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Conserved domains on  [gi|81888054|sp|Q566R0|]
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RecName: Full=Acyl-coenzyme A thioesterase THEM4; Short=Acyl-CoA thioesterase THEM4; AltName: Full=Thioesterase superfamily member 4; Flags: Precursor

Protein Classification

PaaI family thioesterase( domain architecture ID 10130874)

PaaI family thioesterase is a member of the broader hot dog-fold acyl-CoA thioesterase family that catalyzes the conversion of acyl-CoAs back to free fatty acids and coenzyme A, similar to human acyl-coenzyme A thioesterase THEM5, which plays an important role in mitochondrial fatty acid metabolism, and in remodeling of the mitochondrial lipid cardiolipin

EC:  3.1.2.-
Gene Ontology:  GO:0047617|GO:0016790
PubMed:  15307895|16464851
TCDB:  9.B.371

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 110-221 1.50e-20

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


:

Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 82.99  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 110 LGFEyamFYNKAEKRIVCLFQGGLHLQGMPGFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPlLSVVV 185
Cdd:cd03443   2 LGIR---VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALppgaLAVTVDLNVNYLRPAR-GGDLT 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 81888054 186 VNSQLQKIEGRKLFVSCTIQSTDEKtLHTQATALFI 221
Cdd:cd03443  78 ARARVVKLGRRLAVVEVEVTDEDGK-LVATARGTFA 112
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 110-221 1.50e-20

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 82.99  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 110 LGFEyamFYNKAEKRIVCLFQGGLHLQGMPGFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPlLSVVV 185
Cdd:cd03443   2 LGIR---VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALppgaLAVTVDLNVNYLRPAR-GGDLT 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 81888054 186 VNSQLQKIEGRKLFVSCTIQSTDEKtLHTQATALFI 221
Cdd:cd03443  78 ARARVVKLGRRLAVVEVEVTDEDGK-LVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 108-227 1.80e-15

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 70.36  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 108 EGLGFEYAMFynkAEKRIVCLFQGGLHLQGMPGFVHGGAIATIIDITAGMCAFS----EGIVMTANLNIDYKKPIPLLSV 183
Cdd:COG2050  19 ELLGIELVEV---EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSalppGRRAVTIELNINFLRPARLGDR 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 81888054 184 VVVNSQLQKIEGRKLFVSCTIQSTDEKTLHTqATALFIKLDPDK 227
Cdd:COG2050  96 LTAEARVVRRGRRLAVVEVEVTDEDGKLVAT-ATGTFAVLPKRP 138
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 140-212 3.04e-11

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 57.65  E-value: 3.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81888054   140 GFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPLLSVVVVNSQLQKIEGRKLFVSCTIQSTDEKTL 212
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGgsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
Name Accession Description Interval E-value
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 110-221 1.50e-20

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 82.99  E-value: 1.50e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 110 LGFEyamFYNKAEKRIVCLFQGGLHLQGMPGFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPlLSVVV 185
Cdd:cd03443   2 LGIR---VVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALppgaLAVTVDLNVNYLRPAR-GGDLT 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 81888054 186 VNSQLQKIEGRKLFVSCTIQSTDEKtLHTQATALFI 221
Cdd:cd03443  78 ARARVVKLGRRLAVVEVEVTDEDGK-LVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 108-227 1.80e-15

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 70.36  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 108 EGLGFEYAMFynkAEKRIVCLFQGGLHLQGMPGFVHGGAIATIIDITAGMCAFS----EGIVMTANLNIDYKKPIPLLSV 183
Cdd:COG2050  19 ELLGIELVEV---EPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSalppGRRAVTIELNINFLRPARLGDR 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 81888054 184 VVVNSQLQKIEGRKLFVSCTIQSTDEKTLHTqATALFIKLDPDK 227
Cdd:COG2050  96 LTAEARVVRRGRRLAVVEVEVTDEDGKLVAT-ATGTFAVLPKRP 138
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 140-212 3.04e-11

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 57.65  E-value: 3.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81888054   140 GFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPLLSVVVVNSQLQKIEGRKLFVSCTIQSTDEKTL 212
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGgsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 140-221 2.38e-08

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 50.17  E-value: 2.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 140 GFVHGGAIATIIDITAGMCAFSEG----IVMTANLNIDYKKPIPLLSVVVVNSQLQKIEGRKLFVSCTIQSTDEKTLhTQ 215
Cdd:cd03440  16 GIVHGGLLLALADEAAGAAAARLGgrglGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLV-AT 94


                ....*.
gi 81888054 216 ATALFI 221
Cdd:cd03440  95 ATATFV 100
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
140-228 5.73e-06

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 44.79  E-value: 5.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 140 GFVHGGAIATIIDITAGMCA--FSEGIVMTANLN-IDYKKPIPLLSVVVVNSQLQKIeGRKlfvSCTIQ--------STD 208
Cdd:COG1607  22 GTLFGGWLLSWMDEAAAIAAarHARGRVVTASVDsVDFLRPVRVGDIVELYARVVRV-GRT---SMEVGvevwaedlRTG 97

                        90       100
                ....*....|....*....|.
gi 81888054 209 EKTLHTQATALFIKLDPD-KP 228
Cdd:COG1607  98 ERRLVTEAYFTFVAVDEDgKP 118
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 140-227 1.06e-03

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 37.93  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81888054 140 GFVHGGAIATIIDITAGMCA--FSEGIVMTANLN-IDYKKPIPLLSVVVVNSQLQKIeGRKlfvSCTIQ--------STD 208
Cdd:cd03442  23 GTIFGGWLLEWMDELAGIAAyrHAGGRVVTASVDrIDFLKPVRVGDVVELSARVVYT-GRT---SMEVGveveaedpLTG 98

                        90
                ....*....|....*....
gi 81888054 209 EKTLHTQATALFIKLDPDK 227
Cdd:cd03442  99 ERRLVTSAYFTFVALDEDG 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 162-227 3.01e-03

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 36.80  E-value: 3.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81888054 162 EGIVM-TANLNIDYKKPIPLLSVVVVNSQLQKIEGRKLFVSCTIQSTDEKTLHTQATALFIKLDPDK 227
Cdd:COG0824  53 EGIGLvVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLET 119
 
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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