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Conserved domains on  [gi|759751494|ref|WP_043462046|]
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MULTISPECIES: fluoroacetyl-CoA thioesterase [Streptomyces]

Protein Classification

thioesterase family protein( domain architecture ID 10009353)

thioesterase family protein such as Streptomyces cattleya fluoroacetyl-CoA thioesterase that catalyzes the hydrolysis of fluoroacetyl-coenzyme A, preventing it from metabolizing to 4-hydroxy-trans-aconitate, a lethal inhibitor of the tricarboxylic acid cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-138 5.50e-48

Predicted thioesterase [General function prediction only];


:

Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.10  E-value: 5.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759751494   5 LRVGEVFTHSYVVPPDKTVRHLYPespefaGFPEVFATGFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759751494  85 TVTVTAELLSVEKRRIRWRVTAHDGVDAIGSGTHERAVVTLDRFTAGMREKLAR 138
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-138 5.50e-48

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.10  E-value: 5.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759751494   5 LRVGEVFTHSYVVPPDKTVRHLYPespefaGFPEVFATGFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759751494  85 TVTVTAELLSVEKRRIRWRVTAHDGVDAIGSGTHERAVVTLDRFTAGMREKLAR 138
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-117 9.49e-07

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: 44.86  E-value: 9.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759751494  43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGlTVTVTAELLSVEKRRIRWRVTAHDGVD---AIGSGT 117
Cdd:cd03443   34 GAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGklvATARGT 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 43-109 8.08e-03

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: 33.38  E-value: 8.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759751494   43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGLTVTVTAELLSVEKRRIRWRVTAHDG 109
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-138 5.50e-48

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 151.10  E-value: 5.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759751494   5 LRVGEVFTHSYVVPPDKTVRHLYPespefaGFPEVFATGFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGS------GDVPVLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759751494  85 TVTVTAELLSVEKRRIRWRVTAHDGVDAIGSGTHERAVVTLDRFTAGMREKLAR 138
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKAAK 129
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 43-117 1.92e-07

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 47.25  E-value: 1.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759751494  43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGLTVTVTAELLSVEKRRIRWRVTAHDGVD---AIGSGT 117
Cdd:COG2050   53 GALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGklvATATGT 130
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-117 9.49e-07

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: 44.86  E-value: 9.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759751494  43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGlTVTVTAELLSVEKRRIRWRVTAHDGVD---AIGSGT 117
Cdd:cd03443   34 GAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGklvATARGT 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 43-111 1.07e-03

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: 36.30  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759751494  43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGLTVTVTAELLSVEKRRIRWRVTAHDGVD 111
Cdd:cd03440   21 GLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDG 89
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-108 3.07e-03

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 35.63  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759751494   3 DGLRVGEVFTH-SYVVPPDKTVR-----------HLypeSPEFA---GFPEVFATGFMVGLMewtCVRALTPHL-EPGEG 66
Cdd:COG2030    3 EDLEVGDVLPHgGRTVTEEDIVLfagatgdpnpiHL---DEEAAaatGFGGRIAHGMLTLSL---ASGLLVDDLpGTAVA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 759751494  67 SLGTEiRVTHTAATPPGLTVTVTAELLSVEKRR----IRWRVTAHD 108
Cdd:COG2030   77 NLGLQ-EVRFLRPVRVGDTLRARVEVLEKRESKsrgiVTLRTTVTN 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 43-109 8.08e-03

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: 33.38  E-value: 8.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759751494   43 GFMVGLMEWTCVRALTPHLEPGEGSLGTEIRVTHTAATPPGLTVTVTAELLSVEKRRIRWRVTAHDG 109
Cdd:pfam03061   7 GVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
 
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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