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Conserved domains on  [gi|582027887|gb|AHI31222|]
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phosphoserine phosphatase [Marinobacter salarius]

Protein Classification

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH( domain architecture ID 10014284)

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH catalyzes both the dephosphorylation of phosphoserine (P-Ser) and phosphothreonine (P-Thr), and the transfer of a phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-202 4.70e-145

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


:

Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 401.61  E-value: 4.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 582027887 161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEFLKASAIH 202
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARA 202
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-202 4.70e-145

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 401.61  E-value: 4.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 582027887 161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEFLKASAIH 202
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARA 202
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-199 2.08e-114

phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338).


Pssm-ID: 162723  Cd Length: 203  Bit Score: 324.19  E-value: 2.08e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887    1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 582027887  161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEFLKAS 199
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKAS 199
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 8.06e-100

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 287.25  E-value: 8.06e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:cd02607    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:cd02607   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 582027887 161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEF 195
Cdd:cd02607  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-171 6.89e-20

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: 83.73  E-value: 6.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIP-EIWIAFAEKTG----------IEELKATT----RDIPDYDVLMQQRLKLLDqhgyGLPQ------ 59
Cdd:COG0560    3 MRLAVFDLDGTLIAgESIDELARFLGrrglvdrrevLEEVAAITeramAGELDFEESLRFRVALLA----GLPEeeleel 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  60 IQEVIGELDPL-PGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVnEDGRITDYLLR---QRDPKR 134
Cdd:COG0560   79 AERLFEEVPRLyPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEV-EDGRLTGEVVGpivDGEGKA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 582027887 135 QSVRAF-QLLNY---RVIAAGDSYNDTTMLGQAEAGILFHA 171
Cdd:COG0560  158 EALRELaAELGIdleQSYAYGDSANDLPMLEAAGLPVAVNP 198
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 60-163 3.09e-08

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: 51.43  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   60 IQEVIGELDPLPGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRitdyllrqRDPKRQS-- 136
Cdd:pfam00702  90 VIALADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIyl 161

                          90       100
                  ....*....|....*....|....*....
gi 582027887  137 --VRAFQLLNYRVIAAGDSYNDTTMLGQA 163
Cdd:pfam00702 162 aaLERLGVKPEEVLMVGDGVNDIPAAKAA 190
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-202 4.70e-145

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 401.61  E-value: 4.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 582027887 161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEFLKASAIH 202
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARA 202
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-199 2.08e-114

phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338).


Pssm-ID: 162723  Cd Length: 203  Bit Score: 324.19  E-value: 2.08e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887    1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 582027887  161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEFLKAS 199
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKAS 199
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 8.06e-100

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. 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: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 287.25  E-value: 8.06e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIPEIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQIQEVIGELDPLPGAREFLDWL 80
Cdd:cd02607    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  81 RERFQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPKRQSVRAFQLLNYRVIAAGDSYNDTTML 160
Cdd:cd02607   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 582027887 161 GQAEAGILFHAPKNVIEEFPQFPAVHTFEELKGEF 195
Cdd:cd02607  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-171 6.89e-20

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: 83.73  E-value: 6.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIP-EIWIAFAEKTG----------IEELKATT----RDIPDYDVLMQQRLKLLDqhgyGLPQ------ 59
Cdd:COG0560    3 MRLAVFDLDGTLIAgESIDELARFLGrrglvdrrevLEEVAAITeramAGELDFEESLRFRVALLA----GLPEeeleel 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  60 IQEVIGELDPL-PGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVnEDGRITDYLLR---QRDPKR 134
Cdd:COG0560   79 AERLFEEVPRLyPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEV-EDGRLTGEVVGpivDGEGKA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 582027887 135 QSVRAF-QLLNY---RVIAAGDSYNDTTMLGQAEAGILFHA 171
Cdd:COG0560  158 EALRELaAELGIdleQSYAYGDSANDLPMLEAAGLPVAVNP 198
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-160 1.41e-13

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: 65.84  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887    3 LACLDLEGVLIPE--IWIAFAEKTGIE-ELKATTRDIPDYDVLMQQRLKLLDQHGYGLPQ--IQEVIGELDPL--PGARE 75
Cdd:TIGR01488   1 LAIFDFDGTLTRQdsLIDLLAKLLGTNdEVIELTRLAPSGRISFEDALGRRLALLHRSRSeeVAKEFLARQVAlrPGARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   76 FLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYLLRQRDPK--------RQSVRAFQLLNYR 146
Cdd:TIGR01488  81 LISWLKERgIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPIEGQVNPEgeckgkvlKELLEESKITLKK 160

                         170
                  ....*....|....
gi 582027887  147 VIAAGDSYNDTTML 160
Cdd:TIGR01488 161 IIAVGDSVNDLPML 174
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 38-171 6.50e-12

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: 61.41  E-value: 6.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  38 DYDVLMQQRLKLLDqhgyGLPQ--IQEVIGELDPLPGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKL 114
Cdd:cd07500   42 DFEESLRERVALLK----GLPEsvLDEVYERLTLTPGAEELIQTLKAKgYKTAVVSGGFTYFTDRLAEELGLDYAFANEL 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582027887 115 EVnEDGRITDYLLRQ---RDPKRQSVRAF-QLLNY---RVIAAGDSYNDTTMLGQAEAGILFHA 171
Cdd:cd07500  118 EI-KDGKLTGKVLGPivdAQRKAETLQELaARLGIpleQTVAVGDGANDLPMLKAAGLGIAFHA 180
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 3-160 1.78e-08

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: 52.31  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   3 LACLDLEGVLIP-EIWIAFAEKTGIEELKATTRDIPDYDVLMQQRLKLLDQHGY---------GLPQIQEVIGE------ 66
Cdd:cd02612    1 LAFFDLDGTLIAgDSFFAFLRFKGIAERRAPLEELLLLRLMALYALGRLDGAGMeallgfataGLAGELAALVEefveey 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  67 LDPL--PGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVnEDGRIT-DYLLRQ--RDPKRQSVRAF 140
Cdd:cd02612   81 ILRVlyPEARELIAWHKAAgHDVVLISASPEELVAPIARKLGIDNVLGTQLET-EDGRYTgRIIGPPcyGEGKVKRLREW 159

                        170       180
                 ....*....|....*....|....
gi 582027887 141 ---QLLNYR-VIAAGDSYNDTTML 160
Cdd:cd02612  160 laeEGIDLKdSYAYSDSINDLPML 183
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 60-163 3.09e-08

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: 51.43  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   60 IQEVIGELDPLPGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRitdyllrqRDPKRQS-- 136
Cdd:pfam00702  90 VIALADELKLYPGAAEALKALKERgIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIyl 161

                          90       100
                  ....*....|....*....|....*....
gi 582027887  137 --VRAFQLLNYRVIAAGDSYNDTTMLGQA 163
Cdd:pfam00702 162 aaLERLGVKPEEVLMVGDGVNDIPAAKAA 190
HAD pfam12710
haloacid dehalogenase-like hydrolase;
71-160 4.01e-08

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 50.99  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   71 PGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVnEDGRITDYLLRQRDP-----KRQSVRAF---- 140
Cdd:pfam12710  87 PGALELLAAHRAAgDRVVVVTGGLRPLVEPVLAELGFDEVLATELEV-DDGRFTGELRLIGPPcagegKVRRLRAWlaar 165

                          90       100
                  ....*....|....*....|..
gi 582027887  141 --QLLNYRVIAAGDSYNDTTML 160
Cdd:pfam12710 166 glGLDLADSVAYGDSPSDLPML 187
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 5-169 4.20e-06

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: 45.35  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   5 CLDLEGVLIPEIWI-AFAEKTGI-EELKATTR-----DIPDYDVLmQQRLKLLDqhgYGLPQIQEVIGELDPL--PGARE 75
Cdd:cd04309    4 CFDVDSTVIQEEGIdELAKFCGVgDEVAELTRramggSIPFRDAL-RKRLAIIN---PTKEQVDEFLEEHPPRltPGVEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  76 FLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPA--LLCHKLEVNEDGRITDY----LLRQRDPKRQSVRAFQLLNY--R 146
Cdd:cd04309   80 LVSRLKARgVEVYLISGGFRELIEPVASQLGIPLenVFANRLLFDFNGEYAGFdetqPTSRSGGKAKVIEQLKEKHHykR 159

                        170       180
                 ....*....|....*....|...
gi 582027887 147 VIAAGDSYNDTTMLGQAEAGILF 169
Cdd:cd04309  160 VIMIGDGATDLEACPPADAFIGF 182
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 73-171 1.91e-05

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


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 42.00  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  73 AREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGYPALLCHKLEVNEDGRITDYllrqRDPKRQSVRAFQLLNYRVIAAG 151
Cdd:cd01427   12 AVELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGTPKPK----PKPLLLLLLKLGVDPEEVLFVG 87

                         90       100
                 ....*....|....*....|
gi 582027887 152 DSYNDTTMLgqAEAGILFHA 171
Cdd:cd01427   88 DSENDIEAA--RAAGGRTVA 105
COG2503 COG2503
Predicted secreted acid phosphatase [General function prediction only];
65-156 2.14e-03

Predicted secreted acid phosphatase [General function prediction only];


Pssm-ID: 441997 [Multi-domain]  Cd Length: 269  Bit Score: 38.02  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  65 GELDPLPGAREFLDWLRER-FQVVILSD---TFYEFAMPLMAKLGYPAllchkleVNEDgritDYLLRQ----RDPKRQS 136
Cdd:COG2503  120 AQATAVPGAVEFLNYANSKgVTVFYISNrkaEEKAATLANLKALGFPV-------VDED----HLLLKTdgsdKEARRQA 188

                         90       100
                 ....*....|....*....|.
gi 582027887 137 VRAfqllNYRVIA-AGDSYND 156
Cdd:COG2503  189 VAK----RYRIVMlVGDNLGD 205
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
61-192 3.51e-03

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 37.22  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887  61 QEVIGELDPLPGAREFLDWLRER-FQVVILSDTFYEFAMPLMAKLGypallchkLEVNEDGRITDYLLRQRDPKRQSVR- 138
Cdd:COG0546   77 EELLDETRLFPGVRELLEALKARgIKLAVVTNKPREFAERLLEALG--------LDDYFDAIVGGDDVPPAKPKPEPLLe 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582027887 139 AFQLLNY---RVIAAGDSYNDttMLGQAEAGILF-------HAPKNVIEEFPQFpAVHTFEELK 192
Cdd:COG0546  149 ALERLGLdpeEVLMVGDSPHD--IEAARAAGVPFigvtwgyGSAEELEAAGADY-VIDSLAELL 209
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
1-83 3.60e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 37.11  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582027887   1 MELACLDLEGVLIP------EIWIAFAEKTGI---EELKATTRDIPDYDVLMQqrlkLLDQHGYGLPQ----------IQ 61
Cdd:COG0637    2 IKAVIFDMDGTLVDseplhaRAWREAFAELGIdltEEEYRRLMGRSREDILRY----LLEEYGLDLPEeelaarkeelYR 77

                         90       100
                 ....*....|....*....|....
gi 582027887  62 EVI--GELDPLPGAREFLDWLRER 83
Cdd:COG0637   78 ELLaeEGLPLIPGVVELLEALKEA 101
 
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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