NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|503910878|ref|WP_014144872|]
View 

MULTISPECIES: fluoroacetyl-CoA thioesterase [Streptomycetaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-136 6.14e-51

Predicted thioesterase [General function prediction only];


:

Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 6.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503910878   5 MRVGERFTHDFVVPPHKTVRHLYPESPEfaefpeVFATGFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGSGDVP------VLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503910878  85 TVTVTAELRSVEGRRLSWRVSAHDGVDEIGSGTHERAVIHLEKFNAKVRQKT 136
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKA 127
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-136 6.14e-51

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 6.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503910878   5 MRVGERFTHDFVVPPHKTVRHLYPESPEfaefpeVFATGFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGSGDVP------VLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503910878  85 TVTVTAELRSVEGRRLSWRVSAHDGVDEIGSGTHERAVIHLEKFNAKVRQKT 136
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKA 127
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-117 3.23e-04

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: 37.92  E-value: 3.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503910878  43 GFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGlTVTVTAELRSVEGRRLSWRVSAHDGVDEI---GSGT 117
Cdd:cd03443   34 GAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGKLvatARGT 110
 
Name Accession Description Interval E-value
COG5496 COG5496
Predicted thioesterase [General function prediction only];
5-136 6.14e-51

Predicted thioesterase [General function prediction only];


Pssm-ID: 444247  Cd Length: 129  Bit Score: 158.04  E-value: 6.14e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503910878   5 MRVGERFTHDFVVPPHKTVRHLYPESPEfaefpeVFATGFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGL 84
Cdd:COG5496    2 LKPGLTATFEFTVTEEDTAAALGSGDVP------VLATPAMIALMEWAAREALDPHLPEGETTVGTEVDVKHLAPTPVGM 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503910878  85 TVTVTAELRSVEGRRLSWRVSAHDGVDEIGSGTHERAVIHLEKFNAKVRQKT 136
Cdd:COG5496   76 TVTVTAELTEVDGRRLTFEVEAFDEAGLIGEGTHERFIVNKEKFMAKAAEKA 127
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 43-113 8.69e-05

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 39.93  E-value: 8.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503910878  43 GFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGLTVTVTAELRSVEGRRLSWRVSAHDGVDEI 113
Cdd:COG2050   53 GALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKL 123
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 43-117 3.23e-04

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: 37.92  E-value: 3.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503910878  43 GFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGlTVTVTAELRSVEGRRLSWRVSAHDGVDEI---GSGT 117
Cdd:cd03443   34 GAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDGKLvatARGT 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 43-113 6.01e-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: 33.99  E-value: 6.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503910878  43 GFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGLTVTVTAELRSVEGRRLSWRVSAHDGVDEI 113
Cdd:cd03440   21 GLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKL 91
 
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