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Conserved domains on  [gi|15598936|ref|NP_252430|]
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acyl-CoA thioesterase [Pseudomonas aeruginosa PAO1]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787832)

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
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
15-138 3.92e-56

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 171.90  E-value: 3.92e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  15 SETRVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLK 94
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598936  95 VEVEVYLESMYADGREKAIHGLFSFVAIDDEKRPVPVLPGFPAS 138
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPET 128
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
15-138 3.92e-56

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 171.90  E-value: 3.92e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  15 SETRVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLK 94
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598936  95 VEVEVYLESMYADGREKAIHGLFSFVAIDDEKRPVPVLPGFPAS 138
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPET 128
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 10-131 3.51e-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: 145.79  E-value: 3.51e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  10 RRTELSETRVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVG 89
Cdd:cd03442   1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15598936  90 NTSLKVEVEVYLESMYADGREKAIHGLFSFVAIDDEKRPVPV 131
Cdd:cd03442  81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 31-102 5.76e-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: 5.76e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598936    31 HNTLFGGTALAWMDEVSFITATRFCRLP-LVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVYLE 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
25-134 1.05e-14

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 66.03  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936   25 PPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVYLESM 104
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598936  105 YAD---GREKAIHGLFSFVAIDDEKRPVPVLPG 134
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRALPVG 132
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
15-138 3.92e-56

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 171.90  E-value: 3.92e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  15 SETRVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLK 94
Cdd:COG1607   5 SELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSME 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598936  95 VEVEVYLESMYADGREKAIHGLFSFVAIDDEKRPVPVLPGFPAS 138
Cdd:COG1607  85 VGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPET 128
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 10-131 3.51e-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: 145.79  E-value: 3.51e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  10 RRTELSETRVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVG 89
Cdd:cd03442   1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15598936  90 NTSLKVEVEVYLESMYADGREKAIHGLFSFVAIDDEKRPVPV 131
Cdd:cd03442  81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 31-102 5.76e-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: 5.76e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598936    31 HNTLFGGTALAWMDEVSFITATRFCRLP-LVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVYLE 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
25-134 1.05e-14

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 66.03  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936   25 PPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVYLESM 104
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598936  105 YAD---GREKAIHGLFSFVAIDDEKRPVPVLPG 134
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRALPVG 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 18-120 9.41e-12

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: 57.49  E-value: 9.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  18 RVTKAVFPPTTNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTD-RIDFNHPIPAGSIVELVGRVVKVGNTSLKVE 96
Cdd:cd03440   2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                        90       100
                ....*....|....*....|....
gi 15598936  97 VEVylesmYADGREKAIHGLFSFV 120
Cdd:cd03440  82 VEV-----RNEDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 9-100 2.96e-08

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 49.17  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936   9 LRRTELSETRVTkAVFPPT---TNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTD-RIDFNHPIPAGSIVELVGR 84
Cdd:COG2050  23 IELVEVEPGRAV-LRLPVRpehLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEAR 101

                        90
                ....*....|....*.
gi 15598936  85 VVKVGNTSLKVEVEVY 100
Cdd:COG2050 102 VVRRGRRLAVVEVEVT 117
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 9-102 9.79e-07

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: 44.47  E-value: 9.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936   9 LRRTELSETRVTkAVFPPT---TNHHNTLFGGTALAWMDEVSFITATRFCRLPLVTVSTD-RIDFNHPIPAGsIVELVGR 84
Cdd:cd03443   4 IRVVEVGPGRVV-LRLPVRprhLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGG-DLTARAR 81

                        90
                ....*....|....*...
gi 15598936  85 VVKVGNTSLKVEVEVYLE 102
Cdd:cd03443  82 VVKLGRRLAVVEVEVTDE 99
PLN02647 PLN02647
acyl-CoA thioesterase
 57-131 2.67e-04

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 39.39  E-value: 2.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598936   57 LPLVTVSTDRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVyLESMYADGREK---AIHGLFSFVAIDDE-KRPVPV 131
Cdd:PLN02647 142 LLLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEV-IQPTKDESNTSdsvALTANFTFVARDSKtGKSAPV 219
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 56-131 1.37e-03

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: 36.41  E-value: 1.37e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598936  56 RLPLVTVSTdRIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEVYLEsmyaDGREKAIHGLFSFVAID-DEKRPVPV 131
Cdd:COG0824  54 GIGLVVVEA-EIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRA----DDGELLATGETVLVFVDlETGRPVPL 125
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 29-123 3.71e-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: 34.89  E-value: 3.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598936  29 NHHN--TLFGGTALAWMDEVSFITATRFCR-LPLVTVSTDrIDFNHPIPAGSIVELVGRVVKVGNTSLKVEVEvylesMY 105
Cdd:cd00586  19 NNARylRYFEEAREEFLRELGLGYDELEEQgLGLVVVELE-IDYLRPLRLGDRLTVETRVLRLGRKSFTFEQE-----IF 92

                        90
                ....*....|....*...
gi 15598936 106 ADGREKAIHGLFSFVAID 123
Cdd:cd00586  93 REDGELLATAETVLVCVD 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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