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Conserved domains on  [gi|550714597|ref|WP_022647486|]
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MULTISPECIES: pyridoxal phosphatase [Enterobacter]

Protein Classification

HAD family hydrolase( domain architecture ID 11484771)

The HAD (haloacid dehalogenase) family of hydrolase includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-272 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


:

Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 603.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVL 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  81 TSDPLPVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRTSNWALSLPEAQRPVFTQVSSLRQAAEDVQAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 161 TDEDTAKLNTFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|..
gi 550714597 241 GNADDAVKARANVVIGDNTTDSIAQYIYTHLL 272
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSHVL 272
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-272 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 603.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVL 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  81 TSDPLPVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRTSNWALSLPEAQRPVFTQVSSLRQAAEDVQAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 161 TDEDTAKLNTFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|..
gi 550714597 241 GNADDAVKARANVVIGDNTTDSIAQYIYTHLL 272
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSHVL 272
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-267 2.43e-83

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: 250.26  E-value: 2.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKkVLTSDP 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGE-ILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   85 LPVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRTSNWALSLPEaqrPVFTQVSSLRQaaeDVQAIWKFALTDED 164
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPK---LEVVDIQYLPD---DILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  165 TAKLNTFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNAD 244
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 550714597  245 DAVKARANVVIGDNTTDSIAQYI 267
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-268 9.68e-81

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: 243.66  E-value: 9.68e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVLtsDP 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL--ER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  85 LPVPQALQ-LIDLLDEHAIHGLMYVDNAM---LYERPTGHVIRTSNWALSLPEAQRPVftqvsslrqaaedvqAIWKFAL 160
Cdd:cd07516   79 LISKEDVKeLEEFLRKLGIGINIYTNDDWadtIYEENEDDEIIKPAEILDDLLLPPDE---------------DITKILF 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 161 TDEDTAKLNTFAK-HVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVA 239
Cdd:cd07516  144 VGEDEELDELIAKlPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVA 223

                        250       260
                 ....*....|....*....|....*....
gi 550714597 240 MGNADDAVKARANVVIGDNTTDSIAQYIY 268
Cdd:cd07516  224 MGNAIDEVKEAADYVTLTNNEDGVAKAIE 252
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-267 9.00e-79

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 238.68  E-value: 9.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    6 IALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQaKKVLTSDPL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDEN-GKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   86 PVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRtsnwalsLPEAQRPVFTQVSSLRQAAEDVQAIWKFaLTDEDT 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKI-------LKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  166 AKLNTFAKHVEHTLG--LECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNA 243
Cdd:pfam08282 152 EDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 550714597  244 DDAVKARANVVIGDNTTDSIAQYI 267
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-267 1.21e-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: 200.36  E-value: 1.21e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQaKKVLTSD 83
Cdd:COG0561    3 KLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPD-GEVLYER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  84 PLPVPQALQLIDLLDEHAIHGLMYVdnamlyerptghvirtsnwalslpeaqrpvftqvsslrqaaedvqaiwkfaltde 163
Cdd:COG0561   82 PLDPEDVREILELLREHGLHLQVVV------------------------------------------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 164 dtaklntfakhvehtlgleceWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNA 243
Cdd:COG0561  107 ---------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNA 165

                        250       260
                 ....*....|....*....|....
gi 550714597 244 DDAVKARANVVIGDNTTDSIAQYI 267
Cdd:COG0561  166 PPEVKAAADYVTGSNDEDGVAEAL 189
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-272 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 603.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVL 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  81 TSDPLPVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRTSNWALSLPEAQRPVFTQVSSLRQAAEDVQAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 161 TDEDTAKLNTFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|..
gi 550714597 241 GNADDAVKARANVVIGDNTTDSIAQYIYTHLL 272
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSHVL 272
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-267 2.43e-83

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: 250.26  E-value: 2.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKkVLTSDP 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDDQGE-ILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   85 LPVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRTSNWALSLPEaqrPVFTQVSSLRQaaeDVQAIWKFALTDED 164
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEPK---LEVVDIQYLPD---DILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  165 TAKLNTFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNAD 244
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 550714597  245 DAVKARANVVIGDNTTDSIAQYI 267
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-268 9.68e-81

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: 243.66  E-value: 9.68e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVLtsDP 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL--ER 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  85 LPVPQALQ-LIDLLDEHAIHGLMYVDNAM---LYERPTGHVIRTSNWALSLPEAQRPVftqvsslrqaaedvqAIWKFAL 160
Cdd:cd07516   79 LISKEDVKeLEEFLRKLGIGINIYTNDDWadtIYEENEDDEIIKPAEILDDLLLPPDE---------------DITKILF 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 161 TDEDTAKLNTFAK-HVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVA 239
Cdd:cd07516  144 VGEDEELDELIAKlPEEFFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVA 223

                        250       260
                 ....*....|....*....|....*....
gi 550714597 240 MGNADDAVKARANVVIGDNTTDSIAQYIY 268
Cdd:cd07516  224 MGNAIDEVKEAADYVTLTNNEDGVAKAIE 252
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-267 9.00e-79

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 238.68  E-value: 9.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    6 IALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQaKKVLTSDPL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDEN-GKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   86 PVPQALQLIDLLDEHAIHGLMYVDNAMLYERPTGHVIRtsnwalsLPEAQRPVFTQVSSLRQAAEDVQAIWKFaLTDEDT 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKI-------LKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  166 AKLNTFAKHVEHTLG--LECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNA 243
Cdd:pfam08282 152 EDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 550714597  244 DDAVKARANVVIGDNTTDSIAQYI 267
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 4-267 1.21e-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: 200.36  E-value: 1.21e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQaKKVLTSD 83
Cdd:COG0561    3 KLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPD-GEVLYER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  84 PLPVPQALQLIDLLDEHAIHGLMYVdnamlyerptghvirtsnwalslpeaqrpvftqvsslrqaaedvqaiwkfaltde 163
Cdd:COG0561   82 PLDPEDVREILELLREHGLHLQVVV------------------------------------------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 164 dtaklntfakhvehtlgleceWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNA 243
Cdd:COG0561  107 ---------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMGNA 165

                        250       260
                 ....*....|....*....|....
gi 550714597 244 DDAVKARANVVIGDNTTDSIAQYI 267
Cdd:COG0561  166 PPEVKAAADYVTGSNDEDGVAEAL 189
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 4-265 2.05e-40

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


Pssm-ID: 319819 [Multi-domain]  Cd Length: 213  Bit Score: 138.89  E-value: 2.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTpAICCNGTYLYDyqAKKVLTSD 83
Cdd:cd07517    1 KIVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQYVFF--EGEVIYKN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  84 PLPVPQALQLIDLLDEHAiHGLMYVDNAMLYERPTghvirtsnwALSLPEAQRPVFTQVSslrqaaedvqaiwkfaltde 163
Cdd:cd07517   78 PLPQELVERLTEFAKEQG-HPVSFYGQLLLFEDEE---------EEQKYEELRPELRFVR-------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 164 dtaklntfakhvehtlglecewsWHDQ-VDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGN 242
Cdd:cd07517  128 -----------------------WHPLsTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGN 184

                        250       260
                 ....*....|....*....|...
gi 550714597 243 ADDAVKARANVVIGDNTTDSIAQ 265
Cdd:cd07517  185 AHEELKEIADYVTKDVDEDGILK 207
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-267 4.67e-29

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 110.94  E-value: 4.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPA---ICCNGTYLYDYQAK 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGdycITNNGALVQKAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  78 KVLTSDPLPVPQALQLIDLLDEHAIHgLMYVDNAMLY------ERPTGHvirtSNWALSLPEAQRPVFTQVSSLRqaAED 151
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVH-FHALDRNTLYtanrdiSYYTVH----ESFLTGIPLVFREVEKMDPNLQ--FPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 152 VQAIWKFALTDEDTAKLN-------TFAKHVEHTLglecewswhdqvDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDN 224
Cdd:PRK10513 154 VMMIDEPEILDAAIARIPaevkeryTVLKSAPYFL------------EILDKRVNKGTGVKSLAEHLGIKPEEVMAIGDQ 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 550714597 225 YNDISMLEAAGTGVAMGNADDAVKARANVVIGDNTTDSIAQYI 267
Cdd:PRK10513 222 ENDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAI 264
PRK10976 PRK10976
putative hydrolase; Provisional
 4-267 9.84e-25

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 99.35  E-value: 9.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVLTSD 83
Cdd:PRK10976   3 QVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHDTDGNLIFSHN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  84 plpvpqalqlidlLDEHAIHGL--MYVDNAMLYErptgHVIRTSNWALSLPEAQRPVFTQVSSL-----RQAAEDVQAIW 156
Cdd:PRK10976  83 -------------LDRDIASDLfgVVHDNPDIIT----NVYRDDEWFMNRHRPEEMRFFKEAVFkyqlyEPGLLEPDGVS 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 157 KFALTDEDTAKLntfakhvehtLGLE--CEWSWHDQVDIA----------RKGNSKGKRLTQFVESQGWSMQDVIAFGDN 224
Cdd:PRK10976 146 KVFFTCDSHEKL----------LPLEqaINARWGDRVNVSfstltclevmAGGVSKGHALEAVAKKLGYSLKDCIAFGDG 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 550714597 225 YNDISMLEAAGTGVAMGNADDAVK-ARANV-VIGDNTTDSIAQYI 267
Cdd:PRK10976 216 MNDAEMLSMAGKGCIMGNAHQRLKdLLPELeVIGSNADDAVPHYL 260
PRK15126 PRK15126
HMP-PP phosphatase;
4-272 6.37e-24

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 97.46  E-value: 6.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAkKVLTSD 83
Cdd:PRK15126   3 RLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHSLEG-ELLHRQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  84 PLPvPQALQLIdlldehaIHGlMYVDNAMLyerptgHVIRTSNW--ALSLPEAQRPvfTQVSSLRQAAEDVQAIWKFALT 161
Cdd:PRK15126  82 DLP-ADVAELV-------LHQ-QWDTRASM------HVFNDDGWftGKEIPALLQA--HVYSGFRYQLIDLKRLPAHGVT 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 162 D-------EDTAKLNTfakHVEHTLGLECE--WSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLE 232
Cdd:PRK15126 145 KicfcgdhDDLTRLQI---QLNEALGERAHlcFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAMNDREMLG 221

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 550714597 233 AAGTGVAMGNADDAVKARAN--VVIGDNTTDSIAQYIyTHLL 272
Cdd:PRK15126 222 SVGRGFIMGNAMPQLRAELPhlPVIGHCRNQAVSHYL-THWL 262
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 4-267 9.01e-22

Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to the haloacid dehalogenase-like superfamily; Escherichia coli YbiV can act as both a sugar phosphatase and as a phosphotransferase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319820 [Multi-domain]  Cd Length: 184  Bit Score: 89.57  E-value: 9.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSL-EALKRAREAGYQLLIVTGRhhvaihpfyqalgldtpaiccngtylydyqakkvlts 82
Cdd:cd07518    1 KLIATDMDGTFLNDDKTYDHERFfAILDQLLKKGIKFVVASGR------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  83 dplpvpQALQLIDLLDEHAiHGLMYV-DNamlyerptGHVIRTsNWALSLPEAQRPvftqvsslrqaaedvqaiwkfALT 161
Cdd:cd07518   44 ------QYYQLISFFPEIK-DEMSFVaEN--------GAVVYF-KFTLNVPDEAAP---------------------DII 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 162 DEDTAKLNTFAKHVEhtlglecewSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMG 241
Cdd:cd07518   87 DELNQKFGGILRAVT---------SGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAME 157

                        250       260
                 ....*....|....*....|....*.
gi 550714597 242 NADDAVKARANVVIGDNTTDSIAQYI 267
Cdd:cd07518  158 NAPEEVKAAAKYVAPSNNENGVLQVI 183
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-272 1.83e-18

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 81.56  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRhhvaIHPFYQA----LGLDTPAICCNG-TYLYDYQ 75
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGN----VLCFARAaaklIGTSGPVIAENGgVISVGFD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  76 AKKVLTSDplpVPQALQLIDLLDEHaiHGLMYVDNAMLYE--RPTGHVIRTSnwalslpeaqRPVFTQVSSLRQAAEDVQ 153
Cdd:PRK01158  77 GKRIFLGD---IEECEKAYSELKKR--FPEASTSLTKLDPdyRKTEVALRRT----------VPVEEVRELLEELGLDLE 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 154 AIwkfaltdeDTAklntFAKHVEHtlglecewswhdqvdiarKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEA 233
Cdd:PRK01158 142 IV--------DSG----FAIHIKS------------------PGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEV 191

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 550714597 234 AGTGVAMGNADDAVKARANVVIGDNTTDSIAQYIYtHLL 272
Cdd:PRK01158 192 AGFGVAVANADEELKEAADYVTEKSYGEGVAEAIE-HLL 229
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 4-254 3.31e-17

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: 77.86  E-value: 3.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYDYQAKKVLTsd 83
Cdd:TIGR01487   2 KLVAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGNTVPFARALAVLIGTSGPVVAENGGVIFYNKEDIFLA-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   84 plpvpqalqlidLLDEhaihglmyvdNAMLYERPTGHVIRtSNWALSLPEAQRPVftqvsslrqaaedvqaiwkfaltDE 163
Cdd:TIGR01487  80 ------------NMEE----------EWFLDEEKKKRFPR-DRLSNEYPRASLVI-----------------------MR 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  164 DTAKLNTfAKHVEHTLGLECEWS---WHdqvdIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:TIGR01487 114 EGKDVDE-VREIIKERGLNLVASgfaIH----IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKVAV 188

                         250
                  ....*....|....
gi 550714597  241 GNADDAVKARANVV 254
Cdd:TIGR01487 189 ANADDQLKEIADYV 202
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-240 4.01e-17

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: 77.42  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    5 VIALDLDGTLLTPQK-TLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGtYLYDYQAKKVLTSD 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPNAhELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENG-ALIFYPGEILYIEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   84 plpvPQALQLIdlldEHAIHGLMyvdNAMLYErptghvirtsnwalslpEAQRPVFTQVsslRQAAEDVQAIWKFALTDE 163
Cdd:TIGR01484  80 ----SDVFEEI----LGIKFEEI---GAELKS-----------------LSEHYVGTFI---EDKAIAVAIHYVGAELGQ 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  164 DTAKLNtFAKHVEH---TLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:TIGR01484 129 ELDSKM-RERLEKIgrnDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-254 3.40e-16

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


Pssm-ID: 273650 [Multi-domain]  Cd Length: 225  Bit Score: 75.58  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    6 IALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRhhvaIHPFYQAL----GLDTPAICCNGTYLYDYQAKKVlt 81
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGN----SVQFARALakliGTPDPVIAENGGEISYNEGLDD-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   82 sdplpvpqalQLIDLLDEHAIhglmyvdnamLYERPTGHVIRtSNWALSLPEAQRPVFtqvsslrqaaedvqaiwkfalt 161
Cdd:TIGR01482  75 ----------IFLAYLEEEWF----------LDIVIAKTFPF-SRLKVQYPRRASLVK---------------------- 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  162 DEDTAKLNTfAKHVEHTLGLEC-EWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAM 240
Cdd:TIGR01482 112 MRYGIDVDT-VREIIKELGLNLvAVDSGFDIHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAV 190

                         250
                  ....*....|....
gi 550714597  241 GNADDAVKARANVV 254
Cdd:TIGR01482 191 ANAQPELKEWADYV 204
PLN02887 PLN02887
hydrolase family protein
 4-268 5.39e-16

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 77.22  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLD---------TPAICCNGTYLYDY 74
Cdd:PLN02887 309 SYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYGR 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  75 QAKKVLTSD------------------PLPVPQALQLIDLLDEHAIHGLMYVdnamlYERPTGHVIRTSNWALSLPEAQR 136
Cdd:PLN02887 389 QGREIYRSNldqevcreaclyslehkiPLIAFSQDRCLTLFDHPLVDSLHTI-----YHEPKAEIMSSVDQLLAAADIQK 463

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 137 PVFtqVSSLRQAAEDVQAIWKFALTDEdtaklntfaKHVEHTLGlecewswhDQVDIARKGNSKGKRLTQFVESQGWSMQ 216
Cdd:PLN02887 464 VIF--LDTAEGVSSVLRPYWSEATGDR---------ANVVQAQP--------DMLEIVPPGTSKGNGVKMLLNHLGVSPD 524

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550714597 217 DVIAFGDNYNDISMLEAAGTGVAMGNADDAVKARANVVIGDNTTDSIAQYIY 268
Cdd:PLN02887 525 EIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIY 576
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 197-272 3.04e-13

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: 65.30  E-value: 3.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550714597 197 GNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNADDAVKARANVVIGDNTTDSIAQYIYtHLL 272
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAID-KLL 139
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 197-251 3.38e-12

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: 64.09  E-value: 3.38e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 550714597 197 GNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMgNADDAVKARA 251
Cdd:COG0560  153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAA 206
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 5-245 3.25e-11

mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. Several members of this family from thermophiles (and from Dehalococcoides ethenogenes) are now known to act as mannosyl-3-phosphoglycerate (MPG) phosphatase. In these cases, the enzyme acts after MPG synthase to make the compatible solute mannosylglycerate. We propose that other mesophilic members of this family do not act as mannosyl-3-phosphoglycerate phosphatase. A member of this family is found in Escherichia coli, which appears to lack MPG synthase. Mannosylglycerate is imported in E. coli by phosphoenolpyruvate-dependent transporter (), but it appears the phosphorylation is not on the glycerate moiety, that the phosphorylated import is degraded by an alpha-mannosidase from an adjacent gene, and that E. coli would have no pathway to obtain MPG.


Pssm-ID: 130550 [Multi-domain]  Cd Length: 256  Bit Score: 62.03  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYdyqakkvLTSDP 84
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIY-------GPRGW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   85 LPVPQALQLIdlLDEhaihGLMYVDNAMLYERPTGHVIRTSNWALSLPEAQRpvFTQVS--SLRQAAE---DVQAIWKFA 159
Cdd:TIGR01486  74 RPEPEYPVIA--LGI----PYEKIRARLRELSEELGFKFRGLGDLTDEEIAE--LTGLSreLARLAQRreySETILWSEE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  160 LTDEDTAKLNTFakhvehtlGLECEWS---WHdqvdIARKGNSKGK---RLTQFVESQGWSMQdVIAFGDNYNDISMLEA 233
Cdd:TIGR01486 146 RRERFTEALVAV--------GLEVTHGgrfYH----VLGAGSDKGKavnALKAFYNQPGGAIK-VVGLGDSPNDLPLLEV 212

                         250
                  ....*....|..
gi 550714597  234 AGTGVAMGNADD 245
Cdd:TIGR01486 213 VDLAVVVPGPNG 224
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 1-244 6.71e-10

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 58.41  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYdyqakkvl 80
Cdd:PRK00192   2 MMKLLVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIY-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  81 tsdplpVPQALQLIDLLDEHAIHGLMYVDNAMLYERptghvIRTsnwALS-LPEAQRPVFTQVSSLRqaAEDVQaiwkfA 159
Cdd:PRK00192  74 ------IPKNYFPFQPDGERLKGDYWVIELGPPYEE-----LRE---ILDeISDELGYPLKGFGDLS--AEEVA-----E 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 160 LT--DEDTAKLntfAKHVEHT---LGLECEWSWHDQVDIA-------RKGN---------SKGK---RLTQFvesqgWSM 215
Cdd:PRK00192 133 LTglSGESARL---AKDREFSepfLWNGSEAAKERFEEALkrlglkvTRGGrflhllgggDKGKavrWLKEL-----YRR 204

                        250       260       270
                 ....*....|....*....|....*....|..
gi 550714597 216 QD---VIAFGDNYNDISMLEAAGTGVAMGNAD 244
Cdd:PRK00192 205 QDgveTIALGDSPNDLPMLEAADIAVVVPGPD 236
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-234 8.01e-10

haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii mannosyl-3-phosphoglycerate phosphatase and Persephonella marina glucosyl-3-phosphoglycerate phosphatase; This family includes Pyrococcus horikoshii and Thermus thermophilus HB27 mannosyl-3-phosphoglycerate phosphatases (MpgPs) which catalyze the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG), and Persephonella marina glucosyl-3-phosphoglycerate phosphatase (GpgP) which catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) to produce glucosylglycerate (GG). It also includes Methanococcoides burtonii MpgP protein which is able to dephosphorylate GPG to GG, and MPG to MG. Similar flexibilities in substrate specificity have been confirmed in vitro for the MpgPs from Thermus thermophiles and Pyrococcus horikoshii. Screens with natural substrates have not yet detected activity for another member Escherichia Coli YedP. 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: 319810 [Multi-domain]  Cd Length: 255  Bit Score: 57.76  E-value: 8.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   5 VIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLYdyqakkvltsdp 84
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIF------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  85 lpVPQALQLIDLLDEHaIHGLMYVDNAMLYE---------RPTGHVIRTSNWALSLPEAQRPVFTQVSSLRQAAE---DV 152
Cdd:cd07507   69 --IPRGYFKFPGRCKS-EGGYEVIELGKPYReiraalekiREETGFKITGFGDLTEEEIAELTGLPRERAALAKEreySE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 153 QAIWKFalTDEDTAKLNTfakhVEHTLGLECEWS---WHdqvdIARKGNSKGK---RLTQFVESQGwSMQDVIAFGDNYN 226
Cdd:cd07507  146 TIILRS--DEEEDEKVLE----ALEERGLKITKGgrfYH----VLGAGADKGKavaILAALYRQLY-EAIVTVGLGDSPN 214


                 ....*...
gi 550714597 227 DISMLEAA 234
Cdd:cd07507  215 DLPMLEAV 222
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 1-246 2.06e-08

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 53.68  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   1 MTSRVIALDLDGTLL-------TPqktllpsSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNG--TYL 71
Cdd:COG3769    1 MPPLLVFTDLDGTLLdhdtyswAA-------ALPALARLKARGIPVILNTSKTAAEVEPLRQELGLSDPFIVENGaaIFI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  72 ---YDYQAKKVLTSDPLPV-------PQALQLIDLL-DEHAIH----GLMYVDNAMLYerpTGhvirtsnwaLSLPEAQR 136
Cdd:COG3769   74 pkgYFAFPSGTADIDGYWVielgkpyAEIRAVLEQLrEELGFKftgfGDMSAEEVAEL---TG---------LSLEQAAL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 137 pvftqvSSLRQAAEDVqaIWkfaltDEDTAKLNTFAKHVEhTLGLEcewswhdqvdiARKG---------NSKGKRLTQF 207
Cdd:COG3769  142 ------AKQREFSEPL--LW-----LGSDEALERFIAALA-ALGLT-----------VLRGgrflhlmggADKGKAVRWL 196

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 550714597 208 VE--SQGWSMQDV-IAFGDNYNDISMLEAAGTGVAMGNADDA 246
Cdd:COG3769  197 VEqyRQRFGKNVVtIALGDSPNDIPMLEAADIAVVIRSPHGA 238
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-103 3.40e-08

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: 50.47  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   5 VIALDLDGTLLTPqktllpsslEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLD---TPAICCNGTYlydyqakkVLT 81
Cdd:cd01427    1 AVLFDLDGTLLAV---------ELLKRLRAAGIKLAIVTNRSREALRALLEKLGLGdlfDGIIGSDGGG--------TPK 63

                         90       100
                 ....*....|....*....|..
gi 550714597  82 SDPLPVPQALQLIDLLDEHAIH 103
Cdd:cd01427   64 PKPKPLLLLLLKLGVDPEEVLF 85
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 191-271 1.05e-06

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: 48.50  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 191 VDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNA-DDAVKARANVVIGDNTTDSIAQYIYT 269
Cdd:cd02605  161 LDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIALLSTGTRGVIVGNAqPELLKWADRVTRSRLAKGPYAGGILE 240


                 ..
gi 550714597 270 HL 271
Cdd:cd02605  241 GL 242
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 6-80 2.02e-06

Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.


Pssm-ID: 433132  Cd Length: 101  Bit Score: 45.15  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    6 IALDLDGTLLTpQKTLLPSSLEALKRAREAGYQLLIVT---GRHHVAIHPFYQALGLDTPA--ICCNGTYLYDY-----Q 75
Cdd:pfam13344   1 FLFDIDGVLWR-GGEPIPGAAEALRALRAAGKPVVFVTnnsSRSREEYAEKLRKLGFDIDEdeIITSGTAAADYlkerkF 79


                  ....*
gi 550714597   76 AKKVL 80
Cdd:pfam13344  80 GKKVL 84
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 197-239 3.15e-06

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 46.39  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 550714597 197 GNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVA 239
Cdd:cd07500  135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 170-235 3.47e-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: 46.43  E-value: 3.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550714597  170 TFAKHVEHTLGLECEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAG 235
Cdd:pfam00702 126 EAAEALLRLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HisB1/GmhB COG0241
Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino ...
 1-43 4.33e-06

Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily [Amino acid transport and metabolism]; Histidinol phosphatase/D-glycero-mannoheptose bisphosphatephosphatase, HAD superfamily is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 440011 [Multi-domain]  Cd Length: 176  Bit Score: 45.86  E-value: 4.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550714597   1 MTSRVIALDLDGTL-------LTPQK-TLLPSSLEALKRAREAGYQLLIVT 43
Cdd:COG0241    1 MMKKAVFLDRDGTInedvgyvKSPEEfEFLPGVLEALARLNEAGYRLVVVT 51
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 4-244 1.12e-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: 45.33  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597    4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYqLLIVTGRHHVAihpfyqalgldtpaiccngtylydyqAKKVLTSD 83
Cdd:pfam05116   3 LLLVSDLDNTLVDGDNEALARLNQLLEAYRPDVG-LVFATGRSLDS--------------------------AKELLKEK 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   84 PLPVPQALqlidlldehaihgLMYVDNAMLYerpTGHVIRTSNWALSL-----PEAQRPVFTQVSSLRQAAEDVQAIWK- 157
Cdd:pfam05116  56 PLPTPDYL-------------ITSVGTEIYY---GPSLVPDQSWQEHLdyhwdRQAVVEALAKFPGLTLQPEEEQRPHKv 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  158 -FALTDEDTAKLntfAKHVEHTL---GLECE--WSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISML 231
Cdd:pfam05116 120 sYFLDPEAAAAV---LAELEQLLrkrGLDVKviYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEELF 196

                         250
                  ....*....|...
gi 550714597  232 EAAGTGVAMGNAD 244
Cdd:pfam05116 197 IGGTRGVVVGNAQ 209
PRK14502 PRK14502
bifunctional mannosyl-3-phosphoglycerate synthase/mannosyl-3 phosphoglycerate phosphatase; ...
 4-233 5.87e-05

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


Pssm-ID: 184713 [Multi-domain]  Cd Length: 694  Bit Score: 44.15  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597   4 RVIALDLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGTYLY---DY----QA 76
Cdd:PRK14502 417 KIVYTDLDGTLLNPLTYSYSTALDALRLLKDKELPLVFCSAKTMGEQDLYRNELGIKDPFITENGGAIFipkDYfrlpFA 496

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  77 KKVLTSDPLPVPQALQLIDLldEHAIHGLMYVDNAMLYERPT-GHVIRTSNWALSLPEAQRpvFTQVsSLRQAAEDVQAI 155
Cdd:PRK14502 497 YDRVAGNYLVIELGMAYKDI--RHILKKALAEACTEIENSEKaGNIFITSFGDMSVEDVSR--LTDL-NLKQAELAKQRE 571

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597 156 WKFALTDE-DTAKLNTFAKHVEHTlGLecEWSWHDQVDIARKGNSKGKRLTQFVESQGWSMQDVIAF--GDNYNDISMLE 232
Cdd:PRK14502 572 YSETVHIEgDKRSTNIVLNHIQQS-GL--EYSFGGRFYEVTGGNDKGKAIKILNELFRLNFGNIHTFglGDSENDYSMLE 648


                 .
gi 550714597 233 A 233
Cdd:PRK14502 649 T 649
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
4-63 4.15e-04

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 40.86  E-value: 4.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550714597   4 RVIALDLDGTLLTpQKTLLPSSLEALKRAREAGYQLLIVT---GRHHVAIHPFYQALGLDTPA 63
Cdd:COG0647    9 DAFLLDLDGVLYR-GDEPIPGAVEALARLRAAGKPVLFLTnnsSRTPEDVAEKLRRLGIPVAE 70
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-44 6.51e-04

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 40.32  E-value: 6.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 550714597   1 MTSRVIAL-DLDGTLLTPQKTLLPSSLEALKRAREAGYQLLIVTG 44
Cdd:PTZ00174   2 EMKKTILLfDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGG 46
HAD_HisB-N cd07503
histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal ...
 4-43 1.09e-03

histidinol phosphate phosphatase and related phosphatases; This family includes the N-terminal domain of the Escherichia coli bifunctional enzyme histidinol-phosphate phosphatase/imidazole-glycerol-phosphate dehydratase, HisB. The N-terminal histidinol-phosphate phosphatase domain catalyzes the dephosphorylation of histidinol phosphate, the eight step of L-histidine biosynthesis. This family also includes Escherichia coli GmhB phosphatase which is highly specific for D-glycero-D-manno-heptose-1,7-bisphosphate, it removes the C(7)phosphate and not the C(1)phosphate, and this is the third essential step of lipopolysaccharide heptose biosynthesis. 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: 319806 [Multi-domain]  Cd Length: 142  Bit Score: 38.28  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 550714597   4 RVIALDLDGTLL-------TPQK-TLLPSSLEALKRAREAGYQLLIVT 43
Cdd:cd07503    1 KALFLDRDGVINvdvpyvhKPEDlEFLPGVIEALKKLKDAGYLVVVVT 48
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
3-45 1.79e-03

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 38.63  E-value: 1.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 550714597   3 SRVIALDLDGTLL----TPQK-TLLPSSLEALKR-AREAGYQLLIVTGR 45
Cdd:COG1877    3 RLLLFLDFDGTLApivpDPDAaRPPPELRELLRRlAARPGGAVAIVSGR 51
P-type_ATPase cd02609
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ...
 222-258 2.67e-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: 2.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 550714597 222 GDNYNDISMLEAAGTGVAMGNADDAVKARANVVIGDN 258
Cdd:cd02609  527 GDGVNDVLALKEADCSIAMASGSDATRQVAQVVLLDS 563
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 200-254 3.22e-03

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: 37.12  E-value: 3.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 550714597 200 KGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVAMGNADDAVKARANVV 254
Cdd:cd01630   77 KLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYV 131
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 196-239 3.52e-03

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). 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: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 37.67  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 550714597 196 KGNSKGKRLTQFVESQGWSMQDVIAFGDNYNDISMLEAAGTGVA 239
Cdd:cd02612  148 YGEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVGHPVA 191
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
20-102 7.29e-03

Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 36.83  E-value: 7.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714597  20 TLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDT--PAICCNGtylyDYQAKKvltSDPLPVPQALQLIDLL 97
Cdd:COG0546   84 RLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDDyfDAIVGGD----DVPPAK---PKPEPLLEALERLGLD 156


                 ....*
gi 550714597  98 DEHAI 102
Cdd:COG0546  157 PEEVL 161
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
27-58 7.52e-03

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 35.83  E-value: 7.52e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 550714597  27 EALKRAREAGYQLLIVTGrhHVAIHPFYQALG 58
Cdd:COG3153   91 AALEAARERGARAVVLLG--DPSLLPFYERFG 120
HAD-SF-IIIA TIGR01662
HAD-superfamily hydrolase, subfamily IIIA; This subfamily falls within the Haloacid ...
 4-44 7.79e-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: 35.84  E-value: 7.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 550714597    4 RVIALDLDGTLLTP--------QKTLLPSSLEALKRAREAGYQLLIVTG 44
Cdd:TIGR01662   1 KAVVLDLDGTLTDDvpyvsdedERILYPEVPDALAELKEAGYKVVIVTN 49
HAD pfam12710
haloacid dehalogenase-like hydrolase;
21-60 9.74e-03

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 36.36  E-value: 9.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 550714597   21 LLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLD 60
Cdd:pfam12710  85 LHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD 124
HAD_PTase cd07519
hydrolase domain of the bifunctional HAD hydrolase/UbiA family prenyltransferase proteins and ...
 6-69 9.80e-03

hydrolase domain of the bifunctional HAD hydrolase/UbiA family prenyltransferase proteins and related domains; belongs to the haloacid dehalogenase-like superfamily; This family includes bifunctional enzymes that have both an N-terminal HAD hydrolase domain and a C-terminal UbiA family prenyltransferase domain. The haloacid dehalogenase-like (HAD) hydrolases are 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 include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members 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. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases (PTases) and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. PTases catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.


Pssm-ID: 319821  Cd Length: 105  Bit Score: 35.02  E-value: 9.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550714597   6 IALDLDGTLLTPqktLLPSSLEALKRAREAGYQLLIVTGRHHVAIHPFYQALGLDTPAICCNGT 69
Cdd:cd07519    2 LVVDLDGTLLLP---YNAEVLDYIQAARAEGRSIVLATASDQRIADRIAAHLGLFDGVFASDGR 62
 
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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