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Conserved domains on  [gi|557714878|gb|AHA26904|]
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4-hydroxybenzoyl-CoA thioesterase domain protein [Pseudomonas aeruginosa PA1R]

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 ...
 3-138 3.56e-43

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: 138.99  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   3 LWRQTPDLEQLNASQKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYC 82
Cdd:PRK10293   2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557714878  83 VGLEVNANHLRGLRSGRVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVV 138
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-138 3.56e-43

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 138.99  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   3 LWRQTPDLEQLNASQKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYC 82
Cdd:PRK10293   2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557714878  83 VGLEVNANHLRGLRSGRVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVV 138
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 24-137 3.60e-39

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: 128.23  E-value: 3.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   24 LLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYCVGLEVNANHLRGLRSGRVTAV 103
Cdd:TIGR00369   5 FLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQ-AVVGLELNANHLRPAREGKVRAI 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 557714878  104 ARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAV 137
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-139 1.37e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.67  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   7 TPDLEQLNAS-QKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTsQYYCVGL 85
Cdd:COG2050    2 SDPLERLEGFlAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPP-GRRAVTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557714878  86 EVNANHLRGLRSG-RVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVVP 139
Cdd:COG2050   81 ELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 24-137 6.57e-32

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: 109.57  E-value: 6.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878  24 LLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQYyCVGLEVNANHLRGLRSGRVTAV 103
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557714878 104 ARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAV 137
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-129 5.61e-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: 62.66  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   51 FGLLHGGASVVLAESLGSMASYLCVDtSQYYCVGLEVNANHLRGLRSG-RVTAVARAIHLGRTTHVWDIRLSGDDGKPSC 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-138 3.56e-43

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 138.99  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   3 LWRQTPDLEQLNASQKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYC 82
Cdd:PRK10293   2 IWKRKITLEALNAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQ-KV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557714878  83 VGLEVNANHLRGLRSGRVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVV 138
Cdd:PRK10293  81 VGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
PRK10254 PRK10254
proofreading thioesterase EntH;
3-138 3.59e-40

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 131.65  E-value: 3.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   3 LWRQTPDLEQLNASQKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYC 82
Cdd:PRK10254   2 IWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQ-CV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557714878  83 VGLEVNANHLRGLRSGRVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVV 138
Cdd:PRK10254  81 VGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 24-137 3.60e-39

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: 128.23  E-value: 3.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   24 LLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyYCVGLEVNANHLRGLRSGRVTAV 103
Cdd:TIGR00369   5 FLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQ-AVVGLELNANHLRPAREGKVRAI 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 557714878  104 ARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAV 137
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 7-139 1.37e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.67  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   7 TPDLEQLNAS-QKNSIGDLLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTsQYYCVGL 85
Cdd:COG2050    2 SDPLERLEGFlAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPP-GRRAVTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 557714878  86 EVNANHLRGLRSG-RVTAVARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAVVP 139
Cdd:COG2050   81 ELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 24-137 6.57e-32

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: 109.57  E-value: 6.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878  24 LLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQYyCVGLEVNANHLRGLRSGRVTAV 103
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGAL-AVTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557714878 104 ARAIHLGRTTHVWDIRLSGDDGKPSCIARLTMAV 137
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PLN02322 PLN02322
acyl-CoA thioesterase
 24-120 3.50e-14

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 65.47  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878  24 LLGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSQyyCVGLEVNANHLRGLRSGR-VTA 102
Cdd:PLN02322  15 MLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKR--VAGIQLSINHLKSADLGDlVFA 92

                         90
                 ....*....|....*...
gi 557714878 103 VARAIHLGRTTHVWDIRL 120
Cdd:PLN02322  93 EATPVSTGKTIQVWEVKL 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 51-129 5.61e-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: 62.66  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   51 FGLLHGGASVVLAESLGSMASYLCVDtSQYYCVGLEVNANHLRGLRSG-RVTAVARAIHLGRTTHVWDIRLSGDDGKPSC 129
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 37-136 1.61e-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: 51.71  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878  37 LTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDtSQYYCVGLEVNANHLRGLRSG-RVTAVARAIHLGRTTHV 115
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-RGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|.
gi 557714878 116 WDIRLSGDDGKPSCIARLTMA 136
Cdd:cd03440   80 VEVEVRNEDGKLVATATATFV 100
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 25-126 1.16e-05

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 42.02  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557714878   25 LGIRFEAFDDESLTASMPVDSRTHQPFGLLHGGASVVLAESLGSMASYLCVDTSqyycVGLEVNANHLRGLRSG-RVTAV 103
Cdd:TIGR02286   4 LGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAA----VAAQCTIDFLRPGRAGeRLEAE 79

                          90       100
                  ....*....|....*....|...
gi 557714878  104 ARAIHLGRTTHVWDIRLSGDDGK 126
Cdd:TIGR02286  80 AVEVSRGGRTGTYDVEVVNQEGE 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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