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Conserved domains on  [gi|2063634997|gb|QXI48157|]
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thioesterase family protein [Pseudomonas anuradhapurensis]

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;
4-153 2.10e-44

carnitine 3-dehydrogenase;


The actual alignment was detected with superfamily member PRK07531:

Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 152.20  E-value: 2.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   4 LITYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRgQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIG 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYV-AAGHSYYTVETHIRHLGEAKAGQALHVETQLLS 423

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997  84 FDRKRLHVYHSLHRAGvDEALAASEQMLLHVDLAGPKSAPFSERSVGLLQGLVDQQQDLPAAEYLGRVMG 153
Cdd:PRK07531  424 GDEKRLHLFHTLYDAG-GELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVG 492
 
Name Accession Description Interval E-value
PRK07531 PRK07531
carnitine 3-dehydrogenase;
4-153 2.10e-44

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 152.20  E-value: 2.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   4 LITYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRgQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIG 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYV-AAGHSYYTVETHIRHLGEAKAGQALHVETQLLS 423

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997  84 FDRKRLHVYHSLHRAGvDEALAASEQMLLHVDLAGPKSAPFSERSVGLLQGLVDQQQDLPAAEYLGRVMG 153
Cdd:PRK07531  424 GDEKRLHLFHTLYDAG-GELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVG 492
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-126 5.61e-29

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: 102.80  E-value: 5.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997  11 VQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFDRKRLH 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2063634997  91 VYHSLHRAgvDEALAAS-EQMLLHVDLAGPKSAPFSE 126
Cdd:pfam13279  81 LEHRFLSP--DGKLVATaETRLVFVDYETRKPAPIPE 115
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-126 3.32e-24

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: 91.11  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   6 TYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFD 85
Cdd:COG0824     7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2063634997  86 RKRLHVYHSLHRAGVDEALAASEQMLLHVDLAGPKSAPFSE 126
Cdd:COG0824    87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPD 127
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-115 1.01e-22

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: 86.51  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   6 TYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFD 85
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2063634997  86 RKRLHVYHSLHRAGvDEALAASEQMLLHVD 115
Cdd:cd00586    82 RKSFTFEQEIFRED-GELLATAETVLVCVD 110
 
Name Accession Description Interval E-value
PRK07531 PRK07531
carnitine 3-dehydrogenase;
4-153 2.10e-44

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 152.20  E-value: 2.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   4 LITYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRgQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIG 83
Cdd:PRK07531  345 LRLVETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYV-AAGHSYYTVETHIRHLGEAKAGQALHVETQLLS 423

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997  84 FDRKRLHVYHSLHRAGvDEALAASEQMLLHVDLAGPKSAPFSERSVGLLQGLVDQQQDLPAAEYLGRVMG 153
Cdd:PRK07531  424 GDEKRLHLFHTLYDAG-GELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVG 492
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-126 5.61e-29

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: 102.80  E-value: 5.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997  11 VQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFDRKRLH 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2063634997  91 VYHSLHRAgvDEALAAS-EQMLLHVDLAGPKSAPFSE 126
Cdd:pfam13279  81 LEHRFLSP--DGKLVATaETRLVFVDYETRKPAPIPE 115
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-126 3.32e-24

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: 91.11  E-value: 3.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   6 TYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFD 85
Cdd:COG0824     7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2063634997  86 RKRLHVYHSLHRAGVDEALAASEQMLLHVDLAGPKSAPFSE 126
Cdd:COG0824    87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPD 127
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-115 1.01e-22

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: 86.51  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   6 TYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDADSRGQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFD 85
Cdd:cd00586     2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2063634997  86 RKRLHVYHSLHRAGvDEALAASEQMLLHVD 115
Cdd:cd00586    82 RKSFTFEQEIFRED-GELLATAETVLVCVD 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 5-112 3.35e-07

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: 45.93  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2063634997   5 ITYRTPVQEDWVDYNGHLRDAFYLLIFSYATDALMERIGLDadsrgqsGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGF 84
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGR-------GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV 73

                          90       100
                  ....*....|....*....|....*...
gi 2063634997  85 DRKRLHVYHSLHRAGvDEALAASEQMLL 112
Cdd:cd03440    74 GRSSVTVEVEVRNED-GKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 37-103 1.35e-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: 35.69  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2063634997  37 ALMERIGLDADSR-GQSGNSLFTLEAHINYLHEVKLGSEVWVQTQIIGFDRKRLHVYHSLHRAGVDEA 103
Cdd:pfam03061  11 ALADEAAGAAARRlGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
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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