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MULTISPECIES: Cof-type HAD-IIB family hydrolase [unclassified Treponema]

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 ...
 24-276 4.67e-64

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: 201.28  E-value: 4.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFvsrlnIAALESGKYVIAINGCSIFDMHKRIqIYKKTVSGEVLLE 103
Cdd:cd07516    14 DKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPY-----LEELGLDSPLITFNGALVYDPTGKE-ILERLISKEDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETEVYSDGKVfysKETDWTLRDVRMCGLNGEEAPDFEKFLLENqnsFFKMLIPGEPEKIQELQKKLKASL 183
Cdd:cd07516    88 LEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDED---ITKILFVGEDEELDELIAKLPEEF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 GEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:cd07516   162 FDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVT-L 240

                         250
                  ....*....|...
gi 2540503233 264 TNNDDGVADFIEK 276
Cdd:cd07516   241 TNNEDGVAKAIEK 253
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 24-276 4.67e-64

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: 201.28  E-value: 4.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFvsrlnIAALESGKYVIAINGCSIFDMHKRIqIYKKTVSGEVLLE 103
Cdd:cd07516    14 DKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPY-----LEELGLDSPLITFNGALVYDPTGKE-ILERLISKEDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETEVYSDGKVfysKETDWTLRDVRMCGLNGEEAPDFEKFLLENqnsFFKMLIPGEPEKIQELQKKLKASL 183
Cdd:cd07516    88 LEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDED---ITKILFVGEDEELDELIAKLPEEF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 GEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:cd07516   162 FDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVT-L 240

                         250
                  ....*....|...
gi 2540503233 264 TNNDDGVADFIEK 276
Cdd:cd07516   241 TNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 26-274 8.01e-62

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 195.53  E-value: 8.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLEAH 105
Cdd:pfam08282  15 KISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD-----PVICYNGALIYDENGKI-LYSNPISKEAVKEII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 106 KIAVEEGFETEVYSDGKVFYSKETDWtLRDVRMCGLNGEEAPDFEKFLLENQNSFFKMLIPGEPEKIQELQKKLKASLGE 185
Cdd:pfam08282  89 EYLKENNLEILLYTDDGVYILNDNEL-EKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDELEKELKELFGS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 186 KAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeKTN 265
Cdd:pfam08282 168 LITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVT-DSN 246


                  ....*....
gi 2540503233 266 NDDGVADFI 274
Cdd:pfam08282 247 NEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 24-277 4.60e-47

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: 155.68  E-value: 4.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLE 103
Cdd:COG0561    17 DGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-----PLITSNGALIYDPDGEV-LYERPLDPEDVRE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETevysdgkvfysketdwtlrdvrmcglngeeapdfekfllenqnsffkmlipgepekiqelqkklkasl 183
Cdd:COG0561    91 ILELLREHGLHL-------------------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 gekAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:COG0561   103 ---QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVT-G 178

                         250
                  ....*....|....
gi 2540503233 264 TNNDDGVADFIEKY 277
Cdd:COG0561   179 SNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 26-274 1.71e-46

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: 156.27  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLEAH 105
Cdd:TIGR00099  16 TISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT-----PFITANGAAVIDDQGEI-LYKKPLDLDLVEEIL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 106 KIAVEEGFETEVYSDGKVFYSKETDWTLrDVRMCGLNGEEAPDFEKFLLENQNsFFKMLIPGEPEKIQELQKKLKAS-LG 184
Cdd:TIGR00099  90 NFLKKHGLDVILYGDDSIYASKNDPEYF-TIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLDLLIEALNKLeLE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 185 EKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeKT 264
Cdd:TIGR00099 168 ENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYVT-DS 246

                         250
                  ....*....|
gi 2540503233 265 NNDDGVADFI 274
Cdd:TIGR00099 247 NNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 24-279 7.82e-35

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 126.35  E-value: 7.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAleSGKYVIAINGCSIfdmhkriqiyKKTVSGEVLLE 103
Cdd:PRK10513   18 DHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQ--PGDYCITNNGALV----------QKAADGETVAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 A----------HKIAVEEGFETEVYsDGKVFYSKETD---WTLRDVRMCG--LNGEEAPDFEKFLlenqnSFFKMLIPGE 168
Cdd:PRK10513   86 TalsyddylylEKLSREVGVHFHAL-DRNTLYTANRDisyYTVHESFLTGipLVFREVEKMDPNL-----QFPKVMMIDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 169 PEKIQELQKKLKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVN 248
Cdd:PRK10513  160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2540503233 249 GNEHIKSIADFVTeKTNNDDGVADFIEKYIL 279
Cdd:PRK10513  240 AIPSVKEVAQFVT-KSNLEDGVAFAIEKYVL 269
 
Name Accession Description Interval E-value
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 24-276 4.67e-64

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: 201.28  E-value: 4.67e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFvsrlnIAALESGKYVIAINGCSIFDMHKRIqIYKKTVSGEVLLE 103
Cdd:cd07516    14 DKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPY-----LEELGLDSPLITFNGALVYDPTGKE-ILERLISKEDVKE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETEVYSDGKVfysKETDWTLRDVRMCGLNGEEAPDFEKFLLENqnsFFKMLIPGEPEKIQELQKKLKASL 183
Cdd:cd07516    88 LEEFLRKLGIGINIYTNDDW---ADTIYEENEDDEIIKPAEILDDLLLPPDED---ITKILFVGEDEELDELIAKLPEEF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 GEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:cd07516   162 FDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAMGNAIDEVKEAADYVT-L 240

                         250
                  ....*....|...
gi 2540503233 264 TNNDDGVADFIEK 276
Cdd:cd07516   241 TNNEDGVAKAIEK 253
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 26-274 8.01e-62

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 195.53  E-value: 8.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLEAH 105
Cdd:pfam08282  15 KISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDD-----PVICYNGALIYDENGKI-LYSNPISKEAVKEII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 106 KIAVEEGFETEVYSDGKVFYSKETDWtLRDVRMCGLNGEEAPDFEKFLLENQNSFFKMLIPGEPEKIQELQKKLKASLGE 185
Cdd:pfam08282  89 EYLKENNLEILLYTDDGVYILNDNEL-EKILKELNYTKSFVPEIDDFELLEDEDINKILILLDEEDLDELEKELKELFGS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 186 KAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeKTN 265
Cdd:pfam08282 168 LITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNASPEVKAAADYVT-DSN 246


                  ....*....
gi 2540503233 266 NDDGVADFI 274
Cdd:pfam08282 247 NEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 24-277 4.60e-47

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: 155.68  E-value: 4.60e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLE 103
Cdd:COG0561    17 DGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDD-----PLITSNGALIYDPDGEV-LYERPLDPEDVRE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETevysdgkvfysketdwtlrdvrmcglngeeapdfekfllenqnsffkmlipgepekiqelqkklkasl 183
Cdd:COG0561    91 ILELLREHGLHL-------------------------------------------------------------------- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 gekAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:COG0561   103 ---QVVVRSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNAPPEVKAAADYVT-G 178

                         250
                  ....*....|....
gi 2540503233 264 TNNDDGVADFIEKY 277
Cdd:COG0561   179 SNDEDGVAEALEKL 192
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 26-274 1.71e-46

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: 156.27  E-value: 1.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIqIYKKTVSGEVLLEAH 105
Cdd:TIGR00099  16 TISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDT-----PFITANGAAVIDDQGEI-LYKKPLDLDLVEEIL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 106 KIAVEEGFETEVYSDGKVFYSKETDWTLrDVRMCGLNGEEAPDFEKFLLENQNsFFKMLIPGEPEKIQELQKKLKAS-LG 184
Cdd:TIGR00099  90 NFLKKHGLDVILYGDDSIYASKNDPEYF-TIFKKFLGEPKLEVVDIQYLPDDI-LKILLLFLDPEDLDLLIEALNKLeLE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 185 EKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeKT 264
Cdd:TIGR00099 168 ENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNADEELKALADYVT-DS 246

                         250
                  ....*....|
gi 2540503233 265 NNDDGVADFI 274
Cdd:TIGR00099 247 NNEDGVALAL 256
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 24-279 7.82e-35

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 126.35  E-value: 7.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAleSGKYVIAINGCSIfdmhkriqiyKKTVSGEVLLE 103
Cdd:PRK10513   18 DHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQ--PGDYCITNNGALV----------QKAADGETVAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 A----------HKIAVEEGFETEVYsDGKVFYSKETD---WTLRDVRMCG--LNGEEAPDFEKFLlenqnSFFKMLIPGE 168
Cdd:PRK10513   86 TalsyddylylEKLSREVGVHFHAL-DRNTLYTANRDisyYTVHESFLTGipLVFREVEKMDPNL-----QFPKVMMIDE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 169 PEKIQELQKKLKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVN 248
Cdd:PRK10513  160 PEILDAAIARIPAEVKERYTVLKSAPYFLEILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQENDIAMIEYAGVGVAMGN 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2540503233 249 GNEHIKSIADFVTeKTNNDDGVADFIEKYIL 279
Cdd:PRK10513  240 AIPSVKEVAQFVT-KSNLEDGVAFAIEKYVL 269
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 24-277 1.55e-26

phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 103.07  E-value: 1.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIaalesgKYVIAINGCSIFDmHKRIqIYKKTVSGEVLLE 103
Cdd:cd07517    15 DTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGI------DSYVSYNGQYVFF-EGEV-IYKNPLPQELVER 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFEtevysdgkvfysketdwtlrdvrmcglngeeapdfekFLLENQNSFFkmlipgepEKIQELQKKLKASL 183
Cdd:cd07517    87 LTEFAKEQGHP-------------------------------------VSFYGQLLLF--------EDEEEEQKYEELRP 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 184 GEKAVIFTskPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeK 263
Cdd:cd07517   122 ELRFVRWH--PLSTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNAHEELKEIADYVT-K 198

                         250
                  ....*....|....
gi 2540503233 264 TNNDDGVADFIEKY 277
Cdd:cd07517   199 DVDEDGILKALKHF 212
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 160-275 3.98e-20

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: 85.33  E-value: 3.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 160 FFKMLIPGEPEKIQELQKKLKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEK 239
Cdd:cd07518    70 YFKFTLNVPDEAAPDIIDELNQKFGGILRAVTSGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKY 149

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2540503233 240 CGYGVAMVNGNEHIKSIADFVTeKTNNDDGVADFIE 275
Cdd:cd07518   150 AGYSYAMENAPEEVKAAAKYVA-PSNNENGVLQVIE 184
PLN02887 PLN02887
hydrolase family protein
 26-277 4.20e-18

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 83.77  E-value: 4.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIkpfVSRLNIAALESGKYVIA-------INGCSIFDMHKRiQIYKKTVSG 98
Cdd:PLN02887  325 QISETNAKALKEALSRGVKVVIATGKARPAV---IDILKMVDLAGKDGIISesspgvfLQGLLVYGRQGR-EIYRSNLDQ 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  99 EVLLEA------HKIAVeegfetevysdgkVFYSKETDWTLRDVRMCGL--------NGEEAPDFEKFLLENQNSffKML 164
Cdd:PLN02887  401 EVCREAclysleHKIPL-------------IAFSQDRCLTLFDHPLVDSlhtiyhepKAEIMSSVDQLLAAADIQ--KVI 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 165 IPGEPEKIQE-LQKKLKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYG 243
Cdd:PLN02887  466 FLDTAEGVSSvLRPYWSEATGDRANVVQAQPDMLEIVPPGTSKGNGVKMLLNHLGVSPDEIMAIGDGENDIEMLQLASLG 545

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2540503233 244 VAMVNGNEHIKSIADfVTEKTNNDDGVADFIEKY 277
Cdd:PLN02887  546 VALSNGAEKTKAVAD-VIGVSNDEDGVADAIYRY 578
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 24-265 4.22e-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: 77.89  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  24 ERKISDRNAEILKRCAQRGIYVVLCSGRaedgIKPFVSRLNIAALESGkYVIAINGCSIFDMHKRIQIYkktvsgEVLLE 103
Cdd:TIGR01482  13 NRAINESALEAIRKAESKGIPVVLVTGN----SVQFARALAKLIGTPD-PVIAENGGEISYNEGLDDIF------LAYLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 104 AHKIAVEEGFETEVYSDGKVFYSKETD-WTLRDvrmcGLNGEEAPdfekfllenqnsffkmlipgepEKIQELQKKLKAS 182
Cdd:TIGR01482  82 EEWFLDIVIAKTFPFSRLKVQYPRRASlVKMRY----GIDVDTVR----------------------EIIKELGLNLVAV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 183 LGEKAViftskpyflEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTE 262
Cdd:TIGR01482 136 DSGFDI---------HILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAVANAQPELKEWADYVTE 206


                  ...
gi 2540503233 263 KTN 265
Cdd:TIGR01482 207 SPY 209
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 205-277 1.02e-16

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: 74.93  E-value: 1.02e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540503233 205 GKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTEKTNNdDGVADFIEKY 277
Cdd:cd07514    67 DKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYG-DGVLEAIDKL 138
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 26-246 1.50e-15

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: 73.57  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRIQIYKKTVSGEVLLEAH 105
Cdd:TIGR01484  17 ELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPL-----PLIAENGALIFYPGEILYIEPSDVFEEILGIKF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 106 KIAVEegfETEVYSDGKVFYSKETDWTLRDVRMCGLNGEEApdfekfllenqnsffkmLIPGEPEKIqelqKKLKASLGE 185
Cdd:TIGR01484  92 EEIGA---ELKSLSEHYVGTFIEDKAIAVAIHYVGAELGQE-----------------LDSKMRERL----EKIGRNDLE 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540503233 186 KAVIFTSKpYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAM 246
Cdd:TIGR01484 148 LEAIYSGK-TDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 172-279 1.72e-15

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 73.85  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 172 IQELQKKLKaSLGEKAVIFTSKpYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNE 251
Cdd:PRK01158  126 VEEVRELLE-ELGLDLEIVDSG-FAIHIKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADE 203

                          90       100
                  ....*....|....*....|....*...
gi 2540503233 252 HIKSIADFVTEKTNNdDGVADFIEKYIL 279
Cdd:PRK01158  204 ELKEAADYVTEKSYG-EGVAEAIEHLLL 230
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 25-274 7.34e-14

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


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 69.00  E-value: 7.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  25 RKISDRNAEILKRCAQRGIYVVLCSGRaedgIKPFVSRLNIAALESGKyVIAINGCSIFDMHKRIqiykktvsgevllea 104
Cdd:TIGR01487  17 RMISERAIEAIRKAEKKGIPVSLVTGN----TVPFARALAVLIGTSGP-VVAENGGVIFYNKEDI--------------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 105 hkiaveegfetevysdgkVFYSKETDWTLRDvrmcglngEEAPDFEKFLLENQNSFFKMLIPGEPEKIQELQKKLKaslg 184
Cdd:TIGR01487  77 ------------------FLANMEEEWFLDE--------EKKKRFPRDRLSNEYPRASLVIMREGKDVDEVREIIK---- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 185 EKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTEKT 264
Cdd:TIGR01487 127 ERGLNLVASGFAIHIMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAVANADDQLKEIADYVTSNP 206

                         250
                  ....*....|
gi 2540503233 265 NNdDGVADFI 274
Cdd:TIGR01487 207 YG-EGVVEVL 215
PRK15126 PRK15126
HMP-PP phosphatase;
26-248 8.12e-14

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 69.72  E-value: 8.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  26 KISDRNAEILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMHKRiQIYKKTVSGEV---LL 102
Cdd:PRK15126   19 HLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDA-----YLITGNGTRVHSLEGE-LLHRQDLPADVaelVL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 103 EAHkiaveegFETE----VYSDGKVFYSKETDWTLRDVRMCGLNGEEApDFEKfLLENQNSffKMLIPGEPEKIQELQKK 178
Cdd:PRK15126   93 HQQ-------WDTRasmhVFNDDGWFTGKEIPALLQAHVYSGFRYQLI-DLKR-LPAHGVT--KICFCGDHDDLTRLQIQ 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 179 LKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVN 248
Cdd:PRK15126  162 LNEALGERAHLCFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLGSVGRGFIMGN 231
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 211-279 2.96e-13

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 68.13  E-value: 2.96e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540503233 211 EWLSSfIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTeKTNNDDGVADFIEKYIL 279
Cdd:PRK10530  206 QWVEA-QGWSMKNVVAFGDNFNDISMLEAAGLGVAMGNADDAVKARADLVI-GDNTTPSIAEFIYSHVL 272
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 144-252 9.69e-12

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


Pssm-ID: 428314 [Multi-domain]  Cd Length: 246  Bit Score: 63.44  E-value: 9.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 144 EEAPDFEKFLL---ENQN----SFFkmLIP-GEPEKIQELQKKL-KASLGEKaVIFTSKpYFLEILPPDCGKGEAIEWLS 214
Cdd:pfam05116  98 EALAKFPGLTLqpeEEQRphkvSYF--LDPeAAAAVLAELEQLLrKRGLDVK-VIYSSG-RDLDILPLRASKGEALRYLA 173

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2540503233 215 SFIGIDHSTTLAFGDSMNDESMIEKCGYGVaMVnGNEH 252
Cdd:pfam05116 174 LKLGLPLENTLVCGDSGNDEELFIGGTRGV-VV-GNAQ 209
PRK10976 PRK10976
putative hydrolase; Provisional
 33-276 1.19e-10

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 60.45  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  33 EILKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIAAlesgkYVIAINGCSIFDMhkriqiykktvSGEvLLEAHKIAVEEG 112
Cdd:PRK10976   26 ETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKS-----YMITSNGARVHDT-----------DGN-LIFSHNLDRDIA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 113 FE--TEVYSDGKVF--YSKETDWTLrdvrmcglnGEEAPDFEKFLlenQNSFFKMLI--PGE---------------PEK 171
Cdd:PRK10976   89 SDlfGVVHDNPDIItnVYRDDEWFM---------NRHRPEEMRFF---KEAVFKYQLyePGLlepdgvskvfftcdsHEK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 172 IQELQKKLKASLGEKAVIFTSKPYFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNE 251
Cdd:PRK10976  157 LLPLEQAINARWGDRVNVSFSTLTCLEVMAGGVSKGHALEAVAKKLGYSLKDCIAFGDGMNDAEMLSMAGKGCIMGNAHQ 236

                         250       260
                  ....*....|....*....|....*....
gi 2540503233 252 HIKsiaDFVTE----KTNNDDGVADFIEK 276
Cdd:PRK10976  237 RLK---DLLPEleviGSNADDAVPHYLRK 262
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 115-277 8.10e-10

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: 57.74  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 115 TEVYSDGKVFYSKETDWT--LRDVRMCGLNGEEAPDFEKFLL---ENQN----SFFKmlipgEPEKIQELQKKLKA---S 182
Cdd:cd02605    70 TEIYYGESGYLEPDTYWNevLSEGWERFLFEAIADLFKQLKPqseLEQNphkiSFYL-----DPQNDAAVIEQLEEmllK 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 183 LGEKAVIFTSKP--YFLEILPPDCGKGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFV 260
Cdd:cd02605   145 AGLTVRIIYSSGlaYDLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAQPELLKWADRV 224

                         170       180
                  ....*....|....*....|.
gi 2540503233 261 TE----KTNNDDGVADFIEKY 277
Cdd:cd02605   225 TRsrlaKGPYAGGILEGLAHF 245
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 205-258 8.08e-07

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


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 48.68  E-value: 8.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2540503233 205 GKGEAI-EWLSSFiGIDHSTTLAFGDSMNDESMIEKCGYGVAmVNGNEHIKSIAD 258
Cdd:COG0560   155 GKAEALrELAAEL-GIDLEQSYAYGDSANDLPMLEAAGLPVA-VNPDPALREAAD 207
PRK03669 PRK03669
mannosyl-3-phosphoglycerate phosphatase-related protein;
35-244 7.49e-05

mannosyl-3-phosphoglycerate phosphatase-related protein;


Pssm-ID: 179628 [Multi-domain]  Cd Length: 271  Bit Score: 43.08  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233  35 LKRCAQRGIYVVLCSGRAEDGIKPFVSRLNIaaleSGKYVIAINGCSI-FDMHKRIQI-YKKTVSG----EVLLEAHKIA 108
Cdd:PRK03669   33 LTRLREAQVPVILCSSKTAAEMLPLQQTLGL----QGLPLIAENGAVIqLDEQWQDHPdFPRIISGishgEIRQVLNTLR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 109 VEEGFETEVYSDgkvfYSKET--DWTlrdvrmcGLNGEEAPdfekflLENQNSFFKMLI-PGEPEKIQELQKKLkASLGE 185
Cdd:PRK03669  109 EKEGFKFTTFDD----VDDATiaEWT-------GLSRSQAA------LARLHEASVTLIwRDSDERMAQFTARL-AELGL 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540503233 186 KaviFTSKPYFLEILPPDCGKGEAIEWLssfigIDHS--------TTLAFGDSMNDESMIEKCGYGV 244
Cdd:PRK03669  171 Q---FVQGARFWHVLDASAGKDQAANWL-----IATYqqlsgtrpTTLGLGDGPNDAPLLDVMDYAV 229
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 206-275 8.36e-04

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: 39.04  E-value: 8.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 206 KGEAIEWLSSFIGIDHSTTLAFGDSMNDESMIEKCGYGVAMVNGNEHIKSIADFVTEKTNNDDGVADFIE 275
Cdd:cd01630    77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
163-261 1.06e-03

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 38.60  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540503233 163 MLIPGEPEKIQELQKKLKAslgekaVIFTSK------------PYFLEILPPDCG---KGEAIEWLSSfigidhSTTLAF 227
Cdd:COG4087    30 KLIPGVKERLEELAEKLEI------HVLTADtfgtvakelaglPVELHILPSGDQaeeKLEFVEKLGA------ETTVAI 97

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2540503233 228 GDSMNDESMIEKCGYGVAmVNGNE--HIKSI--ADFVT 261
Cdd:COG4087    98 GNGRNDVLMLKEAALGIA-VIGPEgaSVKALlaADIVV 134
 
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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