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Conserved domains on  [gi|1352184751|gb|AVI55767|]
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acyl-CoA thioesterase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10793444)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
1-132 1.37e-92

acyl-CoA thioester hydrolase YciA;


:

Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 263.26  E-value: 1.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   1 MSTTHNVPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80
Cdd:PRK10694    1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184751  81 VQKGTTSVSINIEVWVKKVASEPIGQRYKATEALFKYVAVDPEGKPRALPVE 132
Cdd:PRK10694   81 VKTGTTSISINIEVWVKKVASEPIGQRYKATEALFTYVAVDPEGKPRALPVG 132
 
Name Accession Description Interval E-value
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
1-132 1.37e-92

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 263.26  E-value: 1.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   1 MSTTHNVPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80
Cdd:PRK10694    1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184751  81 VQKGTTSVSINIEVWVKKVASEPIGQRYKATEALFKYVAVDPEGKPRALPVE 132
Cdd:PRK10694   81 VKTGTTSISINIEVWVKKVASEPIGQRYKATEALFTYVAVDPEGKPRALPVG 132
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-130 4.58e-57

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 173.83  E-value: 4.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   7 VPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTT 86
Cdd:COG1607     2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352184751  87 SVSINIEVWVKKVASepiGQRYKATEALFKYVAVDPEGKPRALP 130
Cdd:COG1607    82 SMEVGVEVWAEDLRT---GERRLVTEAYFTFVAVDEDGKPRPVP 122
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-130 1.54e-46

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 146.56  E-value: 1.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   7 VPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTT 86
Cdd:cd03442     3 MEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352184751  87 SVSINIEVWVKkvaSEPIGQRYKATEALFKYVAVDPEGKPRALP 130
Cdd:cd03442    83 SMEVGVEVEAE---DPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-98 5.23e-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: 67.67  E-value: 5.23e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184751  26 NGDIFGGWLMSQMDIGGAILAKEIAHG-RVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTTSVSINIEVWVKK 98
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
 
Name Accession Description Interval E-value
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
1-132 1.37e-92

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 263.26  E-value: 1.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   1 MSTTHNVPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80
Cdd:PRK10694    1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1352184751  81 VQKGTTSVSINIEVWVKKVASEPIGQRYKATEALFKYVAVDPEGKPRALPVE 132
Cdd:PRK10694   81 VKTGTTSISINIEVWVKKVASEPIGQRYKATEALFTYVAVDPEGKPRALPVG 132
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
7-130 4.58e-57

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 173.83  E-value: 4.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   7 VPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTT 86
Cdd:COG1607     2 LPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352184751  87 SVSINIEVWVKKVASepiGQRYKATEALFKYVAVDPEGKPRALP 130
Cdd:COG1607    82 SMEVGVEVWAEDLRT---GERRLVTEAYFTFVAVDEDGKPRPVP 122
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 7-130 1.54e-46

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 146.56  E-value: 1.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751   7 VPQGDLVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTT 86
Cdd:cd03442     3 MEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1352184751  87 SVSINIEVWVKkvaSEPIGQRYKATEALFKYVAVDPEGKPRALP 130
Cdd:cd03442    83 SMEVGVEVEAE---DPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-98 5.23e-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: 67.67  E-value: 5.23e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352184751  26 NGDIFGGWLMSQMDIGGAILAKEIAHG-RVVTVRVEGMTFLRPVAVGDVVCCYARCVQKGTTSVSINIEVWVKK 98
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 12-96 1.24e-10

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: 54.40  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751  12 LVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIA--HGRVVTVRVEgMTFLRPVAVGDVVCCYARCVQKGTTSVS 89
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGgrGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVT 79


                  ....*..
gi 1352184751  90 INIEVWV 96
Cdd:cd03440    80 VEVEVRN 86
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-95 1.31e-09

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.64  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751  16 TLAMPAD---TNANGDIFGGWLMSQMDI--GGAILAKEIAHGRVVTVRVEgMTFLRPVAVGDVVCCYARCVQKGTTSVSI 90
Cdd:COG2050    34 VLRLPVRpehLNPPGTVHGGALAALADSaaGLAANSALPPGRRAVTIELN-INFLRPARLGDRLTAEARVVRRGRRLAVV 112


                  ....*
gi 1352184751  91 NIEVW 95
Cdd:COG2050   113 EVEVT 117
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 16-95 9.61e-06

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 41.77  E-value: 9.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751  16 TLAMPAD---TNANGDIFGGWLMSQMDI--GGAILAKEIAHGRVVTVRVEgMTFLRPVAVGDVVCCyARCVQKGTTSVSI 90
Cdd:cd03443    15 VLRLPVRprhLNPGGIVHGGAIATLADTagGLAALSALPPGALAVTVDLN-VNYLRPARGGDLTAR-ARVVKLGRRLAVV 92


                  ....*
gi 1352184751  91 NIEVW 95
Cdd:cd03443    93 EVEVT 97
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 20-130 1.32e-05

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: 41.81  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751  20 PADTNANGDIFGGWLMSQMDIG--------GAILAKEIAHGRV-VTVRVEgMTFLRPVAVGDVVCCYARCVQKGTTSVSI 90
Cdd:COG0824    14 FGDTDAMGHVNNANYLRYFEEArteflralGLSYAELEEEGIGlVVVEAE-IDYLRPARYGDELTVETRVVRLGGSSLTF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1352184751  91 NIEVWvkkvaSEPIGQRykATEALFKYVAVDPE-GKPRALP 130
Cdd:COG0824    93 EYEIF-----RADDGEL--LATGETVLVFVDLEtGRPVPLP 126
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 20-121 8.45e-03

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: 33.73  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352184751  20 PADTNANGDIFGGWLMSQMD---------IGGAILAKEIAHGRVVTVRVEgMTFLRPVAVGDVVCCYARCVQKGTTSVSI 90
Cdd:cd00586     9 FGDTDAAGHVNNARYLRYFEeareeflreLGLGYDELEEQGLGLVVVELE-IDYLRPLRLGDRLTVETRVLRLGRKSFTF 87

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1352184751  91 NIEVWVKKvasepiGQRykATEALFKYVAVD 121
Cdd:cd00586    88 EQEIFRED------GEL--LATAETVLVCVD 110
 
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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