NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1796349044|gb|QHF03983|]
View 

hotdog fold thioesterase [Pseudomonas asturiensis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 3-138 3.26e-41

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 PRK10293:

Pssm-ID: 469797  Cd Length: 136  Bit Score: 133.98  E-value: 3.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044   3 VWRVTPDIDALMKAQKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKfFC 82
Cdd:PRK10293    2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1796349044  83 VGLEVNANHLRGVRSGRVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVV 138
Cdd:PRK10293   81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-138 3.26e-41

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 133.98  E-value: 3.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044   3 VWRVTPDIDALMKAQKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKfFC 82
Cdd:PRK10293    2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1796349044  83 VGLEVNANHLRGVRSGRVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVV 138
Cdd:PRK10293   81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 20-137 2.39e-40

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: 131.31  E-value: 2.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  20 TIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLlIDSSKFFCVGLEVNANHLRGVRSGR 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYL-CNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1796349044 100 VTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAV 137
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 17-142 2.03e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 114.27  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  17 QKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDsSKFFCVGLEVNANHLRGVR 96
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLRPAR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1796349044  97 SG-RVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVVPHGQ 142
Cdd:COG2050    92 LGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-137 2.50e-29

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: 103.02  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  25 LDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKFfCVGLEVNANHLRGVRSGRVTGVV 104
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTARA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1796349044 105 RPVHIGRTTHVWDIRITTDEGKLSCISRLTVAV 137
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-129 2.82e-14

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: 63.43  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  51 FGLLHGGASVVLAESLGSMASYLLIDSSKFFcVGLEVNANHLRGVRSG-RVTGVVRPVHIGRTTHVWDIRITTDEGKLSC 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVV-VVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-138 3.26e-41

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 133.98  E-value: 3.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044   3 VWRVTPDIDALMKAQKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKfFC 82
Cdd:PRK10293    2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1796349044  83 VGLEVNANHLRGVRSGRVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVV 138
Cdd:PRK10293   81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 20-137 2.39e-40

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: 131.31  E-value: 2.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  20 TIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLlIDSSKFFCVGLEVNANHLRGVRSGR 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYL-CNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1796349044 100 VTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAV 137
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
3-138 4.45e-39

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 128.95  E-value: 4.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044   3 VWRVTPDIDALMKAQKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKfFC 82
Cdd:PRK10254    2 IWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQ-CV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1796349044  83 VGLEVNANHLRGVRSGRVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVV 138
Cdd:PRK10254   81 VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 17-142 2.03e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 114.27  E-value: 2.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  17 QKNTIGEVLDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDsSKFFCVGLEVNANHLRGVR 96
Cdd:COG2050    13 AANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP-PGRRAVTIELNINFLRPAR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1796349044  97 SG-RVTGVVRPVHIGRTTHVWDIRITTDEGKLSCISRLTVAVVPHGQ 142
Cdd:COG2050    92 LGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-137 2.50e-29

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: 103.02  E-value: 2.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  25 LDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKFfCVGLEVNANHLRGVRSGRVTGVV 104
Cdd:cd03443     2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTARA 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1796349044 105 RPVHIGRTTHVWDIRITTDEGKLSCISRLTVAV 137
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-129 2.82e-14

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: 63.43  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  51 FGLLHGGASVVLAESLGSMASYLLIDSSKFFcVGLEVNANHLRGVRSG-RVTGVVRPVHIGRTTHVWDIRITTDEGKLSC 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVV-VVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 25-135 9.30e-14

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 64.31  E-value: 9.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  25 LDIRFESFTEDSLTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLlidSSKFFCV-GLEVNANHLRGVRSGR-VTG 102
Cdd:PLN02322   16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHM---ASGFKRVaGIQLSINHLKSADLGDlVFA 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1796349044 103 VVRPVHIGRTTHVWDIRI--TTDEGKLSCI----SRLTV 135
Cdd:PLN02322   93 EATPVSTGKTIQVWEVKLwkTTDKDKANKIlissSRVTL 131
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 37-136 6.68e-09

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: 50.17  E-value: 6.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796349044  37 LTASMVVDQRTHQPFGLLHGGASVVLAESLGSMASYLLIDSSKFfCVGLEVNANHLRGVRSG-RVTGVVRPVHIGRTTHV 115
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLG-AVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1796349044 116 WDIRITTDEGKLSCISRLTVA 136
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 100
 
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