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Conserved domains on  [gi|313709702|emb|CBJ05044|]
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carboxylic ester hydrolase, partial [Propionibacterium freudenreichii]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 11449257)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
1-159 1.88e-50

Acyl-CoA thioesterase [Lipid transport and metabolism];


:

Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 162.35  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPlDVPPPQECPSFIETIEERYGDAAIWHEWDALD 80
Cdd:COG1946   74 YEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMP-DVPPPEDLPSLPELLIAGVLPLRFFAFLRPFD 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313709702  81 VRYVGDSTPGggmpDDPTRRARMRVWVKTTAALPDEiSIHQAIVAYLSDLTLLSVATLphgvAFMSNQLQIASIDHVMW 159
Cdd:COG1946  153 IRPVEGPLPF----APPSGEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALL----SWLGPPLPAASLDHAMW 222
 
Name Accession Description Interval E-value
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
1-159 1.88e-50

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 162.35  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPlDVPPPQECPSFIETIEERYGDAAIWHEWDALD 80
Cdd:COG1946   74 YEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMP-DVPPPEDLPSLPELLIAGVLPLRFFAFLRPFD 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313709702  81 VRYVGDSTPGggmpDDPTRRARMRVWVKTTAALPDEiSIHQAIVAYLSDLTLLSVATLphgvAFMSNQLQIASIDHVMW 159
Cdd:COG1946  153 IRPVEGPLPF----APPSGEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALL----SWLGPPLPAASLDHAMW 222
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 1-159 2.83e-39

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 134.11  E-value: 2.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPlDVPPPQECPS-------FIETIEERYGDAAIW 73
Cdd:PRK10526  76 YDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMP-SAPAPDGLPSetdiaqsLAHLLPPVLKDKFIC 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702  74 HEwdALDVRYVGDSTPGGGMPDDPTRRarmrVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSNQLQIAS 153
Cdd:PRK10526 155 DR--PLEIRPVEFHNPLKGHVAEPVRQ----VWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIAT 228


                 ....*.
gi 313709702 154 IDHVMW 159
Cdd:PRK10526 229 IDHSMW 234
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 1-159 2.92e-32

acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272951 [Multi-domain]  Cd Length: 271  Bit Score: 115.53  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702    1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPLDVPPPQECPSFIETIE------ERYGDAAIWH 74
Cdd:TIGR00189  65 YDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPRENQLATkypatlPRFLKHVVPF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   75 EWDaLDVR--YVGDSTPGGGMPddptrraRMRVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSnQLQIA 152
Cdd:TIGR00189 145 ERP-FEIRpvNLLNYLGGKEDP-------PQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFC-HSMAA 215


                  ....*..
gi 313709702  153 SIDHVMW 159
Cdd:TIGR00189 216 SLDHSIW 222
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 1-159 2.39e-20

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 83.92  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702    1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPG-FDHSDPEPLDVPPPQECPSfiETIEERYGDAAIWHEW-DA 78
Cdd:pfam13622  51 IRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSeWELTPAAPPPLPPPEDCPL--AADEAPFPLFRRVPGFlDP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   79 LDVRYVgdstpGGGMPDDPTRRARMRVWVKttAALPDEISiHQAIVAYLSDLTLLSVATLPHGVAFMsnqLQIASIDHVM 158
Cdd:pfam13622 129 FEPRFA-----RGGGPFSPGGPGRVRLWVR--LRDGGEPD-PLAALAYLADAFPPRVLSLRLDPPAS---GWFPTLDLTV 197


                  .
gi 313709702  159 W 159
Cdd:pfam13622 198 Y 198
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 1-34 6.41e-13

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 239529 [Multi-domain]  Cd Length: 94  Bit Score: 60.71  E-value: 6.41e-13
                         10        20        30
                 ....*....|....*....|....*....|....
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFH 34
Cdd:cd03445   60 YEVERLRDGRSFATRRVRAVQNGKVIFTATASFQ 93
 
Name Accession Description Interval E-value
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
1-159 1.88e-50

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 162.35  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPlDVPPPQECPSFIETIEERYGDAAIWHEWDALD 80
Cdd:COG1946   74 YEVERLRDGRSFSTRRVTAIQGGRVIFTATASFGVPEEGLEHQAPMP-DVPPPEDLPSLPELLIAGVLPLRFFAFLRPFD 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313709702  81 VRYVGDSTPGggmpDDPTRRARMRVWVKTTAALPDEiSIHQAIVAYLSDLTLLSVATLphgvAFMSNQLQIASIDHVMW 159
Cdd:COG1946  153 IRPVEGPLPF----APPSGEPRQRVWMRARDPLPDD-PLHAALLAYASDATPPATALL----SWLGPPLPAASLDHAMW 222
PRK10526 PRK10526
acyl-CoA thioesterase II; Provisional
 1-159 2.83e-39

acyl-CoA thioesterase II; Provisional


Pssm-ID: 182519 [Multi-domain]  Cd Length: 286  Bit Score: 134.11  E-value: 2.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPlDVPPPQECPS-------FIETIEERYGDAAIW 73
Cdd:PRK10526  76 YDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMP-SAPAPDGLPSetdiaqsLAHLLPPVLKDKFIC 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702  74 HEwdALDVRYVGDSTPGGGMPDDPTRRarmrVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSNQLQIAS 153
Cdd:PRK10526 155 DR--PLEIRPVEFHNPLKGHVAEPVRQ----VWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGMQIAT 228


                 ....*.
gi 313709702 154 IDHVMW 159
Cdd:PRK10526 229 IDHSMW 234
tesB TIGR00189
acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. ...
 1-159 2.92e-32

acyl-CoA thioesterase II; Function: hydrolyzes a broad range of acyl-CoA thioesters. Physiological function is not known. Subunit: homotetramer. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 272951 [Multi-domain]  Cd Length: 271  Bit Score: 115.53  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702    1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPLDVPPPQECPSFIETIE------ERYGDAAIWH 74
Cdd:TIGR00189  65 YDVERLRDGRSFITRRVKAVQHGKTIFTLQASFQAEKSGIEHQSTMPKVPPPESELPRENQLATkypatlPRFLKHVVPF 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   75 EWDaLDVR--YVGDSTPGGGMPddptrraRMRVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSnQLQIA 152
Cdd:TIGR00189 145 ERP-FEIRpvNLLNYLGGKEDP-------PQYVWRRARGSLPDDPRLHQCALAYLSDLTLLPTALNPHNKAGFC-HSMAA 215


                  ....*..
gi 313709702  153 SIDHVMW 159
Cdd:TIGR00189 216 SLDHSIW 222
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 1-159 1.81e-31

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 116.36  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPGFDHSDPEPLDVPPPQECPSFIETIEERYGD----------- 69
Cdd:PLN02868 202 YQVERIRDGHNFATRRVDAIQKGKVIFTLFASFQKEEQGFEHQESTMPHVPPPETLLSREELRERRLTDprlprsyrnkv 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702  70 -AAIWHEWdALDVRYVGDSTPGGGMPDDPtrraRMRVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSnq 148
Cdd:PLN02868 282 aAKPFVPW-PIEIRFCEPNNSTNQTKSPP----RLRYWFRAKGKLSDDQALHRCVAAYASDLIFLGTSLNPHRTKGLK-- 354

                        170
                 ....*....|.
gi 313709702 149 LQIASIDHVMW 159
Cdd:PLN02868 355 FAALSLDHSMW 365
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 1-159 2.39e-20

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 83.92  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702    1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFHELEPG-FDHSDPEPLDVPPPQECPSfiETIEERYGDAAIWHEW-DA 78
Cdd:pfam13622  51 IRVEVVRDGRSFSTRRVELSQDGRVVVTATATFGRLRSSeWELTPAAPPPLPPPEDCPL--AADEAPFPLFRRVPGFlDP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313709702   79 LDVRYVgdstpGGGMPDDPTRRARMRVWVKttAALPDEISiHQAIVAYLSDLTLLSVATLPHGVAFMsnqLQIASIDHVM 158
Cdd:pfam13622 129 FEPRFA-----RGGGPFSPGGPGRVRLWVR--LRDGGEPD-PLAALAYLADAFPPRVLSLRLDPPAS---GWFPTLDLTV 197


                  .
gi 313709702  159 W 159
Cdd:pfam13622 198 Y 198
Thioesterase_II_repeat2 cd03445
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 1-34 6.41e-13

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 239529 [Multi-domain]  Cd Length: 94  Bit Score: 60.71  E-value: 6.41e-13
                         10        20        30
                 ....*....|....*....|....*....|....
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQDGRAIFTMSSSFH 34
Cdd:cd03445   60 YEVERLRDGRSFATRRVRAVQNGKVIFTATASFQ 93
Thioesterase_II_repeat1 cd03444
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 103-159 3.55e-12

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 239528 [Multi-domain]  Cd Length: 104  Bit Score: 59.18  E-value: 3.55e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 313709702 103 MRVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFmSNQLQIASIDHVMW 159
Cdd:cd03444    1 LRVWVRARGPLPDDPRLHAAALAYLSDSLLLGTALRPHGLPL-FDASASASLDHAIW 56
Acyl_CoA_thio pfam02551
Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this ...
 98-159 4.81e-09

Acyl-CoA thioesterase; This family represents the thioesterase II domain. Two copies of this domain are found in a number of acyl-CoA thioesterases.


Pssm-ID: 396894  Cd Length: 132  Bit Score: 51.86  E-value: 4.81e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 313709702   98 TRRARMRVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMSNQlqiASIDHVMW 159
Cdd:pfam02551  26 QVVAHQQSWVAALGTVPDDPRLHSCALAYLSDLTLLLTALYPHGFLCDGIQ---VSLDHSIY 84
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 104-159 2.01e-06

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 43.87  E-value: 2.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 313709702 104 RVWVKTTAALPDEISIHQAIVAYLSDLTLLSVATLPHGVAFMsnqlqiASIDHVMW 159
Cdd:cd00556    2 RFWGRAPGPLPDDRRVFGGQLAAQSDLAALRTVPRPHGASGF------ASLDHHIY 51
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 1-34 2.07e-05

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 41.18  E-value: 2.07e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 313709702   1 YAVEPLRDGRSFSSRRVTALQ-DGRAIFTMSSSFH 34
Cdd:cd00556   64 YEVESLRDGRSRALRRGRAYQrDGKLVASATQSFL 98
 
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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