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Conserved domains on  [gi|32699808|sp|Q87RV2|]
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RecName: Full=Esterase FrsA

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
4-414 0e+00

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 pfam06500:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 414  Bit Score: 749.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808     4 DVSKNLSETLFVKHKQAKETSALTQYMPTSK--KILDDREQQEDRAWYRHLRRLQWAWQGLSPIEMEGVLSRIASSTHSR 81
Cdd:pfam06500   1 MTQANLSETLFKPHFKHPETSTLVRRMPHSAqpPILSALDGQTIPHWYRMINRLMWIWRGIDPREIEEVLSRIASSKAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808    82 THDDWLDTVMGYHSGNWTFEWIKLGMEHQRRANDLKGE-DAADELFTASLCFSIAGYPHLKNDNLALQAQVLANKAYSEG 160
Cdd:pfam06500  81 THDDLLDTVMGYRSGNWIYEWATQGMVWQQKACEEDDPqLAGDHWLHAALLYSIAGYPHLKGDNLAEQAQVLSNRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   161 AEKTQYTIKQIEVPYQK-RKIIANLHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWP 239
Cdd:pfam06500 161 AKRLPYTMKQLEFPYQGgAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   240 LTEDSSCLHQAVLNELYSIPYVDHHKVGLVGFRFGGNAMVRLSFLEQEKIKACVALGAPVHDLFTSPKKLQKMPKMYLDM 319
Cdd:pfam06500 241 LTQDSSCLHQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLESPRVKAVACLGPPVHDLLTSPKKLQKVPKMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   320 LASRLGKSAVDINSMAGQMMAWSLKVQGFLsSRKTKVPILALSLEGDPVSPYSDNQLVALFSHYGQAKKISSKTITKGYE 399
Cdd:pfam06500 321 LASRLGMHDVDDESLRGEMNRYSLKVQGLL-GRRCKTPMLAGYWENDPFSPYEDNQLIASSSADGKLLKIPSKPIYRNFE 399
                         410
                  ....*....|....*
gi 32699808   400 QSLDLAIKWLEDELL 414
Cdd:pfam06500 400 QSLDLAIDWLEDELC 414
 
Name Accession Description Interval E-value
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
4-414 0e+00

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 749.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808     4 DVSKNLSETLFVKHKQAKETSALTQYMPTSK--KILDDREQQEDRAWYRHLRRLQWAWQGLSPIEMEGVLSRIASSTHSR 81
Cdd:pfam06500   1 MTQANLSETLFKPHFKHPETSTLVRRMPHSAqpPILSALDGQTIPHWYRMINRLMWIWRGIDPREIEEVLSRIASSKAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808    82 THDDWLDTVMGYHSGNWTFEWIKLGMEHQRRANDLKGE-DAADELFTASLCFSIAGYPHLKNDNLALQAQVLANKAYSEG 160
Cdd:pfam06500  81 THDDLLDTVMGYRSGNWIYEWATQGMVWQQKACEEDDPqLAGDHWLHAALLYSIAGYPHLKGDNLAEQAQVLSNRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   161 AEKTQYTIKQIEVPYQK-RKIIANLHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWP 239
Cdd:pfam06500 161 AKRLPYTMKQLEFPYQGgAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   240 LTEDSSCLHQAVLNELYSIPYVDHHKVGLVGFRFGGNAMVRLSFLEQEKIKACVALGAPVHDLFTSPKKLQKMPKMYLDM 319
Cdd:pfam06500 241 LTQDSSCLHQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLESPRVKAVACLGPPVHDLLTSPKKLQKVPKMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   320 LASRLGKSAVDINSMAGQMMAWSLKVQGFLsSRKTKVPILALSLEGDPVSPYSDNQLVALFSHYGQAKKISSKTITKGYE 399
Cdd:pfam06500 321 LASRLGMHDVDDESLRGEMNRYSLKVQGLL-GRRCKTPMLAGYWENDPFSPYEDNQLIASSSADGKLLKIPSKPIYRNFE 399
                         410
                  ....*....|....*
gi 32699808   400 QSLDLAIKWLEDELL 414
Cdd:pfam06500 400 QSLDLAIDWLEDELC 414
frsA PRK05077
esterase FrsA;
4-414 0e+00

esterase FrsA;


Pssm-ID: 235337  Cd Length: 414  Bit Score: 737.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808    4 DVSKNLSETLFVKHKQAKETSALTQYMPTSK--KILDDREQQEDRAWYRHLRRLQWAWQGLSPIEMEGVLSRIASSTHSR 81
Cdd:PRK05077   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGSqpPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVLARIAMSDAER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   82 THDDWLDTVMGYHSGNWTFEWIKLGMEHQRRA-NDLKGEDAADELFTASLCFSIAGYPHLKNDNLALQAQVLANKAYSEG 160
Cdd:PRK05077  81 TDDELLDTVIGYRGGNWIYEWAKQAMEWQQKAcAEEDPEEAGRHWLHAANLYSIAAYPHLKGDELAEQAQVLANRAYEEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  161 AEKTQYTIKQIEVPYQ-KRKIIANLHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWP 239
Cdd:PRK05077 161 AKRLPGELKELEFPIPgGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDYYRLFRDYLAPRGIAMLTIDMPSVGFSSKWK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  240 LTEDSSCLHQAVLNELYSIPYVDHHKVGLVGFRFGGNAMVRLSFLEQEKIKACVALGAPVHDLFTSPKKLQKMPKMYLDM 319
Cdd:PRK05077 241 LTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAVRLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  320 LASRLGKSAVDINSMAGQMMAWSLKVQGFLsSRKTKVPILALSLEGDPVSPYSDNQLVALFSHYGQAKKISSKTITKGYE 399
Cdd:PRK05077 321 LASRLGMHDASDEALRVELNRYSLKVQGLL-GRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFD 399
                        410
                 ....*....|....*
gi 32699808  400 QSLDLAIKWLEDELL 414
Cdd:PRK05077 400 KALQEISDWLEDRLC 414
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
184-304 1.62e-13

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 69.66  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808 184 LHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWPLTEDSSCLhQAVLNELYSIPYVDH 263
Cdd:COG1506  14 LYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDV-LAAIDYLAARPYVDP 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32699808 264 HKVGLVGFRFGGNAMVRLSFLEQEKIKACVALgAPVHDLFT 304
Cdd:COG1506  93 DRIGIYGHSYGGYMALLAAARHPDRFKAAVAL-AGVSDLRS 132
 
Name Accession Description Interval E-value
FrsA-like pfam06500
Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha ...
4-414 0e+00

Esterase FrsA-like; The FrsA-like family includes FrsA, an esterase found to have the alpha/beta-hydrolase fold. t also includes the hydrolytic polyketide shortening protein Ayg1 from fungi, 2,6-dihydropseudooxynicotine hydrolase from Paenarthrobacter nicotinovorans and Fus2 from Gibberella species. The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase is involved in the nicotine-degradation pathway of Arthrobacter nicotinovorans. Fus2 is part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Fus2 catalyzes closure of the 2-pyrrolidone ring of the intermediate 20-hydroxy-prefusarin to form another intermediate, 20-hydroxy-fusarin, which is then oxidized by Fus8.


Pssm-ID: 428978 [Multi-domain]  Cd Length: 414  Bit Score: 749.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808     4 DVSKNLSETLFVKHKQAKETSALTQYMPTSK--KILDDREQQEDRAWYRHLRRLQWAWQGLSPIEMEGVLSRIASSTHSR 81
Cdd:pfam06500   1 MTQANLSETLFKPHFKHPETSTLVRRMPHSAqpPILSALDGQTIPHWYRMINRLMWIWRGIDPREIEEVLSRIASSKAER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808    82 THDDWLDTVMGYHSGNWTFEWIKLGMEHQRRANDLKGE-DAADELFTASLCFSIAGYPHLKNDNLALQAQVLANKAYSEG 160
Cdd:pfam06500  81 THDDLLDTVMGYRSGNWIYEWATQGMVWQQKACEEDDPqLAGDHWLHAALLYSIAGYPHLKGDNLAEQAQVLSNRAYEEA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   161 AEKTQYTIKQIEVPYQK-RKIIANLHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWP 239
Cdd:pfam06500 161 AKRLPYTMKQLEFPYQGgAKITGFLHMPKGDGPFPTVLMCGGLDSLQTDYWRLFRDYFAPKGIAMLTIDMPSVGASSHWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   240 LTEDSSCLHQAVLNELYSIPYVDHHKVGLVGFRFGGNAMVRLSFLEQEKIKACVALGAPVHDLFTSPKKLQKMPKMYLDM 319
Cdd:pfam06500 241 LTQDSSCLHQAVLNALADVPWVDHTRVGLFGFRFGANVAVRLAYLESPRVKAVACLGPPVHDLLTSPKKLQKVPKMYLDV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   320 LASRLGKSAVDINSMAGQMMAWSLKVQGFLsSRKTKVPILALSLEGDPVSPYSDNQLVALFSHYGQAKKISSKTITKGYE 399
Cdd:pfam06500 321 LASRLGMHDVDDESLRGEMNRYSLKVQGLL-GRRCKTPMLAGYWENDPFSPYEDNQLIASSSADGKLLKIPSKPIYRNFE 399
                         410
                  ....*....|....*
gi 32699808   400 QSLDLAIKWLEDELL 414
Cdd:pfam06500 400 QSLDLAIDWLEDELC 414
frsA PRK05077
esterase FrsA;
4-414 0e+00

esterase FrsA;


Pssm-ID: 235337  Cd Length: 414  Bit Score: 737.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808    4 DVSKNLSETLFVKHKQAKETSALTQYMPTSK--KILDDREQQEDRAWYRHLRRLQWAWQGLSPIEMEGVLSRIASSTHSR 81
Cdd:PRK05077   1 MTQANLSETLFKPRFKHPETSTLVRRFNHGSqpPIQSALDGKTVPHWYRMINRLMWIWRGIDPIEIEEVLARIAMSDAER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   82 THDDWLDTVMGYHSGNWTFEWIKLGMEHQRRA-NDLKGEDAADELFTASLCFSIAGYPHLKNDNLALQAQVLANKAYSEG 160
Cdd:PRK05077  81 TDDELLDTVIGYRGGNWIYEWAKQAMEWQQKAcAEEDPEEAGRHWLHAANLYSIAAYPHLKGDELAEQAQVLANRAYEEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  161 AEKTQYTIKQIEVPYQ-KRKIIANLHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWP 239
Cdd:PRK05077 161 AKRLPGELKELEFPIPgGGPITGFLHLPKGDGPFPTVLVCGGLDSLQTDYYRLFRDYLAPRGIAMLTIDMPSVGFSSKWK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  240 LTEDSSCLHQAVLNELYSIPYVDHHKVGLVGFRFGGNAMVRLSFLEQEKIKACVALGAPVHDLFTSPKKLQKMPKMYLDM 319
Cdd:PRK05077 241 LTQDSSLLHQAVLNALPNVPWVDHTRVAAFGFRFGANVAVRLAYLEPPRLKAVACLGPVVHTLLTDPKRQQQVPEMYLDV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808  320 LASRLGKSAVDINSMAGQMMAWSLKVQGFLsSRKTKVPILALSLEGDPVSPYSDNQLVALFSHYGQAKKISSKTITKGYE 399
Cdd:PRK05077 321 LASRLGMHDASDEALRVELNRYSLKVQGLL-GRRCPTPMLSGYWKNDPFSPEEDSRLIASSSADGKLLEIPFKPVYRNFD 399
                        410
                 ....*....|....*
gi 32699808  400 QSLDLAIKWLEDELL 414
Cdd:PRK05077 400 KALQEISDWLEDRLC 414
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
184-304 1.62e-13

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 69.66  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808 184 LHLPRTDKQLPVVMVSAGLDSLQTDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWPLTEDSSCLhQAVLNELYSIPYVDH 263
Cdd:COG1506  14 LYLPADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDV-LAAIDYLAARPYVDP 92
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 32699808 264 HKVGLVGFRFGGNAMVRLSFLEQEKIKACVALgAPVHDLFT 304
Cdd:COG1506  93 DRIGIYGHSYGGYMALLAAARHPDRFKAAVAL-AGVSDLRS 132
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
194-323 1.65e-03

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: 39.80  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699808   194 PVVMVSAGLDSLqtDMWRLFRNHFAPKDIAMLTVDMPSVGHSSHWPLTED-SSCLHQAVLNELysipyVDHH---KVGLV 269
Cdd:pfam00561   2 PVLLLHGLPGSS--DLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYI-----LEALgleKVNLV 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32699808   270 GFRFGGNAMVRLSFLEQEKIKACVALGAPvhDLFTSPKKLQKMPKMYLDMLASR 323
Cdd:pfam00561  75 GHSMGGLIALAYAAKYPDRVKALVLLGAL--DPPHELDEADRFILALFPGFFDG 126
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
249-301 7.39e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 37.64  E-value: 7.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 32699808 249 QAVLNELYSIPYVDHHKVGLVGFRFGGnamvRLSFL---EQEKIKACVAL-GAPVHD 301
Cdd:COG0412  94 RAALDWLKAQPEVDAGRVGVVGFCFGG----GLALLaaaRGPDLAAAVSFyGGLPAD 146
 
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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