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Conserved domains on  [gi|193207462|ref|NP_001122878|]
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Epoxide hydrolase [Caenorhabditis elegans]

Protein Classification

epoxide hydrolase( domain architecture ID 10534184)

epoxide hydrolase such as juvenile hormone epoxide hydrolase, which catalyzes juvenile hormone hydrolysis; belongs to the alpha/beta hydrolase superfamily

CATH:  3.40.50.1820
EC:  3.3.2.9
Gene Ontology:  GO:0004301|GO:0097176
SCOP:  3000102

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
51-154 4.35e-25

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


:

Pssm-ID: 461913  Cd Length: 106  Bit Score: 99.08  E-value: 4.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462   51 IYSFTIDIKESEVSNFKEKLESERFLPTLYDTNYD-----NYLNELKQVLL-GFNWKQHQHFLNTFKQYKTEIEGLKIHF 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWygvplDYLRELVDYWRdGYDWRAQEARLNSFPQFTTEIDGLDIHF 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 193207462  125 LRVstppKDKKSRVVPLLIFHGFPGSFWDF 154
Cdd:pfam06441  81 VHV----RSNKPDAIPLLLLHGWPGSFLEF 106
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
140-378 1.29e-13

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 70.23  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  140 PLLIFHGFPGSFWDFFKIIPILtnpSRHGFDfgveeaiqfeVIVPSLPGFIFSDKPTKQ-GFNAIATARIIAKLMYRLNL 218
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPAL---ARDGFR----------VIALDLRGFGKSSRPKAQdDYRTDDLAEDLEYILEALGL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  219 NNYFVHGTEgYGSDVATLLSSLYPTRIAGLHLSNPfVNPTFSTFTLAKYALKAM-----GQKDEDRENQENRETGK---- 289
Cdd:pfam00561  69 EKVNLVGHS-MGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFpgffdGFVADFAPNPLGRLVAKllal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  290 -----DNRDQMTDLADYFKQDKFAYPTNSQAFGAAFLNSpsgtakYIESRWKQLSTFFAETNLNELFTMDEIATEIYLYW 364
Cdd:pfam00561 147 lllrlRLLKALPLLNKRFPSGDYALAKSLVTGALLFIET------WSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEK 220
                         250
                  ....*....|....
gi 193207462  365 LTDTLPSALTILDS 378
Cdd:pfam00561 221 LAQLFPNARLVVIP 234
 
Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
51-154 4.35e-25

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


Pssm-ID: 461913  Cd Length: 106  Bit Score: 99.08  E-value: 4.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462   51 IYSFTIDIKESEVSNFKEKLESERFLPTLYDTNYD-----NYLNELKQVLL-GFNWKQHQHFLNTFKQYKTEIEGLKIHF 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWygvplDYLRELVDYWRdGYDWRAQEARLNSFPQFTTEIDGLDIHF 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 193207462  125 LRVstppKDKKSRVVPLLIFHGFPGSFWDF 154
Cdd:pfam06441  81 VHV----RSNKPDAIPLLLLHGWPGSFLEF 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
140-378 1.29e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 70.23  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  140 PLLIFHGFPGSFWDFFKIIPILtnpSRHGFDfgveeaiqfeVIVPSLPGFIFSDKPTKQ-GFNAIATARIIAKLMYRLNL 218
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPAL---ARDGFR----------VIALDLRGFGKSSRPKAQdDYRTDDLAEDLEYILEALGL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  219 NNYFVHGTEgYGSDVATLLSSLYPTRIAGLHLSNPfVNPTFSTFTLAKYALKAM-----GQKDEDRENQENRETGK---- 289
Cdd:pfam00561  69 EKVNLVGHS-MGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFpgffdGFVADFAPNPLGRLVAKllal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  290 -----DNRDQMTDLADYFKQDKFAYPTNSQAFGAAFLNSpsgtakYIESRWKQLSTFFAETNLNELFTMDEIATEIYLYW 364
Cdd:pfam00561 147 lllrlRLLKALPLLNKRFPSGDYALAKSLVTGALLFIET------WSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEK 220
                         250
                  ....*....|....
gi 193207462  365 LTDTLPSALTILDS 378
Cdd:pfam00561 221 LAQLFPNARLVVIP 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
116-255 2.36e-12

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 116 EIEGLKIHFLRVSTPPKdkksrvvPLLIFHGFPGSFWDFFKIIPILTNpsrhgfdfgveeaiQFEVIVPSLPGFIFSDKP 195
Cdd:COG0596    8 TVDGVRLHYREAGPDGP-------PVVLLHGLPGSSYEWRPLIPALAA--------------GYRVIAPDLRGHGRSDKP 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 196 TkQGFNAIATARIIAKLMYRLNLNNYFVHGTeGYGSDVATLLSSLYPTRIAGLHLSNPFV 255
Cdd:COG0596   67 A-GGYTLDDLADDLAALLDALGLERVVLVGH-SMGGMVALELAARHPERVAGLVLVDEVL 124
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
120-199 4.31e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.26  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 120 LKIHFlrVSTPPKDKKsrvvPLLIFHGFPGsfWDFF--KIIPILTnpsrhgfdfgveeAIQFEVIVPSLPGFIFSDKPTK 197
Cdd:PRK00870  34 LRMHY--VDEGPADGP----PVLLLHGEPS--WSYLyrKMIPILA-------------AAGHRVIAPDLIGFGRSDKPTR 92

                 ..
gi 193207462 198 QG 199
Cdd:PRK00870  93 RE 94
 
Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
51-154 4.35e-25

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


Pssm-ID: 461913  Cd Length: 106  Bit Score: 99.08  E-value: 4.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462   51 IYSFTIDIKESEVSNFKEKLESERFLPTLYDTNYD-----NYLNELKQVLL-GFNWKQHQHFLNTFKQYKTEIEGLKIHF 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWygvplDYLRELVDYWRdGYDWRAQEARLNSFPQFTTEIDGLDIHF 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 193207462  125 LRVstppKDKKSRVVPLLIFHGFPGSFWDF 154
Cdd:pfam06441  81 VHV----RSNKPDAIPLLLLHGWPGSFLEF 106
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
140-378 1.29e-13

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 70.23  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  140 PLLIFHGFPGSFWDFFKIIPILtnpSRHGFDfgveeaiqfeVIVPSLPGFIFSDKPTKQ-GFNAIATARIIAKLMYRLNL 218
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPAL---ARDGFR----------VIALDLRGFGKSSRPKAQdDYRTDDLAEDLEYILEALGL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  219 NNYFVHGTEgYGSDVATLLSSLYPTRIAGLHLSNPfVNPTFSTFTLAKYALKAM-----GQKDEDRENQENRETGK---- 289
Cdd:pfam00561  69 EKVNLVGHS-MGGLIALAYAAKYPDRVKALVLLGA-LDPPHELDEADRFILALFpgffdGFVADFAPNPLGRLVAKllal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462  290 -----DNRDQMTDLADYFKQDKFAYPTNSQAFGAAFLNSpsgtakYIESRWKQLSTFFAETNLNELFTMDEIATEIYLYW 364
Cdd:pfam00561 147 lllrlRLLKALPLLNKRFPSGDYALAKSLVTGALLFIET------WSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEK 220
                         250
                  ....*....|....
gi 193207462  365 LTDTLPSALTILDS 378
Cdd:pfam00561 221 LAQLFPNARLVVIP 234
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
116-255 2.36e-12

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 116 EIEGLKIHFLRVSTPPKdkksrvvPLLIFHGFPGSFWDFFKIIPILTNpsrhgfdfgveeaiQFEVIVPSLPGFIFSDKP 195
Cdd:COG0596    8 TVDGVRLHYREAGPDGP-------PVVLLHGLPGSSYEWRPLIPALAA--------------GYRVIAPDLRGHGRSDKP 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 196 TkQGFNAIATARIIAKLMYRLNLNNYFVHGTeGYGSDVATLLSSLYPTRIAGLHLSNPFV 255
Cdd:COG0596   67 A-GGYTLDDLADDLAALLDALGLERVVLVGH-SMGGMVALELAARHPERVAGLVLVDEVL 124
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
120-199 4.31e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.26  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 120 LKIHFlrVSTPPKDKKsrvvPLLIFHGFPGsfWDFF--KIIPILTnpsrhgfdfgveeAIQFEVIVPSLPGFIFSDKPTK 197
Cdd:PRK00870  34 LRMHY--VDEGPADGP----PVLLLHGEPS--WSYLyrKMIPILA-------------AAGHRVIAPDLIGFGRSDKPTR 92

                 ..
gi 193207462 198 QG 199
Cdd:PRK00870  93 RE 94
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
140-261 2.17e-03

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 40.25  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207462 140 PLLIFHGFPGSFWDFFKIIPILTNPSRhgfdfgveeAIQFEVIvpslpGFIFSDKPT-KQGFNAIATARI--IAKLMYRL 216
Cdd:PLN03084 129 PVLLIHGFPSQAYSYRKVLPVLSKNYH---------AIAFDWL-----GFGFSDKPQpGYGFNYTLDEYVssLESLIDEL 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 193207462 217 NLNNYFVHgTEGYGSDVATLLSSLYPTRIAGLHLSNPFVNPTFST 261
Cdd:PLN03084 195 KSDKVSLV-VQGYFSPPVVKYASAHPDKIKKLILLNPPLTKEHAK 238
 
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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