242 HAHYVVNHVK-DAVNHVI 258
Cdd:TIGR00099 239 LADYVTDSNNeDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-260 4.33e-45

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: 152.36  E-value: 4.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   4 MFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATF 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  84 DSSILPDLLAmtnedpYFRYVSDEHNYYIEEKTPFIQ-ELEQQVTMTSVEEPNLLQKIDDTIFPNKISVGGTKESLQLLQ 162
Cdd:cd07516   81 SKEDVKELEE------FLRKLGIGINIYTNDDWADTIyEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDELI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 163 KKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNH 242
Cdd:cd07516  155 AKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEA 234

                        250
                 ....*....|....*....
gi 446516899 243 AHYV-VNHVKDAVNHVIAH 260
Cdd:cd07516  235 ADYVtLTNNEDGVAKAIEK 253
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-260 6.18e-40

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: 136.80  E-value: 6.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLS 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  81 ATFDSSILPDLLAmtnedpyfryVSDEHNYYIeektpfiqeleqqvtmtsveepnllqkiddtifpnkisvggtkeslql 160
Cdd:COG0561   81 RPLDPEDVREILE----------LLREHGLHL------------------------------------------------ 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 161 lqkkidekfhgkVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVK 240
Cdd:COG0561  103 ------------QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVK 170

                        250       260
                 ....*....|....*....|.
gi 446516899 241 NHAHYVV-NHVKDAVNHVIAH 260
Cdd:COG0561  171 AAADYVTgSNDEDGVAEALEK 191
PRK15126 PRK15126
HMP-PP phosphatase;
1-235 2.56e-17

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 79.35  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLS 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  81 ATFDSSILPDLLAMTNEDPYFRYVSDEHNYYIEEKTPfiqELEQQVTMTSVEepnlLQKIDDTIFP----NKISVGGTKE 156
Cdd:PRK15126  81 QDLPADVAELVLHQQWDTRASMHVFNDDGWFTGKEIP---ALLQAHVYSGFR----YQLIDLKRLPahgvTKICFCGDHD 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446516899 157 SLQLLQKKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQA 235
Cdd:PRK15126 154 DLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNA 232
 
Name Accession Description Interval E-value
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 5-258 3.52e-52

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 170.50  E-value: 3.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    5 FVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATFD 84
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKILYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   85 SSILPDLL-AMTNEDPYFRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLqKIDDTIFPNKISVGGTKESLQLLQK 163
Cdd:pfam08282  81 KEAVKEIIeYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDF-ELLEDEDINKILILLDEEDLDELEK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  164 KIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHA 243
Cdd:pfam08282 160 ELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAA 239

                         250
                  ....*....|....*.
gi 446516899  244 HYVVNHV-KDAVNHVI 258
Cdd:pfam08282 240 DYVTDSNnEDGVAKAL 255
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 4-258 2.64e-45

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: 152.81  E-value: 2.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    4 MFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATF 83
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEILYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   84 DSSILPDLLAMTNEDPY-FRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLQKIDDTIFpnKISVGGTKESLQLLQ 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLdVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK--ILLLFLDPEDLDLLI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  163 KKIDEK-FHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKN 241
Cdd:TIGR00099 159 EALNKLeLEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKA 238

                         250
                  ....*....|....*...
gi 446516899  242 HAHYVVNHVK-DAVNHVI 258
Cdd:TIGR00099 239 LADYVTDSNNeDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 4-260 4.33e-45

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: 152.36  E-value: 4.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   4 MFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLSATF 83
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEILERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  84 DSSILPDLLAmtnedpYFRYVSDEHNYYIEEKTPFIQ-ELEQQVTMTSVEEPNLLQKIDDTIFPNKISVGGTKESLQLLQ 162
Cdd:cd07516   81 SKEDVKELEE------FLRKLGIGINIYTNDDWADTIyEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDELI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 163 KKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNH 242
Cdd:cd07516  155 AKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEA 234

                        250
                 ....*....|....*....
gi 446516899 243 AHYV-VNHVKDAVNHVIAH 260
Cdd:cd07516  235 ADYVtLTNNEDGVAKAIEK 253
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-260 6.18e-40

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: 136.80  E-value: 6.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLS 80
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGEVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  81 ATFDSSILPDLLAmtnedpyfryVSDEHNYYIeektpfiqeleqqvtmtsveepnllqkiddtifpnkisvggtkeslql 160
Cdd:COG0561   81 RPLDPEDVREILE----------LLREHGLHL------------------------------------------------ 102

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 161 lqkkidekfhgkVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVK 240
Cdd:COG0561  103 ------------QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVK 170

                        250       260
                 ....*....|....*....|.
gi 446516899 241 NHAHYVV-NHVKDAVNHVIAH 260
Cdd:COG0561  171 AAADYVTgSNDEDGVAEALEK 191
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 147-258 9.34e-24

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: 94.57  E-value: 9.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 147 NKISVGGTKESLQLLQKKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLT 226
Cdd:cd07518   71 FKFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYA 150

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446516899 227 PHSFAMSQADNAVKNHAHYVVNH-VKDAVNHVI 258
Cdd:cd07518  151 GYSYAMENAPEEVKAAAKYVAPSnNENGVLQVI 183
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 4-232 3.89e-21

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


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 88.21  E-value: 3.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    4 MFVSDIDGTMMQHGGL-IDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLlsAT 82
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAHeLSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILY--IE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   83 FDSSILPDLLAMTNEDPYFRYVSDEH--NYYIEEKtpfiqELEQQVTMTSveePNLLQKIDDTIFpnkisvggtkESLQL 160
Cdd:TIGR01484  79 PSDVFEEILGIKFEEIGAELKSLSEHyvGTFIEDK-----AIAVAIHYVG---AELGQELDSKMR----------ERLEK 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446516899  161 LqKKIDEKFHgkvsTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAM 232
Cdd:TIGR01484 141 I-GRNDLELE----AIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK15126 PRK15126
HMP-PP phosphatase;
1-235 2.56e-17

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 79.35  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLS 80
Cdd:PRK15126   1 MARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  81 ATFDSSILPDLLAMTNEDPYFRYVSDEHNYYIEEKTPfiqELEQQVTMTSVEepnlLQKIDDTIFP----NKISVGGTKE 156
Cdd:PRK15126  81 QDLPADVAELVLHQQWDTRASMHVFNDDGWFTGKEIP---ALLQAHVYSGFR----YQLIDLKRLPahgvTKICFCGDHD 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446516899 157 SLQLLQKKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQA 235
Cdd:PRK15126 154 DLTRLQIQLNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGNA 232
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 8-250 1.03e-16

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: 76.49  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   8 DIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHrISVNGVFVYTHENKqLLSATFDSSI 87
Cdd:cd07517    6 DIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDSY-VSYNGQYVFFEGEV-IYKNPLPQEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  88 LPDLLAMTNEDPYFryVSdehnyYIEEKTPFIQEleqqvtmtsveepnllqkiddtifpnkisvggtkESLQLLQKKIDE 167
Cdd:cd07517   84 VERLTEFAKEQGHP--VS-----FYGQLLLFEDE----------------------------------EEEQKYEELRPE 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 168 ----KFHgKVSTfisaeqclDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHA 243
Cdd:cd07517  123 lrfvRWH-PLST--------DVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIA 193


                 ....*..
gi 446516899 244 HYVVNHV 250
Cdd:cd07517  194 DYVTKDV 200
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-248 6.87e-16

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: 74.42  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    6 VSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGvfvythenkqllsatfdS 85
Cdd:TIGR01482   2 ASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENG-----------------G 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   86 SIlpdllamtnedpYFRYVSDEHNYYIEEKTPFIQELEQQVTMTSveepNLLQKIDDTIFPNKISVGGTKESLQLLQKKI 165
Cdd:TIGR01482  65 EI------------SYNEGLDDIFLAYLEEEWFLDIVIAKTFPFS----RLKVQYPRRASLVKMRYGIDVDTVREIIKEL 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  166 DEKFHGKVSTFisaeqCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHY 245
Cdd:TIGR01482 129 GLNLVAVDSGF-----DIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADY 203


                  ...
gi 446516899  246 VVN 248
Cdd:TIGR01482 204 VTE 206
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 4-249 7.99e-15

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: 72.00  E-value: 7.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   4 MFVSDIDGTMMQHGglIDEQDVAALRSLAEQ-----NVILCFASGRLDNEIADLMKAVNTNF--HRISVNGVFVYTHENK 76
Cdd:cd02605    1 LLVSDLDETLVGHD--TNLQALERLQDLLEQltadnDVILVYATGRSPESVLELIKEVMLPKpdFIISDVGTEIYYGESG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  77 QLLSATFDSSILP------------DLLAMTNEDPYFRYVSDEHNYYIEEK--TPFIQELEQQvtmtsveepnlLQKIDD 142
Cdd:cd02605   79 YLEPDTYWNEVLSegwerflfeaiaDLFKQLKPQSELEQNPHKISFYLDPQndAAVIEQLEEM-----------LLKAGL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 143 TIFPNkISVGGTKEslqllqkkidekfhgkvstfisaeqcLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPM 222
Cdd:cd02605  148 TVRII-YSSGLAYD--------------------------LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIAL 200

                        250       260
                 ....*....|....*....|....*...
gi 446516899 223 FSLTPHSFAMSQA-DNAVKNHAHYVVNH 249
Cdd:cd02605  201 LSTGTRGVIVGNAqPELLKWADRVTRSR 228
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-246 2.73e-13

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 67.31  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNV--------ILCFASGrldneiadLMKAVNTNFHRISVNGVFVYT 72
Cdd:PRK01158   2 KIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIpvilatgnVLCFARA--------AAKLIGTSGPVIAENGGVISV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  73 HENKQllsatfdSSILPDllaMTNEDPYFRYVSdehNYYIEEKTPFIQ-ELEQQVTMTSVEEPNLLQKIDDTIfpnkisv 151
Cdd:PRK01158  74 GFDGK-------RIFLGD---IEECEKAYSELK---KRFPEASTSLTKlDPDYRKTEVALRRTVPVEEVRELL------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 152 ggtkESLQLLQKKIDEKFhgkvstfisaeqCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFA 231
Cdd:PRK01158 134 ----EELGLDLEIVDSGF------------AIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVA 197

                        250
                 ....*....|....*
gi 446516899 232 MSQADNAVKNHAHYV 246
Cdd:PRK01158 198 VANADEELKEAADYV 212
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 190-247 1.86e-12

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


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 62.99  E-value: 1.86e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446516899 190 VSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYVV 247
Cdd:cd07514   66 VDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVT 123
PLN02887 PLN02887
hydrolase family protein
 8-258 5.00e-12

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 65.67  E-value: 5.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   8 DIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHR---------ISVNGVFVYTHENKQL 78
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDgiisesspgVFLQGLLVYGRQGREI 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  79 LSATFDSSILPD--LLAMTNEDPYFRYVSDE-------------HNYYIEEKTPFIQELEQQVTMTSVeepnllQKIddt 143
Cdd:PLN02887 394 YRSNLDQEVCREacLYSLEHKIPLIAFSQDRcltlfdhplvdslHTIYHEPKAEIMSSVDQLLAAADI------QKV--- 464

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 144 IFPNkisvggTKESLQL-LQKKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPM 222
Cdd:PLN02887 465 IFLD------TAEGVSSvLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEM 538

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446516899 223 FSLTPHSFAMSQADNAVKNHAHYV-VNHVKDAVNHVI 258
Cdd:PLN02887 539 LQLASLGVALSNGAEKTKAVADVIgVSNDEDGVADAI 575
PRK10976 PRK10976
putative hydrolase; Provisional
 1-241 1.66e-11

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 62.76  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   1 MIKMFVSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLS 80
Cdd:PRK10976   1 MYQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  81 ATFDSSILPDLLAMTNEDP-----YFRyvsDEH---NYYIEEKTPFIQEleqQVTMTSVEEPNLLQkiddtifPNKIS-- 150
Cdd:PRK10976  81 HNLDRDIASDLFGVVHDNPdiitnVYR---DDEwfmNRHRPEEMRFFKE---AVFKYQLYEPGLLE-------PDGVSkv 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 151 --VGGTKESLQLLQKKIDEKFHGKVSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPH 228
Cdd:PRK10976 148 ffTCDSHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGK 227

                        250
                 ....*....|...
gi 446516899 229 SFAMSQADNAVKN 241
Cdd:PRK10976 228 GCIMGNAHQRLKD 240
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 185-246 5.02e-11

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: 60.91  E-value: 5.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446516899  185 VMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYV 246
Cdd:TIGR01487 141 IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYV 202
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 3-223 3.66e-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: 58.82  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    3 KMFVSDIDGTMMQHggliDEQDVAALRSLAEQ---NVILCFASGRLDNEIADLMKAVNTNFHRI---SVNGVFVYTHEN- 75
Cdd:pfam05116   3 LLLVSDLDNTLVDG----DNEALARLNQLLEAyrpDVGLVFATGRSLDSAKELLKEKPLPTPDYlitSVGTEIYYGPSLv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   76 -----KQLLSATFDSSI-------LPDLL--AMTNEDPYfrYVSdehnYYIEEKT--PFIQELEQQvtmtsveepnllqk 139
Cdd:pfam05116  79 pdqswQEHLDYHWDRQAvvealakFPGLTlqPEEEQRPH--KVS----YFLDPEAaaAVLAELEQL-------------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  140 iddtifpnkisvggtkeslqLLQKKIDEKFHgkvstfISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYND 219
Cdd:pfam05116 139 --------------------LRKRGLDVKVI------YSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGND 192


                  ....
gi 446516899  220 IPMF 223
Cdd:pfam05116 193 EELF 196
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 192-246 7.06e-09

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: 53.90  E-value: 7.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446516899 192 KGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYV 246
Cdd:COG1778   84 KLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYV 138
PLN02382 PLN02382
probable sucrose-phosphatase
 4-224 1.04e-07

probable sucrose-phosphatase


Pssm-ID: 178008 [Multi-domain]  Cd Length: 413  Bit Score: 52.29  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   4 MFVSDIDGTMMQHGgliDEQDVAALR--SLAE----QNVILCFASGRLDNEIADLMKavntnfhrisvngvfvytheNKQ 77
Cdd:PLN02382  11 MIVSDLDHTMVDHH---DPENLSLLRfnALWEaeyrHDSLLVFSTGRSPTLYKELRK--------------------EKP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  78 LLSatfdssilPDLLAMTnedpyfryVSDEHNYYiEEKTP---FIQELEQQ-----VTMTSVEEPNLLQKIDDTIFPNKI 149
Cdd:PLN02382  68 LLT--------PDITIMS--------VGTEIAYG-ESMVPdhgWVEYLNKKwdreiVVEETSKFPELKLQPETEQRPHKV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 150 SVGGTKESLQLLQKKIDEKFHGK---VSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIK---PEEIACIGDSYNDIPMF 223
Cdd:PLN02382 131 SFYVDKKKAQEVIKELSERLEKRgldVKIIYSGGIDLDVLPQGAGKGQALAYLLKKLKAEgkaPVNTLVCGDSGNDAELF 210


                 .
gi 446516899 224 S 224
Cdd:PLN02382 211 S 211
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 192-246 2.51e-07

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 49.06  E-value: 2.51e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446516899 192 KGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYV 246
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYV 131
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 178-258 2.44e-06

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 47.77  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 178 SAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYVV-NHVKDAVNH 256
Cdd:PRK10513 183 SAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTkSNLEDGVAF 262


                 ..
gi 446516899 257 VI 258
Cdd:PRK10513 263 AI 264
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 8-258 3.94e-06

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 46.94  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   8 DIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKQLLsatfDSSI 87
Cdd:PRK10530   9 DLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL----EADP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  88 LP-----DLLAMTNED--PYFRYVSDEHNY-----YIEEKTPFIQEL--EQQVTMTSVEepNLLQKIDDTIFPNKISVGG 153
Cdd:PRK10530  85 LPvqqalQVIEMLDEHqiHGLMYVDDAMLYehptgHVIRTLNWAQTLppEQRPTFTQVD--SLAQAARQVNAIWKFALTH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899 154 TK-ESLQLLQKKIDEK--------FHGKVstfisaeqclDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFS 224
Cdd:PRK10530 163 EDlPQLQHFAKHVEHElglecewsWHDQV----------DIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLE 232

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446516899 225 LTPHSFAMSQADNAVKNHAHYVV-NHVKDAVNHVI 258
Cdd:PRK10530 233 AAGLGVAMGNADDAVKARADLVIgDNTTPSIAEFI 267
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 166-244 6.74e-06

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: 45.98  E-value: 6.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446516899 166 DEKFHGKVSTFISAEQcldvmppnvSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSqADNAVKNHAH 244
Cdd:COG0560  139 DGRLTGEVVGPIVDGE---------GKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAVN-PDPALREAAD 207
SPP_plant-cyano TIGR01485
sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate ...
 4-225 3.34e-05

sucrose-6F-phosphate phosphohydrolase; This model describes the sucrose phosphate phosphohydrolase from plants and cyanobacteria (SPP). SPP is a member of the Class IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. SPP catalyzes the final step in the biosynthesis of sucrose, a critically important molecule for plants. Sucrose phosphate synthase (SPS), the prior step in the biosynthesis of sucrose, contains a domain which exhibits considerable similarity to SPP albeit without conservation of the catalytic residues. The catalytic machinery of the synthase resides in another domain. It seems likely that the phosphatase-like domain is involved in substrate binding, possibly binding both substrates in a "product-like" orientation prior to ligation by the synthase catalytic domain.


Pssm-ID: 130549  Cd Length: 249  Bit Score: 44.03  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    4 MFVSDIDGTMMQHGGLiDEQDVAALRSLAE----QNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVYTHENKqll 79
Cdd:TIGR01485   3 LLVSDLDNTLVDHTDG-DNQALLRLNALLEdhrgEDSLLVYSTGRSPHSYKELQKQKPLLTPDIWVTSVGSEIYYGG--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   80 satfdssilpdllAMTNEDPYFRYVSD--EHNYYIEEKTPFiQELEQQvtmtsveePNLLQKiddtifPNKISVGGTKES 157
Cdd:TIGR01485  79 -------------AEVPDQHWAEYLSEkwQRDIVVAITDKF-EELKPQ--------PDLEQR------PHKVSFFLDPEA 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446516899  158 LQLLQKKIDEKFHGK---VSTFISAEQCLDVMPPNVSKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSL 225
Cdd:TIGR01485 131 APEVIKQLTEMLKETgldVKLIYSSGKDLDILPQGSGKGQALQYLLQKLAMEPSQTLVCGDSGNDIELFEI 201
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 6-223 3.96e-05

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: 43.93  E-value: 3.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899    6 VSDIDGTMMQHGGLIDEQDVAALRSLAEQNVILCFASGRLDNEIADLMKAVNTNFHRISVNGVFVY------TH-ENKQL 78
Cdd:TIGR01486   3 FTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIYgprgwrPEpEYPVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899   79 LSATFDSSILPDLLAMTNEDPY-FRYVSDEHNYYIEEKTPFIQELEQQVTMTSVEEPNLLQKIDDTIFPNKISVGGTkes 157
Cdd:TIGR01486  83 ALGIPYEKIRARLRELSEELGFkFRGLGDLTDEEIAELTGLSRELARLAQRREYSETILWSEERRERFTEALVAVGL--- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446516899  158 lqllqkkidEKFHG-KVSTFISAeqcldvmppNVSKGSAISVLLNEFQIKPEEIACI--GDSYNDIPMF 223
Cdd:TIGR01486 160 ---------EVTHGgRFYHVLGA---------GSDKGKAVNALKAFYNQPGGAIKVVglGDSPNDLPLL 210
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 166-249 9.46e-05

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 42.34  E-value: 9.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446516899  166 DEKFHGKVSTFISAEQCldvmppnvsKGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSlTPHSFAMSQADNAVKNHAHY 245
Cdd:TIGR00338 136 DGKLTGLVEGPIVDASY---------KGKTLLILLRKEGISPENTVAVGDGANDLSMIK-AAGLGIAFNAKPKLQQKADI 205


                  ....
gi 446516899  246 VVNH 249
Cdd:TIGR00338 206 CINK 209
osmo_MPG_phos TIGR02461
mannosyl-3-phosphoglycerate phosphatase; Members of this family are ...
 189-223 4.54e-04

mannosyl-3-phosphoglycerate phosphatase; Members of this family are mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70). It acts sequentially after mannosyl-3-phosphoglycerate synthase (EC 2.4.1.217) in a two-step pathway of biosynthesis of the compatible solute mannosylglycerate, a typical osmolyte of thermophiles.


Pssm-ID: 131514  Cd Length: 225  Bit Score: 40.53  E-value: 4.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 446516899  189 NVSKGSAISVLLNEFQIKPEEIAC--IGDSYNDIPMF 223
Cdd:TIGR02461 179 GSDKGKAIKRLLDLYKLRPGAIESvgLGDSENDFPMF 215
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 189-223 1.47e-03

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 39.15  E-value: 1.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446516899 189 NVSKGSAISVLLNEFQiKPEEIACI--GDSYNDIPMF 223
Cdd:PRK00192 188 GGDKGKAVRWLKELYR-RQDGVETIalGDSPNDLPML 223
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 192-223 1.79e-03

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: 38.34  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446516899  192 KGSAISVLLNEFQIKPEEIACIGDSYNDIPMF 223
Cdd:pfam00702 156 KPEIYLAALERLGVKPEEVLMVGDGVNDIPAA 187
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 192-226 1.89e-03

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


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 38.10  E-value: 1.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446516899  192 KGSAISVLLNEFQIKPEEIACIGDSYNDIPMFSLT 226
Cdd:TIGR01488 143 KGKVLKELLEESKITLKKIIAVGDSVNDLPMLKLA 177
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 191-223 5.98e-03

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: 36.76  E-value: 5.98e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446516899 191 SKGSAISVLLNEFQIKPEEIACIGDSYNDIPMF 223
Cdd:cd07500  137 RKAETLQELAARLGIPLEQTVAVGDGANDLPML 169
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
199-246 8.67e-03

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 36.45  E-value: 8.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446516899 199 LLNEFQIKPEEIACIGDSYNDIPMFSLTPHSFAMSQADNAVKNHAHYV 246
Cdd:PRK09484 104 LLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYV 151
 
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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