NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|32565865|ref|NP_872068|]
View 

Thioesterase domain-containing protein [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
28-140 3.53e-24

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: 89.92  E-value: 3.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865  28 AGNVRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGeTLVLD 106
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADtAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTAR 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 32565865 107 STVIKQGKTLAFTKAELYRKsDNVMIATGVHTKA 140
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDE-DGKLVATARGTFA 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 ...
28-140 3.53e-24

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: 89.92  E-value: 3.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865  28 AGNVRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGeTLVLD 106
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADtAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTAR 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 32565865 107 STVIKQGKTLAFTKAELYRKsDNVMIATGVHTKA 140
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDE-DGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
6-135 5.61e-20

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 79.99  E-value: 5.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865   6 MQLAKEIIKNYGTKGQFGCVSGagnVRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLIDI-FTTGALLLTKPARPG 84
Cdd:COG2050   1 MSDPLERLEGFLAANPFAELLG---IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSaAGLAANSALPPGRRA 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32565865  85 VSVDLHVTYLTAAKIGETLVLDSTVIKQGKTLAFTKAELYRKSDNVmIATG 135
Cdd:COG2050  78 VTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKL-VATA 127
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
55-132 6.90e-13

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: 59.96  E-value: 6.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565865    55 FNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGETLVLDSTVIKQGKTLAFTKAELYRKSDNVMI 132
Cdd:pfam03061   1 GGVVHGGVYLALADeAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
31-117 2.32e-09

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 51.96  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865    31 VRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLIDifTTGALLLTKPARPG---VSVDLHVTYLTAAKIGeTLVLDS 107
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALAD--TAGSAAGYLCNSGGqavVGLELNANHLRPAREG-KVRAIA 84
                          90
                  ....*....|
gi 32565865   108 TVIKQGKTLA 117
Cdd:TIGR00369  85 QVVHLGRQTG 94
PRK11688 PRK11688
thioesterase family protein;
54-138 4.56e-04

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 38.29  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865   54 HFNTLHGGCTSTLIDifTTGAL-----------------LLTKPARPGvSVDLHVTYLTAAkIGETLVLDSTVIKQGKTL 116
Cdd:PRK11688  54 AQSILHGGVIASVLD--VAGGLvcvggilarhediseeeLRQRLSRLG-TIDLRVDYLRPG-RGERFTATSSVLRAGNKV 129
                         90       100
                 ....*....|....*....|..
gi 32565865  117 AFTKAELyRKSDNVMIATGVHT 138
Cdd:PRK11688 130 AVARMEL-HNEQGVHIASGTAT 150
 
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 ...
28-140 3.53e-24

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: 89.92  E-value: 3.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865  28 AGNVRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGeTLVLD 106
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADtAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTAR 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 32565865 107 STVIKQGKTLAFTKAELYRKsDNVMIATGVHTKA 140
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDE-DGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
6-135 5.61e-20

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 79.99  E-value: 5.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865   6 MQLAKEIIKNYGTKGQFGCVSGagnVRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLIDI-FTTGALLLTKPARPG 84
Cdd:COG2050   1 MSDPLERLEGFLAANPFAELLG---IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSaAGLAANSALPPGRRA 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 32565865  85 VSVDLHVTYLTAAKIGETLVLDSTVIKQGKTLAFTKAELYRKSDNVmIATG 135
Cdd:COG2050  78 VTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKL-VATA 127
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
55-132 6.90e-13

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: 59.96  E-value: 6.90e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565865    55 FNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGETLVLDSTVIKQGKTLAFTKAELYRKSDNVMI 132
Cdd:pfam03061   1 GGVVHGGVYLALADeAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
41-138 5.29e-12

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: 58.26  E-value: 5.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865  41 LRVEFEVEKDQSNHFNTLHGGCTSTLID-IFTTGALLLTKPARPGVSVDLHVTYLTAAKIGETLVLDSTVIKQGKTLAFT 119
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADeAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80
                        90
                ....*....|....*....
gi 32565865 120 KAELYRKSDNVmIATGVHT 138
Cdd:cd03440  81 EVEVRNEDGKL-VATATAT 98
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
31-117 2.32e-09

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 51.96  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865    31 VRAVHAEEGNLRVEFEVEKDQSNHFNTLHGGCTSTLIDifTTGALLLTKPARPG---VSVDLHVTYLTAAKIGeTLVLDS 107
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALAD--TAGSAAGYLCNSGGqavVGLELNANHLRPAREG-KVRAIA 84
                          90
                  ....*....|
gi 32565865   108 TVIKQGKTLA 117
Cdd:TIGR00369  85 QVVHLGRQTG 94
PRK11688 PRK11688
thioesterase family protein;
54-138 4.56e-04

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 38.29  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565865   54 HFNTLHGGCTSTLIDifTTGAL-----------------LLTKPARPGvSVDLHVTYLTAAkIGETLVLDSTVIKQGKTL 116
Cdd:PRK11688  54 AQSILHGGVIASVLD--VAGGLvcvggilarhediseeeLRQRLSRLG-TIDLRVDYLRPG-RGERFTATSSVLRAGNKV 129
                         90       100
                 ....*....|....*....|..
gi 32565865  117 AFTKAELyRKSDNVMIATGVHT 138
Cdd:PRK11688 130 AVARMEL-HNEQGVHIASGTAT 150
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH