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Conserved domains on  [gi|815713647|ref|WP_046446120|]
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thioesterase family protein [Sutterella wadsworthensis]

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 ...
1-134 2.13e-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: 94.58  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   1 MTDQRriYQEVFTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTI 80
Cdd:COG0824    1 MTLFT--FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815713647  81 TTWVQSLRGpASLR-RYVMQRE--GMPVMAGATEWVFIDLARRRPAFLDPDIEATFT 134
Cdd:COG0824   79 ETRVVRLGG-SSLTfEYEIFRAddGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-134 2.13e-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: 94.58  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   1 MTDQRriYQEVFTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTI 80
Cdd:COG0824    1 MTLFT--FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815713647  81 TTWVQSLRGpASLR-RYVMQRE--GMPVMAGATEWVFIDLARRRPAFLDPDIEATFT 134
Cdd:COG0824   79 ETRVVRLGG-SSLTfEYEIFRAddGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
12-116 4.21e-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: 84.97  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647  12 FTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLrGPA 91
Cdd:cd00586    5 IRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL-GRK 83
                         90       100
                 ....*....|....*....|....*..
gi 815713647  92 SLRRY--VMQREGMPVMAGATEWVFID 116
Cdd:cd00586   84 SFTFEqeIFREDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
14-123 3.05e-13

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: 62.44  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   14 VADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRGPASL 93
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFV 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 815713647   94 RRYVMQRE-GMPVMAGATEWVFIDLARRRPA 123
Cdd:TIGR00051  84 FSQEIFNEdEALLKAATVIVVCVDPKKQKPV 114
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
19-129 1.05e-09

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: 53.11  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   19 IDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRGPaslRRYVM 98
Cdd:pfam13279   6 IDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAK---RFHLE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 815713647   99 QR----EGMPVMAGATEWVFIDLARRRPAFLDPDI 129
Cdd:pfam13279  83 HRflspDGKLVATAETRLVFVDYETRKPAPIPEEL 117
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
1-134 2.13e-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: 94.58  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   1 MTDQRriYQEVFTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTI 80
Cdd:COG0824    1 MTLFT--FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815713647  81 TTWVQSLRGpASLR-RYVMQRE--GMPVMAGATEWVFIDLARRRPAFLDPDIEATFT 134
Cdd:COG0824   79 ETRVVRLGG-SSLTfEYEIFRAddGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
12-116 4.21e-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: 84.97  E-value: 4.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647  12 FTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLrGPA 91
Cdd:cd00586    5 IRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL-GRK 83
                         90       100
                 ....*....|....*....|....*..
gi 815713647  92 SLRRY--VMQREGMPVMAGATEWVFID 116
Cdd:cd00586   84 SFTFEqeIFREDGELLATAETVLVCVD 110
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
8-135 3.23e-21

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 86.16  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   8 YQEVFTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSL 87
Cdd:COG3884    1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSGY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 815713647  88 RGPASLRRYVMQ-REGMPVMAGATEWVFIDLARRRPAFLDPDIEATFTL 135
Cdd:COG3884   81 NRFFAYRDFRILdEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGL 129
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
14-123 3.05e-13

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: 62.44  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   14 VADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRGPASL 93
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFV 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 815713647   94 RRYVMQRE-GMPVMAGATEWVFIDLARRRPA 123
Cdd:TIGR00051  84 FSQEIFNEdEALLKAATVIVVCVDPKKQKPV 114
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
19-129 1.05e-09

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: 53.11  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   19 IDVQGHVNNREYLRWMEGVATRHAALLGWDFETLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRGPaslRRYVM 98
Cdd:pfam13279   6 IDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAK---RFHLE 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 815713647   99 QR----EGMPVMAGATEWVFIDLARRRPAFLDPDI 129
Cdd:pfam13279  83 HRflspDGKLVATAETRLVFVDYETRKPAPIPEEL 117
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
12-113 3.88e-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: 48.63  E-value: 3.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647  12 FTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWdfetlkaRNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRGPA 91
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS 77
                         90       100
                 ....*....|....*....|...
gi 815713647  92 SLRRYVM-QREGMPVMAGATEWV 113
Cdd:cd03440   78 VTVEVEVrNEDGKLVATATATFV 100
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
8-133 5.12e-08

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 50.43  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647    8 YQEVFTVADASIDVQGHVNNREYLRWMEGVATRHAALLGWDFE-TLKARNRSWVAREHWIEYLQPCFAGDELTITTWVQS 86
Cdd:pfam01643   4 FKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLSDDgFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETWASS 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 815713647   87 LRGPASLRRY-VMQREGMPVMAGATEWVFIDLARRRPAFLDPDIEATF 133
Cdd:pfam01643  84 YNKFFCYRRFrVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPY 131
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
12-112 4.66e-05

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 41.86  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647  12 FTVADASIDVQGHVNNREYLRWMEGVatrhaallgWDFETLKARNRSWVArehwIEYLQPCFAGDELTITTWVQSlrGPA 91
Cdd:COG3884  154 FTVRYSDIDTNGHVNNARYLEWALDA---------LPLEFLKNHRLKRLE----INYLKEVRLGDTVEVRSARDE--DGR 218
                         90       100
                 ....*....|....*....|.
gi 815713647  92 SLRRYVMQREGMPVMAGATEW 112
Cdd:COG3884  219 TLHRIVGDDDGKELARARIEW 239
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
22-89 2.81e-04

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: 37.62  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815713647   22 QGHVNNREYLRWMEGVATRHAALLGwdfetlkARNRSWVAREHWIEYLQPCFAGDELTITTWVQSLRG 89
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG-------GSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGR 61
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
12-112 3.68e-03

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 36.56  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815713647   12 FTVADASIDVQGHVNNREYLRWMEGVATRHAALlgwDFETLKARnrswvarehwIEYLQPCFAGDELTITTWVQSLRGPA 91
Cdd:pfam01643 159 YHVRYSDIDMNQHVNNVKYLEWILEVLPLDFLD---THEPKKIT----------LKYEKEVQYGDDIEIITESAGSEEGL 225
                          90       100
                  ....*....|....*....|.
gi 815713647   92 SLRRYVMQREGMPVMAGATEW 112
Cdd:pfam01643 226 KTLHEIRNSTGEEIAQARTDW 246
 
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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