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Conserved domains on  [gi|1142877545|gb|AQL24089|]
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alpha/beta hydrolase (plasmid) [Klebsiella variicola]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-314 2.12e-25

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: 101.23  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  52 ISVQTQG-SGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGF-ASTPAISNRGgkiIAPVVDAIAEYIRTQHIKA 129
Cdd:COG0596    14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHgRSDKPAGGYT---LDDLADDLAALLDALGLER 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 130 PAIIGHSLGGEIALMLGARHPDLVGRLMIVDALpfytlmidpaatsetasqraiatrdwilaqspeeflafqktsIARLA 209
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEV------------------------------------------LAALA 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 210 RTeavrpalvAAGLSSDRRTIADAVYELMITDLRPELGRIRAPIEIVY-AYDALfgVPASGVDEMYRRAytntPDIHFTR 288
Cdd:COG0596   129 EP--------LRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWgEKDPI--VPPALARRLAELL----PNAELVV 194

                         250       260
                  ....*....|....*....|....*.
gi 1142877545 289 IDDSFHFIMLDQPERFSSAVQSFLNK 314
Cdd:COG0596   195 LPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-314 2.12e-25

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: 101.23  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  52 ISVQTQG-SGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGF-ASTPAISNRGgkiIAPVVDAIAEYIRTQHIKA 129
Cdd:COG0596    14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHgRSDKPAGGYT---LDDLADDLAALLDALGLER 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 130 PAIIGHSLGGEIALMLGARHPDLVGRLMIVDALpfytlmidpaatsetasqraiatrdwilaqspeeflafqktsIARLA 209
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEV------------------------------------------LAALA 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 210 RTeavrpalvAAGLSSDRRTIADAVYELMITDLRPELGRIRAPIEIVY-AYDALfgVPASGVDEMYRRAytntPDIHFTR 288
Cdd:COG0596   129 EP--------LRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWgEKDPI--VPPALARRLAELL----PNAELVV 194

                         250       260
                  ....*....|....*....|....*.
gi 1142877545 289 IDDSFHFIMLDQPERFSSAVQSFLNK 314
Cdd:COG0596   195 LPGAGHFPPLEQPEAFAAALRDFLAR 220
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 62-311 1.55e-16

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 77.55  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  62 DVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFASTPAIsnrGGKIIAPVVDAIAeyirtQHIKAPAII-GHSLGGE 140
Cdd:TIGR01738   6 HLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGF---GPLSLADMAEAIA-----AQAPDPAIWlGWSLGGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 141 IALMLGARHPDLVGRLMIVDALPFYTLMID-PAATSETA-SQRAIATRDwILAQSPEEFLAFQK--TSIARlARTEAVRP 216
Cdd:TIGR01738  78 VALHIAATHPDRVRALVTVASSPCFSAREDwPEGIKPDVlTGFQQQLSD-DYQRTIERFLALQTlgTPTAR-QDARALKQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 217 ALVAAGLsSDRRTIADAVYELMITDLRPELGRIRAPIEIVYAY-DALfgVPASGVDEMYRRAytntPDIHFTRIDDSFHF 295
Cdd:TIGR01738 156 TLLARPT-PNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYlDGL--VPAKVVPMLDKLA----PHSELYIFAKAAHA 228

                         250
                  ....*....|....*.
gi 1142877545 296 IMLDQPERFSSAVQSF 311
Cdd:TIGR01738 229 PFLSHAEAFCALLVAF 244
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 63-301 4.53e-15

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: 73.31  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGLQLSH-RVHILELAGFASTPAISNRGGKIIAPVVDAIaEYIRTQH-IKAPAIIGHSLGGE 140
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDDLAEDL-EYILEALgLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 141 IALMLGARHPDLVGRLMIVDALPF---------YTLMIDP------AATSETASQRAIATRDWILAQSPEEFLAFQKTSI 205
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPpheldeadrFILALFPgffdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 206 ARLARTEAVRPALVAAGLSSDRRTIAdavyelmITDLRPELGRIRAPIEIVYAYDALFGVPASGVDemYRRAytnTPDIH 285
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLFIETWS-------TELRAKFLGRLDEPTLIIWGDQDPLVPPQALEK--LAQL---FPNAR 229

                         250
                  ....*....|....*.
gi 1142877545 286 FTRIDDSFHFIMLDQP 301
Cdd:pfam00561 230 LVVIPDAGHFAFLEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-156 4.10e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  58 GSGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGF-ASTPAIsnrGGKIIAPVVDAIAEYIRTQHIKAPAIIGHS 136
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHgASSKAV---GAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                          90       100
                  ....*....|....*....|
gi 1142877545 137 LGGEIALMLGARHPDLVGRL 156
Cdd:PRK14875  206 MGGAVALRLAARAPQRVASL 225
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-314 2.12e-25

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: 101.23  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  52 ISVQTQG-SGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGF-ASTPAISNRGgkiIAPVVDAIAEYIRTQHIKA 129
Cdd:COG0596    14 LHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHgRSDKPAGGYT---LDDLADDLAALLDALGLER 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 130 PAIIGHSLGGEIALMLGARHPDLVGRLMIVDALpfytlmidpaatsetasqraiatrdwilaqspeeflafqktsIARLA 209
Cdd:COG0596    91 VVLVGHSMGGMVALELAARHPERVAGLVLVDEV------------------------------------------LAALA 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 210 RTeavrpalvAAGLSSDRRTIADAVYELMITDLRPELGRIRAPIEIVY-AYDALfgVPASGVDEMYRRAytntPDIHFTR 288
Cdd:COG0596   129 EP--------LRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWgEKDPI--VPPALARRLAELL----PNAELVV 194

                         250       260
                  ....*....|....*....|....*.
gi 1142877545 289 IDDSFHFIMLDQPERFSSAVQSFLNK 314
Cdd:COG0596   195 LPGAGHFPPLEQPEAFAAALRDFLAR 220
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 62-311 1.55e-16

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 77.55  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  62 DVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFASTPAIsnrGGKIIAPVVDAIAeyirtQHIKAPAII-GHSLGGE 140
Cdd:TIGR01738   6 HLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGF---GPLSLADMAEAIA-----AQAPDPAIWlGWSLGGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 141 IALMLGARHPDLVGRLMIVDALPFYTLMID-PAATSETA-SQRAIATRDwILAQSPEEFLAFQK--TSIARlARTEAVRP 216
Cdd:TIGR01738  78 VALHIAATHPDRVRALVTVASSPCFSAREDwPEGIKPDVlTGFQQQLSD-DYQRTIERFLALQTlgTPTAR-QDARALKQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 217 ALVAAGLsSDRRTIADAVYELMITDLRPELGRIRAPIEIVYAY-DALfgVPASGVDEMYRRAytntPDIHFTRIDDSFHF 295
Cdd:TIGR01738 156 TLLARPT-PNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYlDGL--VPAKVVPMLDKLA----PHSELYIFAKAAHA 228

                         250
                  ....*....|....*.
gi 1142877545 296 IMLDQPERFSSAVQSF 311
Cdd:TIGR01738 229 PFLSHAEAFCALLVAF 244
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 63-301 4.53e-15

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: 73.31  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGLQLSH-RVHILELAGFASTPAISNRGGKIIAPVVDAIaEYIRTQH-IKAPAIIGHSLGGE 140
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGfRVIALDLRGFGKSSRPKAQDDYRTDDLAEDL-EYILEALgLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 141 IALMLGARHPDLVGRLMIVDALPF---------YTLMIDP------AATSETASQRAIATRDWILAQSPEEFLAFQKTSI 205
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPpheldeadrFILALFPgffdgfVADFAPNPLGRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 206 ARLARTEAVRPALVAAGLSSDRRTIAdavyelmITDLRPELGRIRAPIEIVYAYDALFGVPASGVDemYRRAytnTPDIH 285
Cdd:pfam00561 162 KRFPSGDYALAKSLVTGALLFIETWS-------TELRAKFLGRLDEPTLIIWGDQDPLVPPQALEK--LAQL---FPNAR 229

                         250
                  ....*....|....*.
gi 1142877545 286 FTRIDDSFHFIMLDQP 301
Cdd:pfam00561 230 LVVIPDAGHFAFLEGP 245
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
63-314 1.50e-13

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 69.20  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGL-QLSHRVHILELAGFASTP-AISNRGGKIIAPVVDAIAEYIRTQHiKAPAIIGHSLGGE 140
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALaKAGYTVYAPRLPGHGTSPeDLLKTTWEDWLEDVEEAYEILKAGY-DKVIVIGLSMGGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 141 IALMLGARHPDlvgrlmiVDALpfytLMIDPAATSETASQRAIATRDWIlaqspEEFLAFQKTSIARLARTEAVRPalva 220
Cdd:COG1647    97 LALLLAARYPD-------VAGL----VLLSPALKIDDPSAPLLPLLKYL-----ARSLRGIGSDIEDPEVAEYAYD---- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 221 aglssdrRTIADAVYEL--MITDLRPELGRIRAPIEIVYA-YDALfgVPASGVDEMYRRAytNTPDIHFTRIDDSFHFIM 297
Cdd:COG1647   157 -------RTPLRALAELqrLIREVRRDLPKITAPTLIIQSrKDEV--VPPESARYIYERL--GSPDKELVWLEDSGHVIT 225

                         250
                  ....*....|....*...
gi 1142877545 298 LD-QPERFSSAVQSFLNK 314
Cdd:COG1647   226 LDkDREEVAEEILDFLER 243
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-156 4.10e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 56.88  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  58 GSGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGF-ASTPAIsnrGGKIIAPVVDAIAEYIRTQHIKAPAIIGHS 136
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHgASSKAV---GAGSLDELAAAVLAFLDALGIERAHLVGHS 205

                          90       100
                  ....*....|....*....|
gi 1142877545 137 LGGEIALMLGARHPDLVGRL 156
Cdd:PRK14875  206 MGGAVALRLAARAPQRVASL 225
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 115-299 2.03e-07

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 51.06  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 115 VDAIAEYIRTQHIKAP-AIIGHSLGGEIALMLGARHPDLVGRLMIVDAlpfytlMIDPAATSETASQRAIAtrdWILaqs 193
Cdd:pfam12146  62 LDTFVDKIREEHPGLPlFLLGHSMGGLIAALYALRYPDKVDGLILSAP------ALKIKPYLAPPILKLLA---KLL--- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 194 peeflafqktsiARLARTEAVRPALVAAGLSSD--------------RRTIADAVYELM--ITDLRPELGRIRAPIEIVY 257
Cdd:pfam12146 130 ------------GKLFPRLRVPNNLLPDSLSRDpevvaayaadplvhGGISARTLYELLdaGERLLRRAAAITVPLLLLH 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1142877545 258 A-YDALfgVPASGVDEMYRRAytNTPDIHFTRIDDSFHFIMLD 299
Cdd:pfam12146 198 GgADRV--VDPAGSREFYERA--GSTDKTLKLYPGLYHELLNE 236
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 63-156 9.46e-07

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 46.75  E-value: 9.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGLQLS-HRVHILELAGFASTPAISnrgGKIIAPVVDAIAEYIRTQHIkapAIIGHSLGGEI 141
Cdd:COG1075     8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIEDS---AEQLAAFVDAVLAATGAEKV---DLVGHSMGGLV 81

                          90
                  ....*....|....*..
gi 1142877545 142 A--LMLGARHPDLVGRL 156
Cdd:COG1075    82 AryYLKRLGGAAKVARV 98
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 63-312 1.48e-06

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 48.15  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFASTPAISNRggkiIAPVVDAIAEYIRTQHIKAP-AIIGHSLGGEI 141
Cdd:pfam00975   3 LFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNS----IEALADEYAEALRQIQPEGPyALFGHSMGGML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 142 ALMLGARhpdLVGRLMIVDALpfytLMIDPAATSETASQraiATRDWILAQSPEEFLAFQKTSIARLARTEAVRPALVAA 221
Cdd:pfam00975  79 AFEVARR---LERQGEAVRSL----FLSDASAPHTVRYE---ASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPAL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 222 GlssdrrtiadAVYELMITDLRPELGRIRApiEIVYAYDALFGvpasGVDEMYRRAYTNTPDIHFTRIDDSFHFIMLDQP 301
Cdd:pfam00975 149 R----------ADYRALESYSCPPLDAQSA--TLFYGSDDPLH----DADDLAEWVRDHTPGEFDVHVFDGDHFYLIEHL 212

                         250
                  ....*....|.
gi 1142877545 302 ERFSSAVQSFL 312
Cdd:pfam00975 213 EAVLEIIEAKL 223
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
63-314 2.73e-06

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 47.30  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAIWTDLVSGLQLS-HRVHILELAGF-ASTPAISNRGG-KIIAPVVDAIAEYIRTQHIKAPAIIGHSLGG 139
Cdd:COG2267    31 VVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHgRSDGPRGHVDSfDDYVDDLRAALDALRARPGLPVVLLGHSMGG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 140 EIALMLGARHPDLVGRLMIVDalpfytlmidpaatsetasqraiatrdwilaqspeeflafqktsiarlarteavrPALV 219
Cdd:COG2267   111 LIALLYAARYPDRVAGLVLLA-------------------------------------------------------PAYR 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 220 AAGLSSDRrtiADAVYELMITDlrpELGRIRAPIEIVYA-YDALfgVPASGVDEMYRRAytnTPDIHFTRIDDSFHFIML 298
Cdd:COG2267   136 ADPLLGPS---ARWLRALRLAE---ALARIDVPVLVLHGgADRV--VPPEAARRLAARL---SPDVELVLLPGARHELLN 204

                         250
                  ....*....|....*..
gi 1142877545 299 DQP-ERFSSAVQSFLNK 314
Cdd:COG2267   205 EPArEEVLAAILAWLER 221
PLN02578 PLN02578
hydrolase
 57-161 1.02e-05

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 46.37  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  57 QGSGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFA-STPAISNRGGKIIApvvDAIAEYIRtQHIKAPAII-G 134
Cdd:PLN02578   83 QGEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGwSDKALIEYDAMVWR---DQVADFVK-EVVKEPAVLvG 158

                          90       100
                  ....*....|....*....|....*..
gi 1142877545 135 HSLGGEIALMLGARHPDLVGRLMIVDA 161
Cdd:PLN02578  159 NSLGGFTALSTAVGYPELVAGVALLNS 185
PLN03087 PLN03087
BODYGUARD 1 domain containing hydrolase; Provisional
 62-186 1.51e-05

BODYGUARD 1 domain containing hydrolase; Provisional


Pssm-ID: 215567  Cd Length: 481  Bit Score: 46.34  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  62 DVILIPGLASSRAIWTDLV-----SGLQLSHRVHILELAGFASTPAiSNRGGKIIAPVVDAIAEYIRTQH-IKAPAIIGH 135
Cdd:PLN03087  203 DVLFIHGFISSSAFWTETLfpnfsDAAKSTYRLFAVDLLGFGRSPK-PADSLYTLREHLEMIERSVLERYkVKSFHIVAH 281

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1142877545 136 SLGGEIALMLGARHPDLVGRLMIVdALPFYtlmidPAATSETASQ---RAIATR 186
Cdd:PLN03087  282 SLGCILALALAVKHPGAVKSLTLL-APPYY-----PVPKGVQATQyvmRKVAPR 329
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 63-307 9.92e-05

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.85  E-value: 9.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  63 VILIPGLASSRAiwtDLVSGLQLSHRVHILELAGFASTPAISNRggkiIAPVVDAIAEYIRTQHIKAPAIIGHSLGGEIA 142
Cdd:pfam12697   1 VVLVHGAGLSAA---PLAALLAAGVAVLAPDLPGHGSSSPPPLD----LADLADLAALLDELGAARPVVLVGHSLGGAVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 143 LMLgARHPDLVGRLmiVDALPFYTLMIDPAATSETASQRAIATRDWILAQSPEEFLaFQKTSIARLARTEAVRPALVAAG 222
Cdd:pfam12697  74 LAA-AAAALVVGVL--VAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGF-LDDLPADAEWAAALARLAALLAA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 223 LSSDRrtiadavyelmitdlRPELGRIRAPIEIVYAYDALfgvpasgVDEMYRRAYTNTPDIHFTRIDDSFHFImLDQPE 302
Cdd:pfam12697 150 LALLP---------------LAAWRDLPVPVLVLAEEDRL-------VPELAQRLLAALAGARLVVLPGAGHLP-LDDPE 206


                  ....*
gi 1142877545 303 RFSSA 307
Cdd:pfam12697 207 EVAEA 211
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 131-155 3.30e-04

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 41.29  E-value: 3.30e-04
                          10        20
                  ....*....|....*....|....*
gi 1142877545 131 AIIGHSLGGEIALMLGARHPDLVGR 155
Cdd:pfam00756 113 ALAGQSMGGLGALYLALKYPDLFGS 137
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
55-259 5.80e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 40.77  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  55 QTQGSGT-DVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFASTpaiSNRGGKIIAPVVDAIAEYIRTQHIkapaII 133
Cdd:PRK10349    7 QTKGQGNvHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRS---RGFGALSLADMAEAVLQQAPDKAI----WL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 134 GHSLGGEIALMLGARHPDLVGRLMIVDALPFYTLM-----IDPAATSETASQraiATRDWilAQSPEEFLAFQkTSIARL 208
Cdd:PRK10349   80 GWSLGGLVASQIALTHPERVQALVTVASSPCFSARdewpgIKPDVLAGFQQQ---LSDDF--QRTVERFLALQ-TMGTET 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1142877545 209 ARTEAVRPALVAAGLSSDRRTIADAVYELMIT-DLRPELGRIRAPIEIVYAY 259
Cdd:PRK10349  154 ARQDARALKKTVLALPMPEVDVLNGGLEILKTvDLRQPLQNVSMPFLRLYGY 205
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
105-153 1.52e-03

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 39.23  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1142877545 105 NRGGKIIAPVVDAIAEYIRTQHIKAP--AIIGHSLGGEIALMLGARHPDLV 153
Cdd:COG1506    68 DWGGDEVDDVLAAIDYLAARPYVDPDriGIYGHSYGGYMALLAAARHPDRF 118
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
115-199 4.24e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545 115 VDAIAEYIRTQHIKAP---AIIGHSLGGEIALMLGARHPDLVGrlmivdALPFYTLMIDPAATSETASQRA-----IATR 186
Cdd:COG0412    93 LRAALDWLKAQPEVDAgrvGVVGFCFGGGLALLAAARGPDLAA------AVSFYGGLPADDLLDLAARIKApvlllYGEK 166

                          90
                  ....*....|....
gi 1142877545 187 D-WILAQSPEEFLA 199
Cdd:COG0412   167 DpLVPPEQVAALEA 180
PRK10673 PRK10673
esterase;
48-163 4.72e-03

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 37.79  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1142877545  48 NLQLISVQTQGSGTDVILIPGLASSRAIWTDLVSGLQLSHRVHILELAGFASTPAISNRGGKIIApvvDAIAEYIRTQHI 127
Cdd:PRK10673    4 NIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMA---QDLLDTLDALQI 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1142877545 128 KAPAIIGHSLGGEIALMLGARHPDLVGRLMIVDALP 163
Cdd:PRK10673   81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAP 116
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
114-157 6.44e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 37.91  E-value: 6.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1142877545 114 VVDAIAEYIRTQHIKAP-AIIGHSLGGEIALMLGARHPDLVGRLM 157
Cdd:COG2382   181 LIPFVEKNYRVSADPEHrAIAGLSMGGLAALYAALRHPDLFGYVG 225
 
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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