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Cof-type HAD-IIB family hydrolase [Clostridioides difficile]

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 ...
 5-267 2.21e-78

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: 237.49  E-value: 2.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   5 LICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVL 82
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKeiLERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 SKEALKKIYTIGEKYNLNKHFkgckivisnneIGEEHPYRLINSKNKEEDRIEIIENAscETLLEKADNEILKCILFSEN 162
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINI-----------YTNDDWADTIYEENEDDEIIKPAEIL--DDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 163 VD-SLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNA 241
Cdd:cd07516  148 EElDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 544954195 242 TDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-267 2.21e-78

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: 237.49  E-value: 2.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   5 LICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVL 82
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKeiLERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 SKEALKKIYTIGEKYNLNKHFkgckivisnneIGEEHPYRLINSKNKEEDRIEIIENAscETLLEKADNEILKCILFSEN 162
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINI-----------YTNDDWADTIYEENEDDEIIKPAEIL--DDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 163 VD-SLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNA 241
Cdd:cd07516  148 EElDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 544954195 242 TDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-265 2.02e-69

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 214.79  E-value: 2.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    6 ICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVLS 83
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKilYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   84 KEALKKIYTIGEKYNLNKHFKGCKIVISNNEIGEEHPYRLINSKNKEEDRIEIIENascetlleKADNEILKcILFSENV 163
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFEL--------LEDEDINK-ILILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  164 DSLREAKEEFKKQ--EDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNA 241
Cdd:pfam08282 152 EDLDELEKELKELfgSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 544954195  242 TDEVKSMADFVTDTNVNDGVAKAL 265
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-268 9.53e-64

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: 198.05  E-value: 9.53e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   2 RYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTY-FKLLG-YEYK 79
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALiYDPDGeVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  80 KVLSKEALKKIYTIGEKYNLNKHFkgckivisnneigeehpyrlinsknkeedrieiienascetllekadneilkcilf 159
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQV-------------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 160 senvdslreakeefkkqedleVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMG 239
Cdd:COG0561  105 ---------------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 544954195 240 NATDEVKSMADFVTDTNVNDGVAKALRKI 268
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-265 2.31e-59

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: 189.02  E-value: 2.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    5 LICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVL 82
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEilYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   83 SKEALKKIYTIGEKYNLNKHFKGCKIVISNNEIGEEHPyrlINSKNKEEDRIEIIENasceTLLEKADNEILKCILFSEN 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFT---IFKKFLGEPKLEVVDI----QYLPDDILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  163 VDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNAT 242
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 544954195  243 DEVKSMADFVTDTNVNDGVAKAL 265
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-267 1.66e-39

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 138.23  E-value: 1.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   1 MRYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYfkLLGYEYKK 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTY--LYDYQAKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  81 VLSKEALkkiyTIGEKYNLNKHFKGCKI---VISNNEIGEEHPY-RLINSKN-----KEEDRIEIIENASCETLLEKADN 151
Cdd:PRK10530  79 VLEADPL----PVQQALQVIEMLDEHQIhglMYVDDAMLYEHPTgHVIRTLNwaqtlPPEQRPTFTQVDSLAQAARQVNA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 152 eILKCILFSENVDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKF 231
Cdd:PRK10530 155 -IWKFALTHEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEA 233

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 544954195 232 AGLGIAMGNATDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:PRK10530 234 AGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-267 2.21e-78

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: 237.49  E-value: 2.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   5 LICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVL 82
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKeiLERLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 SKEALKKIYTIGEKYNLNKHFkgckivisnneIGEEHPYRLINSKNKEEDRIEIIENAscETLLEKADNEILKCILFSEN 162
Cdd:cd07516   81 SKEDVKELEEFLRKLGIGINI-----------YTNDDWADTIYEENEDDEIIKPAEIL--DDLLLPPDEDITKILFVGED 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 163 VD-SLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNA 241
Cdd:cd07516  148 EElDELIAKLPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNA 227

                        250       260
                 ....*....|....*....|....*.
gi 544954195 242 TDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:cd07516  228 IDEVKEAADYVTLTNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-265 2.02e-69

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 214.79  E-value: 2.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    6 ICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVLS 83
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDENGKilYSNPIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   84 KEALKKIYTIGEKYNLNKHFKGCKIVISNNEIGEEHPYRLINSKNKEEDRIEIIENascetlleKADNEILKcILFSENV 163
Cdd:pfam08282  81 KEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKILKELNYTKSFVPEIDDFEL--------LEDEDINK-ILILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  164 DSLREAKEEFKKQ--EDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNA 241
Cdd:pfam08282 152 EDLDELEKELKELfgSLITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 544954195  242 TDEVKSMADFVTDTNVNDGVAKAL 265
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-268 9.53e-64

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: 198.05  E-value: 9.53e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   2 RYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTY-FKLLG-YEYK 79
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALiYDPDGeVLYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  80 KVLSKEALKKIYTIGEKYNLNKHFkgckivisnneigeehpyrlinsknkeedrieiienascetllekadneilkcilf 159
Cdd:COG0561   81 RPLDPEDVREILELLREHGLHLQV-------------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 160 senvdslreakeefkkqedleVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMG 239
Cdd:COG0561  105 ---------------------VVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 544954195 240 NATDEVKSMADFVTDTNVNDGVAKALRKI 268
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-265 2.31e-59

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: 189.02  E-value: 2.31e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    5 LICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKKVL 82
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGEilYKKPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   83 SKEALKKIYTIGEKYNLNKHFKGCKIVISNNEIGEEHPyrlINSKNKEEDRIEIIENasceTLLEKADNEILKCILFSEN 162
Cdd:TIGR00099  81 DLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFT---IFKKFLGEPKLEVVDI----QYLPDDILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  163 VDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNAT 242
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 544954195  243 DEVKSMADFVTDTNVNDGVAKAL 265
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-267 1.66e-39

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 138.23  E-value: 1.66e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   1 MRYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYfkLLGYEYKK 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTY--LYDYQAKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  81 VLSKEALkkiyTIGEKYNLNKHFKGCKI---VISNNEIGEEHPY-RLINSKN-----KEEDRIEIIENASCETLLEKADN 151
Cdd:PRK10530  79 VLEADPL----PVQQALQVIEMLDEHQIhglMYVDDAMLYEHPTgHVIRTLNwaqtlPPEQRPTFTQVDSLAQAARQVNA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 152 eILKCILFSENVDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKF 231
Cdd:PRK10530 155 -IWKFALTHEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEA 233

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 544954195 232 AGLGIAMGNATDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:PRK10530 234 AGLGVAMGNADDAVKARADLVIGDNTTPSIAEFIYS 269
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-267 8.18e-39

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: 134.66  E-value: 8.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   4 KLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDiYIISTNGTYFKLLGYE-YKKVL 82
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGID-SYVSYNGQYVFFEGEViYKNPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 SKEALKKIYTIGEKynlnkhfkgckivisnneigEEHPYRLINsknkeedrieiienascetllekadneiLKCILFSEN 162
Cdd:cd07517   80 PQELVERLTEFAKE--------------------QGHPVSFYG----------------------------QLLLFEDEE 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 163 vdslrEAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNAT 242
Cdd:cd07517  112 -----EEQKYEELRPELRFVRWHPLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAH 186

                        250       260
                 ....*....|....*....|....*
gi 544954195 243 DEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:cd07517  187 EELKEIADYVTKDVDEDGILKALKH 211
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-267 1.47e-37

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 133.28  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   1 MRYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLG---DDIYIISTNGTYFKLLG-- 75
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHmeqPGDYCITNNGALVQKAAdg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  76 ------------YEYKKVLSKE------ALKKIYTigekYNLNKHfkgckivISNNEIGEEH----P--YRLInsknKEE 131
Cdd:PRK10513  81 etvaqtalsyddYLYLEKLSREvgvhfhALDRNTL----YTANRD-------ISYYTVHESFltgiPlvFREV----EKM 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 132 DR------IEIIENAScetLLEKADNEILKcilfsenvdslrEAKEEFKkqedleVVSSGKINFEVMSKGTSKGIAVKKF 205
Cdd:PRK10513 146 DPnlqfpkVMMIDEPE---ILDAAIARIPA------------EVKERYT------VLKSAPYFLEILDKRVNKGTGVKSL 204

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544954195 206 CDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATDEVKSMADFVTDTNVNDGVAKALRK 267
Cdd:PRK10513 205 AEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEK 266
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-270 4.23e-37

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 130.86  E-value: 4.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   1 MRYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRP----YNAMKYftsvLGDDIYIISTNGtyfkllgy 76
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGNVlcfaRAAAKL----IGTSGPVIAENG-------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  77 eykKVLSKEALKKIYTIGEKYnlnkhfkgcKIVISNNEIGEEHPYRlinsknkeedrieiienascETLLEKADNEILK- 155
Cdd:PRK01158  69 ---GVISVGFDGKRIFLGDIE---------ECEKAYSELKKRFPEA--------------------STSLTKLDPDYRKt 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 156 --CILFSENVDSLREAKEEFKKqeDLEVVSSGkINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAG 233
Cdd:PRK01158 117 evALRRTVPVEEVRELLEELGL--DLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAG 193

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 544954195 234 LGIAMGNATDEVKSMADFVTDTNVNDGVAKALRKILS 270
Cdd:PRK01158 194 FGVAVANADEELKEAADYVTEKSYGEGVAEAIEHLLL 230
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-266 6.62e-30

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: 110.75  E-value: 6.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   4 KLICTDMDGTLM-GKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYfkllgyeykkvl 82
Cdd:cd07518    1 KLIATDMDGTFLnDDKTYDHERFFAILDQLLKKGIKFVVASGRQYYQLISFFPEIKDEMSFVAENGAV------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 skealkkIYTigekynlnkhfkgckivisnneigeehpyrlinsknkeedRIEIIENASCETLLEKADNEILKcilfsen 162
Cdd:cd07518   69 -------VYF----------------------------------------KFTLNVPDEAAPDIIDELNQKFG------- 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 163 vdslreakeefkkqEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNAT 242
Cdd:cd07518   95 --------------GILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAP 160

                        250       260
                 ....*....|....*....|....
gi 544954195 243 DEVKSMADFVTDTNVNDGVAKALR 266
Cdd:cd07518  161 EEVKAAAKYVAPSNNENGVLQVIE 184
PLN02887 PLN02887
hydrolase family protein
 2-265 3.25e-28

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 113.05  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   2 RYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTG--RP--YNAMKYFTSVLGDDIYIISTNGTYFK-LLGY 76
Cdd:PLN02887 307 KFSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGkaRPavIDILKMVDLAGKDGIISESSPGVFLQgLLVY 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  77 E------YKKVLSKEALKK--IYTIGEKYNLnkhfkgckIVISNNEIGE--EHPyrLINSKNK--EEDRIEIIenASCET 144
Cdd:PLN02887 387 GrqgreiYRSNLDQEVCREacLYSLEHKIPL--------IAFSQDRCLTlfDHP--LVDSLHTiyHEPKAEIM--SSVDQ 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 145 LLEKADneILKCILF--SENVDS-LREAKEEfKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGD 221
Cdd:PLN02887 455 LLAAAD--IQKVIFLdtAEGVSSvLRPYWSE-ATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGD 531

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 544954195 222 NENDISMIKFAGLGIAMGNATDEVKSMADFVTDTNVNDGVAKAL 265
Cdd:PLN02887 532 GENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAI 575
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-270 9.97e-27

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: 103.70  E-value: 9.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    6 ICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTyfkllgyeykkvlske 85
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGNSVQFARALAKLIGTPDPVIAENGG---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   86 alkkiytigekynlnkhfkgckiVISNNEIGEEHPYRLINSKNKEEDRIEIIENAScETLLEKADNEILKCILFSENVDS 165
Cdd:TIGR01482  65 -----------------------EISYNEGLDDIFLAYLEEEWFLDIVIAKTFPFS-RLKVQYPRRASLVKMRYGIDVDT 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  166 LREAKEEFKkqEDLEVVSSGKiNFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATDEV 245
Cdd:TIGR01482 121 VREIIKELG--LNLVAVDSGF-DIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPEL 197

                         250       260
                  ....*....|....*....|....*
gi 544954195  246 KSMADFVTDTNVNDGVAKALRKILS 270
Cdd:TIGR01482 198 KEWADYVTESPYGEGGAEAIGEILQ 222
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-265 1.28e-25

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: 100.59  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    4 KLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTyfkLLGYEYKKvls 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGG---VIFYNKED--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   84 kealkkiytigekynlnkhfkgckIVISNneigEEHPYRLINSKNKEEDRieiienascETLLEKADNEILKCILFSENV 163
Cdd:TIGR01487  76 ------------------------IFLAN----MEEEWFLDEEKKKRFPR---------DRLSNEYPRASLVIMREGKDV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  164 DSLREAKEEFKkqedLEVVSSGkINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATD 243
Cdd:TIGR01487 119 DEVREIIKERG----LNLVASG-FAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADD 193

                         250       260
                  ....*....|....*....|..
gi 544954195  244 EVKSMADFVTDTNVNDGVAKAL 265
Cdd:TIGR01487 194 QLKEIADYVTSNPYGEGVVEVL 215
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 195-269 6.39e-24

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: 93.81  E-value: 6.39e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544954195 195 GTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATDEVKSMADFVTDTNVNDGVAKALRKIL 269
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAIDKLL 139
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-238 1.29e-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: 95.14  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195    5 LICTDMDGTLMG-KGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGyeykkvls 83
Cdd:TIGR01484   1 LLFFDLDGTLLDpNAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPG-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   84 kealkkiytiGEKYNLNKHFkgckivisnNEIGEEHPYRLINSKNKEEDRI---EIIENASCETLLEKADNEilkciLFS 160
Cdd:TIGR01484  73 ----------EILYIEPSDV---------FEEILGIKFEEIGAELKSLSEHyvgTFIEDKAIAVAIHYVGAE-----LGQ 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544954195  161 ENVDSLREAKEEFK-KQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAM 238
Cdd:TIGR01484 129 ELDSKMRERLEKIGrNDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK10976 PRK10976
putative hydrolase; Provisional
 3-268 2.03e-12

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 65.45  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   3 YKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTyfkllgyeykkvl 82
Cdd:PRK10976   2 YQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGA------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  83 skealkKIY-TIGE---KYNLNKHFKG--CKIVISNNEIgEEHPYR----LINSKNKEEDRI--------EIIENASCET 144
Cdd:PRK10976  69 ------RVHdTDGNlifSHNLDRDIASdlFGVVHDNPDI-ITNVYRddewFMNRHRPEEMRFfkeavfkyQLYEPGLLEP 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 145 llekadNEILKCILFSENVDSLREAKEEFKKQ--EDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDN 222
Cdd:PRK10976 142 ------DGVSKVFFTCDSHEKLLPLEQAINARwgDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDG 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 544954195 223 ENDISMIKFAGLGIAMGNATDEVKSMADF--VTDTNVNDGVAKALRKI 268
Cdd:PRK10976 216 MNDAEMLSMAGKGCIMGNAHQRLKDLLPEleVIGSNADDAVPHYLRKL 263
PRK15126 PRK15126
HMP-PP phosphatase;
3-247 7.98e-12

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 63.94  E-value: 7.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   3 YKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGTYFKLLGYE--YKK 80
Cdd:PRK15126   2 ARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEGEllHRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  81 VLSKE-ALKKIYTIGEK------YNLNKHFKGCKIvisnNEIGEEHP-----YRLINSKnkeedRIEIIENAScetllek 148
Cdd:PRK15126  82 DLPADvAELVLHQQWDTrasmhvFNDDGWFTGKEI----PALLQAHVysgfrYQLIDLK-----RLPAHGVTK------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 149 adneilkcILFSENVDSLREAK----EEFKKQEDLevVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNEN 224
Cdd:PRK15126 146 --------ICFCGDHDDLTRLQiqlnEALGERAHL--CFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMN 215

                        250       260
                 ....*....|....*....|...
gi 544954195 225 DISMIKFAGLGIAMGNATDEVKS 247
Cdd:PRK15126 216 DREMLGSVGRGFIMGNAMPQLRA 238
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-268 1.79e-09

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: 56.59  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   5 LICTDMDGTLMGKGFEVSE-ENIKALKEAMEK--GIKVALVTGRPY----NAMKYFTSVLGDdiYIISTNGT---YFKLL 74
Cdd:cd02605    1 LLVSDLDETLVGHDTNLQAlERLQDLLEQLTAdnDVILVYATGRSPesvlELIKEVMLPKPD--FIISDVGTeiyYGESG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  75 GYE----YKKVLSK----EALKKIytigekynlnkhfKGCKIVISNNEIGEEHPYRlINSKNKEEDRIEIIENasCETLL 146
Cdd:cd02605   79 YLEpdtyWNEVLSEgwerFLFEAI-------------ADLFKQLKPQSELEQNPHK-ISFYLDPQNDAAVIEQ--LEEML 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 147 EKADneiLKC-ILFSENVDSlreakeefkkqeDLEVVSsgkinfevmsKGTSKGIAVKKFCDILGIDSKEVICIGDNEND 225
Cdd:cd02605  143 LKAG---LTVrIIYSSGLAY------------DLDILP----------LGAGKGEALRYLQEKWNFPPERTLVCGDSGND 197

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 544954195 226 ISMIKFAGLGIAMGNATDEVKSMADFVTDTNVND-----GVAKALRKI 268
Cdd:cd02605  198 IALLSTGTRGVIVGNAQPELLKWADRVTRSRLAKgpyagGILEGLAHF 245
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 179-237 5.12e-09

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: 54.48  E-value: 5.12e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544954195 179 LEVVS---SGKINFEVMSKgTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIA 237
Cdd:cd07500  117 LEIKDgklTGKVLGPIVDA-QRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 178-250 1.25e-08

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 54.07  E-value: 1.25e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544954195 178 DLEVVS---SGKINfEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMgNATDEVKSMAD 250
Cdd:COG0560  134 ELEVEDgrlTGEVV-GPIVDGEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 5-242 4.40e-07

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 49.94  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   5 LICTDMDGTLMGK---GFEVSEENIKALKEameKGIKVALVTGRPYNAMKYFTSVLG-DDIYIIStNG-------TYFK- 72
Cdd:PRK00192   6 LVFTDLDGTLLDHhtySYEPAKPALKALKE---KGIPVIPCTSKTAAEVEVLRKELGlEDPFIVE-NGaaiyipkNYFPf 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  73 ------LLGYEYKKVLSK--EALKKIytigekynLNKHfkgckivisNNEIGEehPYRLINSKNKEEdrIEIIENASCET 144
Cdd:PRK00192  82 qpdgerLKGDYWVIELGPpyEELREI--------LDEI---------SDELGY--PLKGFGDLSAEE--VAELTGLSGES 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 145 LLEKADNEilkcilFSENVDSL--REAKEEFK---KQEDLEVVSSGKinFEVMSKGTSKGIAVKKFCDILGI-DSKEVIC 218
Cdd:PRK00192 141 ARLAKDRE------FSEPFLWNgsEAAKERFEealKRLGLKVTRGGR--FLHLLGGGDKGKAVRWLKELYRRqDGVETIA 212

                        250       260
                 ....*....|....*....|....
gi 544954195 219 IGDNENDISMIKFAGLGIAMGNAT 242
Cdd:PRK00192 213 LGDSPNDLPMLEAADIAVVVPGPD 236
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 198-253 4.84e-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: 4.84e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544954195 198 KGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATDEVKSMADFVT 253
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVT 132
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-70 8.62e-07

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: 46.62  E-value: 8.62e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544954195   5 LICTDMDGTLmgkgfeVSEENIKALKEameKGIKVALVTGRPYNAMKYFTSVLGDDIY---IISTNGTY 70
Cdd:cd01427    1 AVLFDLDGTL------LAVELLKRLRA---AGIKLAIVTNRSREALRALLEKLGLGDLfdgIIGSDGGG 60
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 182-250 3.54e-06

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: 46.58  E-value: 3.54e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544954195  182 VSSGKINFEV---MSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMgNATDEVKSMAD 250
Cdd:TIGR00338 134 VEDGKLTGLVegpIVDASYKGKTLLILLRKEGISPENTVAVGDGANDLSMIKAAGLGIAF-NAKPKLQQKAD 204
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 62-233 8.57e-06

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


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 45.27  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   62 YIISTNGTYFKLLGYEYKKVLSKEALKKIYTIGEKYNLNKHFKGCKIVISNNEIGEEHPYRLINSKNKEEDRIEIIENAs 141
Cdd:pfam00702  25 ELASEHPLAKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGA- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  142 cETLLEKADNEILKCILFSenvDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGD 221
Cdd:pfam00702 104 -AEALKALKERGIKVAILT---GDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGD 179

                         170
                  ....*....|..
gi 544954195  222 NENDISMIKFAG 233
Cdd:pfam00702 180 GVNDIPAAKAAG 191
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 166-244 1.66e-05

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: 44.95  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  166 LREAKEEFKKQE-DLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFAGLGIAMGNATDE 244
Cdd:pfam05116 132 LAELEQLLRKRGlDVKVIYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELFIGGTRGVVVGNAQPE 211
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 143-238 3.75e-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: 42.00  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 143 ETLLEKADNEILKCILFSenvDSLREAKEEFKKQEDLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDN 222
Cdd:cd01427   13 VELLKRLRAAGIKLAIVT---NRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPKPKPLLLLLLKLGVDPEEVLFVGDS 89

                         90
                 ....*....|....*..
gi 544954195 223 ENDISMIKFAG-LGIAM 238
Cdd:cd01427   90 ENDIEAARAAGgRTVAV 106
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-115 1.66e-04

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 41.86  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   1 MRYKLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKyftSVLGDDI-----YIISTNGTYFkllg 75
Cdd:PTZ00174   3 MKKTILLFDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKIK---EQLGEDVledfdYVFSENGLVA---- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 544954195  76 YEYKKVLSKEALKKIytIGEKyNLNKHFKGCKIVISNNEI 115
Cdd:PTZ00174  76 YKDGELFHSQSILKF--LGEE-KLKKFINFCLRYIADLDI 112
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
 178-239 5.59e-04

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: 40.35  E-value: 5.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544954195 178 DLEVVSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISMIKFA----GLGIAMG 239
Cdd:cd01627  145 KALEVVPGKKVVEVRPVGVNKGEAVERILGELPFAGDFVLCAGDDVTDEDAFRALngegGFSVKVG 210
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
 164-228 6.51e-04

trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 40.20  E-value: 6.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544954195  164 DSLREAKEEFKKQEDLEVvSSGKINFEVMSKGTSKGIAVKKFCDILGIDSKEVICIGDNENDISM 228
Cdd:TIGR00685 135 FRAKELKEKILSFTDLEV-MDGKAVVELKPRFVNKGEIVKRLLWHQPGSGISPVYLGDDITDEDA 198
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 25-118 6.74e-04

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 39.96  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   25 NIKALKEAMEKGIKVALVTGrpYNAMKYFTSvlGDDIYIISTNGTYFKLLGYEykkvlskEALKKIYTIGEKYNLNKH-- 102
Cdd:TIGR01378 108 NLNLLLEYAKRGIEVRLIDE--QNVIRLLLP--GKYQIFKEPKGTYISLLPFG-------GDVHGLTTKGLKYPLNNAdl 176

                          90
                  ....*....|....*.
gi 544954195  103 FKGCKIVISNNEIGEE 118
Cdd:TIGR01378 177 KFGGTRGISNEFIGNK 192
serB PRK11133
phosphoserine phosphatase; Provisional
 209-237 8.87e-04

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 39.93  E-value: 8.87e-04
                         10        20
                 ....*....|....*....|....*....
gi 544954195 209 LGIDSKEVICIGDNENDISMIKFAGLGIA 237
Cdd:PRK11133 260 YEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 4-57 2.08e-03

HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class III subfamilies are characterized by the lack of any domains located between either between the first and second conserved catalytic motifs (as in the Class I subfamilies, TIGR01493, TIGR01509, TIGR01488 and TIGR01494) or between the second and third conserved catalytic motifs (as in the Class II subfamilies, TIGR01460 and TIGR01484) of the superfamily domain. The IIIA subfamily contains five major clades: histidinol-phosphatase (TIGR01261) and histidinol-phosphatase-related protein (TIGR00213) which together form a subfamily (TIGR01656), DNA 3'-phosphatase (TIGR01663, TIGR01664), YqeG (TIGR01668) and YrbI (TIGR01670). In the case of histidinol phosphatase and PNK-3'-phosphatase, this model represents a domain of a bifunctional system. In the histidinol phosphatase HisB, a C-terminal domain is an imidazoleglycerol-phosphate dehydratase which catalyzes a related step in histidine biosynthesis. In PNK-3'-phosphatase, N- and C-terminal domains constitute the polynucleotide kinase and DNA-binding components of the enzyme. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273742 [Multi-domain]  Cd Length: 135  Bit Score: 37.38  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544954195    4 KLICTDMDGTLMGKGFEVSEEN--------IKALKEAMEKGIKVALVTGRPYNAMKYFTSVL 57
Cdd:TIGR01662   1 KAVVLDLDGTLTDDVPYVSDEDerilypevPDALAELKEAGYKVVIVTNQSGIGRGYFSRSF 62
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 4-230 2.89e-03

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


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 38.75  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195   4 KLICTDMDGTLMGKGFEVSEENIKALKEAMEKGIKVALVTGRPYNAMKYFTSVLGDDIYIISTNGT-------YFKlLGY 76
Cdd:PRK14502 417 KIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGaifipkdYFR-LPF 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195  77 EYKKVLSKEAlkkIYTIGEKYNLNKHfkgcKIVISNNEIGEEHpyrlinSKNKEEDRIEI-------IENASCETLLEKA 149
Cdd:PRK14502 496 AYDRVAGNYL---VIELGMAYKDIRH----ILKKALAEACTEI------ENSEKAGNIFItsfgdmsVEDVSRLTDLNLK 562

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544954195 150 DNEILKCILFSENV--DSLREAKE---EFKKQEDLEVVSSGKinFEVMSKGTSKGIAVKKFCDILGIDSKEVIC--IGDN 222
Cdd:PRK14502 563 QAELAKQREYSETVhiEGDKRSTNivlNHIQQSGLEYSFGGR--FYEVTGGNDKGKAIKILNELFRLNFGNIHTfgLGDS 640


                 ....*...
gi 544954195 223 ENDISMIK 230
Cdd:PRK14502 641 ENDYSMLE 648
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
 216-252 3.22e-03

uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids. They are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine.


Pssm-ID: 319795 [Multi-domain]  Cd Length: 661  Bit Score: 38.80  E-value: 3.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 544954195 216 VICIGDNENDISMIKFAGLGIAMGNATDEVKSMADFV 252
Cdd:cd02609  523 VAMTGDGVNDVLALKEADCSIAMASGSDATRQVAQVV 559
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-43 3.75e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 37.78  E-value: 3.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 544954195   1 MRYKLICTDMDGTLMgKGFEVSEENIKALKEAMEKGIKVALVT 43
Cdd:COG0647    6 DRYDAFLLDLDGVLY-RGDEPIPGAVEALARLRAAGKPVLFLT 47
 
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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