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Conserved domains on  [gi|1397890681|gb|PXW91526|]
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hypothetical protein DES38_105147 [Streptohalobacillus salinus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 1-260 3.47e-97

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: 285.26  E-value: 3.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgSYIVSFNGGKVTNCKTNaTIF 80
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLD---SPLITFNGALVYDPTGK-EIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIvteKNNPYTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKSL 160
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 ERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:cd07516   154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKE 233

                         250       260
                  ....*....|....*....|
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQ 260
Cdd:cd07516   234 AADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 1-260 3.47e-97

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: 285.26  E-value: 3.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgSYIVSFNGGKVTNCKTNaTIF 80
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLD---SPLITFNGALVYDPTGK-EIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIvteKNNPYTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKSL 160
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 ERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:cd07516   154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKE 233

                         250       260
                  ....*....|....*....|
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQ 260
Cdd:cd07516   234 AADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 2-257 1.43e-75

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 230.20  E-value: 1.43e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVTNcKTNATIFS 81
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGL---DDPVICYNGALIYD-ENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  82 STVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNNP--YTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKS 159
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNEleKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 160 LERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIK 239
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*...
gi 1397890681 240 EIADFVTLSNMEDGVAHV 257
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKA 254
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 1-257 1.55e-68

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: 212.51  E-value: 1.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVTNCKTNaTIF 80
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGL---DTPFITANGAAVIDDQGE-ILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKN-NPYTTIEADITGLPVIEVEDFVAAvTEEPVKILMVE-DPEILK 158
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNdPEYFTIFKKFLGEPKLEVVDIQYL-PDDILKILLLFlDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 159 SLERKLQR-TLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPED 237
Cdd:TIGR00099 156 LLIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|
gi 1397890681 238 IKEIADFVTLSNMEDGVAHV 257
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALA 255
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-262 1.65e-68

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 212.63  E-value: 1.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQFGSYIVSFNGGKVTNCKTNATIF 80
Cdd:PRK10513    5 LIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADGETVA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNN--PYTTIEADITGLPVI--EVEDFVAAVTEepVKILMVEDPEI 156
Cdd:PRK10513   85 QTALSYDDYLYLEKLSREVGVHFHALDRNTLYTANRDisYYTVHESFLTGIPLVfrEVEKMDPNLQF--PKVMMIDEPEI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 157 LKSLERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPE 236
Cdd:PRK10513  163 LDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIP 242

                         250       260
                  ....*....|....*....|....*.
gi 1397890681 237 DIKEIADFVTLSNMEDGVAHVVEQFI 262
Cdd:PRK10513  243 SVKEVAQFVTKSNLEDGVAFAIEKYV 268
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-261 2.41e-66

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: 204.60  E-value: 2.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQfgsYIVSFNGGKVTNCKtNATIF 80
Cdd:COG0561     4 LIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD---PLITSNGALIYDPD-GEVLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTyvgdvivteknnpyttieaditglpvievedfvaavteepvkilmvedpeilksl 160
Cdd:COG0561    80 ERPLDPEDVREILELLREHGLHLQV------------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 erklqrtlsdrfsVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:COG0561   105 -------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                         250       260
                  ....*....|....*....|.
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQF 261
Cdd:COG0561   172 AADYVTGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 1-260 3.47e-97

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: 285.26  E-value: 3.47e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgSYIVSFNGGKVTNCKTNaTIF 80
Cdd:cd07516     1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLD---SPLITFNGALVYDPTGK-EIL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIvteKNNPYTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKSL 160
Cdd:cd07516    77 ERLISKEDVKELEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDEDITKILFVGEDEELDEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 ERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:cd07516   154 IAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKE 233

                         250       260
                  ....*....|....*....|
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQ 260
Cdd:cd07516   234 AADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 2-257 1.43e-75

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 230.20  E-value: 1.43e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVTNcKTNATIFS 81
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGL---DDPVICYNGALIYD-ENGKILYS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  82 STVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNNP--YTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKS 159
Cdd:pfam08282  77 NPISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNEleKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 160 LERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIK 239
Cdd:pfam08282 157 LEKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVK 236

                         250
                  ....*....|....*...
gi 1397890681 240 EIADFVTLSNMEDGVAHV 257
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKA 254
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 1-257 1.55e-68

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: 212.51  E-value: 1.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVTNCKTNaTIF 80
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGL---DTPFITANGAAVIDDQGE-ILY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKN-NPYTTIEADITGLPVIEVEDFVAAvTEEPVKILMVE-DPEILK 158
Cdd:TIGR00099  77 KKPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNdPEYFTIFKKFLGEPKLEVVDIQYL-PDDILKILLLFlDPEDLD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 159 SLERKLQR-TLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPED 237
Cdd:TIGR00099 156 LLIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEE 235

                         250       260
                  ....*....|....*....|
gi 1397890681 238 IKEIADFVTLSNMEDGVAHV 257
Cdd:TIGR00099 236 LKALADYVTDSNNEDGVALA 255
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-262 1.65e-68

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 212.63  E-value: 1.65e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQFGSYIVSFNGGKVTNCKTNATIF 80
Cdd:PRK10513    5 LIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKAADGETVA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNN--PYTTIEADITGLPVI--EVEDFVAAVTEepVKILMVEDPEI 156
Cdd:PRK10513   85 QTALSYDDYLYLEKLSREVGVHFHALDRNTLYTANRDisYYTVHESFLTGIPLVfrEVEKMDPNLQF--PKVMMIDEPEI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 157 LKSLERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPE 236
Cdd:PRK10513  163 LDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIP 242

                         250       260
                  ....*....|....*....|....*.
gi 1397890681 237 DIKEIADFVTLSNMEDGVAHVVEQFI 262
Cdd:PRK10513  243 SVKEVAQFVTKSNLEDGVAFAIEKYV 268
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 1-261 2.41e-66

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: 204.60  E-value: 2.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQfgsYIVSFNGGKVTNCKtNATIF 80
Cdd:COG0561     4 LIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD---PLITSNGALIYDPD-GEVLY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKESVHIHTyvgdvivteknnpyttieaditglpvievedfvaavteepvkilmvedpeilksl 160
Cdd:COG0561    80 ERPLDPEDVREILELLREHGLHLQV------------------------------------------------------- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 erklqrtlsdrfsVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:COG0561   105 -------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKA 171

                         250       260
                  ....*....|....*....|.
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQF 261
Cdd:COG0561   172 AADYVTGSNDEDGVAEALEKL 192
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 1-261 2.32e-40

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: 138.51  E-value: 2.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgsYIVSFNGGKVTNCKTnaTIF 80
Cdd:cd07517     2 IVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGID----SYVSYNGQYVFFEGE--VIY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  81 SSTVRSKDVKDLYDISKKEsvhihtyvgdvivteknnpyttieaditGLPVIEVEDFVAAVTEEPVKILMVEDPEilksl 160
Cdd:cd07517    76 KNPLPQELVERLTEFAKEQ----------------------------GHPVSFYGQLLLFEDEEEEQKYEELRPE----- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 erklqrtlsdrFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKE 240
Cdd:cd07517   123 -----------LRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKE 191

                         250       260
                  ....*....|....*....|.
gi 1397890681 241 IADFVTLSNMEDGVAHVVEQF 261
Cdd:cd07517   192 IADYVTKDVDEDGILKALKHF 212
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 146-259 2.05e-26

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: 101.51  E-value: 2.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 146 VKILMVEDPEILKSLERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFA 225
Cdd:cd07518    71 FKFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYA 150

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1397890681 226 GLGVAMGNAPEDIKEIADFVTLSNMEDGVAHVVE 259
Cdd:cd07518   151 GYSYAMENAPEEVKAAAKYVAPSNNENGVLQVIE 184
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 2-262 8.02e-25

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 99.71  E-value: 8.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQ-----FGSYIVSFNGGKVtncktn 76
Cdd:PRK10530    6 IALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTpaiccNGTYLYDYQAKKV------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  77 atIFSSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKnnPYTTIEADIT---GLP------VIEVEDFVAAvTEEPVK 147
Cdd:PRK10530   80 --LEADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEH--PTGHVIRTLNwaqTLPpeqrptFTQVDSLAQA-ARQVNA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 148 I----LMVEDPEILKSLERKLQRTLS--------DRFSVVRskpyflefteKGVTKGTSLDFLIKQLDIKREEVIAVGDS 215
Cdd:PRK10530  155 IwkfaLTHEDLPQLQHFAKHVEHELGlecewswhDQVDIAR----------KGNSKGKRLTQWVEAQGWSMKNVVAFGDN 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1397890681 216 YNDQAMIEFAGLGVAMGNAPEDIKEIADFVTLSNMEDGVAHVVEQFI 262
Cdd:PRK10530  225 FNDISMLEAAGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYSHV 271
PRK10976 PRK10976
putative hydrolase; Provisional
 5-256 3.89e-24

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 97.81  E-value: 3.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   5 DLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgSYIVSFNGGKVTNCKTNaTIFSSTV 84
Cdd:PRK10976    8 DLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIK---SYMITSNGARVHDTDGN-LIFSHNL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  85 RSKDVKDLYDIsKKESVHIHT--YVGDVIVTEKNNPYttieaditglpviEVEDFVAAV------------TEEPVKILM 150
Cdd:PRK10976   84 DRDIASDLFGV-VHDNPDIITnvYRDDEWFMNRHRPE-------------EMRFFKEAVfkyqlyepgllePDGVSKVFF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 151 V-EDPEILKSLERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGV 229
Cdd:PRK10976  150 TcDSHEKLLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGC 229

                         250       260
                  ....*....|....*....|....*....
gi 1397890681 230 AMGNAPEDIKEIADF--VTLSNMEDGVAH 256
Cdd:PRK10976  230 IMGNAHQRLKDLLPEleVIGSNADDAVPH 258
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 2-261 6.11e-24

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 96.20  E-value: 6.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELAnelELHQFGSYIVSFNGGKVTNCKTNATIFs 81
Cdd:PRK01158    6 IAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAA---KLIGTSGPVIAENGGVISVGFDGKRIF- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  82 stvrskdvkdLYDISKKESV--HIHTYVGdvivtEKNNPYTTIEADITGLPVIEVEDFvaavteePVKILMvedpEILKS 159
Cdd:PRK01158   82 ----------LGDIEECEKAysELKKRFP-----EASTSLTKLDPDYRKTEVALRRTV-------PVEEVR----ELLEE 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 160 LERKLQrtlsdrfsVVRSKpYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIK 239
Cdd:PRK01158  136 LGLDLE--------IVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELK 206

                         250       260
                  ....*....|....*....|..
gi 1397890681 240 EIADFVTLSNMEDGVAHVVEQF 261
Cdd:PRK01158  207 EAADYVTEKSYGEGVAEAIEHL 228
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 1-231 1.17e-23

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: 94.75  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   1 MIVLDLDDTLLM-EDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVtncKTNATI 79
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNL---PLPLIAENGALI---FYPGEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  80 FssTVRSKDVKDLYDISKKESVHIHTYVgdvIVTeknnpyTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEILKS 159
Cdd:TIGR01484  75 L--YIEPSDVFEEILGIKFEEIGAELKS---LSE------HYVGTFIEDKAIAVAIHYVGAELGQELDSKMRERLEKIGR 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397890681 160 LERKLQRTLSDRfsvvrskpYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAM 231
Cdd:TIGR01484 144 NDLELEAIYSGK--------TDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 188-261 1.21e-20

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: 84.95  E-value: 1.21e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397890681 188 GVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEIADFVTLSNMEDGVAHVVEQF 261
Cdd:cd07514    65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKL 138
PLN02887 PLN02887
hydrolase family protein
 2-263 7.07e-19

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 85.70  E-value: 7.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHQFGSYIVSFN-----GGKVTNCKTN 76
Cdd:PLN02887  311 IFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAGKDGIISESSpgvflQGLLVYGRQG 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  77 ATIFSSTVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNNP--------YTTIEADItglpVIEVEDFVAAVteEPVKI 148
Cdd:PLN02887  391 REIYRSNLDQEVCREACLYSLEHKIPLIAFSQDRCLTLFDHPlvdslhtiYHEPKAEI----MSSVDQLLAAA--DIQKV 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 149 LMVEDPE-ILKSLERKLQRTLSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGL 227
Cdd:PLN02887  465 IFLDTAEgVSSVLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASL 544

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1397890681 228 GVAMGNAPEDIKEIADFVTLSNMEDGVAHVVEQFIF 263
Cdd:PLN02887  545 GVALSNGAEKTKAVADVIGVSNDEDGVADAIYRYAF 580
PRK15126 PRK15126
HMP-PP phosphatase;
5-256 1.91e-17

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 79.74  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   5 DLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELHqfgSYIVSFNGGKVtnCKTNATIFSSTV 84
Cdd:PRK15126    8 DMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLD---AYLITGNGTRV--HSLEGELLHRQD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  85 RSKDVKDLY---DISKKESVHIhtYVGDVIVTEKNNP------------YTTIeaDITGLPVIEVEdfvaavteepvKIL 149
Cdd:PRK15126   83 LPADVAELVlhqQWDTRASMHV--FNDDGWFTGKEIPallqahvysgfrYQLI--DLKRLPAHGVT-----------KIC 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 150 MVEDPEILKSLERKLQRTLSDR----FSVVRSkpyfLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFA 225
Cdd:PRK15126  148 FCGDHDDLTRLQIQLNEALGERahlcFSATDC----LEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSV 223

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1397890681 226 GLGVAMGNA-PEDIKEIADFVTLSNMED-GVAH 256
Cdd:PRK15126  224 GRGFIMGNAmPQLRAELPHLPVIGHCRNqAVSH 256
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 2-259 1.50e-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: 76.35  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLLMEDHTISPLTKRTLIKAQEEGIYVVLASGRPTYAMRELANELELhqfGSYIVSFNGGKVTNCKTNATIFS 81
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGT---PDPVIAENGGEISYNEGLDDIFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  82 StvrSKDVKDLYDISKKESVhihtyvgdvIVTEKNNPYTTiEADitglpvievedfvaavteePVKILMVEDPEILKSLE 161
Cdd:TIGR01482  78 A---YLEEEWFLDIVIAKTF---------PFSRLKVQYPR-RAS-------------------LVKMRYGIDVDTVREII 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 162 RKLQRTLsdrfsVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEI 241
Cdd:TIGR01482 126 KELGLNL-----VAVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEW 200

                         250
                  ....*....|....*....
gi 1397890681 242 ADFVTLS-NMEDGVAHVVE 259
Cdd:TIGR01482 201 ADYVTESpYGEGGAEAIGE 219
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 187-258 1.28e-14

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: 70.93  E-value: 1.28e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397890681 187 KGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEIADFVTLSNMEDGVAHVV 258
Cdd:TIGR01487 144 KGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNPYGEGVVEVL 215
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 153-253 2.09e-13

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: 67.76  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 153 DPEILKSLERKLqRTLSDRFSVVRSKP--YFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVA 230
Cdd:cd02605   131 DAAVIEQLEEML-LKAGLTVRIIYSSGlaYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVI 209

                          90       100
                  ....*....|....*....|...
gi 1397890681 231 MGNAPEDIKEIADFVTLSNMEDG 253
Cdd:cd02605   210 VGNAQPELLKWADRVTRSRLAKG 232
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 2-243 1.81e-08

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 53.79  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681   2 IVLDLDDTLlMEDHTISPLTKRTLIKA-QEEGIYVVLASGRpTYA-MRELANELELHqfGSYIVSfNGGKVTNCKTNATI 79
Cdd:PRK00192    7 VFTDLDGTL-LDHHTYSYEPAKPALKAlKEKGIPVIPCTSK-TAAeVEVLRKELGLE--DPFIVE-NGAAIYIPKNYFPF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  80 FSSTVRSKDV--------------KDLYDISKKESVHIhTYVGDVivteknnpytTIE--ADITGLPviEVEDFVAAVTE 143
Cdd:PRK00192   82 QPDGERLKGDywvielgppyeelrEILDEISDELGYPL-KGFGDL----------SAEevAELTGLS--GESARLAKDRE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 144 --EPVkiLMVEDPEILKSLERKLQR-----TLSDRFSVVRSkpyfleftekGVTKGTSLDFLIKQLDIKRE-EVIAVGDS 215
Cdd:PRK00192  149 fsEPF--LWNGSEAAKERFEEALKRlglkvTRGGRFLHLLG----------GGDKGKAVRWLKELYRRQDGvETIALGDS 216

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1397890681 216 YNDQAMIEFAGLGVAMGNA----PEDIKEIAD 243
Cdd:PRK00192  217 PNDLPMLEAADIAVVVPGPdgpnPPLLPGIAD 248
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 154-236 9.55e-08

Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 51.50  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 154 PEILKSLERKLQRTlSDRFSVVRSKPYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGN 233
Cdd:pfam05116 129 AAVLAELEQLLRKR-GLDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGN 207


                  ....
gi 1397890681 234 A-PE 236
Cdd:pfam05116 208 AqPE 211
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 191-243 3.43e-07

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: 49.84  E-value: 3.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1397890681 191 KGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMgNAPEDIKEIAD 243
Cdd:COG0560   156 KAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 191-246 4.00e-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: 48.29  E-value: 4.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1397890681 191 KGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEIADFVT 246
Cdd:cd01630    77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 190-230 2.75e-06

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 46.39  E-value: 2.75e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1397890681 190 TKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVA 230
Cdd:cd07500   137 RKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 1-68 6.15e-06

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: 43.92  E-value: 6.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397890681   1 MIVLDLDDTLLMEDhtispltkrTLIKAQEEGIYVVLASGRPTYAMRELANELELHQFGSYIVSFNGG 68
Cdd:cd01427     1 AVLFDLDGTLLAVE---------LLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGG 59
serB PRK11133
phosphoserine phosphatase; Provisional
 190-230 7.68e-05

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 43.40  E-value: 7.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1397890681 190 TKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVA 230
Cdd:PRK11133  248 YKADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 83-226 3.92e-04

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 40.26  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681  83 TVRSKDVKDLYDISKKESVHIHTYVGDVIVTEKNNPYTTIEADITGLPVIEVEDFVAAVTEEPVKILMVEDPEiLKSLER 162
Cdd:pfam00702  52 ARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDN-PEAAEA 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397890681 163 KLQRT-LSDRFSVVrskpYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAG 226
Cdd:pfam00702 131 LLRLLgLDDYFDVV----ISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
196-244 2.45e-03

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 37.98  E-value: 2.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1397890681 196 DFLIKQLDIKRE----------EVIAVGDSYNDQAMIEFAGLGVaMGNAPEDIkeIADF 244
Cdd:PRK13582  124 GYDLRQPDGKRQavkalkslgyRVIAAGDSYNDTTMLGEADAGI-LFRPPANV--IAEF 179
ATPase-IB_hvy TIGR01525
heavy metal translocating P-type ATPase; This model encompasses two equivalog models for the ...
 198-259 3.74e-03

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


Pssm-ID: 273669 [Multi-domain]  Cd Length: 558  Bit Score: 38.38  E-value: 3.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397890681 198 LIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEIADFVTLSNMEDGVAHVVE 259
Cdd:TIGR01525 442 IVKKLQEEGGPVAMVGDGINDAPALAAADVGIAMGSGSDVAIEAADIVLLNDDLRSLPTAID 503
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 152-235 5.14e-03

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


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 37.27  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 152 EDPEILKSLERKLQRTLSDRFSVVRSKpYFLEFTEKGVTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFA----GL 227
Cdd:cd01627   127 EGARAALELALHLASDLLKALEVVPGK-KVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRALngegGF 205


                  ....*...
gi 1397890681 228 GVAMGNAP 235
Cdd:cd01627   206 SVKVGEGP 213
P-type_ATPase_HM cd07550
P-type heavy metal-transporting ATPase; uncharacterized subfamily; Uncharacterized subfamily ...
 197-259 8.67e-03

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


Pssm-ID: 319848 [Multi-domain]  Cd Length: 592  Bit Score: 37.25  E-value: 8.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397890681 197 FLIKQLDIKREEVIAVGDSYNDQAMIEFAGLGVAMGNAPEDIKEIADfVTLsnMEDGVAHVVE 259
Cdd:cd07550   475 EIVEKLQAEGRTVAFVGDGINDSPALSYADVGISMRGGTDIARETAD-VVL--LEDDLRGLAE 534
HAD_PGPase cd04303
phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase ...
 161-252 9.05e-03

phosphoglycolate phosphatase, similar to Synechococcus elongates phosphoglycolate phosphatase PGP/CbbZ; Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. 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: 319799 [Multi-domain]  Cd Length: 201  Bit Score: 36.57  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397890681 161 ERKLQRT-LSDRFSVVRSKPYFleftekgvTKGTSLDFLIKQLDIKREEVIAVGDSYNDQAMIEFAGL---GVAMG-NAP 235
Cdd:cd04303   110 RRVLGPEeLISLFAVIEGSSLF--------GKAKKIRRVLRRTKITAAQVIYVGDETRDIEAARKVGLafaAVSWGyAKP 181

                          90
                  ....*....|....*..
gi 1397890681 236 EDIKEIADFVTLSNMED 252
Cdd:cd04303   182 EVLKALAPDHMLEDPED 198
 
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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