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Conserved domains on  [gi|9947735|gb|AAG05146|]
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homoserine kinase [Pseudomonas aeruginosa PAO1]

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;
1-205 5.22e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


:

Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 417.02  E-value: 5.22e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 9947735   161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSLSL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-205 5.22e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 417.02  E-value: 5.22e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 9947735   161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSLSL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-203 9.90e-143

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: 395.83  E-value: 9.90e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735      1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 9947735    161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 1.38e-126

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: 355.04  E-value: 1.38e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:cd02607   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:cd02607  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 9947735  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREF 195
Cdd:cd02607 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-171 1.60e-16

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: 74.49  E-value: 1.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    1 MEIACLDLEGVLVPE----IWIAFAEKTGIDALKATTRDIP-----------DYDVLMKQRLRILdeHGLKLGDIQEVIA 65
Cdd:COG0560   3 MRLAVFDLDGTLIAGesidELARFLGRRGLVDRREVLEEVAaiteramagelDFEESLRFRVALL--AGLPEEELEELAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   66 TLKP-----LEGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDD---SDRVVGYQLRQKDpKRQS 136
Cdd:COG0560  81 RLFEevprlYPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDgrlTGEVVGPIVDGEG-KAEA 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 9947735  137 VIAFKSLYY----RVIAAGDSYNDTTMLSEAHAGILFHA 171
Cdd:COG0560 160 LRELAAELGidleQSYAYGDSANDLPMLEAAGLPVAVNP 198
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 13-164 6.36e-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: 50.66  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     13 VPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWLRER-FQVVILSD 91
Cdd:pfam00702  43 LPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERgIKVAILTG 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9947735     92 TFYEFSQPLMRQLGFPTLLCHKLEIDDSDRvvgyqlrqKDPKRQSVIA----FKSLYYRVIAAGDSYNDTTMLSEAH 164
Cdd:pfam00702 123 DNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIYLAalerLGVKPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-205 5.22e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 417.02  E-value: 5.22e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 9947735   161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSLSL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-203 9.90e-143

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: 395.83  E-value: 9.90e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735      1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 9947735    161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 1.38e-126

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: 355.04  E-value: 1.38e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80
Cdd:cd02607   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160
Cdd:cd02607  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 9947735  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREF 195
Cdd:cd02607 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-171 1.60e-16

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: 74.49  E-value: 1.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    1 MEIACLDLEGVLVPE----IWIAFAEKTGIDALKATTRDIP-----------DYDVLMKQRLRILdeHGLKLGDIQEVIA 65
Cdd:COG0560   3 MRLAVFDLDGTLIAGesidELARFLGRRGLVDRREVLEEVAaiteramagelDFEESLRFRVALL--AGLPEEELEELAE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   66 TLKP-----LEGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDD---SDRVVGYQLRQKDpKRQS 136
Cdd:COG0560  81 RLFEevprlYPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDgrlTGEVVGPIVDGEG-KAEA 159

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 9947735  137 VIAFKSLYY----RVIAAGDSYNDTTMLSEAHAGILFHA 171
Cdd:COG0560 160 LRELAAELGidleQSYAYGDSANDLPMLEAAGLPVAVNP 198
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 38-171 1.82e-13

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: 65.65  E-value: 1.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   38 DYDVLMKQRLRILDehGLKLGDIQEVIATLKPLEGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEI 116
Cdd:cd07500  42 DFEESLRERVALLK--GLPESVLDEVYERLTLTPGAEELIQTLKAKgYKTAVVSGGFTYFTDRLAEELGLDYAFANELEI 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9947735  117 DD---SDRVVGyQLRQKDPKRQSVIAFKSLY----YRVIAAGDSYNDTTMLSEAHAGILFHA 171
Cdd:cd07500 120 KDgklTGKVLG-PIVDAQRKAETLQELAARLgiplEQTVAVGDGANDLPMLKAAGLGIAFHA 180
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-163 6.09e-12

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: 61.60  E-value: 6.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735      3 IACLDLEGVLVPE--IWIAFAEKTGI-DALKATTRDIPD----YDVLMKQRLRiLDEHGLKLGDIQEVIAT-LKPLEGAV 74
Cdd:TIGR01488   1 LAIFDFDGTLTRQdsLIDLLAKLLGTnDEVIELTRLAPSgrisFEDALGRRLA-LLHRSRSEEVAKEFLARqVALRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     75 EFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQ---SVIA-----FKSLYY 145
Cdd:TIGR01488  80 ELISWLKERgIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPIEGQVNPEGEckgKVLKelleeSKITLK 159

                         170
                  ....*....|....*...
gi 9947735    146 RVIAAGDSYNDTTMLSEA 163
Cdd:TIGR01488 160 KIIAVGDSVNDLPMLKLA 177
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 13-164 6.36e-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: 50.66  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     13 VPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWLRER-FQVVILSD 91
Cdd:pfam00702  43 LPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERgIKVAILTG 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9947735     92 TFYEFSQPLMRQLGFPTLLCHKLEIDDSDRvvgyqlrqKDPKRQSVIA----FKSLYYRVIAAGDSYNDTTMLSEAH 164
Cdd:pfam00702 123 DNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIYLAalerLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD pfam12710
haloacid dehalogenase-like hydrolase;
57-161 6.66e-07

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 47.53  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     57 LGDIQEVIATLKPLEGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDsDRVVGYQL-------- 127
Cdd:pfam12710  73 LERFVAEVALPRLHPGALELLAAHRAAgDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDD-GRFTGELRligppcag 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 9947735    128 RQKDPKRQSVIAFKSL---YYRVIAAGDSYNDTTMLS 161
Cdd:pfam12710 152 EGKVRRLRAWLAARGLgldLADSVAYGDSPSDLPMLR 188
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 2-178 1.71e-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: 46.51  E-value: 1.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    2 EIACLDLEGVLVPEIWI-AFAEKTGI-DALKATTR-----DIPDYDVLmKQRLRILDehgLKLGDIQEVIATLKPL--EG 72
Cdd:cd04309   1 DAVCFDVDSTVIQEEGIdELAKFCGVgDEVAELTRramggSIPFRDAL-RKRLAIIN---PTKEQVDEFLEEHPPRltPG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   73 AVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPT--LLCHKLEIDDSDRVVGY---QLRQKDPKRQSVIAF---KSL 143
Cdd:cd04309  77 VEELVSRLKARgVEVYLISGGFRELIEPVASQLGIPLenVFANRLLFDFNGEYAGFdetQPTSRSGGKAKVIEQlkeKHH 156

                       170       180       190
                ....*....|....*....|....*....|....*
gi 9947735  144 YYRVIAAGDSYNDTTMLSEAHAGILFhaPENVIRE 178
Cdd:cd04309 157 YKRVIMIGDGATDLEACPPADAFIGF--GGNVIRE 189
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 7-161 1.91e-06

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: 46.53  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    7 DLEGVLVP-EIWIAFAEKTGIDALKATTRDIPDYDvLMKQRLRILDEHGLK-----------LGDIQE-----VIATLKP 69
Cdd:cd02612   5 DLDGTLIAgDSFFAFLRFKGIAERRAPLEELLLLR-LMALYALGRLDGAGMeallgfataglAGELAAlveefVEEYILR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   70 L--EGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDD---SDRVVGYQLRQKdpkrQSVIAFKSL 143
Cdd:cd02612  84 VlyPEARELIAWHKAAgHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDgryTGRIIGPPCYGE----GKVKRLREW 159

                       170       180
                ....*....|....*....|....*
gi 9947735  144 -------YYRVIAAGDSYNDTTMLS 161
Cdd:cd02612 160 laeegidLKDSYAYSDSINDLPMLE 184
HAD-SF-IB-hyp1 TIGR01490
HAD-superfamily subfamily IB hydrolase, TIGR01490; This hypothetical equivalog is a member of ...
 71-161 1.94e-05

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: 43.48  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735     71 EGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVG-------------YQLRQKDPKRQs 136
Cdd:TIGR01490  90 PEARDLIRWHKAEgHTIVLVSASLTILVKPLARILGIDNAIGTRLEESEDGIYTGnidgnnckgegkvHALAELLAEEQ- 168

                          90       100
                  ....*....|....*....|....*
gi 9947735    137 vIAFKSLYyrviAAGDSYNDTTMLS 161
Cdd:TIGR01490 169 -IDLKDSY----AYGDSISDLPLLS 188
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 73-165 7.10e-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: 40.46  E-value: 7.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735   73 AVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRvvgyqlRQKDPKRQSVIAFKSLYY--RVIA 149
Cdd:cd01427  12 AVELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT------PKPKPKPLLLLLLKLGVDpeEVLF 85

                        90
                ....*....|....*.
gi 9947735  150 AGDSYNDTTMLSEAHA 165
Cdd:cd01427  86 VGDSENDIEAARAAGG 101
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-83 6.15e-03

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 36.34  E-value: 6.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947735    7 DLEGVLVP------EIWIAFAEKTGIDALKATTRDI---PDYDVLMkqrlRILDEHGLKLGD----------IQEVIAT- 66
Cdd:COG0637   8 DMDGTLVDseplhaRAWREAFAELGIDLTEEEYRRLmgrSREDILR----YLLEEYGLDLPEeelaarkeelYRELLAEe 83

                        90
                ....*....|....*...
gi 9947735   67 -LKPLEGAVEFVDWLRER 83
Cdd:COG0637  84 gLPLIPGVVELLEALKEA 101
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 48-106 8.79e-03

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: 35.77  E-value: 8.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9947735   48 RILDEHGLKLGD------IQEVIATLKPLEGAVEFVDWLRER-FQVVILSDTFYEFSQPLMRQLGF 106
Cdd:COG1011  67 RLLEELGLDLAEelaeafLAALPELVEPYPDALELLEALKARgYRLALLTNGSAELQEAKLRRLGL 132
Cof COG0561
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ...
 146-174 9.88e-03

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: 35.50  E-value: 9.88e-03
                        10        20
                ....*....|....*....|....*....
gi 9947735  146 RVIAAGDSYNDTTMLSEAHAGIlfhAPEN 174
Cdd:COG0561 139 EVIAFGDSGNDLEMLEAAGLGV---AMGN 164
 
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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