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Conserved domains on  [gi|489187175|ref|WP_003096582|]
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MULTISPECIES: thioesterase family protein [Pseudomonadota]

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 ...
 9-144 1.51e-43

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: 140.42  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   9 NYTFFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPaDLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTR 88
Cdd:COG0824    3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYA-ELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489187175  89 VARLGRSSLVFELGIWR--DEQLLTVGELVYVYADANERQSQPVPDWLREKIRAFERQ 144
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRadDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 9-144 1.51e-43

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: 140.42  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   9 NYTFFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPaDLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTR 88
Cdd:COG0824    3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYA-ELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489187175  89 VARLGRSSLVFELGIWR--DEQLLTVGELVYVYADANERQSQPVPDWLREKIRAFERQ 144
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRadDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 12-121 1.73e-30

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: 106.15  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175  12 FFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYpADLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTRVAR 91
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGY-DELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489187175  92 LGRSSLVFELGIWR-DEQLLTVGELVYVYAD 121
Cdd:cd00586   80 LGRKSFTFEQEIFReDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 16-118 1.14e-28

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 101.73  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   16 LRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYpADLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTRVARLGRS 95
Cdd:TIGR00051   2 VRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQ-SVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100
                  ....*....|....*....|...
gi 489187175   96 SLVFELGIWRDEQLLTVGELVYV 118
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIV 103
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-110 1.36e-16

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: 69.59  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   26 QGIVFNGNYLTYLDVATTEYYRQLGMSYpadllrggGDLFAVKSTLEYRAPAHFDDWLDIGTRVARLGRSSLVFELGIWR 105
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ--------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72


                  ....*
gi 489187175  106 DEQLL 110
Cdd:pfam03061  73 EDGRL 77
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 16-131 7.44e-09

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 50.90  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175  16 LRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPAdlLRGGGDLFAVKS-TLEYRAPAHFDDWLDIGTRVARLGR 94
Cdd:PRK10800   7 VRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQA--LLAERVAFVVRKmTVEYYAPARLDDMLEVQSEITSMRG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489187175  95 SSLVFELGIWRDE-QLLTVGELVYVYADANERQSQPVP 131
Cdd:PRK10800  85 TSLTFTQRIVNAEgTLLNEAEVLIVCVDPLKMKPRALP 122
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 9-144 1.51e-43

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: 140.42  E-value: 1.51e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   9 NYTFFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPaDLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTR 88
Cdd:COG0824    3 LFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYA-ELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489187175  89 VARLGRSSLVFELGIWR--DEQLLTVGELVYVYADANERQSQPVPDWLREKIRAFERQ 144
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRadDGELLATGETVLVFVDLETGRPVPLPDELRAALEALLAA 139
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 12-121 1.73e-30

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: 106.15  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175  12 FFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYpADLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTRVAR 91
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGY-DELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489187175  92 LGRSSLVFELGIWR-DEQLLTVGELVYVYAD 121
Cdd:cd00586   80 LGRKSFTFEQEIFReDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 16-118 1.14e-28

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 101.73  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   16 LRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYpADLLRGGGDLFAVKSTLEYRAPAHFDDWLDIGTRVARLGRS 95
Cdd:TIGR00051   2 VRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQ-SVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100
                  ....*....|....*....|...
gi 489187175   96 SLVFELGIWRDEQLLTVGELVYV 118
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIV 103
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-110 1.36e-16

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: 69.59  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   26 QGIVFNGNYLTYLDVATTEYYRQLGMSYpadllrggGDLFAVKSTLEYRAPAHFDDWLDIGTRVARLGRSSLVFELGIWR 105
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ--------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRD 72


                  ....*
gi 489187175  106 DEQLL 110
Cdd:pfam03061  73 EDGRL 77
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 18-138 2.03e-16

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: 70.45  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175   18 VRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPADLLRGGGdLFAVKSTLEYRAPAHFDDWLDIGTRVARLGRSSL 97
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIG-LILAEAHVRYRRELKLGDELTVETRLIDWDAKRF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489187175   98 VFELGIWR-DEQLLTVGELVYVYADANERQSQPVPDWLREKI 138
Cdd:pfam13279  80 HLEHRFLSpDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 12-118 1.01e-14

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: 65.57  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175  12 FFHSLRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMsypadllrGGGDLFAVKSTLEYRAPAHFDDWLDIGTRVAR 91
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG--------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVR 72

                         90       100
                 ....*....|....*....|....*...
gi 489187175  92 LGRSSLVFELGIWR-DEQLLTVGELVYV 118
Cdd:cd03440   73 VGRSSVTVEVEVRNeDGKLVATATATFV 100
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 16-131 7.44e-09

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 50.90  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187175  16 LRVRWAEVDPQGIVFNGNYLTYLDVATTEYYRQLGMSYPAdlLRGGGDLFAVKS-TLEYRAPAHFDDWLDIGTRVARLGR 94
Cdd:PRK10800   7 VRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQA--LLAERVAFVVRKmTVEYYAPARLDDMLEVQSEITSMRG 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489187175  95 SSLVFELGIWRDE-QLLTVGELVYVYADANERQSQPVP 131
Cdd:PRK10800  85 TSLTFTQRIVNAEgTLLNEAEVLIVCVDPLKMKPRALP 122
 
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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