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Conserved domains on  [gi|1234899280|gb|ASU78676|]
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hypothetical protein CDG81_10750 [Actinopolyspora erythraea]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10002786)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016787
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-143 4.59e-15

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: 67.23  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280   1 MS-TTFDIEHTVTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRL 79
Cdd:COG0824     1 MTlFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234899280  80 SIptVYFNLATLRFAYHLLAPDDTDpLIARGEQQVACVRRDGNEnvPAGWPREVLRAAEELGGD 143
Cdd:COG0824    81 RV--VRLGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGR--PVPLPDELRAALEALLAA 139
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-143 4.59e-15

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: 67.23  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280   1 MS-TTFDIEHTVTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRL 79
Cdd:COG0824     1 MTlFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234899280  80 SIptVYFNLATLRFAYHLLAPDDTDpLIARGEQQVACVRRDGNEnvPAGWPREVLRAAEELGGD 143
Cdd:COG0824    81 RV--VRLGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGR--PVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 5-117 5.19e-12

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: 58.77  E-value: 5.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280   5 FDIEHTVTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRLSIptV 84
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRV--L 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1234899280  85 YFNLATLRFAYHLLAPDDTdpLIARGEQQVACV 117
Cdd:cd00586    79 RLGRKSFTFEQEIFREDGE--LLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-136 1.98e-07

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: 46.95  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280  11 VTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRLSIptVYFNLAT 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRL--IDWDAKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1234899280  91 LRFAYHLLAPDDTdpLIARGEQQVACVRRDGNENVPagWPREVLRA 136
Cdd:pfam13279  79 FHLEHRFLSPDGK--LVATAETRLVFVDYETRKPAP--IPEELLEA 120
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-143 4.59e-15

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: 67.23  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280   1 MS-TTFDIEHTVTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRL 79
Cdd:COG0824     1 MTlFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1234899280  80 SIptVYFNLATLRFAYHLLAPDDTDpLIARGEQQVACVRRDGNEnvPAGWPREVLRAAEELGGD 143
Cdd:COG0824    81 RV--VRLGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGR--PVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 5-117 5.19e-12

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: 58.77  E-value: 5.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280   5 FDIEHTVTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRLSIptV 84
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRV--L 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1234899280  85 YFNLATLRFAYHLLAPDDTdpLIARGEQQVACV 117
Cdd:cd00586    79 RLGRKSFTFEQEIFREDGE--LLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-136 1.98e-07

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: 46.95  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1234899280  11 VTADDTDYAGNVFFADFLKWQGHSRDRFLMRYAPAFLEELNSARTVVTIRCQCEYLLGITVADAVSIRLSIptVYFNLAT 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRL--IDWDAKR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1234899280  91 LRFAYHLLAPDDTdpLIARGEQQVACVRRDGNENVPagWPREVLRA 136
Cdd:pfam13279  79 FHLEHRFLSPDGK--LVATAETRLVFVDYETRKPAP--IPEELLEA 120
 
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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