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Conserved domains on  [gi|1060099537|gb|AOG29652|]
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GEO07616p1, partial [Drosophila melanogaster]

Protein Classification

PaaI family thioesterase( domain architecture ID 10130874)

PaaI family thioesterase such as Arthrobacter sp. hot-dog fold enzyme hydroxybenzoyl-CoA thioesterase, a member of the broader acyl-CoA thioesterase family that catalyzes the conversion of acyl-CoAs back to free fatty acids and coenzyme A, and 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
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 ...
 31-140 4.12e-27

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: 97.63  E-value: 4.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  31 IKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMS--KGSHPGVTANLNVSYIAAAKPGELIeIDCNT 108
Cdd:cd03443     4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSalPPGALAVTVDLNVNYLRPARGGDLT-ARARV 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1060099537 109 VRAGKKMAYLDCILRRKsDGKIIAKGGQVKYI 140
Cdd:cd03443    83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
 
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 ...
 31-140 4.12e-27

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: 97.63  E-value: 4.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  31 IKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMS--KGSHPGVTANLNVSYIAAAKPGELIeIDCNT 108
Cdd:cd03443     4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSalPPGALAVTVDLNVNYLRPARGGDLT-ARARV 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1060099537 109 VRAGKKMAYLDCILRRKsDGKIIAKGGQVKYI 140
Cdd:cd03443    83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 8-134 2.95e-23

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 88.46  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537   8 MDFVKQMSEYASGSNGFDRVLKmIKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMS--KGSHPGVT 85
Cdd:COG2050     1 MSDPLERLEGFLAANPFAELLG-IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSalPPGRRAVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1060099537  86 ANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRkSDGKIIAKG 134
Cdd:COG2050    80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTD-EDGKLVATA 127
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 55-131 5.68e-15

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: 65.35  E-value: 5.68e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099537  55 QGTLHGGLTATIVDNCTTYALMSKGS--HPGVTANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRKSDGKII 131
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 31-114 1.72e-07

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: 46.95  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  31 IKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDncTTYALMSKGSHPG----VTANLNVSYIAAAKPGELIEIdC 106
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALAD--TAGSAAGYLCNSGgqavVGLELNANHLRPAREGKVRAI-A 84


                  ....*...
gi 1060099537 107 NTVRAGKK 114
Cdd:TIGR00369  85 QVVHLGRQ 92
 
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 ...
 31-140 4.12e-27

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: 97.63  E-value: 4.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  31 IKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMS--KGSHPGVTANLNVSYIAAAKPGELIeIDCNT 108
Cdd:cd03443     4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSalPPGALAVTVDLNVNYLRPARGGDLT-ARARV 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1060099537 109 VRAGKKMAYLDCILRRKsDGKIIAKGGQVKYI 140
Cdd:cd03443    83 VKLGRRLAVVEVEVTDE-DGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 8-134 2.95e-23

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 88.46  E-value: 2.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537   8 MDFVKQMSEYASGSNGFDRVLKmIKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMS--KGSHPGVT 85
Cdd:COG2050     1 MSDPLERLEGFLAANPFAELLG-IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSalPPGRRAVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1060099537  86 ANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRkSDGKIIAKG 134
Cdd:COG2050    80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTD-EDGKLVATA 127
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 55-131 5.68e-15

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: 65.35  E-value: 5.68e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060099537  55 QGTLHGGLTATIVDNCTTYALMSKGS--HPGVTANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRKSDGKII 131
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 41-137 6.23e-14

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: 63.26  E-value: 6.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  41 AIGEFTVANEHLNRQGTLHGGLTATIVDNCTTYALMSKG--SHPGVTANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYL 118
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                          90
                  ....*....|....*....
gi 1060099537 119 DCILRRKsDGKIIAKGGQV 137
Cdd:cd03440    81 EVEVRNE-DGKLVATATAT 98
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 31-114 1.72e-07

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: 46.95  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060099537  31 IKITGGGDGRAIGEFTVANEHLNRQGTLHGGLTATIVDncTTYALMSKGSHPG----VTANLNVSYIAAAKPGELIEIdC 106
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALAD--TAGSAAGYLCNSGgqavVGLELNANHLRPAREGKVRAI-A 84


                  ....*...
gi 1060099537 107 NTVRAGKK 114
Cdd:TIGR00369  85 QVVHLGRQ 92
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 72-146 1.37e-06

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: 44.89  E-value: 1.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060099537  72 TYALMSKGSHPGVTANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRKSDGKIIAKgGQVKYIQFDKEK 146
Cdd:COG0824    46 SYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLAT-GETVLVFVDLET 119
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 72-134 6.05e-05

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 39.90  E-value: 6.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060099537  72 TYALMSKGSHPGVTANLNVSYIAAAKPGELIEIDCNTVRAGKKMAYLDCILRRKsDGKIIAKG 134
Cdd:cd00586    41 GYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFRE-DGELLATA 102
 
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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