NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|299525761|gb|ADJ24230|]
View 

tol-pal system-associated acyl-CoA thioesterase [Hyphomicrobium denitrificans ATCC 51888]

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 ...
 22-150 4.15e-49

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 TIGR02799:

Pssm-ID: 469797  Cd Length: 126  Bit Score: 154.29  E-value: 4.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDGSDnrepAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:TIGR02799   1 FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEETG----LVFVVRSMELDYLKPARLDDLLTVTT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 299525761  102 RVKEIGGASVTLIQTVTRDGNRIAEAEVTVVLISVS-GKPLRLSQAVRGA 150
Cdd:TIGR02799  77 RVVELKGASLVFAQEVRRGDTLLCEATVEVACVDASdMRPRRLPAELRAA 126
 
Name Accession Description Interval E-value
thio_ybgC TIGR02799
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ...
 22-150 4.15e-49

tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism).


Pssm-ID: 274304  Cd Length: 126  Bit Score: 154.29  E-value: 4.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDGSDnrepAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:TIGR02799   1 FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEETG----LVFVVRSMELDYLKPARLDDLLTVTT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 299525761  102 RVKEIGGASVTLIQTVTRDGNRIAEAEVTVVLISVS-GKPLRLSQAVRGA 150
Cdd:TIGR02799  77 RVVELKGASLVFAQEVRRGDTLLCEATVEVACVDASdMRPRRLPAELRAA 126
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 21-154 1.02e-37

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: 125.78  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  21 RHVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLidgsdNREPAAFVVRRMTFDFFRPARMDDLLEVE 100
Cdd:COG0824    5 TFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAEL-----EEEGIGLVVVEAEIDYLRPARYGDELTVE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299525761 101 TRVKEIGGASVTLIQTVTR--DGNRIAEAEVTVVLIS-VSGKPLRLSQAVRGAFLAH 154
Cdd:COG0824   80 TRVVRLGGSSLTFEYEIFRadDGELLATGETVLVFVDlETGRPVPLPDELRAALEAL 136
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 25-151 1.36e-36

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 122.55  E-value: 1.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  25 PVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDgsdnrEPAAFVVRRMTFDFFRPARMDDLLEVETRVK 104
Cdd:PRK10800   6 PVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLA-----ERVAFVVRKMTVEYYAPARLDDMLEVQSEIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 299525761 105 EIGGASVTLIQ-TVTRDGNRIAEAEVTVVLISVSG-KPLRLSQAVRGAF 151
Cdd:PRK10800  81 SMRGTSLTFTQrIVNAEGTLLNEAEVLIVCVDPLKmKPRALPKSIVAEF 129
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 22-135 2.22e-30

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: 106.15  E-value: 2.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLidgsdNREPAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDEL-----EEQGLGLVVVELEIDYLRPLRLGDRLTVET 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 299525761 102 RVKEIGGASVTLIQTVTR-DGNRIAEAEVTVVLIS 135
Cdd:cd00586   76 RVLRLGRKSFTFEQEIFReDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 28-151 7.97e-15

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 66.59  E-value: 7.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   28 VYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIdgsdnREPAAFVVRRMTFDFFRPARMDDLLEVETRVKEIG 107
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYRE-----ALGIGLILAEAHVRYRRELKLGDELTVETRLIDWD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 299525761  108 GASVTLIQTVTR-DGNRIAEAEVTVVLISV-SGKPLRLSQAVRGAF 151
Cdd:pfam13279  76 AKRFHLEHRFLSpDGKLVATAETRLVFVDYeTRKPAPIPEELLEAL 121
 
Name Accession Description Interval E-value
thio_ybgC TIGR02799
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ...
 22-150 4.15e-49

tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism).


Pssm-ID: 274304  Cd Length: 126  Bit Score: 154.29  E-value: 4.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDGSDnrepAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:TIGR02799   1 FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEETG----LVFVVRSMELDYLKPARLDDLLTVTT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 299525761  102 RVKEIGGASVTLIQTVTRDGNRIAEAEVTVVLISVS-GKPLRLSQAVRGA 150
Cdd:TIGR02799  77 RVVELKGASLVFAQEVRRGDTLLCEATVEVACVDASdMRPRRLPAELRAA 126
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 21-154 1.02e-37

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: 125.78  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  21 RHVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLidgsdNREPAAFVVRRMTFDFFRPARMDDLLEVE 100
Cdd:COG0824    5 TFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAEL-----EEEGIGLVVVEAEIDYLRPARYGDELTVE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 299525761 101 TRVKEIGGASVTLIQTVTR--DGNRIAEAEVTVVLIS-VSGKPLRLSQAVRGAFLAH 154
Cdd:COG0824   80 TRVVRLGGSSLTFEYEIFRadDGELLATGETVLVFVDlETGRPVPLPDELRAALEAL 136
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 25-151 1.36e-36

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 122.55  E-value: 1.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  25 PVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDgsdnrEPAAFVVRRMTFDFFRPARMDDLLEVETRVK 104
Cdd:PRK10800   6 PVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLA-----ERVAFVVRKMTVEYYAPARLDDMLEVQSEIT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 299525761 105 EIGGASVTLIQ-TVTRDGNRIAEAEVTVVLISVSG-KPLRLSQAVRGAF 151
Cdd:PRK10800  81 SMRGTSLTFTQrIVNAEGTLLNEAEVLIVCVDPLKmKPRALPKSIVAEF 129
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 25-144 2.61e-33

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 114.05  E-value: 2.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   25 PVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIDgsdnrEPAAFVVRRMTFDFFRPARMDDLLEVETRVK 104
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRA-----EGVAFVVVNINIEYKKPARLDDVLEIRTQIE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 299525761  105 EIGGASVTLIQTVTRDGNRIAEAEVTVVLISV--SGKPLRLS 144
Cdd:TIGR00051  76 ELNGFSFVFSQEIFNEDEALLKAATVIVVCVDpkKQKPVAIP 117
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 22-135 2.22e-30

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: 106.15  E-value: 2.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLidgsdNREPAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDEL-----EEQGLGLVVVELEIDYLRPLRLGDRLTVET 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 299525761 102 RVKEIGGASVTLIQTVTR-DGNRIAEAEVTVVLIS 135
Cdd:cd00586   76 RVLRLGRKSFTFEQEIFReDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 28-151 7.97e-15

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 66.59  E-value: 7.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   28 VYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGTDARRLIdgsdnREPAAFVVRRMTFDFFRPARMDDLLEVETRVKEIG 107
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYRE-----ALGIGLILAEAHVRYRRELKLGDELTVETRLIDWD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 299525761  108 GASVTLIQTVTR-DGNRIAEAEVTVVLISV-SGKPLRLSQAVRGAF 151
Cdd:pfam13279  76 AKRFHLEHRFLSpDGKLVATAETRLVFVDYeTRKPAPIPEELLEAL 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 36-126 2.01e-12

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: 59.19  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761   36 GGVVYHASYVRFCERGRTDFLRLLGtdarrlidgsdnREPAAFVVRRMTFDFFRPARMDDLLEVETRVKEIGGASVTLIQ 115
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG------------GSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEV 68

                          90
                  ....*....|.
gi 299525761  116 TVTRDGNRIAE 126
Cdd:pfam03061  69 EVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 22-132 1.10e-11

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: 57.87  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299525761  22 HVLPVRVYFEDTDAGGVVYHASYVRFCERGRTDFLRLLGtdarrlidgsdnREPAAFVVRRMTFDFFRPARMDDLLEVET 101
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG------------GRGLGAVTLSLDVRFLRPVRPGDTLTVEA 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 299525761 102 RVKEIGGASVTLIQTVTR-DGNRIAEAEVTVV 132
Cdd:cd03440   69 EVVRVGRSSVTVEVEVRNeDGKLVATATATFV 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