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Conserved domains on  [gi|1027816425|ref|WP_063722778|]
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phosphonoacetaldehyde hydrolase [Lactiplantibacillus plantarum]

Protein Classification

phosphonoacetaldehyde hydrolase( domain architecture ID 11492487)

phosphonoacetaldehyde hydrolase is a HAD (haloacid dehalogenase) family phosphatase that catalyzes the dephosphorylation of phosphonoacetaldehyde, forming acetaldehyde and phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
phosphonatase TIGR01422
phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous ...
2-255 4.93e-134

phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous bond of a phosphonate. The mechanism depends on the substrate having a carbonyl one carbon away from the cleavage position. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), and contains a modified version of the conserved catalytic motifs of that superfamily: the first motif is usually DxDx(T/V), here it is DxAxT, and in the third motif the normal conserved lysine is instead an arginine. Additionally, the enzyme contains a unique conserved catalytic lysine (B. cereus pos. 53) which is involved in the binding and activation of the substrate through the formation of a Schiff base. The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilized by microorganisms as a chemical warfare agent. [Central intermediary metabolism, Other]


:

Pssm-ID: 188140 [Multi-domain]  Cd Length: 253  Bit Score: 378.61  E-value: 4.93e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   2 TIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDCN 81
Cdd:TIGR01422   1 RIEAVIFDWAGTTVDFGSFAPTGAFVEAFAEFGVQITLEEARKPMGLGKWDHIRALLKMPAVAERWQAKFGRLPTEADVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  82 QIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPAP 161
Cdd:TIGR01422  81 ALYEAFEPMQLAKLAEYASPIPGAIEVIAYLRARGIKIGSTTGYTREMMDVVAPEAAAQGYRPDYNVTADDVPA-GRPAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 162 AMLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGAD 241
Cdd:TIGR01422 160 WMALKNATELGVYDPAAVVKVGDTVPDIEEGRNAGMWTVGVILSSNELGLSEEEYRALPPAELEERRARARARLKAAGAH 239
                         250
                  ....*....|....
gi 1027816425 242 YILQSMAELPALLD 255
Cdd:TIGR01422 240 YVIDTLADLPAVIA 253
 
Name Accession Description Interval E-value
phosphonatase TIGR01422
phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous ...
2-255 4.93e-134

phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous bond of a phosphonate. The mechanism depends on the substrate having a carbonyl one carbon away from the cleavage position. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), and contains a modified version of the conserved catalytic motifs of that superfamily: the first motif is usually DxDx(T/V), here it is DxAxT, and in the third motif the normal conserved lysine is instead an arginine. Additionally, the enzyme contains a unique conserved catalytic lysine (B. cereus pos. 53) which is involved in the binding and activation of the substrate through the formation of a Schiff base. The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilized by microorganisms as a chemical warfare agent. [Central intermediary metabolism, Other]


Pssm-ID: 188140 [Multi-domain]  Cd Length: 253  Bit Score: 378.61  E-value: 4.93e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   2 TIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDCN 81
Cdd:TIGR01422   1 RIEAVIFDWAGTTVDFGSFAPTGAFVEAFAEFGVQITLEEARKPMGLGKWDHIRALLKMPAVAERWQAKFGRLPTEADVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  82 QIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPAP 161
Cdd:TIGR01422  81 ALYEAFEPMQLAKLAEYASPIPGAIEVIAYLRARGIKIGSTTGYTREMMDVVAPEAAAQGYRPDYNVTADDVPA-GRPAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 162 AMLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGAD 241
Cdd:TIGR01422 160 WMALKNATELGVYDPAAVVKVGDTVPDIEEGRNAGMWTVGVILSSNELGLSEEEYRALPPAELEERRARARARLKAAGAH 239
                         250
                  ....*....|....
gi 1027816425 242 YILQSMAELPALLD 255
Cdd:TIGR01422 240 YVIDTLADLPAVIA 253
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
1-265 6.88e-122

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 348.39  E-value: 6.88e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   1 MTIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDC 80
Cdd:PRK13478    2 MKIQAVIFDWAGTTVDFGSFAPTQAFVEAFAQFGVEITLEEARGPMGLGKWDHIRALLKMPRVAARWQAVFGRLPTEADV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  81 NQIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPA 160
Cdd:PRK13478   82 DALYAAFEPLQIAKLADYATPIPGVLEVIAALRARGIKIGSTTGYTREMMDVVVPLAAAQGYRPDHVVTTDDVPA-GRPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 161 PAMLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGA 240
Cdd:PRK13478  161 PWMALKNAIELGVYDVAACVKVDDTVPGIEEGLNAGMWTVGVILSGNELGLSEEEYQALSAAELAARRERARARLRAAGA 240
                         250       260
                  ....*....|....*....|....*
gi 1027816425 241 DYILQSMAELPALLDQINQPVATDH 265
Cdd:PRK13478  241 HYVIDTIADLPAVIADIEARLARGE 265
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
3-245 8.02e-122

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 346.98  E-value: 8.02e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   3 IKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDCNQ 82
Cdd:cd02586     1 IEAVIFDWAGTTVDYGSFAPVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLEMPRVAEAWRAVFGRLPTEADVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  83 IFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPAPA 162
Cdd:cd02586    81 LYEEFEPILIASLAEYSSPIPGVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRPDSLVTPDDVPA-GRPYPW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 163 MLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGADY 242
Cdd:cd02586   160 MCYKNAIELGVYDVAAVVKVGDTVPDIKEGLNAGMWTVGVILSGNELGLSEEEVEALDSEELAARRAEVRQRFKAAGAHY 239

                  ...
gi 1027816425 243 ILQ 245
Cdd:cd02586   240 VID 242
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-250 2.75e-16

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 75.25  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   2 TIKAVIFDWAGTTIDYgSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMdlpavqndwqARFQVLPTEDDcn 81
Cdd:COG0637     1 MIKAVIFDMDGTLVDS-EPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLL----------EEYGLDLPEEE-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  82 qIFSNFKAILLSSLTEFG-KLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVnITSEQTG------ 154
Cdd:COG0637    68 -LAARKEELYRELLAEEGlPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVI-VTGDDVArgkpdp 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 155 ----------GVgrpapamlalaaeqltitDPTTVMKIGDSVNDILEGNNADAVSVGIidgsnimglselafnalspaeq 224
Cdd:COG0637   146 diyllaaerlGV------------------DPEECVVFEDSPAGIRAAKAAGMRVVGV---------------------- 185
                         250       260
                  ....*....|....*....|....*.
gi 1027816425 225 aerRAHVTAAYQRAGADYILQSMAEL 250
Cdd:COG0637   186 ---PDGGTAEEELAGADLVVDDLAEL 208
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-196 1.04e-06

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 47.97  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   3 IKAVIFDWAGTTIDY-----------GSRAPI-VAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQAR 70
Cdd:pfam00702   1 IKAVVFDLDGTLTDGepvvteaiaelASEHPLaKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  71 FQVLPTEDDCNQIFsnfkaillssltEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITS 150
Cdd:pfam00702  81 TVVLVELLGVIALA------------DELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGD 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1027816425 151 EQtgGVGRPAPAMLALAAEQLTItDPTTVMKIGDSVNDILEGNNAD 196
Cdd:pfam00702 149 DV--GVGKPKPEIYLAALERLGV-KPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
phosphonatase TIGR01422
phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous ...
2-255 4.93e-134

phosphonoacetaldehyde hydrolase; This enzyme catalyzes the cleavage of the carbon phosphorous bond of a phosphonate. The mechanism depends on the substrate having a carbonyl one carbon away from the cleavage position. This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (pfam00702), and contains a modified version of the conserved catalytic motifs of that superfamily: the first motif is usually DxDx(T/V), here it is DxAxT, and in the third motif the normal conserved lysine is instead an arginine. Additionally, the enzyme contains a unique conserved catalytic lysine (B. cereus pos. 53) which is involved in the binding and activation of the substrate through the formation of a Schiff base. The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilized by microorganisms as a chemical warfare agent. [Central intermediary metabolism, Other]


Pssm-ID: 188140 [Multi-domain]  Cd Length: 253  Bit Score: 378.61  E-value: 4.93e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   2 TIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDCN 81
Cdd:TIGR01422   1 RIEAVIFDWAGTTVDFGSFAPTGAFVEAFAEFGVQITLEEARKPMGLGKWDHIRALLKMPAVAERWQAKFGRLPTEADVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  82 QIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPAP 161
Cdd:TIGR01422  81 ALYEAFEPMQLAKLAEYASPIPGAIEVIAYLRARGIKIGSTTGYTREMMDVVAPEAAAQGYRPDYNVTADDVPA-GRPAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 162 AMLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGAD 241
Cdd:TIGR01422 160 WMALKNATELGVYDPAAVVKVGDTVPDIEEGRNAGMWTVGVILSSNELGLSEEEYRALPPAELEERRARARARLKAAGAH 239
                         250
                  ....*....|....
gi 1027816425 242 YILQSMAELPALLD 255
Cdd:TIGR01422 240 YVIDTLADLPAVIA 253
PRK13478 PRK13478
phosphonoacetaldehyde hydrolase; Provisional
1-265 6.88e-122

phosphonoacetaldehyde hydrolase; Provisional


Pssm-ID: 184075 [Multi-domain]  Cd Length: 267  Bit Score: 348.39  E-value: 6.88e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   1 MTIKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDC 80
Cdd:PRK13478    2 MKIQAVIFDWAGTTVDFGSFAPTQAFVEAFAQFGVEITLEEARGPMGLGKWDHIRALLKMPRVAARWQAVFGRLPTEADV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  81 NQIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPA 160
Cdd:PRK13478   82 DALYAAFEPLQIAKLADYATPIPGVLEVIAALRARGIKIGSTTGYTREMMDVVVPLAAAQGYRPDHVVTTDDVPA-GRPY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 161 PAMLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGA 240
Cdd:PRK13478  161 PWMALKNAIELGVYDVAACVKVDDTVPGIEEGLNAGMWTVGVILSGNELGLSEEEYQALSAAELAARRERARARLRAAGA 240
                         250       260
                  ....*....|....*....|....*
gi 1027816425 241 DYILQSMAELPALLDQINQPVATDH 265
Cdd:PRK13478  241 HYVIDTIADLPAVIADIEARLARGE 265
HAD_PHN cd02586
Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; ...
3-245 8.02e-122

Phosphonoacetaldehyde hydrolase (phosphonatase); similar to Bacillus cereus phosphonatase; Degradation of the ubiquitous natural phosphonate 2-aminoethylphosphonate (AEP) into useable forms of nitrogen, carbon, and phosphorus is a two-step metabolic pathway. The first step, catalyzed by AEP transaminase, involves the transfer of NH3 from AEP to pyruvate, yielding phosphonoacetaldehyde (P-Ald) and alanine. In the second step, phosphonatase catalyzes the hydrolytic P-C bond cleavage of P-Ald to form orthophosphate and acetaldehyde. 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: 319785 [Multi-domain]  Cd Length: 242  Bit Score: 346.98  E-value: 8.02e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   3 IKAVIFDWAGTTIDYGSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQVLPTEDDCNQ 82
Cdd:cd02586     1 IEAVIFDWAGTTVDYGSFAPVNAFVEAFAQRGVQITLEEARKPMGLLKIDHIRALLEMPRVAEAWRAVFGRLPTEADVDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  83 IFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITSEQTGGvGRPAPA 162
Cdd:cd02586    81 LYEEFEPILIASLAEYSSPIPGVLEVIAKLRARGIKIGSTTGYTREMMDIVLPEAAAQGYRPDSLVTPDDVPA-GRPYPW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 163 MLALAAEQLTITDPTTVMKIGDSVNDILEGNNADAVSVGIIDGSNIMGLSELAFNALSPAEQAERRAHVTAAYQRAGADY 242
Cdd:cd02586   160 MCYKNAIELGVYDVAAVVKVGDTVPDIKEGLNAGMWTVGVILSGNELGLSEEEVEALDSEELAARRAEVRQRFKAAGAHY 239

                  ...
gi 1027816425 243 ILQ 245
Cdd:cd02586   240 VID 242
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
2-250 2.75e-16

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


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 75.25  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   2 TIKAVIFDWAGTTIDYgSRAPIVAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMdlpavqndwqARFQVLPTEDDcn 81
Cdd:COG0637     1 MIKAVIFDMDGTLVDS-EPLHARAWREAFAELGIDLTEEEYRRLMGRSREDILRYLL----------EEYGLDLPEEE-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  82 qIFSNFKAILLSSLTEFG-KLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVnITSEQTG------ 154
Cdd:COG0637    68 -LAARKEELYRELLAEEGlPLIPGVVELLEALKEAGIKIAVATSSPRENAEAVLEAAGLLDYFDVI-VTGDDVArgkpdp 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 155 ----------GVgrpapamlalaaeqltitDPTTVMKIGDSVNDILEGNNADAVSVGIidgsnimglselafnalspaeq 224
Cdd:COG0637   146 diyllaaerlGV------------------DPEECVVFEDSPAGIRAAKAAGMRVVGV---------------------- 185
                         250       260
                  ....*....|....*....|....*.
gi 1027816425 225 aerRAHVTAAYQRAGADYILQSMAEL 250
Cdd:COG0637   186 ---PDGGTAEEELAGADLVVDDLAEL 208
Gph COG0546
Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion];
3-256 2.88e-16

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


Pssm-ID: 440312 [Multi-domain]  Cd Length: 214  Bit Score: 75.35  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   3 IKAVIFDWAGTTIDygSRAPIV-AFQKAFANVGIQ-ISEAEIRQDMGLDKYTHIHKIMDLPAvqndwqarfqvlptEDDC 80
Cdd:COG0546     1 IKLVLFDLDGTLVD--SAPDIAaALNEALAELGLPpLDLEELRALIGLGLRELLRRLLGEDP--------------DEEL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  81 NQIFSNFKAILLSSLTEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLpiaAKQGYRPAVN-ITSEQTGGVGRP 159
Cdd:COG0546    65 EELLARFRELYEEELLDETRLFPGVRELLEALKARGIKLAVVTNKPREFAERLL---EALGLDDYFDaIVGGDDVPPAKP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425 160 APAMLALAAEQLTITDPTTVMkIGDSVNDILEGNNADAVSVGIidgsnimglselAFNALSPAEQAErrahvtaayqrAG 239
Cdd:COG0546   142 KPEPLLEALERLGLDPEEVLM-VGDSPHDIEAARAAGVPFIGV------------TWGYGSAEELEA-----------AG 197
                         250
                  ....*....|....*..
gi 1027816425 240 ADYILQSMAELPALLDQ 256
Cdd:COG0546   198 ADYVIDSLAELLALLAE 214
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
3-196 1.04e-06

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 47.97  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   3 IKAVIFDWAGTTIDY-----------GSRAPI-VAFQKAFANVGIQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQAR 70
Cdd:pfam00702   1 IKAVVFDLDGTLTDGepvvteaiaelASEHPLaKAIVAAAEDLPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  71 FQVLPTEDDCNQIFsnfkaillssltEFGKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVNITS 150
Cdd:pfam00702  81 TVVLVELLGVIALA------------DELKLYPGAAEALKALKERGIKVAILTGDNPEAAEALLRLLGLDDYFDVVISGD 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1027816425 151 EQtgGVGRPAPAMLALAAEQLTItDPTTVMKIGDSVNDILEGNNAD 196
Cdd:pfam00702 149 DV--GVGKPKPEIYLAALERLGV-KPEEVLMVGDGVNDIPAAKAAG 191
HAD_2 pfam13419
Haloacid dehalogenase-like hydrolase;
6-195 1.53e-04

Haloacid dehalogenase-like hydrolase;


Pssm-ID: 404323 [Multi-domain]  Cd Length: 178  Bit Score: 41.42  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425   6 VIFDWAGTTIDyGSRAPIVAFQKAFANVG-IQISEAEIRQDMGLDKYTHIHKIMDLPAVQNDWQARFQvlpteddcnqif 84
Cdd:pfam13419   1 IIFDFDGTLLD-TEELIIKSFNYLLEEFGyGELSEEEILKFIGLPLREIFRYLGVSEDEEEKIEFYLR------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027816425  85 sNFKAILLSSLTefgKLKPGMSAVIDYLTAHNISYGTTTGYDAEMLALVLPIAAKQGYRPAVnITSEQTGGVgRPAPAML 164
Cdd:pfam13419  68 -KYNEELHDKLV---KPYPGIKELLEELKEQGYKLGIVTSKSRENVEEFLKQLGLEDYFDVI-VGGDDVEGK-KPDPDPI 141
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1027816425 165 ALAAEQLTItDPTTVMKIGDSVNDILEGNNA 195
Cdd:pfam13419 142 LKALEQLGL-KPEEVIYVGDSPRDIEAAKNA 171
 
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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