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Conserved domains on  [gi|808356728|ref|NP_001293892|]
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Phosphoserine phosphatase [Caenorhabditis elegans]

Protein Classification

phosphoserine phosphatase( domain architecture ID 11560826)

phosphoserine phosphatase is a HAD (haloacid dehalogenase) family hydrolase that catalyzes the dephosphorylation of phosphoserine (P-Ser)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 57-264 3.80e-119

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 339.64  E-value: 3.80e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 136
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 137 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 216
Cdd:cd04309   79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808356728 217 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 264
Cdd:cd04309  155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 57-264 3.80e-119

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 339.64  E-value: 3.80e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 136
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 137 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 216
Cdd:cd04309   79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808356728 217 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 264
Cdd:cd04309  155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 47-272 8.78e-113

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 324.34  E-value: 8.78e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  47 EEVKRVWRKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNI 126
Cdd:PLN02954   3 KDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFE--EALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 127 SKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGK 206
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSG----GK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356728 207 PAVIALLKKMYNYKTVVMVGDGATDVEASPP--ADAFIGFGGNVIREGVKARAKWYVTDFDVLRKDLD 272
Cdd:PLN02954 157 AEAVQHIKKKHGYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 54-264 4.41e-48

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 159.44  E-value: 4.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   54 RKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVnISKPKLTV 133
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDF--KASLRERVALLKGLPVELLKEV-RENLPLTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  134 GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsrIYANEILFDKfGKYHGFDTSELTsDSGSKetGKPAVIALL 213
Cdd:TIGR00338  89 GAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIV-DASYK--GKTLLILLR 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356728  214 KKMYNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVK--ARAKWYVTDF 264
Cdd:TIGR00338 163 KEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKAdiCINKKDLTDI 215
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 54-233 9.45e-28

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: 106.46  E-value: 9.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  54 RKADAVCFDVDSTVCQDEGIDELAAYLG---------VGEAVANVTRTAMNGnaRFRYRDALAARLQVMKPNH-EQLEQF 123
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAG--ELDFEESLRFRVALLAGLPeEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 124 VN---ISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKfGKYHGfDTSELTSDSG 200
Cdd:COG0560   79 AErlfEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVED-GRLTG-EVVGPIVDGE 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 808356728 201 SKETgkpAVIALLKKM-YNYKTVVMVGDGATDVE 233
Cdd:COG0560  155 GKAE---ALRELAAELgIDLEQSYAYGDSANDLP 185
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 57-234 3.35e-13

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: 66.46  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   57 DAVCFDVDSTVCQDE----------------GIDELAAYLGVGEAVANVTRTAMNGNARF-------RYRDALAARLQVM 113
Cdd:pfam00702   2 KAVVFDLDGTLTDGEpvvteaiaelasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWleeldilRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  114 KPNHEQLEQFVNISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHgfdts 193
Cdd:pfam00702  82 VVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK----- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 808356728  194 eltsdsgsketgkPAVIALLKKMYN--YKTVVMVGDGATDVEA 234
Cdd:pfam00702 157 -------------PEIYLAALERLGvkPEEVLMVGDGVNDIPA 186
 
Name Accession Description Interval E-value
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 57-264 3.80e-119

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine 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: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 339.64  E-value: 3.80e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNISKPKLTVGIR 136
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIDELAKFCGVGDEVAELTRRAMGGSIPFR--DALRKRLAIINPTKEQVDEFLEEHPPRLTPGVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 137 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 216
Cdd:cd04309   79 ELVSRLKARGVEVYLISGGFRELIEPVASQLGIPLENVFANRLLFDFNGEYAGFDETQPTSRSG----GKAKVIEQLKEK 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808356728 217 YNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVKARAKWYVTDF 264
Cdd:cd04309  155 HHYKRVIMIGDGATDLEACPPADAFIGFGGNVIREKVKARADWYVTDF 202
PLN02954 PLN02954
phosphoserine phosphatase
 47-272 8.78e-113

phosphoserine phosphatase


Pssm-ID: 215514 [Multi-domain]  Cd Length: 224  Bit Score: 324.34  E-value: 8.78e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  47 EEVKRVWRKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFRyrDALAARLQVMKPNHEQLEQFVNI 126
Cdd:PLN02954   3 KDVLELWRSADAVCFDVDSTVCVDEGIDELAEFCGAGEAVAEWTAKAMGGSVPFE--EALAARLSLFKPSLSQVEEFLEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 127 SKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTSELTSDSGsketGK 206
Cdd:PLN02954  81 RPPRLSPGIPELVKKLRARGTDVYLVSGGFRQMIAPVAAILGIPPENIFANQILFGDSGEYAGFDENEPTSRSG----GK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808356728 207 PAVIALLKKMYNYKTVVMVGDGATDVEASPP--ADAFIGFGGNVIREGVKARAKWYVTDFDVLRKDLD 272
Cdd:PLN02954 157 AEAVQHIKKKHGYKTMVMIGDGATDLEARKPggADLFIGYGGVQVREAVAAKADWFVTDFQDLIEVLD 224
serB TIGR00338
phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction ...
 54-264 4.41e-48

phosphoserine phosphatase SerB; Phosphoserine phosphatase catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate. It catalyzes the last of three steps in the biosynthesis of serine from D-3-phosphoglycerate. Note that this enzyme acts on free phosphoserine, not on phosphoserine residues of phosphoproteins. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273022 [Multi-domain]  Cd Length: 219  Bit Score: 159.44  E-value: 4.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   54 RKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVnISKPKLTV 133
Cdd:TIGR00338  12 RSKKLVVFDMDSTLINAETIDEIAKIAGVEEEVSEITERAMRGELDF--KASLRERVALLKGLPVELLKEV-RENLPLTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  134 GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsrIYANEILFDKfGKYHGFDTSELTsDSGSKetGKPAVIALL 213
Cdd:TIGR00338  89 GAEELVKTLKEKGYKVAVISGGFDLFAEHVKDKLGLDA--AFANRLEVED-GKLTGLVEGPIV-DASYK--GKTLLILLR 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808356728  214 KKMYNYKTVVMVGDGATDVEASPPADAFIGFGGNVIREGVK--ARAKWYVTDF 264
Cdd:TIGR00338 163 KEGISPENTVAVGDGANDLSMIKAAGLGIAFNAKPKLQQKAdiCINKKDLTDI 215
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 54-233 9.45e-28

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: 106.46  E-value: 9.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  54 RKADAVCFDVDSTVCQDEGIDELAAYLG---------VGEAVANVTRTAMNGnaRFRYRDALAARLQVMKPNH-EQLEQF 123
Cdd:COG0560    1 RKMRLAVFDLDGTLIAGESIDELARFLGrrglvdrreVLEEVAAITERAMAG--ELDFEESLRFRVALLAGLPeEELEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 124 VN---ISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKfGKYHGfDTSELTSDSG 200
Cdd:COG0560   79 AErlfEEVPRLYPGARELIAEHRAAGHKVAIVSGGFTFFVEPIAERLGID--HVIANELEVED-GRLTG-EVVGPIVDGE 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 808356728 201 SKETgkpAVIALLKKM-YNYKTVVMVGDGATDVE 233
Cdd:COG0560  155 GKAE---ALRELAAELgIDLEQSYAYGDSANDLP 185
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 58-238 2.95e-27

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 103.97  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   58 AVCFDVDSTVC-QDEGIDELAAYLGVGEAVANVTRTAMNGNARFRYRDALAARLQVMKpNHEQLEQFVNISKPKLTVGIR 136
Cdd:TIGR01488   1 LAIFDFDGTLTrQDSLIDLLAKLLGTNDEVIELTRLAPSGRISFEDALGRRLALLHRS-RSEEVAKEFLARQVALRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  137 ELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKFGKYHGFDTSELTSDSGsketGKPAVIALLKKM 216
Cdd:TIGR01488  80 ELISWLKERGIDTVIVSGGFDFFVEPVAEKLGID--DVFANRLEFDDNGLLTGPIEGQVNPEGE----CKGKVLKELLEE 153

                         170       180
                  ....*....|....*....|....
gi 808356728  217 YNY--KTVVMVGDGATDVEASPPA 238
Cdd:TIGR01488 154 SKItlKKIIAVGDSVNDLPMLKLA 177
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 59-231 7.41e-25

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: 97.62  E-value: 7.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  59 VCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVnISKPKLTVGIREL 138
Cdd:cd07500    2 IVFDMDSTLIQQEVIDELAAEAGVGEEVAAITERAMRGELDF--EESLRERVALLKGLPESVLDEV-YERLTLTPGAEEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 139 VSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsrIYANEILFDKfgkyhGFDTSELTSDSGSKETgKPAVIALLKKMYN 218
Cdd:cd07500   79 IQTLKAKGYKTAVVSGGFTYFTDRLAEELGLDY--AFANELEIKD-----GKLTGKVLGPIVDAQR-KAETLQELAARLG 150

                        170
                 ....*....|....*
gi 808356728 219 YKT--VVMVGDGATD 231
Cdd:cd07500  151 IPLeqTVAVGDGAND 165
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 57-234 3.35e-13

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: 66.46  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   57 DAVCFDVDSTVCQDE----------------GIDELAAYLGVGEAVANVTRTAMNGNARF-------RYRDALAARLQVM 113
Cdd:pfam00702   2 KAVVFDLDGTLTDGEpvvteaiaelasehplAKAIVAAAEDLPIPVEDFTARLLLGKRDWleeldilRGLVETLEAEGLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  114 KPNHEQLEQFVNISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHgfdts 193
Cdd:pfam00702  82 VVLVELLGVIALADELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGVGKPK----- 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 808356728  194 eltsdsgsketgkPAVIALLKKMYN--YKTVVMVGDGATDVEA 234
Cdd:pfam00702 157 -------------PEIYLAALERLGvkPEEVLMVGDGVNDIPA 186
serB PRK11133
phosphoserine phosphatase; Provisional
 54-231 2.06e-12

phosphoserine phosphatase; Provisional


Pssm-ID: 182988 [Multi-domain]  Cd Length: 322  Bit Score: 66.13  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  54 RKADAVCFDVDSTVCQDEGIDELAAYLGVGEAVANVTRTAMNGNARFryRDALAARLQVMKPNHEQLEQFVNISKPkLTV 133
Cdd:PRK11133 108 RTPGLLVMDMDSTAIQIECIDEIAKLAGTGEEVAEVTERAMRGELDF--EASLRQRVATLKGADANILQQVRENLP-LMP 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 134 GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIekSRIYANEilfdkFGKYHGFDTSELTSDSGSKETgKPAVIALL 213
Cdd:PRK11133 185 GLTELVLKLQALGWKVAIASGGFTYFADYLRDKLRL--DAAVANE-----LEIMDGKLTGNVLGDIVDAQY-KADTLTRL 256

                        170       180
                 ....*....|....*....|
gi 808356728 214 KKMYNYKT--VVMVGDGATD 231
Cdd:PRK11133 257 AQEYEIPLaqTVAIGDGAND 276
HAD pfam12710
haloacid dehalogenase-like hydrolase;
59-234 2.29e-12

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 64.09  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   59 VCFDVDSTVCQDEGIDELAAYLGvgEAVANVTRTAMNGNARFRYRDALAARLQVMK-------------PNHEQLEQFV- 124
Cdd:pfam12710   1 ALFDLDGTLLDGDSLFLLIRALL--RRGGPDLWRALLVLLLLALLRLLGRLSRAGArellrallaglpeEDAAELERFVa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  125 NISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKfgkyHGFDTSELTSDSGSKET 204
Cdd:pfam12710  79 EVALPRLHPGALELLAAHRAAGDRVVVVTGGLRPLVEPVLAELGFD--EVLATELEVDD----GRFTGELRLIGPPCAGE 152

                         170       180       190
                  ....*....|....*....|....*....|....
gi 808356728  205 GKPAVIA--LLKKMYN--YKTVVMVGDGATDVEA 234
Cdd:pfam12710 153 GKVRRLRawLAARGLGldLADSVAYGDSPSDLPM 186
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
57-234 5.77e-11

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 60.71  E-value: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQDEG-----IDELAAYLGVGEAVANVTRTAMNGNARFRYRDALAARLQvmkpnhEQLEQFV------- 124
Cdd:COG0546    2 KLVLFDLDGTLVDSAPdiaaaLNEALAELGLPPLDLEELRALIGLGLRELLRRLLGEDPD------EELEELLarfrely 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 125 ---NISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsriyaneiLFDkfgkyhgfdtSELTSDSGS 201
Cdd:COG0546   76 eeeLLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLLEALGLDD--------YFD----------AIVGGDDVP 137

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 808356728 202 KETGKPAVIALLKKMYNYK--TVVMVGDGATDVEA 234
Cdd:COG0546  138 PAKPKPEPLLEALERLGLDpeEVLMVGDSPHDIEA 172
HAD_Pase cd07524
phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like ...
 62-239 5.00e-09

phosphatase, similar to Bacillus subtilis MtnX; belongs to the haloacid dehalogenase-like superfamily; Bacillus subtilis recycles two toxic byproducts of polyamine metabolism, methylthioadenosine and methylthioribose, into methionine by a salvage pathway. The sixth reaction in this pathway is catalyzed by B. subtilis MtnX: the dephosphorylation of 2- hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HKMTP- 1-P) into 1,2-dihydroxy-3-keto-5-methylthiopentene. The hydrolysis of HK-MTP-1-P is a two-step mechanism involving the formation of a transiently phosphorylated aspartyl intermediate. 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: 319826 [Multi-domain]  Cd Length: 211  Bit Score: 55.03  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  62 DVDSTVCQDEGIDELAAYLGVGEAVanvtRTAMNG---NARFRYRDALAARLQVMKPN-HEQLEQFVnISKPKLTVGIRE 137
Cdd:cd07524    5 DFDGTITENDNIIYLMDEFAPPLEE----WEALKEgvlSQTLSFREGVGQMFELLPSSlKDEIIEFL-EKTAKIRPGFKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 138 LVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKSRIYANEILFDKFGKYHGFDTS-ELTSDSGskeTGKPAVIALLKKM 216
Cdd:cd07524   80 FVAFCQEHGIPFIIVSGGMDFFIEPLLEGLVIEKIAIYCNGSDFSGEQIHIDWPHEcDCTNGCG---CCKSSIIRKYSKP 156

                        170       180
                 ....*....|....*....|...
gi 808356728 217 YNYKtvVMVGDGATDVEASPPAD 239
Cdd:cd07524  157 RPFI--IVIGDSVTDLEAAKEAD 177
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 135-234 4.22e-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: 50.09  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 135 IRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksriyaneILFDKFgkyhgfdtseLTSDSG--SKETGKPAVIAL 212
Cdd:cd01427   12 AVELLKRLRAAGIKLAIVTNRSREALRALLEKLGLG--------DLFDGI----------IGSDGGgtPKPKPKPLLLLL 73

                         90       100
                 ....*....|....*....|..
gi 808356728 213 LKKMYNYKTVVMVGDGATDVEA 234
Cdd:cd01427   74 LKLGVDPEEVLFVGDSENDIEA 95
mtnX PRK09552
2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed
 117-239 4.79e-05

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase; Reviewed


Pssm-ID: 236562  Cd Length: 219  Bit Score: 43.43  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 117 HEQLEQFVnISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLgIEKSRIYANEILFDkfGKY------HGF 190
Cdd:PRK09552  62 KEEIIQFL-LETAEIREGFHEFVQFVKENNIPFYVVSGGMDFFVYPLLQGL-IPKEQIYCNGSDFS--GEYititwpHPC 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 808356728 191 DTSeLTSDSGskeTGKPAVIALLKKMYNYKtvVMVGDGATDVEASPPAD 239
Cdd:PRK09552 138 DEH-CQNHCG---CCKPSLIRKLSDTNDFH--IVIGDSITDLEAAKQAD 180
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 57-234 1.20e-04

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 42.32  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQ-----DEGIDELAAYLGVGEAVANVTRT--AMNGNARFRYR----------DALAARLQVmKPNHEQ 119
Cdd:COG1011    2 KAVLFDLDGTLLDfdpviAEALRALAERLGLLDEAEELAEAyrAIEYALWRRYErgeitfaellRRLLEELGL-DLAEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728 120 LEQFVNISKPKLTV--GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEKsriyaneiLFDKFgkyhgfdtseLTS 197
Cdd:COG1011   81 AEAFLAALPELVEPypDALELLEALKARGYRLALLTNGSAELQEAKLRRLGLDD--------LFDAV----------VSS 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 808356728 198 DsgskETG--KPAviallKKMYNY---------KTVVMVGD-GATDVEA 234
Cdd:COG1011  143 E----EVGvrKPD-----PEIFELalerlgvppEEALFVGDsPETDVAG 182
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 58-233 2.26e-04

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: 41.17  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   58 AVCFDVDSTVCQDEGIDELAAYLG-----VGEAVANVTRTAMNGNARfRYRDALAA-RLQVMKPNHEQL--------EQF 123
Cdd:TIGR01490   1 LAFFDFDGTLTAKDTLFIFLKFLAsknilFEELRLPKVLARFEFFLN-RGLDYMAYyRAFALDALAGLLeedvraivEEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  124 VN-ISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksRIYANEILFDKFGKYhgfdTSELTSDSGSK 202
Cdd:TIGR01490  80 VNqKIESILYPEARDLIRWHKAEGHTIVLVSASLTILVKPLARILGID--NAIGTRLEESEDGIY----TGNIDGNNCKG 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 808356728  203 ETGKPAVIALL-KKMYNYKTVVMVGDGATDVE 233
Cdd:TIGR01490 154 EGKVHALAELLaEEQIDLKDSYAYGDSISDLP 185
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 58-171 2.61e-04

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: 41.14  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  58 AVCFDVDSTVCQDE---------GIDELAAYLGVGEAVANVTRTAMNGNARFRYRDALAArlqVMKPNHEQLEQFVN--- 125
Cdd:cd02612    1 LAFFDLDGTLIAGDsffaflrfkGIAERRAPLEELLLLRLMALYALGRLDGAGMEALLGF---ATAGLAGELAALVEefv 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 808356728 126 --ISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEK 171
Cdd:cd02612   78 eeYILRVLYPEARELIAWHKAAGHDVVLISASPEELVAPIARKLGIDN 125
HAD-SF-IA-v1 TIGR01549
haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or ...
 58-234 3.00e-03

haloacid dehalogenase superfamily, subfamily IA, variant 1 with third motif having Dx(3-4)D or Dx(3-4)E; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions.The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)(D/E), (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 1 (this model) is found in the enzymes phosphoglycolate phosphatase (TIGR01449) and enolase-phosphatase. These three variant models (see also TIGR01493 and TIGR01509) were created withthe knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly relatedHAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273686 [Multi-domain]  Cd Length: 164  Bit Score: 37.38  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   58 AVCFDVDSTVC-QDEGIDELAAYLGVGEAVANVTRTAMNG----NARFRYRDALAARLQVMkpnhEQLEQFVNISKPKLt 132
Cdd:TIGR01549   1 AILFDIDGTLVdIKFAIRRAFPQTFEEFGLDPASFKALKQagglAEEEWYRIATSALEELQ----GRFWSEYDAEEAYI- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  133 VGIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEksrIYANEILFDkfgkyhgfdtseltSDSGSKETGKpAVIAL 212
Cdd:TIGR01549  76 RGAADLLARLKSAGIKLGIISNGSLRAQKLLLRLFGLG---DYFELILVS--------------DEPGSKPEPE-IFLAA 137

                         170       180
                  ....*....|....*....|..
gi 808356728  213 LKKMYNYKTVVMVGDGATDVEA 234
Cdd:TIGR01549 138 LESLGVPPEVLHVGDNLNDIEG 159
HAD-SF-IA-v3 TIGR01509
haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; ...
 99-183 4.03e-03

haloacid dehalogenase superfamily, subfamily IA, variant 3 with third motif having DD or ED; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called "capping domain", or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 3 (this model) is found in the enzymes beta-phosphoglucomutase (TIGR01990) and deoxyglucose-6-phosphatase, while many other enzymes of subfamily IA exhibit this variant as well as variant 1 (TIGR01549). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273662 [Multi-domain]  Cd Length: 178  Bit Score: 37.40  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728   99 RFRYRDALAARLQVMKPNHEQLEQFVNISKPKLTVGIRELVSRLHARGTHVYLVSGGFRRLILpVAELLGIEK---SRIY 175
Cdd:TIGR01509  49 KAQYGRTISPEDAQLLYKQLFYEQIEEEAKLKPLPGVRALLEALRARGKKLALLTNSPRAHKL-VLALLGLRDlfdVVID 127


                  ....*...
gi 808356728  176 ANEILFDK 183
Cdd:TIGR01509 128 SSDVGLGK 135
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
57-171 6.00e-03

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 37.11  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808356728  57 DAVCFDVDSTVCQDEGI-----DELAAYLGVgeavaNVTR---TAMNGNARFRYRDALAARLQVMKPNHEQLEQFVN--- 125
Cdd:COG0637    3 KAVIFDMDGTLVDSEPLharawREAFAELGI-----DLTEeeyRRLMGRSREDILRYLLEEYGLDLPEEELAARKEElyr 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 808356728 126 --ISKPKLTV--GIRELVSRLHARGTHVYLVSGGFRRLILPVAELLGIEK 171
Cdd:COG0637   78 elLAEEGLPLipGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLD 127
 
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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