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Conserved domains on  [gi|488984263|ref|WP_002895056|]
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MULTISPECIES: tol-pal system-associated acyl-CoA thioesterase [Bacteria]

Protein Classification

tol-pal system-associated acyl-CoA thioesterase( domain architecture ID 10793479)

tol-pal system-associated acyl-CoA thioesterase YbgC catalyzes the hydrolysis of short chain aliphatic acyl-CoA thioesters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0047617
PubMed:  15307895
SCOP:  3000149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 4-133 4.46e-90

acyl-CoA thioesterase YbgC; Provisional


:

Pssm-ID: 182742  Cd Length: 130  Bit Score: 256.98  E-value: 4.46e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   4 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEIT 83
Cdd:PRK10800   1 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488984263  84 SMRGTSLVFTQRIVNAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAEFK 133
Cdd:PRK10800  81 SMRGTSLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALPKSIVAEFK 130
 
Name Accession Description Interval E-value
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 4-133 4.46e-90

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 256.98  E-value: 4.46e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   4 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEIT 83
Cdd:PRK10800   1 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488984263  84 SMRGTSLVFTQRIVNAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAEFK 133
Cdd:PRK10800  81 SMRGTSLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALPKSIVAEFK 130
thio_ybgC TIGR02799
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ...
 6-131 4.67e-65

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: 193.58  E-value: 4.67e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263    6 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAE-RVAFVVRKMTLEYFAPARLDDMLEVQTEITS 84
Cdd:TIGR02799   1 FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEEtGLVFVVRSMELDYLKPARLDDLLTVTTRVVE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 488984263   85 MRGTSLVFTQRIVnAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAE 131
Cdd:TIGR02799  81 LKGASLVFAQEVR-RGDTLLCEATVEVACVDASDMRPRRLPAELRAA 126
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-134 3.94e-43

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: 138.49  E-value: 3.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   1 MNTTLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQT 80
Cdd:COG0824    1 MTLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488984263  81 EITSMRGTSLVFTQRIVNAEN-TVLNEAEVLIVCVDPLLMKPRALPKSIVAEFKQ 134
Cdd:COG0824   81 RVVRLGGSSLTFEYEIFRADDgELLATGETVLVFVDLETGRPVPLPDELRAALEA 135
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-115 1.47e-33

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: 113.08  E-value: 1.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   6 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEITSM 85
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 488984263  86 RGTSLVFTQRIVNAENTVLNEAEVLIVCVD 115
Cdd:cd00586   81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 15-132 1.84e-16

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: 70.06  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   15 EDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEITSMRGTSLVFTQ 94
Cdd:pfam13279   4 GDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEH 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488984263   95 RIVNAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAEF 132
Cdd:pfam13279  84 RFLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
 
Name Accession Description Interval E-value
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 4-133 4.46e-90

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 256.98  E-value: 4.46e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   4 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEIT 83
Cdd:PRK10800   1 TLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEIT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488984263  84 SMRGTSLVFTQRIVNAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAEFK 133
Cdd:PRK10800  81 SMRGTSLTFTQRIVNAEGTLLNEAEVLIVCVDPLKMKPRALPKSIVAEFK 130
thio_ybgC TIGR02799
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ...
 6-131 4.67e-65

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: 193.58  E-value: 4.67e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263    6 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAE-RVAFVVRKMTLEYFAPARLDDMLEVQTEITS 84
Cdd:TIGR02799   1 FRWPIRVYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEEtGLVFVVRSMELDYLKPARLDDLLTVTTRVVE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 488984263   85 MRGTSLVFTQRIVnAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAE 131
Cdd:TIGR02799  81 LKGASLVFAQEVR-RGDTLLCEATVEVACVDASDMRPRRLPAELRAA 126
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 9-125 3.60e-56

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: 170.68  E-value: 3.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263    9 PVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEITSMRGT 88
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488984263   89 SLVFTQRIVNAENTVLNEAEVLIVCVDPLLMKPRALP 125
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVVCVDPKKQKPVAIP 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-134 3.94e-43

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: 138.49  E-value: 3.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   1 MNTTLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQT 80
Cdd:COG0824    1 MTLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488984263  81 EITSMRGTSLVFTQRIVNAEN-TVLNEAEVLIVCVDPLLMKPRALPKSIVAEFKQ 134
Cdd:COG0824   81 RVVRLGGSSLTFEYEIFRADDgELLATGETVLVFVDLETGRPVPLPDELRAALEA 135
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-115 1.47e-33

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: 113.08  E-value: 1.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   6 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEITSM 85
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 488984263  86 RGTSLVFTQRIVNAENTVLNEAEVLIVCVD 115
Cdd:cd00586   81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 15-132 1.84e-16

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: 70.06  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   15 EDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQVLLAERVAFVVRKMTLEYFAPARLDDMLEVQTEITSMRGTSLVFTQ 94
Cdd:pfam13279   4 GDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEH 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488984263   95 RIVNAENTVLNEAEVLIVCVDPLLMKPRALPKSIVAEF 132
Cdd:pfam13279  84 RFLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 20-104 2.04e-15

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: 66.12  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   20 GGVVYHASYVAFYERARTEMLRHHHFSQQVllaervaFVVRKMTLEYFAPARLDDMLEVQTEITSMRGTSLVFTQRIVNA 99
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQV-------VVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*
gi 488984263  100 ENTVL 104
Cdd:pfam03061  74 DGRLV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 6-112 1.03e-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: 59.80  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984263   6 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFsqqvllaERVAFVVRKMTLEYFAPARLDDMLEVQTEITSM 85
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV 73

                         90       100
                 ....*....|....*....|....*..
gi 488984263  86 RGTSLVFTQRIVNAENTVLNEAEVLIV 112
Cdd:cd03440   74 GRSSVTVEVEVRNEDGKLVATATATFV 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.
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