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Conserved domains on  [gi|517180560|ref|WP_018369378|]
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Cof-type HAD-IIB family hydrolase [Streptococcus marimammalium]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 1.03e-82

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


:

Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 248.66  E-value: 1.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   6 LLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqEDYSITFNGGLIQKNNGHCLFQ 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  86 KTLSREDVENITEMLLSLGLPVDIISDSKsytltapNHNSLYPT--ANVQLDFHDIKTLDELPHGIVYNKIVTVFDANYL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDD-------WADTIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 DRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 517180560 244 VRKEFERTTsRTNDESGVAEAIEK 267
Cdd:cd07516  231 VKEAADYVT-LTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 1.03e-82

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


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 248.66  E-value: 1.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   6 LLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqEDYSITFNGGLIQKNNGHCLFQ 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  86 KTLSREDVENITEMLLSLGLPVDIISDSKsytltapNHNSLYPT--ANVQLDFHDIKTLDELPHGIVYNKIVTVFDANYL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDD-------WADTIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 DRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 517180560 244 VRKEFERTTsRTNDESGVAEAIEK 267
Cdd:cd07516  231 VKEAADYVT-LTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-265 1.25e-64

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 202.85  E-value: 1.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    7 LALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKsqeDYSITFNGGLIQKNNGHCLFQK 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLD---DPVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   87 TLSREDVENITEMLLSLGLPVDIISDSKSYTLTAPNHNSLYPTANVQLDFHDIKTLDELPHGIVYNKIVTVFDANYLDRQ 166
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  167 LPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVrK 246
Cdd:pfam08282 158 EKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV-K 236

                         250
                  ....*....|....*....
gi 517180560  247 EFERTTSRTNDESGVAEAI 265
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 4-271 2.83e-63

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 199.92  E-value: 2.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   4 IKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSQEDYSITFNGGLIQK-NNGHC 82
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKaADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  83 LFQKTLSREDVENITEMLLSLGLPVDIISDSKSYTltaPNHN-SLYPTANVQLDFHDIK--TLDELPHGIVYNKIVTVFD 159
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT---ANRDiSYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMIDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 160 ANYLDRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKN 239
Cdd:PRK10513 160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 517180560 240 ASVAVrKEFERTTSRTNDESGVAEAIEKYILR 271
Cdd:PRK10513 240 AIPSV-KEVAQFVTKSNLEDGVAFAIEKYVLN 270
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-268 3.17e-60

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: 189.19  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   4 IKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqEDYSITFNGGLIQKNNGHCL 83
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIYDPDGEVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  84 FQKTLSREDVENITEMLLSLGLPVDIIsdsksytltapnhnslyptanvqldfhdiktldelphgivynkivtvfdanyl 163
Cdd:COG0561   79 YERPLDPEDVREILELLREHGLHLQVV----------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 drqlpnipkhfhqefelFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:COG0561  106 -----------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....*
gi 517180560 244 VRKEFERTTsRTNDESGVAEAIEKY 268
Cdd:COG0561  169 VKAAADYVT-GSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-265 3.03e-54

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: 176.30  E-value: 3.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    6 LLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSqedYSITFNGGLIQKNNGHCLFQ 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   86 KTLSREDVENITEMLLSLGLPVDIISDSKSYTLTAPNHNSLYPTANVQLDFHDIKTLDELPHGIVYnKIVTVFDANYLDR 165
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK-ILLLFLDPEDLDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  166 QLPNIPK-HFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAV 244
Cdd:TIGR00099 157 LIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEEL 236

                         250       260
                  ....*....|....*....|.
gi 517180560  245 RKEFERTTSrTNDESGVAEAI 265
Cdd:TIGR00099 237 KALADYVTD-SNNEDGVALAL 256
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 6-267 1.03e-82

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


Pssm-ID: 319818 [Multi-domain]  Cd Length: 253  Bit Score: 248.66  E-value: 1.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   6 LLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqEDYSITFNGGLIQKNNGHCLFQ 85
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGL---DSPLITFNGALVYDPTGKEILE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  86 KTLSREDVENITEMLLSLGLPVDIISDSKsytltapNHNSLYPT--ANVQLDFHDIKTLDELPHGIVYNKIVTVFDANYL 163
Cdd:cd07516   78 RLISKEDVKELEEFLRKLGIGINIYTNDD-------WADTIYEEneDDEIIKPAEILDDLLLPPDEDITKILFVGEDEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 DRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:cd07516  151 DELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDE 230

                        250       260
                 ....*....|....*....|....
gi 517180560 244 VRKEFERTTsRTNDESGVAEAIEK 267
Cdd:cd07516  231 VKEAADYVT-LTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 7-265 1.25e-64

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 202.85  E-value: 1.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    7 LALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKsqeDYSITFNGGLIQKNNGHCLFQK 86
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLD---DPVICYNGALIYDENGKILYSN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   87 TLSREDVENITEMLLSLGLPVDIISDSKSYTLTAPNHNSLYPTANVQLDFHDIKTLDELPHGIVYNKIVTVFDANYLDRQ 166
Cdd:pfam08282  78 PISKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  167 LPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVrK 246
Cdd:pfam08282 158 EKELKELFGSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEV-K 236

                         250
                  ....*....|....*....
gi 517180560  247 EFERTTSRTNDESGVAEAI 265
Cdd:pfam08282 237 AAADYVTDSNNEDGVAKAL 255
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 4-271 2.83e-63

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 199.92  E-value: 2.83e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   4 IKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSQEDYSITFNGGLIQK-NNGHC 82
Cdd:PRK10513   3 IKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGDYCITNNGALVQKaADGET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  83 LFQKTLSREDVENITEMLLSLGLPVDIISDSKSYTltaPNHN-SLYPTANVQLDFHDIK--TLDELPHGIVYNKIVTVFD 159
Cdd:PRK10513  83 VAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYT---ANRDiSYYTVHESFLTGIPLVfrEVEKMDPNLQFPKVMMIDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 160 ANYLDRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKN 239
Cdd:PRK10513 160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 517180560 240 ASVAVrKEFERTTSRTNDESGVAEAIEKYILR 271
Cdd:PRK10513 240 AIPSV-KEVAQFVTKSNLEDGVAFAIEKYVLN 270
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-268 3.17e-60

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: 189.19  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   4 IKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqEDYSITFNGGLIQKNNGHCL 83
Cdd:COG0561    2 IKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGL---DDPLITSNGALIYDPDGEVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  84 FQKTLSREDVENITEMLLSLGLPVDIIsdsksytltapnhnslyptanvqldfhdiktldelphgivynkivtvfdanyl 163
Cdd:COG0561   79 YERPLDPEDVREILELLREHGLHLQVV----------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 drqlpnipkhfhqefelFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:COG0561  106 -----------------VRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPE 168

                        250       260
                 ....*....|....*....|....*
gi 517180560 244 VRKEFERTTsRTNDESGVAEAIEKY 268
Cdd:COG0561  169 VKAAADYVT-GSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 6-265 3.03e-54

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: 176.30  E-value: 3.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    6 LLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSqedYSITFNGGLIQKNNGHCLFQ 85
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT---PFITANGAAVIDDQGEILYK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   86 KTLSREDVENITEMLLSLGLPVDIISDSKSYTLTAPNHNSLYPTANVQLDFHDIKTLDELPHGIVYnKIVTVFDANYLDR 165
Cdd:TIGR00099  78 KPLDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPKLEVVDIQYLPDDILK-ILLLFLDPEDLDL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  166 QLPNIPK-HFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAV 244
Cdd:TIGR00099 157 LIEALNKlELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEEL 236

                         250       260
                  ....*....|....*....|.
gi 517180560  245 RKEFERTTSrTNDESGVAEAI 265
Cdd:TIGR00099 237 KALADYVTD-SNNEDGVALAL 256
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 5-268 1.87e-35

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: 126.18  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   5 KLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqeDYSITFNGGLIQkNNGHCLF 84
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGI----DSYVSYNGQYVF-FEGEVIY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  85 QKTLSREDVENITEMLlslglpvdiisdsksytltapnhnslyptanvqldfhdiktlDELPHGIVY-NKIVTVFDANYL 163
Cdd:cd07517   76 KNPLPQELVERLTEFA------------------------------------------KEQGHPVSFyGQLLLFEDEEEE 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 DRQLPNIPkhfhqEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:cd07517  114 QKYEELRP-----ELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEE 188

                        250       260
                 ....*....|....*....|....*
gi 517180560 244 VrKEFERTTSRTNDESGVAEAIEKY 268
Cdd:cd07517  189 L-KEIADYVTKDVDEDGILKALKHF 212
PLN02887 PLN02887
hydrolase family protein
 10-268 1.40e-24

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 102.65  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  10 DLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLK------SQEDYSITFNGGLIQKNNGHCL 83
Cdd:PLN02887 314 DMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiiSESSPGVFLQGLLVYGRQGREI 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  84 FQKTLSREDVENitEMLLSLGLPVDIISDSKSYTLTAPNH---NSLY-----PTANVqldfhdIKTLDELPHGIVYNKIV 155
Cdd:PLN02887 394 YRSNLDQEVCRE--ACLYSLEHKIPLIAFSQDRCLTLFDHplvDSLHtiyhePKAEI------MSSVDQLLAAADIQKVI 465

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 156 TVFDANYLDRQL-PNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLP 234
Cdd:PLN02887 466 FLDTAEGVSSVLrPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLG 545

                        250       260       270
                 ....*....|....*....|....*....|....
gi 517180560 235 VIMKNASVAVrKEFERTTSRTNDESGVAEAIEKY 268
Cdd:PLN02887 546 VALSNGAEKT-KAVADVIGVSNDEDGVADAIYRY 578
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 6-237 3.66e-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: 93.98  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    6 LLALDLDGTLFNNQK-EVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKsqeDYSITFNGGLIQKNNG---- 80
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLP---LPLIAENGALIFYPGEilyi 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   81 -HCLFQKTLSREDVENITEMLLSlglpvdIISDSKSYTLTAPNH--NSLYPTANVQLDFhDIKTLDELphgivynkivTV 157
Cdd:TIGR01484  78 ePSDVFEEILGIKFEEIGAELKS------LSEHYVGTFIEDKAIavAIHYVGAELGQEL-DSKMRERL----------EK 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  158 FDANYLDRQLPNIPKHFhqefelfksrdimLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIM 237
Cdd:TIGR01484 141 IGRNDLELEAIYSGKTD-------------LEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 5-266 2.51e-22

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: 91.11  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   5 KLLALDLDGTLFNNQKEVSFLNKMAII-QAKNKGVKIVITTGRPLkaIGNLLDFLDLKSQEDYsITFNGGliqknnghcl 83
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFFAILdQLLKKGIKFVVASGRQY--YQLISFFPEIKDEMSF-VAENGA---------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  84 fqktlsredvenitemllslglpvdiisdsksytltapnhnslyptanvqldfhdiktldelphgIVYNKIVTVFDANYL 163
Cdd:cd07518   68 -----------------------------------------------------------------VVYFKFTLNVPDEAA 82

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 164 DRQLPNIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVA 243
Cdd:cd07518   83 PDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEE 162

                        250       260
                 ....*....|....*....|...
gi 517180560 244 VrKEFERTTSRTNDESGVAEAIE 266
Cdd:cd07518  163 V-KAAAKYVAPSNNENGVLQVIE 184
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 2-270 1.62e-19

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 84.64  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   2 TQIKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPL---KAIGNLLDFldlksqEDYSITFNGGLIQKN 78
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVLcfaRAAAKLIGT------SGPVIAENGGVISVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  79 NghclfqktlsreDVENItemllslglpvdiISDSKSYTLTAPNHNS-LYPTANVQLDFHDIktlDELPHGIVYNKIVTV 157
Cdd:PRK01158  75 F------------DGKRI-------------FLGDIEECEKAYSELKkRFPEASTSLTKLDP---DYRKTEVALRRTVPV 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 158 FDANyldrqlpnipkhfhqefELFKSRDIMLEIV---------PKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSML 228
Cdd:PRK01158 127 EEVR-----------------ELLEELGLDLEIVdsgfaihikSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMF 189

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 517180560 229 RWVGLPVIMKNASVAVRKEFERTTSRTNDEsGVAEAIEKYIL 270
Cdd:PRK01158 190 EVAGFGVAVANADEELKEAADYVTEKSYGE-GVAEAIEHLLL 230
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 5-270 1.63e-19

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 85.46  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   5 KLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSQedySITFNGG-LIQKNNGHCL 83
Cdd:PRK10530   4 RVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTP---AICCNGTyLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  84 FQKTLSREDVENITEMLLSLGLP----VDiisDSKSYTltapnhnslYPTANVqldfhdIKTL---DELPHG--IVYNKI 154
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHglmyVD---DAMLYE---------HPTGHV------IRTLnwaQTLPPEqrPTFTQV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 155 VTVFDANYLDRQL-------PNIPK--HFHQEFElfksRDIMLE----------IVPKGVNKGRALAILGEHLGIKKEEM 215
Cdd:PRK10530 143 DSLAQAARQVNAIwkfalthEDLPQlqHFAKHVE----HELGLEcewswhdqvdIARKGNSKGKRLTQWVEAQGWSMKNV 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517180560 216 MAIGDEENDLSMLRWVGLPVIMKNASVAVRKEFERTTsRTNDESGVAEAIEKYIL 270
Cdd:PRK10530 219 VAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVI-GDNTTPSIAEFIYSHVL 272
PRK15126 PRK15126
HMP-PP phosphatase;
5-240 1.98e-17

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 79.74  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   5 KLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSqedYSITFNGGLIQKNNGHCLF 84
Cdd:PRK15126   3 RLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDA---YLITGNGTRVHSLEGELLH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  85 QKTLSREDVENITEMLLSLGLPVDIISDSKSYT------LTAPNHNSlyptanvqlDFH-DIKTLDELP-HGIvyNKIVT 156
Cdd:PRK15126  80 RQDLPADVAELVLHQQWDTRASMHVFNDDGWFTgkeipaLLQAHVYS---------GFRyQLIDLKRLPaHGV--TKICF 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 157 VFDANYLDRQLPNIPKHFHQEFEL-FKSRDImLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPV 235
Cdd:PRK15126 149 CGDHDDLTRLQIQLNEALGERAHLcFSATDC-LEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGF 227


                 ....*
gi 517180560 236 IMKNA 240
Cdd:PRK15126 228 IMGNA 232
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 7-266 2.26e-17

sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP equivalog model (TIGR01485), encompassing plants and cyanobacteria, as well as those archaeal sequences which are the closest relatives (TIGR01487). It remains to be shown whether these archaeal sequences catalyze the same reaction as SPP.


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 78.66  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    7 LALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLdlkSQEDYSITFNGGLIQKNNGhcLFQK 86
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLI---GTPDPVIAENGGEISYNEG--LDDI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   87 TLSREDVENITEMLLSLGLPVDIISdsksytLTAPNHNSLYptanVQLDFHDIKTLDELPH--GIVYNKIVTVFDAnyld 164
Cdd:TIGR01482  76 FLAYLEEEWFLDIVIAKTFPFSRLK------VQYPRRASLV----KMRYGIDVDTVREIIKelGLNLVAVDSGFDI---- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  165 rqlpnipkhfhqefelfksrDIMleivPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAV 244
Cdd:TIGR01482 142 --------------------HIL----PQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPEL 197

                         250       260
                  ....*....|....*....|..
gi 517180560  245 RKEFERTTSRTNDESGVAEAIE 266
Cdd:TIGR01482 198 KEWADYVTESPYGEGGAEAIGE 219
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 194-268 6.43e-17

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


Pssm-ID: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 75.32  E-value: 6.43e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517180560 194 GVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVRKEFERTTSRTNDEsGVAEAIEKY 268
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGD-GVLEAIDKL 138
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-265 8.24e-15

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: 71.31  E-value: 8.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    4 IKLLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLksqedysitfNGGLIQKNNGHCL 83
Cdd:TIGR01487   1 IKLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGT----------SGPVVAENGGVIF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   84 FQKT---LSREDVENITEMLLSLGLPVDIISDSksytltapnhnslYPTANVQLDFHDIKTlDELPHGIVYNKIVtVFDA 160
Cdd:TIGR01487  71 YNKEdifLANMEEEWFLDEEKKKRFPRDRLSNE-------------YPRASLVIMREGKDV-DEVREIIKERGLN-LVAS 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  161 NYldrqlpnipkhfhqefelfksrDIMleIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNA 240
Cdd:TIGR01487 136 GF----------------------AIH--IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANA 191

                         250       260
                  ....*....|....*....|....*
gi 517180560  241 SVAVRKEFERTTSRTNDEsGVAEAI 265
Cdd:TIGR01487 192 DDQLKEIADYVTSNPYGE-GVVEVL 215
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 6-268 5.47e-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: 66.99  E-value: 5.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   6 LLALDLDGTLFNNQKEVSFLNKMAII---QAKNKGVKIVITTGRPLKAIGNLLDFLDLkSQEDYSITFNGGLIQKNNGHC 82
Cdd:cd02605    1 LLVSDLDETLVGHDTNLQALERLQDLleqLTADNDVILVYATGRSPESVLELIKEVML-PKPDFIISDVGTEIYYGESGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  83 LFQKTLSREdvenitemLLSLGLPVDIISDsksytltapnhnslypTANVQLDFHDIKTLDELPHGIVYNkivtvFDANY 162
Cdd:cd02605   80 LEPDTYWNE--------VLSEGWERFLFEA----------------IADLFKQLKPQSELEQNPHKISFY-----LDPQN 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 163 LDRQLPNIPKHFHQE-------FELFKSRDimLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPV 235
Cdd:cd02605  131 DAAVIEQLEEMLLKAgltvriiYSSGLAYD--LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGV 208

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517180560 236 IMKNASVAVRKE-FERTTSRTNDE---SGVAEAIEKY 268
Cdd:cd02605  209 IVGNAQPELLKWaDRVTRSRLAKGpyaGGILEGLAHF 245
PRK10976 PRK10976
putative hydrolase; Provisional
 1-240 2.21e-09

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 56.60  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   1 MTQIklLALDLDGTLFNNQKEVSFLNKMAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSqedYSITFNGGLIQKNNG 80
Cdd:PRK10976   1 MYQV--VASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKS---YMITSNGARVHDTDG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  81 HCLFQKTLSREDVENITEMLLSlglPVDIIS-----DSKSYTLTAPNHNSLYPTANVQLDFHDIKTLDelPHGI--VYnk 153
Cdd:PRK10976  76 NLIFSHNLDRDIASDLFGVVHD---NPDIITnvyrdDEWFMNRHRPEEMRFFKEAVFKYQLYEPGLLE--PDGVskVF-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 154 ivtvFDANYLDRQLP---NIPKHFHQEFELFKSRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRW 230
Cdd:PRK10976 149 ----FTCDSHEKLLPleqAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSM 224

                        250
                 ....*....|
gi 517180560 231 VGLPVIMKNA 240
Cdd:PRK10976 225 AGKGCIMGNA 234
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 196-266 2.42e-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: 2.42e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517180560 196 NKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVRKEFERTTSRTNDESGVAEAIE 266
Cdd:cd01630   76 DKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 183-241 5.81e-07

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: 49.57  E-value: 5.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 517180560  183 SRDIMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNAS 241
Cdd:pfam05116 151 SSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQ 209
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 196-246 8.86e-07

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: 47.74  E-value: 8.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517180560 196 NKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVRK 246
Cdd:COG1778   83 DKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKA 133
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 182-274 4.59e-06

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 45.59  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560  182 KSRDIMLEIVPKGV-NKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMKNASVAVRKEFERTTSRTNDESG 260
Cdd:TIGR01670  61 RCKTLGITHLYQGQsNKLIAFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGA 140

                          90
                  ....*....|....
gi 517180560  261 VAEAIEKYILREGK 274
Cdd:TIGR01670 141 VREVCELLLLAQGK 154
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 194-247 2.25e-05

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: 44.44  E-value: 2.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517180560 194 GVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPVIMkNASVAVRKE 247
Cdd:COG0560  153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREA 205
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 6-83 2.85e-05

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 42.38  E-value: 2.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517180560   6 LLALDLDGTLFNnqKEvsflnkmAIIQAKNKGVKIVITTGRPLKAIGNLLDFLDLKSQEDYSITFNGGLIQKNNGHCL 83
Cdd:cd01427    1 AVLFDLDGTLLA--VE-------LLKRLRAAGIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPL 69
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 139-236 5.82e-05

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 41.23  E-value: 5.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 139 IKTLDELPHGIVynkIVTVFDANYLDRQLPNIpkHFHQEFELFKSRDImleiVPKGVNKGRALAILGEHLGIKKEEMMAI 218
Cdd:cd01427   16 LKRLRAAGIKLA---IVTNRSREALRALLEKL--GLGDLFDGIIGSDG----GGTPKPKPKPLLLLLLKLGVDPEEVLFV 86

                         90
                 ....*....|....*...
gi 517180560 219 GDEENDLSMLRWVGLPVI 236
Cdd:cd01427   87 GDSENDIEAARAAGGRTV 104
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 4-232 5.88e-05

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 42.96  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560    4 IKLLALDLDGTLFNNQKEVSFLNKMAiiqaknkgvkiviTTGRPLkAIGNLLDFLDLKSQ-EDYSITFNGGLIQKNNGHC 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGEPVVTEAIAEL-------------ASEHPL-AKAIVAAAEDLPIPvEDFTARLLLGKRDWLEELD 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560   83 LFQKTLSREDVENITEMLLSLGlpvdiisdsksYTLTAPNHNSLYPTAnvqldfhdIKTLDEL-PHGIvynKIVTVFDAN 161
Cdd:pfam00702  67 ILRGLVETLEAEGLTVVLVELL-----------GVIALADELKLYPGA--------AEALKALkERGI---KVAILTGDN 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517180560  162 yldrqlPNIPKHFHQEFELFKSRD--IMLEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVG 232
Cdd:pfam00702 125 ------PEAAEALLRLLGLDDYFDvvISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 194-241 8.45e-05

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 42.89  E-value: 8.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517180560 194 GVNKGRALAILGEHLGIKKEE---MMAIGDEENDLSMLRWVGLPVIMKNAS 241
Cdd:COG3769  186 GADKGKAVRWLVEQYRQRFGKnvvTIALGDSPNDIPMLEAADIAVVIRSPH 236
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 194-269 8.96e-05

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 43.01  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517180560 194 GVNKGRALAILGEHLGIKKE-EMMAIGDEENDLSMLRWVGLPVIMKNAS----VAVRKEFERTTSRTNDE--SGVAEAIE 266
Cdd:PRK00192 188 GGDKGKAVRWLKELYRRQDGvETIALGDSPNDLPMLEAADIAVVVPGPDgpnpPLLPGIADGEFILASAPgpEGWAEAIN 267


                 ...
gi 517180560 267 KYI 269
Cdd:PRK00192 268 KLL 270
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 189-235 7.28e-04

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: 39.45  E-value: 7.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 517180560 189 EIVpKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGLPV 235
Cdd:cd07500  131 PIV-DAQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGI 176
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 175-231 2.49e-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: 38.42  E-value: 2.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517180560 175 HQEFELFKSRDIM-----LEIVPKGVNKGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWV 231
Cdd:cd01627  138 HLASDLLKALEVVpgkkvVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRAL 199
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
188-232 4.72e-03

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 37.48  E-value: 4.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 517180560 188 LEIVPKGVNKGRALAILGEHLGIkKEEMMAIGDEENDLSMLRWVG 232
Cdd:COG1877  160 VELRPAGVDKGRAVRALLAELPF-GRAPVFIGDDVTDEDAFAALP 203
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 197-247 6.94e-03

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: 36.95  E-value: 6.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517180560  197 KGRALAILGEHLGIKKEEMMAIGDEENDLSMLRWVGL-------PVIMKNASVAVRKE 247
Cdd:TIGR00338 153 KGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLgiafnakPKLQQKADICINKK 210
 
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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