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Conserved domains on  [gi|2097492762|ref|XP_043607921|]
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1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1-like [Erigeron canadensis]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 1-141 3.61e-71

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.


The actual alignment was detected with superfamily member PLN02322:

Pssm-ID: 469797  Cd Length: 154  Bit Score: 210.69  E-value: 3.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   1 MDLPLHAIGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGD 80
Cdd:PLN02322    9 IDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINHLKSADLGD 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2097492762  81 LVFAEATPLQTGRTIQVWEVILWKMDPSNSEKRLLISSSRVTLITNLHVPKDAEDAAQNLK 141
Cdd:PLN02322   89 LVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLR 149
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 1-141 3.61e-71

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 210.69  E-value: 3.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   1 MDLPLHAIGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGD 80
Cdd:PLN02322    9 IDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINHLKSADLGD 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2097492762  81 LVFAEATPLQTGRTIQVWEVILWKMDPSNSEKRLLISSSRVTLITNLHVPKDAEDAAQNLK 141
Cdd:PLN02322   89 LVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLR 149
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 7-124 1.05e-22

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: 86.46  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   7 AIGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGWSR-VAGLQLSINHIKSANLGDLVfAE 85
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAlAVTVDLNVNYLRPARGGDLT-AR 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2097492762  86 ATPLQTGRTIQVWEVILWkmdpsnSEKRLLISSSRVTLI 124
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT------DEDGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 8-124 1.89e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.54  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   8 IGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGW-SRVAGLQLSINHIKSANLGDLVFAEA 86
Cdd:COG2050    21 LGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRPARLGDRLTAEA 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2097492762  87 TPLQTGRTIQVWEVILWkmdpsnSEKRLLISSSRVTLI 124
Cdd:COG2050   101 RVVRRGRRLAVVEVEVT------DEDGKLVATATGTFA 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 34-104 3.22e-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: 61.12  E-value: 3.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2097492762  34 FKVLHGGVS-ALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGDLVFAEATPLQTGRTIQVWEVILWK 104
Cdd:pfam03061   1 GGVVHGGVYlALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 26-124 3.29e-13

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: 61.98  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762  26 LTEKACQPFKVLHGGVS-ALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGDLVfAEATPLQTGRTIQVWEvilwk 104
Cdd:TIGR00369  24 VDERTLQPFGSLHGGVSaALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR-AIAQVVHLGRQTGVAE----- 97

                          90       100
                  ....*....|....*....|
gi 2097492762 105 MDPSNSEKRLLISSSRVTLI 124
Cdd:TIGR00369  98 IEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 1-141 3.61e-71

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 210.69  E-value: 3.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   1 MDLPLHAIGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGD 80
Cdd:PLN02322    9 IDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSINHLKSADLGD 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2097492762  81 LVFAEATPLQTGRTIQVWEVILWKMDPSNSEKRLLISSSRVTLITNLHVPKDAEDAAQNLK 141
Cdd:PLN02322   89 LVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLR 149
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 7-124 1.05e-22

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: 86.46  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   7 AIGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGWSR-VAGLQLSINHIKSANLGDLVfAE 85
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAlAVTVDLNVNYLRPARGGDLT-AR 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2097492762  86 ATPLQTGRTIQVWEVILWkmdpsnSEKRLLISSSRVTLI 124
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT------DEDGKLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 8-124 1.89e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.54  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762   8 IGFQVDDLSPRKVTGHLHLTEKACQPFKVLHGGVSALISEALASMGAHMASGW-SRVAGLQLSINHIKSANLGDLVFAEA 86
Cdd:COG2050    21 LGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRPARLGDRLTAEA 100

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2097492762  87 TPLQTGRTIQVWEVILWkmdpsnSEKRLLISSSRVTLI 124
Cdd:COG2050   101 RVVRRGRRLAVVEVEVT------DEDGKLVATATGTFA 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 34-104 3.22e-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: 61.12  E-value: 3.22e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2097492762  34 FKVLHGGVS-ALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGDLVFAEATPLQTGRTIQVWEVILWK 104
Cdd:pfam03061   1 GGVVHGGVYlALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 26-124 3.29e-13

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: 61.98  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762  26 LTEKACQPFKVLHGGVS-ALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGDLVfAEATPLQTGRTIQVWEvilwk 104
Cdd:TIGR00369  24 VDERTLQPFGSLHGGVSaALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR-AIAQVVHLGRQTGVAE----- 97

                          90       100
                  ....*....|....*....|
gi 2097492762 105 MDPSNSEKRLLISSSRVTLI 124
Cdd:TIGR00369  98 IEIVDEQGRLCALSRGTTAV 117
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
32-122 1.24e-10

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 55.79  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762  32 QPFKVLHGGVSALISEALASMGAHMAS-GWSRVAGLQLSINHIKSANLGDlVFAEATPLQTGRTIQVWEVILWkmdpsnS 110
Cdd:PRK10293   48 QPFGLLHGGASVVLAESIGSVAGYLCTeGEQKVVGLEINANHVRSAREGR-VRGVCKPLHLGSRHQVWQIEIF------D 120

                          90
                  ....*....|..
gi 2097492762 111 EKRLLISSSRVT 122
Cdd:PRK10293  121 EKGRLCCSSRLT 132
PRK10254 PRK10254
proofreading thioesterase EntH;
32-103 9.89e-10

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 53.45  E-value: 9.89e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2097492762  32 QPFKVLHGGVSALISEALASM-GAHMASGWSRVAGLQLSINHIKSANLGDlVFAEATPLQTGRTIQVWEVILW 103
Cdd:PRK10254   48 QPFGLLHGGASAALAETLGSMaGFLMTRDGQCVVGTELNATHHRPVSEGK-VRGVCQPLHLGRQNQSWEIVVF 119
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 20-103 9.68e-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: 47.08  E-value: 9.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2097492762  20 VTGHLHLTEKACQPFKVLHGGV-SALISEALASMGAHMASGWSRVAGLQLSINHIKSANLGDLVFAEATPLQTGRTIQVW 98
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLlLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80


                  ....*
gi 2097492762  99 EVILW 103
Cdd:cd03440    81 EVEVR 85
 
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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