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Conserved domains on  [gi|231567183|ref|NP_001153566|]
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acyl-coenzyme A thioesterase 13 isoform 2 [Homo sapiens]

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 ...
 5-115 5.87e-33

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: 111.11  E-value: 5.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183   5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALLCT-ERGAPGVSVDMNITYMSPAKLGeDIVITAHV 83
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 231567183  84 LKQGKTLAFTSVDLTNkATGKLIAQGRHTKHL 115
Cdd:cd03443   83 VKLGRRLAVVEVEVTD-EDGKLVATARGTFAV 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 ...
 5-115 5.87e-33

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: 111.11  E-value: 5.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183   5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALLCT-ERGAPGVSVDMNITYMSPAKLGeDIVITAHV 83
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 231567183  84 LKQGKTLAFTSVDLTNkATGKLIAQGRHTKHL 115
Cdd:cd03443   83 VKLGRRLAVVEVEVTD-EDGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-110 2.52e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.71  E-value: 2.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183   5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALL-CTERGAPGVSVDMNITYMSPAKLGEDIVITAHV 83
Cdd:COG2050   23 IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsALPPGRRAVTIELNINFLRPARLGDRLTAEARV 102

                         90       100
                 ....*....|....*....|....*..
gi 231567183  84 LKQGKTLAFTSVDLTNkATGKLIAQGR 110
Cdd:COG2050  103 VRRGRRLAVVEVEVTD-EDGKLVATAT 128
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-106 4.37e-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: 64.58  E-value: 4.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 231567183   30 GTLHGGLTATLVDNISTMALL-CTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNKATGKLI 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 5-114 5.34e-14

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: 62.75  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183    5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMA-LLCTERGAPGVSVDMNITYMSPAKLGEdIVITAHV 83
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAgYLCNSGGQAVVGLELNANHLRPAREGK-VRAIAQV 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 231567183   84 LKQGKTLAFTSVDLTNKAtGKLIAQGRHTKH 114
Cdd:TIGR00369  87 VHLGRQTGVAEIEIVDEQ-GRLCALSRGTTA 116
PRK10254 PRK10254
proofreading thioesterase EntH;
18-75 6.14e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 34.19  E-value: 6.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 231567183  18 EMKVEEEHTNAIGTLHGGLTATLVDNISTMA-LLCTERGAPGVSVDMNITYMSPAKLGE 75
Cdd:PRK10254  39 EMPVDTRTHQPFGLLHGGASAALAETLGSMAgFLMTRDGQCVVGTELNATHHRPVSEGK 97
 
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 ...
 5-115 5.87e-33

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: 111.11  E-value: 5.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183   5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALLCT-ERGAPGVSVDMNITYMSPAKLGeDIVITAHV 83
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlPPGALAVTVDLNVNYLRPARGG-DLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 231567183  84 LKQGKTLAFTSVDLTNkATGKLIAQGRHTKHL 115
Cdd:cd03443   83 VKLGRRLAVVEVEVTD-EDGKLVATARGTFAV 113
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 5-110 2.52e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.71  E-value: 2.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183   5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALL-CTERGAPGVSVDMNITYMSPAKLGEDIVITAHV 83
Cdd:COG2050   23 IELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANsALPPGRRAVTIELNINFLRPARLGDRLTAEARV 102

                         90       100
                 ....*....|....*....|....*..
gi 231567183  84 LKQGKTLAFTSVDLTNkATGKLIAQGR 110
Cdd:COG2050  103 VRRGRRLAVVEVEVTD-EDGKLVATAT 128
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 15-112 2.93e-16

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: 68.27  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183  15 VICEMKVEEEHTNAIGTLHGGLTATLVDNISTMALL-CTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFT 93
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAArLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*....
gi 231567183  94 SVDLTNkATGKLIAQGRHT 112
Cdd:cd03440   81 EVEVRN-EDGKLVATATAT 98
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-106 4.37e-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: 64.58  E-value: 4.37e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 231567183   30 GTLHGGLTATLVDNISTMALL-CTERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNKATGKLI 106
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARrLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 5-114 5.34e-14

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: 62.75  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183    5 ITLVSAAPGKVICEMKVEEEHTNAIGTLHGGLTATLVDNISTMA-LLCTERGAPGVSVDMNITYMSPAKLGEdIVITAHV 83
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAgYLCNSGGQAVVGLELNANHLRPAREGK-VRAIAQV 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 231567183   84 LKQGKTLAFTSVDLTNKAtGKLIAQGRHTKH 114
Cdd:TIGR00369  87 VHLGRQTGVAEIEIVDEQ-GRLCALSRGTTA 116
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
21-89 9.64e-07

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 44.40  E-value: 9.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 231567183  21 VEEEHTNAIGTLHGGLTATLVDNIstmALLCTERGAPG----VSVDmNITYMSPAKLGEDIVITAHVLKQGKT 89
Cdd:COG1607   13 VMPEDTNHHGTLFGGWLLSWMDEA---AAIAAARHARGrvvtASVD-SVDFLRPVRVGDIVELYARVVRVGRT 81
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 53-112 9.51e-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: 41.81  E-value: 9.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 231567183  53 ERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNKATGKLIAQGRHT 112
Cdd:COG0824   52 EEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLATGETV 111
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 21-89 6.20e-05

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: 39.47  E-value: 6.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 231567183  21 VEEEHTNAIGTLHGGLTATLVDNIstmALLCTERGAPG----VSVDmNITYMSPAKLGEDIVITAHVLKQGKT 89
Cdd:cd03442   14 VLPEDTNHHGTIFGGWLLEWMDEL---AGIAAYRHAGGrvvtASVD-RIDFLKPVRVGDVVELSARVVYTGRT 82
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 52-112 7.43e-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: 38.74  E-value: 7.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 231567183  52 TERGAPGVSVDMNITYMSPAKLGEDIVITAHVLKQGKTLAFTSVDLTNkATGKLIAQGRHT 112
Cdd:cd00586   46 EEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFR-EDGELLATAETV 105
PRK10254 PRK10254
proofreading thioesterase EntH;
18-75 6.14e-03

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 34.19  E-value: 6.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 231567183  18 EMKVEEEHTNAIGTLHGGLTATLVDNISTMA-LLCTERGAPGVSVDMNITYMSPAKLGE 75
Cdd:PRK10254  39 EMPVDTRTHQPFGLLHGGASAALAETLGSMAgFLMTRDGQCVVGTELNATHHRPVSEGK 97
 
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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