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Conserved domains on  [gi|2221513321|gb|UOP12637|]
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thioesterase family protein [Pseudomonas palleroniana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK07531 super family cl35593
carnitine 3-dehydrogenase;
4-155 4.02e-45

carnitine 3-dehydrogenase;


The actual alignment was detected with superfamily member PRK07531:

Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 154.13  E-value: 4.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   4 LTTYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREAsGHSLFTLELHLNYLHEVKLGAQVQVHTQLIA 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYVAA-GHSYYTVETHIRHLGEAKAGQALHVETQLLS 423
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221513321  84 HDAKRLHLYHSLHGVGDaKELAGNEQMLLHVDLAGPSATPFTEATLEKLAAILAEQADLPRPALLGRVIGLP 155
Cdd:PRK07531  424 GDEKRLHLFHTLYDAGG-ELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVGQR 494
 
Name Accession Description Interval E-value
PRK07531 PRK07531
carnitine 3-dehydrogenase;
4-155 4.02e-45

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 154.13  E-value: 4.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   4 LTTYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREAsGHSLFTLELHLNYLHEVKLGAQVQVHTQLIA 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYVAA-GHSYYTVETHIRHLGEAKAGQALHVETQLLS 423
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221513321  84 HDAKRLHLYHSLHGVGDaKELAGNEQMLLHVDLAGPSATPFTEATLEKLAAILAEQADLPRPALLGRVIGLP 155
Cdd:PRK07531  424 GDEKRLHLFHTLYDAGG-ELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVGQR 494
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
11-132 3.05e-27

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: 98.57  E-value: 3.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321  11 VHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHTQLIAHDAKRLH 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221513321  91 LYHSLHgVGDAKELAGNEQMLLHVDLAGPSATPFTEATLEKL 132
Cdd:pfam13279  81 LEHRFL-SPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-138 3.33e-25

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: 93.81  E-value: 3.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   1 MPALT-TYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHT 79
Cdd:COG0824     1 MTLFTfETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2221513321  80 QLIAHDAKRLHLYHSLHGVGDAKELAGNEQMLLHVDLAGPSATPFTEATLEKLAAILAE 138
Cdd:COG0824    81 RVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
6-115 2.48e-21

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: 83.04  E-value: 2.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   6 TYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHTQLIAHD 85
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221513321  86 AKRLHLYHSLHgVGDAKELAGNEQMLLHVD 115
Cdd:cd00586    82 RKSFTFEQEIF-REDGELLATAETVLVCVD 110
 
Name Accession Description Interval E-value
PRK07531 PRK07531
carnitine 3-dehydrogenase;
4-155 4.02e-45

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 154.13  E-value: 4.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   4 LTTYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREAsGHSLFTLELHLNYLHEVKLGAQVQVHTQLIA 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYVAA-GHSYYTVETHIRHLGEAKAGQALHVETQLLS 423
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2221513321  84 HDAKRLHLYHSLHGVGDaKELAGNEQMLLHVDLAGPSATPFTEATLEKLAAILAEQADLPRPALLGRVIGLP 155
Cdd:PRK07531  424 GDEKRLHLFHTLYDAGG-ELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVGQR 494
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
11-132 3.05e-27

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: 98.57  E-value: 3.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321  11 VHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHTQLIAHDAKRLH 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2221513321  91 LYHSLHgVGDAKELAGNEQMLLHVDLAGPSATPFTEATLEKL 132
Cdd:pfam13279  81 LEHRFL-SPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-138 3.33e-25

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: 93.81  E-value: 3.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   1 MPALT-TYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHT 79
Cdd:COG0824     1 MTLFTfETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2221513321  80 QLIAHDAKRLHLYHSLHGVGDAKELAGNEQMLLHVDLAGPSATPFTEATLEKLAAILAE 138
Cdd:COG0824    81 RVVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
6-115 2.48e-21

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: 83.04  E-value: 2.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   6 TYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLTCENREASGHSLFTLELHLNYLHEVKLGAQVQVHTQLIAHD 85
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2221513321  86 AKRLHLYHSLHgVGDAKELAGNEQMLLHVD 115
Cdd:cd00586    82 RKSFTFEQEIF-REDGELLATAETVLVCVD 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
6-112 1.83e-05

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: 41.31  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2221513321   6 TYTTQVHPDWVDYNGHLRDAFYLLIFSYATDALMDTLGLtcenreaSGHSLFTLELHLNYLHEVKLGAQVQVHTQLIAHD 85
Cdd:cd03440     2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVG 74
                          90       100
                  ....*....|....*....|....*..
gi 2221513321  86 AKRLHLYHSLHgVGDAKELAGNEQMLL 112
Cdd:cd03440    75 RSSVTVEVEVR-NEDGKLVATATATFV 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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