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Conserved domains on  [gi|1841675129|gb|QJT14719|]
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hotdog fold thioesterase [Aeromonas sp. 2692-1]

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 ...
 8-142 1.16e-52

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 PRK10254:

Pssm-ID: 469797  Cd Length: 137  Bit Score: 163.62  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129   8 IWRKPMSLEGLNASSRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCV 87
Cdd:PRK10254    2 IWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1841675129  88 GLEVNANHLRAKREGVVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVL 142
Cdd:PRK10254   82 GTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
 
Name Accession Description Interval E-value
PRK10254 PRK10254
proofreading thioesterase EntH;
8-142 1.16e-52

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 163.62  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129   8 IWRKPMSLEGLNASSRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCV 87
Cdd:PRK10254    2 IWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1841675129  88 GLEVNANHLRAKREGVVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVL 142
Cdd:PRK10254   82 GTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 25-141 8.54e-45

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: 142.87  E-value: 8.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  25 TLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREGVV 104
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1841675129 105 TGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAV 141
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 22-146 1.51e-40

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 132.76  E-value: 1.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  22 SRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKRE 101
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1841675129 102 G-VVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVLKHKR 146
Cdd:COG2050    93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 29-141 9.47e-37

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: 122.28  E-value: 9.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  29 HLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREGVVTGRC 108
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1841675129 109 TPLHLGATTQVWQIEIRDERGRLLCTSRLTMAV 141
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-133 1.96e-16

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: 69.21  E-value: 1.96e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841675129  56 LGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREG-VVTGRCTPLHLGATTQVWQIEIRDERGRLLC 133
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PRK10254 PRK10254
proofreading thioesterase EntH;
8-142 1.16e-52

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 163.62  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129   8 IWRKPMSLEGLNASSRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCV 87
Cdd:PRK10254    2 IWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1841675129  88 GLEVNANHLRAKREGVVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVL 142
Cdd:PRK10254   82 GTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
8-142 6.95e-50

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 156.32  E-value: 6.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129   8 IWRKPMSLEGLNASSRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCV 87
Cdd:PRK10293    2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1841675129  88 GLEVNANHLRAKREGVVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVL 142
Cdd:PRK10293   82 GLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 25-141 8.54e-45

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: 142.87  E-value: 8.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  25 TLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREGVV 104
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1841675129 105 TGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAV 141
Cdd:TIGR00369  81 RAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 22-146 1.51e-40

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 132.76  E-value: 1.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  22 SRNTLMAHLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKRE 101
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARL 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1841675129 102 G-VVTGRCTPLHLGATTQVWQIEIRDERGRLLCTSRLTMAVLKHKR 146
Cdd:COG2050    93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 29-141 9.47e-37

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: 122.28  E-value: 9.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  29 HLDIVYTAFGPDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREGVVTGRC 108
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1841675129 109 TPLHLGATTQVWQIEIRDERGRLLCTSRLTMAV 141
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-133 1.96e-16

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: 69.21  E-value: 1.96e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841675129  56 LGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREG-VVTGRCTPLHLGATTQVWQIEIRDERGRLLC 133
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 20-139 3.73e-14

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 65.47  E-value: 3.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  20 ASSRNTlmAHLDIVYTAFG-------PDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSyCVGLEVN 92
Cdd:PLN02322    1 SASSNT--KAIDPPLHMLGfefdelsPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKR-VAGIQLS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1841675129  93 ANHLRAKREG-VVTGRCTPLHLGATTQVWQIEI-----RDERGR-LLCTSRLTM 139
Cdd:PLN02322   78 INHLKSADLGdLVFAEATPVSTGKTIQVWEVKLwkttdKDKANKiLISSSRVTL 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 42-140 2.07e-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: 59.41  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  42 LEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAANMAVGPDSYCVGLEVNANHLRAKREG-VVTGRCTPLHLGATTQVW 120
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVTV 80

                          90       100
                  ....*....|....*....|
gi 1841675129 121 QIEIRDERGRLLCTSRLTMA 140
Cdd:cd03440    81 EVEVRNEDGKLVATATATFV 100
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 39-141 6.60e-03

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 34.93  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841675129  39 PDWLEATMPVDHRTHQPLGMLHGGASVVLAETLGSLAAnMAVGPDSYCV---GLEVNanhLRAKREGVVTG--RCTPLHL 113
Cdd:pfam14539  27 PGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGLMA-EASLPDTHRWipkGMTVD---YLAKATGDLTAvaELDPEDW 102

                          90       100
                  ....*....|....*....|....*....
gi 1841675129 114 GATT-QVWQIEIRDERGRLLCTSRLTMAV 141
Cdd:pfam14539 103 GEKGdLPVPVEVRDDAGTEVVRATITLWV 131
 
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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