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Conserved domains on  [gi|1678043302|dbj|BBK27366|]
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thioesterase [Staphylococcus arlettae]

Protein Classification

thioesterase family protein( domain architecture ID 10594194)

thioesterase family protein belonging to the Hotdog fold superfamily, similar to 1,4-dihydroxy-2-naphthoyl-CoA hydrolase, which catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) during the synthesis of menaquinones and phylloquinone (vitamin K1)

CATH:  3.10.129.10
Gene Ontology:  GO:0016790
PubMed:  15307895
SCOP:  3000149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-134 9.57e-35

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: 117.44  E-value: 9.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  14 VKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTKRIH 93
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1678043302  94 VFMNLYDEACNKCATYEVMLMGIATETTKPAPFPEEFKSAL 134
Cdd:pfam13279  81 LEHRFLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
 
Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-134 9.57e-35

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: 117.44  E-value: 9.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  14 VKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTKRIH 93
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1678043302  94 VFMNLYDEACNKCATYEVMLMGIATETTKPAPFPEEFKSAL 134
Cdd:pfam13279  81 LEHRFLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
PRK07531 PRK07531
carnitine 3-dehydrogenase;
11-158 1.06e-30

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 115.22  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  11 QTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTInELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTK 90
Cdd:PRK07531  349 ETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYV-AAGHSYYTVETHIRHLGEAKAGQALHVETQLLSGDEK 427

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678043302  91 RIHVFMNLYDEACNKCATYEVMLMGIATETTKPAPFPEEFKSALEAYATIATEDIKPRELGHKIEIKR 158
Cdd:PRK07531  428 RLHLFHTLYDAGGELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVGQRR 495
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 3-138 5.08e-28

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: 101.13  E-value: 5.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302   3 MTTKKFNYQTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEV 82
Cdd:COG0824     1 MTLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678043302  83 TVIDYDTKRIHVFMNLYDEACNK-CATYEVMLMGIATETTKPAPFPEEFKSALEAYA 138
Cdd:COG0824    81 RVVRLGGSSLTFEYEIFRADDGElLATGETVLVFVDLETGRPVPLPDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-116 7.62e-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: 81.88  E-value: 7.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302   8 FNYQTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDY 87
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                          90       100
                  ....*....|....*....|....*....
gi 1678043302  88 DTKRIHVFMNLYDEACNKCATYEVMLMGI 116
Cdd:cd00586    81 GRKSFTFEQEIFREDGELLATAETVLVCV 109
 
Name Accession Description Interval E-value
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-134 9.57e-35

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: 117.44  E-value: 9.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  14 VKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTKRIH 93
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1678043302  94 VFMNLYDEACNKCATYEVMLMGIATETTKPAPFPEEFKSAL 134
Cdd:pfam13279  81 LEHRFLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
PRK07531 PRK07531
carnitine 3-dehydrogenase;
11-158 1.06e-30

carnitine 3-dehydrogenase;


Pssm-ID: 236044 [Multi-domain]  Cd Length: 495  Bit Score: 115.22  E-value: 1.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  11 QTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTInELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTK 90
Cdd:PRK07531  349 ETKVPPAWVDYNGHMTEHRYLQVFGDTTDALLRLIGVDAAYV-AAGHSYYTVETHIRHLGEAKAGQALHVETQLLSGDEK 427

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678043302  91 RIHVFMNLYDEACNKCATYEVMLMGIATETTKPAPFPEEFKSALEAYATIATEDIKPRELGHKIEIKR 158
Cdd:PRK07531  428 RLHLFHTLYDAGGELIATAEHMLLHVDLKAGKAVPAPAAVLAALKPIAEAHAELPLPEGAGRHVGQRR 495
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 3-138 5.08e-28

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: 101.13  E-value: 5.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302   3 MTTKKFNYQTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEV 82
Cdd:COG0824     1 MTLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678043302  83 TVIDYDTKRIHVFMNLYDEACNK-CATYEVMLMGIATETTKPAPFPEEFKSALEAYA 138
Cdd:COG0824    81 RVVRLGGSSLTFEYEIFRADDGElLATGETVLVFVDLETGRPVPLPDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-116 7.62e-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: 81.88  E-value: 7.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302   8 FNYQTVVKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNEQTINELKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDY 87
Cdd:cd00586     1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                          90       100
                  ....*....|....*....|....*....
gi 1678043302  88 DTKRIHVFMNLYDEACNKCATYEVMLMGI 116
Cdd:cd00586    81 GRKSFTFEQEIFREDGELLATAETVLVCV 109
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 14-114 5.03e-08

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: 48.24  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678043302  14 VKPEWVDHNNHMNDAEYNRVFSDATDAWLAQLGLNeqtinelKYTIFTLENHVLYLKEIKVNQRIQCEVTVIDYDTKRIH 93
Cdd:cd03440     7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGR-------GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1678043302  94 VFMNLYDEACNKCATYEVMLM 114
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 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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