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Conserved domains on  [gi|695748135|ref|WP_032674400|]
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MULTISPECIES: pyridoxal phosphatase [Enterobacteriaceae]

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
 1-270 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


:

Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 527.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   1 MDYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVI 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  81 ASDPLQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRTENWAKSLPESQRPVFKQVPSLSEASQNVDAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 161 TDSDTEKLHRFGQIVERELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 695748135 241 GNAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSH 270
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-270 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 527.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   1 MDYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVI 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  81 ASDPLQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRTENWAKSLPESQRPVFKQVPSLSEASQNVDAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 161 TDSDTEKLHRFGQIVERELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 695748135 241 GNAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSH 270
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-269 4.03e-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: 244.81  E-value: 4.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVIaSDP 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL-ERL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  85 LQPEQATQLVNLLDSYNVHSLMYADDAM---FYQNPTGHIIRTENWAKSLPESQRPvfkqvpslseasqnvDAIWKFALT 161
Cdd:cd07516   80 ISKEDVKELEEFLRKLGIGINIYTNDDWadtIYEENEDDEIIKPAEILDDLLLPPD---------------EDITKILFV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 162 DSDTEKLHRFGQIVER-ELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:cd07516  145 GEDEELDELIAKLPEEfFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAM 224

                        250       260
                 ....*....|....*....|....*....
gi 695748135 241 GNAVDEVKACADLVIGNNTETGIADVLNQ 269
Cdd:cd07516  225 GNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-267 3.65e-74

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: 227.15  E-value: 3.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYaEKRVIASDP 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDD-QGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   85 LQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRTENWAKSLPesqrpvFKQVPSLSEASQNVDAIWKFALTDSD 164
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEP------KLEVVDIQYLPDDILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  165 TEKLHRFGQIVERELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNAV 244
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 695748135  245 DEVKACADLVIGNNTETGIADVL 267
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-267 1.41e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 225.58  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    6 IALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYaEKRVIASDPL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE-NGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   86 QPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRtenwaksLPESQRPVFKQVPSLSEASQNVDAIWKFaLTDSDT 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKI-------LKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  166 EKLHRFGQIVERELG--LACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNA 243
Cdd:pfam08282 152 EDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 695748135  244 VDEVKACADLVIGNNTETGIADVL 267
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-270 3.61e-67

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: 206.91  E-value: 3.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   2 DYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKrVIA 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGE-VLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  82 SDPLQPEQATQLVNLLDSYNVHSLMYAddamfyqnptghiirtenwakslpesqrpvfkqvpslseasqnvdaiwkfalt 161
Cdd:COG0561   80 ERPLDPEDVREILELLREHGLHLQVVV----------------------------------------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 162 dsdteklhrfgqiverelglaceWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMG 241
Cdd:COG0561  107 -----------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 695748135 242 NAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
 
Name Accession Description Interval E-value
PRK10530 PRK10530
pyridoxal phosphate (PLP) phosphatase; Provisional
 1-270 0e+00

pyridoxal phosphate (PLP) phosphatase; Provisional


Pssm-ID: 182523 [Multi-domain]  Cd Length: 272  Bit Score: 527.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   1 MDYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVI 80
Cdd:PRK10530   1 MTYRVIALDLDGTLLTPKKTILPESLEALARAREAGYKVIIVTGRHHVAIHPFYQALALDTPAICCNGTYLYDYQAKKVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  81 ASDPLQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRTENWAKSLPESQRPVFKQVPSLSEASQNVDAIWKFAL 160
Cdd:PRK10530  81 EADPLPVQQALQVIEMLDEHQIHGLMYVDDAMLYEHPTGHVIRTLNWAQTLPPEQRPTFTQVDSLAQAARQVNAIWKFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 161 TDSDTEKLHRFGQIVERELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:PRK10530 161 THEDLPQLQHFAKHVEHELGLECEWSWHDQVDIARKGNSKGKRLTQWVEAQGWSMKNVVAFGDNFNDISMLEAAGLGVAM 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 695748135 241 GNAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:PRK10530 241 GNADDAVKARADLVIGDNTTPSIAEFIYSH 270
HAD_Pase cd07516
phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the ...
 5-269 4.03e-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: 244.81  E-value: 4.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVIaSDP 84
Cdd:cd07516    1 LIALDLDGTLLNSDKEISPRTKEAIKKAKEKGIKVVIATGRPLRGAQPYLEELGLDSPLITFNGALVYDPTGKEIL-ERL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  85 LQPEQATQLVNLLDSYNVHSLMYADDAM---FYQNPTGHIIRTENWAKSLPESQRPvfkqvpslseasqnvDAIWKFALT 161
Cdd:cd07516   80 ISKEDVKELEEFLRKLGIGINIYTNDDWadtIYEENEDDEIIKPAEILDDLLLPPD---------------EDITKILFV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 162 DSDTEKLHRFGQIVER-ELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:cd07516  145 GEDEELDELIAKLPEEfFDDLSVVRSAPFYLEIMPKGVSKGNALKKLAEYLGISLEEVIAFGDNENDLSMLEYAGLGVAM 224

                        250       260
                 ....*....|....*....|....*....
gi 695748135 241 GNAVDEVKACADLVIGNNTETGIADVLNQ 269
Cdd:cd07516  225 GNAIDEVKEAADYVTLTNNEDGVAKAIEK 253
Cof-subfamily TIGR00099
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ...
 5-267 3.65e-74

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: 227.15  E-value: 3.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYaEKRVIASDP 84
Cdd:TIGR00099   1 LIFIDLDGTLLNDDHTISPSTKEALAKLREKGIKVVLATGRPYKEVKNILKELGLDTPFITANGAAVIDD-QGEILYKKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   85 LQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRTENWAKSLPesqrpvFKQVPSLSEASQNVDAIWKFALTDSD 164
Cdd:TIGR00099  80 LDLDLVEEILNFLKKHGLDVILYGDDSIYASKNDPEYFTIFKKFLGEP------KLEVVDIQYLPDDILKILLLFLDPED 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  165 TEKLHRFGQIVERELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNAV 244
Cdd:TIGR00099 154 LDLLIEALNKLELEENVSVVSSGPYSIEITAKGVSKGSALQSLAEALGISLEDVIAFGDGMNDIEMLEAAGYGVAMGNAD 233

                         250       260
                  ....*....|....*....|...
gi 695748135  245 DEVKACADLVIGNNTETGIADVL 267
Cdd:TIGR00099 234 EELKALADYVTDSNNEDGVALAL 256
Hydrolase_3 pfam08282
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ...
 6-267 1.41e-73

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


Pssm-ID: 429897 [Multi-domain]  Cd Length: 255  Bit Score: 225.58  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    6 IALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYaEKRVIASDPL 85
Cdd:pfam08282   1 IASDLDGTLLNSDKKISEKTKEAIKKLKEKGIKFVIATGRPYRAILPVIKELGLDDPVICYNGALIYDE-NGKILYSNPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   86 QPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIRtenwaksLPESQRPVFKQVPSLSEASQNVDAIWKFaLTDSDT 165
Cdd:pfam08282  80 SKEAVKEIIEYLKENNLEILLYTDDGVYILNDNELEKI-------LKELNYTKSFVPEIDDFELLEDEDINKI-LILLDE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  166 EKLHRFGQIVERELG--LACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNA 243
Cdd:pfam08282 152 EDLDELEKELKELFGslITITSSGPGYLEIMPKGVSKGTALKALAKHLNISLEEVIAFGDGENDIEMLEAAGLGVAMGNA 231

                         250       260
                  ....*....|....*....|....
gi 695748135  244 VDEVKACADLVIGNNTETGIADVL 267
Cdd:pfam08282 232 SPEVKAAADYVTDSNNEDGVAKAL 255
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 2-270 3.61e-67

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: 206.91  E-value: 3.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   2 DYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKrVIA 81
Cdd:COG0561    1 MIKLIALDLDGTLLNDDGEISPRTKEALRRLREKGIKVVIATGRPLRSALPLLEELGLDDPLITSNGALIYDPDGE-VLY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  82 SDPLQPEQATQLVNLLDSYNVHSLMYAddamfyqnptghiirtenwakslpesqrpvfkqvpslseasqnvdaiwkfalt 161
Cdd:COG0561   80 ERPLDPEDVREILELLREHGLHLQVVV----------------------------------------------------- 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 162 dsdteklhrfgqiverelglaceWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMG 241
Cdd:COG0561  107 -----------------------RSGPGFLEILPKGVSKGSALKKLAERLGIPPEEVIAFGDSGNDLEMLEAAGLGVAMG 163

                        250       260
                 ....*....|....*....|....*....
gi 695748135 242 NAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:COG0561  164 NAPPEVKAAADYVTGSNDEDGVAEALEKL 192
PRK10513 PRK10513
sugar phosphate phosphatase; Provisional
 1-270 2.20e-40

sugar phosphate phosphatase; Provisional


Pssm-ID: 182509 [Multi-domain]  Cd Length: 270  Bit Score: 140.98  E-value: 2.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   1 MDYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPA---ICCNGALLYDYAEK 77
Cdd:PRK10513   1 MAIKLIAIDMDGTLLLPDHTISPAVKQAIAAARAKGVNVVLTTGRPYAGVHRYLKELHMEQPGdycITNNGALVQKAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  78 RVIASDPLQPEQATQLVNLLDSYNVHSLMYADDAMFYQNP-----TGHiirtENWAKSLPESQRPVFKQVPSLS------ 146
Cdd:PRK10513  81 ETVAQTALSYDDYLYLEKLSREVGVHFHALDRNTLYTANRdisyyTVH----ESFLTGIPLVFREVEKMDPNLQfpkvmm 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 147 -EASQNVDAiwkfALTDSDTEKLHRFGQIVERELGLACewsWHDQVDiaqagnsKGKRLAQWVESQGLSMSQVMAFGDNF 225
Cdd:PRK10513 157 iDEPEILDA----AIARIPAEVKERYTVLKSAPYFLEI---LDKRVN-------KGTGVKSLAEHLGIKPEEVMAIGDQE 222

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 695748135 226 NDLSMLETAGLGVAMGNAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:PRK10513 223 NDIAMIEYAGVGVAMGNAIPSVKEVAQFVTKSNLEDGVAFAIEKY 267
HAD_HPP cd07517
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ...
 5-270 3.32e-38

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: 133.50  E-value: 3.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTpAICCNGAllYDYAEKRVIASDP 84
Cdd:cd07517    2 IVFFDIDGTLLDEDTTIPESTKEAIAALKEKGILVVIATGRAPFEIQPIVKALGIDS-YVSYNGQ--YVFFEGEVIYKNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  85 LQPEQATQLVNLLDSYNvHSLMYADDAMFYQnptghiirTENwAKSLPESQRPVFKQVpslseasqnvdaiwkfaltdsd 164
Cdd:cd07517   79 LPQELVERLTEFAKEQG-HPVSFYGQLLLFE--------DEE-EEQKYEELRPELRFV---------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 165 teklhrfgqiverelglacewSWHDQ-VDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNA 243
Cdd:cd07517  127 ---------------------RWHPLsTDVIPKGGSKAKGIQKVIEHLGIKKEETMAFGDGLNDIEMLEAVGIGIAMGNA 185

                        250       260
                 ....*....|....*....|....*..
gi 695748135 244 VDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:cd07517  186 HEELKEIADYVTKDVDEDGILKALKHF 212
PRK15126 PRK15126
HMP-PP phosphatase;
3-272 3.09e-24

HMP-PP phosphatase;


Pssm-ID: 185080 [Multi-domain]  Cd Length: 272  Bit Score: 98.23  E-value: 3.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   3 YQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDyAEKRVIAS 82
Cdd:PRK15126   2 ARLAAFDMDGTLLMPDHHLGEKTLSTLARLRERDITLTFATGRHVLEMQHILGALSLDAYLITGNGTRVHS-LEGELLHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  83 DPLQPEQATQLVnlldsynvHSLMYADDAMfyqnptgHIIRTENWAKSlpesqrpvfKQVPSLSEAsqNVDAIWKFALTD 162
Cdd:PRK15126  81 QDLPADVAELVL--------HQQWDTRASM-------HVFNDDGWFTG---------KEIPALLQA--HVYSGFRYQLID 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 163 ---------------SDTEKLHRFGQIVERELGLACE--WSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNF 225
Cdd:PRK15126 135 lkrlpahgvtkicfcGDHDDLTRLQIQLNEALGERAHlcFSATDCLEVLPVGCNKGAALAVLSQHLGLSLADCMAFGDAM 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695748135 226 NDLSMLETAGLGVAMGNAVDEVKacADL----VIGNNTETGIADVLNQYFS 272
Cdd:PRK15126 215 NDREMLGSVGRGFIMGNAMPQLR--AELphlpVIGHCRNQAVSHYLTHWLD 263
PRK10976 PRK10976
putative hydrolase; Provisional
 3-273 1.50e-21

putative hydrolase; Provisional


Pssm-ID: 182878 [Multi-domain]  Cd Length: 266  Bit Score: 90.88  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   3 YQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDyAEKRVIAS 82
Cdd:PRK10976   2 YQVVASDLDGTLLSPDHTLSPYAKETLKLLTARGIHFVFATGRHHVDVGQIRDNLEIKSYMITSNGARVHD-TDGNLIFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  83 DPLQPEQATQLVNLldsynVHslmyaDDAMFYQNptghIIRTENW--AKSLPES----QRPVFK-QV--PSLSEAsqnvD 153
Cdd:PRK10976  81 HNLDRDIASDLFGV-----VH-----DNPDIITN----VYRDDEWfmNRHRPEEmrffKEAVFKyQLyePGLLEP----D 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 154 AIWKFALTDSDTEKLHRFGQ-IVERelglacewsWHDQVDIA----------QAGNSKGKRLAQWVESQGLSMSQVMAFG 222
Cdd:PRK10976 143 GVSKVFFTCDSHEKLLPLEQaINAR---------WGDRVNVSfstltclevmAGGVSKGHALEAVAKKLGYSLKDCIAFG 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 695748135 223 DNFNDLSMLETAGLGVAMGNAVDEVKacaDL-----VIGNNTETGIADVLNQYFSV 273
Cdd:PRK10976 214 DGMNDAEMLSMAGKGCIMGNAHQRLK---DLlpeleVIGSNADDAVPHYLRKLYLS 266
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 1-267 3.09e-21

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 89.26  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   1 MDYQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRhfvaIHPFYQALA----LNTPAICCNG-ALLYDYA 75
Cdd:PRK01158   1 MKIKAIAIDIDGTITDKDRRLSLKAVEAIRKAEKLGIPVILATGN----VLCFARAAAkligTSGPVIAENGgVISVGFD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  76 EKRVIASDPlqpEQATQLVNLLDSYnvhslmyaddamFYQNPTGHIIRTENWAKSLPESQR--PVFKQVPSLSEASQNVD 153
Cdd:PRK01158  77 GKRIFLGDI---EECEKAYSELKKR------------FPEASTSLTKLDPDYRKTEVALRRtvPVEEVRELLEELGLDLE 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 154 AIwkfaltdsDTeklhrfgqiverelGLAcewsWHdqvdIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLET 233
Cdd:PRK01158 142 IV--------DS--------------GFA----IH----IKSPGVNKGTGLKKLAELMGIDPEEVAAIGDSENDLEMFEV 191

                        250       260       270
                 ....*....|....*....|....*....|....
gi 695748135 234 AGLGVAMGNAVDEVKACADLVIGNNTETGIADVL 267
Cdd:PRK01158 192 AGFGVAVANADEELKEAADYVTEKSYGEGVAEAI 225
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
 5-240 1.54e-19

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: 84.35  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    5 VIALDLDGTLLTP-EKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYDYAEKRVIASD 83
Cdd:TIGR01484   1 LLFFDLDGTLLDPnAHELSPETIEALERLREAGVKVVIVTGRSLAEIKELLKQLNLPLPLIAENGALIFYPGEILYIEPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   84 PLQPEQATQLVNLLDSYNVHSLMYADDAMFYQNPTGHIIrtenwakslpesqrpvfkqvpslSEASQNVDAIWKFALTDS 163
Cdd:TIGR01484  81 DVFEEILGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAI-----------------------HYVGAELGQELDSKMRER 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695748135  164 dTEKLHRfgqiveRELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:TIGR01484 138 -LEKIGR------NDLELEAIYSGKTDLEVLPAGVNKGSALQALLQELNGKKDEILAFGDSGNDEEMFEVAGLAVAV 207
HAD_YbiV-Like cd07518
Escherichia coli YbiV sugar phosphatase/phosphotransferase and related proteins; belongs to ...
 186-267 7.11e-19

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: 81.86  E-value: 7.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 186 SWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNAVDEVKACADLVIGNNTETGIAD 265
Cdd:cd07518  102 SGFGSIDIIPPGVNKATGLKQLLKHWGISPDEVMAFGDGGNDIEMLKYAGYSYAMENAPEEVKAAAKYVAPSNNENGVLQ 181


                 ..
gi 695748135 266 VL 267
Cdd:cd07518  182 VI 183
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
 6-267 3.15e-18

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: 80.94  E-value: 3.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    6 IALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRhfvaIHPFYQALA----LNTPAICCNGALLYDYAEKRVIA 81
Cdd:TIGR01487   4 VAIDIDGTLTDPNRMISERAIEAIRKAEKKGIPVSLVTGN----TVPFARALAvligTSGPVVAENGGVIFYNKEDIFLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   82 SDplqpEQATQLVNLLDsynvhslmyaddaMFYQNptghiirtENWAKSLPESQRPVFKQVPSLSEASQnvdaiwkfalt 161
Cdd:TIGR01487  80 NM----EEEWFLDEEKK-------------KRFPR--------DRLSNEYPRASLVIMREGKDVDEVRE----------- 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  162 dsdteklhrfgqiVERELGL---ACEWSWHdqvdIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGV 238
Cdd:TIGR01487 124 -------------IIKERGLnlvASGFAIH----IMKKGVDKGVGVEKLKELLGIKPEEVAAIGDSENDIDLFRVVGFKV 186

                         250       260
                  ....*....|....*....|....*....
gi 695748135  239 AMGNAVDEVKACADLVIGNNTETGIADVL 267
Cdd:TIGR01487 187 AVANADDQLKEIADYVTSNPYGEGVVEVL 215
PLN02887 PLN02887
hydrolase family protein
 3-270 3.58e-18

hydrolase family protein


Pssm-ID: 215479 [Multi-domain]  Cd Length: 580  Bit Score: 84.16  E-value: 3.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   3 YQVIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALN---------TPAICCNGALLYD 73
Cdd:PLN02887 308 FSYIFCDMDGTLLNSKSQISETNAKALKEALSRGVKVVIATGKARPAVIDILKMVDLAgkdgiisesSPGVFLQGLLVYG 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  74 YAEKRVIASD------------------PLQPEQATQLVNLLDSYNVHSLMYaddamFYQNPTGHIIRTENWAKSLPESQ 135
Cdd:PLN02887 388 RQGREIYRSNldqevcreaclyslehkiPLIAFSQDRCLTLFDHPLVDSLHT-----IYHEPKAEIMSSVDQLLAAADIQ 462

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 136 RPVFKQVPSlsEASQNVDAIWKFALTDSdteklhrfGQIVERElglacewswHDQVDIAQAGNSKGKRLAQWVESQGLSM 215
Cdd:PLN02887 463 KVIFLDTAE--GVSSVLRPYWSEATGDR--------ANVVQAQ---------PDMLEIVPPGTSKGNGVKMLLNHLGVSP 523

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 695748135 216 SQVMAFGDNFNDLSMLETAGLGVAMGNAVDEVKACADLVIGNNTETGIADVLNQY 270
Cdd:PLN02887 524 DEIMAIGDGENDIEMLQLASLGVALSNGAEKTKAVADVIGVSNDEDGVADAIYRY 578
SPP-subfamily TIGR01482
sucrose-phosphate phosphatase subfamily; This model includes both the members of the SPP ...
 6-267 1.11e-14

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: 71.34  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    6 IALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRhfvaIHPFYQALA----LNTPAICCNG-ALLYDYAEKRVI 80
Cdd:TIGR01482   1 IASDIDGTLTDPNRAINESALEAIRKAESKGIPVVLVTGN----SVQFARALAkligTPDPVIAENGgEISYNEGLDDIF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   81 ASDplqpeqatqLVNLLDSYNVHSLMYADDAMFYQNPTghiirtenwakslpeSQRPVFkqvpsLSEASqNVDAIWKfaL 160
Cdd:TIGR01482  77 LAY---------LEEEWFLDIVIAKTFPFSRLKVQYPR---------------RASLVK-----MRYGI-DVDTVRE--I 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  161 TDSDTEKLhrfgqiVERELGLAcewswhdqVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAM 240
Cdd:TIGR01482 125 IKELGLNL------VAVDSGFD--------IHILPQGVNKGVAVKKLKEKLGIKPGETLVCGDSENDIDLFEVPGFGVAV 190

                         250       260       270
                  ....*....|....*....|....*....|.
gi 695748135  241 GNAVDEVKACADLV----IGNNTETGIADVL 267
Cdd:TIGR01482 191 ANAQPELKEWADYVtespYGEGGAEAIGEIL 221
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 197-267 1.90e-11

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: 60.30  E-value: 1.90e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695748135 197 GNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNAVDEVKACADLVIGNNTETGIADVL 267
Cdd:cd07514   65 GVDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDGVLEAI 135
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 197-252 3.64e-11

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: 61.39  E-value: 3.64e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 695748135 197 GNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMgNAVDEVKACAD 252
Cdd:COG0560  153 GEGKAEALRELAAELGIDLEQSYAYGDSANDLPMLEAAGLPVAV-NPDPALREAAD 207
S6PP pfam05116
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ...
 5-243 8.47e-11

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: 60.74  E-value: 8.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    5 VIALDLDGTLLTPEKTILpASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTP--AICCNGALLYDyaekrviaS 82
Cdd:pfam05116   4 LLVSDLDNTLVDGDNEAL-ARLNQLLEAYRPDVGLVFATGRSLDSAKELLKEKPLPTPdyLITSVGTEIYY--------G 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   83 DPLQPEQAtqLVNLLDSynvhslmyaddamfyqNPTGHIIRTEnwAKSLPE-------SQRPvFKqvpslseasqnvdai 155
Cdd:pfam05116  75 PSLVPDQS--WQEHLDY----------------HWDRQAVVEA--LAKFPGltlqpeeEQRP-HK--------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  156 WKFALTDSDTEKLHrfgQIVEREL---GLACE--WSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSM 230
Cdd:pfam05116 119 VSYFLDPEAAAAVL---AELEQLLrkrGLDVKviYSSGRDLDILPLRASKGEALRYLALKLGLPLENTLVCGDSGNDEEL 195

                         250
                  ....*....|...
gi 695748135  231 LETAGLGVAMGNA 243
Cdd:pfam05116 196 FIGGTRGVVVGNA 208
HAD_SPP cd02605
sucrose-phosphatase, similar to Synechocystis sp PCC 6803 SPP; Sucrose-phosphatase (SPP; EC 3. ...
 5-254 2.43e-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: 59.28  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLtpEKTILPASLTALQN-----ARKSGAKVVIVTGRHFVAIHPFYQALALNTPAiccngallydyaekrV 79
Cdd:cd02605    1 LLVSDLDETLV--GHDTNLQALERLQDlleqlTADNDVILVYATGRSPESVLELIKEVMLPKPD---------------F 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  80 IASDplqpeqatqlvnlldsynVHSLMYADDAMFYQNPTG-HIIRTENWAKSLPESQRPVFKQVPSLSEASQNVdaiWK- 157
Cdd:cd02605   64 IISD------------------VGTEIYYGESGYLEPDTYwNEVLSEGWERFLFEAIADLFKQLKPQSELEQNP---HKi 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 158 -FALTDSDTEKLhrFGQIVEREL--GLACEWSW---HDQ-VDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSM 230
Cdd:cd02605  123 sFYLDPQNDAAV--IEQLEEMLLkaGLTVRIIYssgLAYdLDILPLGAGKGEALRYLQEKWNFPPERTLVCGDSGNDIAL 200

                        250       260
                 ....*....|....*....|....
gi 695748135 231 LETAGLGVAMGNAVDEVKACADLV 254
Cdd:cd02605  201 LSTGTRGVIVGNAQPELLKWADRV 224
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 197-239 2.60e-09

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


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 55.25  E-value: 2.60e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 695748135 197 GNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVA 239
Cdd:cd07500  135 AQRKAETLQELAARLGIPLEQTVAVGDGANDLPMLKAAGLGIA 177
PRK00192 PRK00192
mannosyl-3-phosphoglycerate phosphatase; Reviewed
 5-244 4.57e-09

mannosyl-3-phosphoglycerate phosphatase; Reviewed


Pssm-ID: 234684 [Multi-domain]  Cd Length: 273  Bit Score: 55.72  E-value: 4.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYdyaekrvIASDp 84
Cdd:PRK00192   6 LVFTDLDGTLLDHHTYSYEPAKPALKALKEKGIPVIPCTSKTAAEVEVLRKELGLEDPFIVENGAAIY-------IPKN- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  85 lqpeqatqlvnlldsynvhslmyaddaMFYQNPTGHIIRTENWAKSLPESqRPVFKQVpsLSEASQNVDAIWKfALTDSD 164
Cdd:PRK00192  78 ---------------------------YFPFQPDGERLKGDYWVIELGPP-YEELREI--LDEISDELGYPLK-GFGDLS 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 165 TEKLHRFGQIVERELGLA-------------CEWSWHDQVDIAQA----------------GNSKGK---RLAQWVESQG 212
Cdd:PRK00192 127 AEEVAELTGLSGESARLAkdrefsepflwngSEAAKERFEEALKRlglkvtrggrflhllgGGDKGKavrWLKELYRRQD 206

                        250       260       270
                 ....*....|....*....|....*....|..
gi 695748135 213 LsmSQVMAFGDNFNDLSMLETAGLGVAMGNAV 244
Cdd:PRK00192 207 G--VETIALGDSPNDLPMLEAADIAVVVPGPD 236
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 192-254 4.22e-08

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: 51.37  E-value: 4.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695748135 192 DIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVAMGNAVDEVKACADLV 254
Cdd:cd01630   69 DLFQGVKDKLEALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYV 131
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 3-235 1.97e-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: 47.20  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    3 YQVIALDLDGTLLTPEktilPASLTALQNArksgakvvivtgrhfVAIHPFYQALALNTPAICcngALLYDYAEKRVIAS 82
Cdd:pfam00702   1 IKAVVFDLDGTLTDGE----PVVTEAIAEL---------------ASEHPLAKAIVAAAEDLP---IPVEDFTARLLLGK 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   83 DPLQPEQATQLVNlldsynVHSLMYADDAMFYQNPTGHIIRTENWaKSLPESqRPVFKQvpsLSEASQNVdaiwkFALTD 162
Cdd:pfam00702  59 RDWLEELDILRGL------VETLEAEGLTVVLVELLGVIALADEL-KLYPGA-AEALKA---LKERGIKV-----AILTG 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695748135  163 SDTEKLHRFGqiveRELGLACEWSWHDQVDIAQAGNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAG 235
Cdd:pfam00702 123 DNPEAAEALL----RLLGLDDYFDVVISGDDVGVGKPKPEIYLAALERLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD-SF-IIB-MPGP TIGR01486
mannosyl-3-phosphoglycerate phosphatase family; This small group of proteins is a member of ...
 5-238 2.43e-06

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: 47.78  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLY---DYAEK---R 78
Cdd:TIGR01486   1 WIFTDLDGTLLDPHGYDWGPAKEVLERLQELGIPVIPCTSKTAAEVEYLRKELGLEDPFIVENGGAIYgprGWRPEpeyP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   79 VIASDPLQPEQATQLVNLLDSYNVHSLMYAD-DAMFYQNPTGhiirtenwaksLPESQRPVFKQvpslSEASQnvdAIWk 157
Cdd:TIGR01486  81 VIALGIPYEKIRARLRELSEELGFKFRGLGDlTDEEIAELTG-----------LSRELARLAQR----REYSE---TIL- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  158 faltdSDTEKLHRFGQIVeRELGLACEWS---WHdqvdIAQAGNSKGK---RLAQWVESQGLSMsQVMAFGDNFNDLSML 231
Cdd:TIGR01486 142 -----WSEERRERFTEAL-VAVGLEVTHGgrfYH----VLGAGSDKGKavnALKAFYNQPGGAI-KVVGLGDSPNDLPLL 210


                  ....*..
gi 695748135  232 ETAGLGV 238
Cdd:TIGR01486 211 EVVDLAV 217
COG4087 COG4087
Soluble P-type ATPase [General function prediction only];
160-268 5.88e-06

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


Pssm-ID: 443263 [Multi-domain]  Cd Length: 156  Bit Score: 45.15  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 160 LTdSDTeklhrFGQiVEREL-GLACEwswhdqVDIAQAGN-SKGKrlAQWVESQGLSmsQVMAFGDNFNDLSMLETAGLG 237
Cdd:COG4087   51 LT-ADT-----FGT-VAKELaGLPVE------LHILPSGDqAEEK--LEFVEKLGAE--TTVAIGNGRNDVLMLKEAALG 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695748135 238 VAM----GNAVDEVkACADLVIgnnteTGIADVLN 268
Cdd:COG4087  114 IAVigpeGASVKAL-LAADIVV-----KSILDALD 142
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 5-81 7.49e-06

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 43.92  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLLTPEktilpasltALQNARKSGAKVVIVTGRHFVAIHPFYQALALN---TPAICCNGALLYDYAEKRVIA 81
Cdd:cd01427    1 AVLFDLDGTLLAVE---------LLKRLRAAGIKLAIVTNRSREALRALLEKLGLGdlfDGIIGSDGGGTPKPKPKPLLL 71
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
5-100 3.35e-05

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


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 44.03  E-value: 3.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   5 VIALDLDGTLL----TPEK-TILPASLTALQN-ARKSGAKVVIVTGR------HFVAIHPFyqalalntPAICCNGA-LL 71
Cdd:COG1877    5 LLFLDFDGTLApivpDPDAaRPPPELRELLRRlAARPGGAVAIVSGRdladldRLLGPLGL--------PLAGSHGAeRR 76

                         90       100
                 ....*....|....*....|....*....
gi 695748135  72 YDYAEKRVIASDPLQPEQATQLVNLLDSY 100
Cdd:COG1877   77 LPGGEWEVLPLAAEAPEWLDALRAALEAL 105
Hydrolase_6 pfam13344
Haloacid dehalogenase-like hydrolase; This family is part of the HAD superfamily.
 6-85 1.06e-04

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


Pssm-ID: 433132  Cd Length: 101  Bit Score: 40.53  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135    6 IALDLDGTLLTpEKTILPASLTALQNARKSGAKVVIVT---GRHFVAIHPFYQALALNTPA--ICCNGALLYDYAEKR-- 78
Cdd:pfam13344   1 FLFDIDGVLWR-GGEPIPGAAEALRALRAAGKPVVFVTnnsSRSREEYAEKLRKLGFDIDEdeIITSGTAAADYLKERkf 79

                          90
                  ....*....|..
gi 695748135   79 -----VIASDPL 85
Cdd:pfam13344  80 gkkvlVIGSEGL 91
YedP COG3769
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ...
 9-246 7.25e-04

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


Pssm-ID: 442983 [Multi-domain]  Cd Length: 268  Bit Score: 40.20  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135   9 DLDGTLLTPE----KTILPAsLTALQNArksGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLYdyaekrvIASDP 84
Cdd:COG3769    9 DLDGTLLDHDtyswAAALPA-LARLKAR---GIPVILNTSKTAAEVEPLRQELGLSDPFIVENGAAIF-------IPKGY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135  85 LQPEQATQLVnllDSYNVHSLmyaddAMFYQnptgHIIRTenwAKSLPESQRPVFKqvpSLSEAS-QNV---------DA 154
Cdd:COG3769   78 FAFPSGTADI---DGYWVIEL-----GKPYA----EIRAV---LEQLREELGFKFT---GFGDMSaEEVaeltglsleQA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695748135 155 ------------IWKfaltDSDtEKLHRFGQIVErELGLACewS-----WHdqvdiAQAGNSKGK---RLAQWVESQGLS 214
Cdd:COG3769  140 alakqrefseplLWL----GSD-EALERFIAALA-ALGLTV--LrggrfLH-----LMGGADKGKavrWLVEQYRQRFGK 206

                        250       260       270
                 ....*....|....*....|....*....|..
gi 695748135 215 MSQVMAFGDNFNDLSMLETAGLGVAMGNAVDE 246
Cdd:COG3769  207 NVVTIALGDSPNDIPMLEAADIAVVIRSPHGA 238
PTZ00174 PTZ00174
phosphomannomutase; Provisional
 1-50 9.59e-04

phosphomannomutase; Provisional


Pssm-ID: 240305  Cd Length: 247  Bit Score: 39.55  E-value: 9.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695748135   1 MDYQVIAL-DLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAI 50
Cdd:PTZ00174   2 EMKKTILLfDVDGTLTKPRNPITQEMKDTLAKLKSKGFKIGVVGGSDYPKI 52
NagD COG0647
Ribonucleotide monophosphatase NagD, HAD superfamily [Nucleotide transport and metabolism];
1-43 1.91e-03

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


Pssm-ID: 440412 [Multi-domain]  Cd Length: 259  Bit Score: 38.94  E-value: 1.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 695748135   1 MDYQVIALDLDGTLLTpEKTILPASLTALQNARKSGAKVVIVT 43
Cdd:COG0647    6 DRYDAFLLDLDGVLYR-GDEPIPGAVEALARLRAAGKPVLFLT 47
serB PRK11133
phosphoserine phosphatase; Provisional
 189-239 3.49e-03

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 38.39  E-value: 3.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695748135 189 DQVDiAQAgnsKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAGLGVA 239
Cdd:PRK11133 242 DIVD-AQY---KADTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIA 288
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 197-235 3.96e-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: 3.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 695748135 197 GNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAG 235
Cdd:cd02612  149 GEGKVKRLREWLAEEGIDLKDSYAYSDSINDLPMLEAVG 187
HAD_Pase cd07507
haloacid dehalogenase-like superfamily phosphatase similar to Pyrococcus horikoshii ...
 5-72 4.61e-03

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: 37.73  E-value: 4.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695748135   5 VIALDLDGTLLTPEKTILPASLTALQNARKSGAKVVIVTGRHFVAIHPFYQALALNTPAICCNGALLY 72
Cdd:cd07507    1 VIFTDLDGTLLDHHTYSFDPARPALERLKERGIPVVPCTSKTRAEVEYLRKELGIEDPFIVENGGAIF 68
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 197-235 8.97e-03

HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273654 [Multi-domain]  Cd Length: 202  Bit Score: 36.55  E-value: 8.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 695748135  197 GNSKGKRLAQWVESQGLSMSQVMAFGDNFNDLSMLETAG 235
Cdd:TIGR01490 153 GEGKVHALAELLAEEQIDLKDSYAYGDSISDLPLLSLVG 191
 
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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