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Conserved domains on  [gi|1799464207|gb|QHL91953|]
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acyl-CoA thioesterase [Sphingomonas changnyeongensis]

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];
1-108 3.68e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 168.05  E-value: 3.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:COG1607    14 MPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAED 93

                          90       100
                  ....*....|....*....|....*...
gi 1799464207  81 RHGEQLCKVTEARFVFVAIDEARRPRAI 108
Cdd:COG1607    94 LRTGERRLVTEAYFTFVAVDEDGKPRPV 121
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
1-108 3.68e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 168.05  E-value: 3.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:COG1607    14 MPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAED 93

                          90       100
                  ....*....|....*....|....*...
gi 1799464207  81 RHGEQLCKVTEARFVFVAIDEARRPRAI 108
Cdd:COG1607    94 LRTGERRLVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-108 1.23e-47

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: 148.49  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:cd03442    15 LPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVGVEVEAED 94

                          90       100
                  ....*....|....*....|....*...
gi 1799464207  81 RHGEQLCKVTEARFVFVAIDEARRPRAI 108
Cdd:cd03442    95 PLTGERRLVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
1-111 2.21e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 122.66  E-value: 2.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:PRK10694   19 MPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKK 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1799464207  81 RHGE---QLCKVTEARFVFVAIDEARRPRAISAG 111
Cdd:PRK10694   99 VASEpigQRYKATEALFTYVAVDPEGKPRALPVG 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 8-82 3.62e-18

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: 72.29  E-value: 3.62e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799464207   8 YGDIFGGWLMSQMDMAAGLVAARHAKG-RAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRDRH 82
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
1-108 3.68e-55

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 168.05  E-value: 3.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:COG1607    14 MPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVGVEVWAED 93

                          90       100
                  ....*....|....*....|....*...
gi 1799464207  81 RHGEQLCKVTEARFVFVAIDEARRPRAI 108
Cdd:COG1607    94 LRTGERRLVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 1-108 1.23e-47

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: 148.49  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:cd03442    15 LPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVGVEVEAED 94

                          90       100
                  ....*....|....*....|....*...
gi 1799464207  81 RHGEQLCKVTEARFVFVAIDEARRPRAI 108
Cdd:cd03442    95 PLTGERRLVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
1-111 2.21e-37

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 122.66  E-value: 2.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   1 MPADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRD 80
Cdd:PRK10694   19 MPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKK 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1799464207  81 RHGE---QLCKVTEARFVFVAIDEARRPRAISAG 111
Cdd:PRK10694   99 VASEpigQRYKATEALFTYVAVDPEGKPRALPVG 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 8-82 3.62e-18

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: 72.29  E-value: 3.62e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1799464207   8 YGDIFGGWLMSQMDMAAGLVAARHAKG-RAVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTIEVESWCRDRH 82
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 2-97 1.31e-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: 58.64  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   2 PADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDA-MQFHRPVVVGDEVSVYARLVRVGRTSMTIEVEswCRD 80
Cdd:cd03440     9 PEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLdVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVE--VRN 86

                          90
                  ....*....|....*..
gi 1799464207  81 RHGEqlcKVTEARFVFV 97
Cdd:cd03440    87 EDGK---LVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 6-90 2.77e-12

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 58.80  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   6 NPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDA-MQFHRPVVVGDEVSVYARLVRVGRTSMTIEVEswCRDRHGE 84
Cdd:COG2050    45 NPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELnINFLRPARLGDRLTAEARVVRRGRRLAVVEVE--VTDEDGK 122


                  ....*.
gi 1799464207  85 QLCKVT 90
Cdd:COG2050   123 LVATAT 128
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 23-110 5.99e-09

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: 50.28  E-value: 5.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207  23 AAGLVAARHAKGRAVTIAVDA-MQFHRPVVVGDEVSVYARLVRVGRTSMTIEVEswCRDRHGEQLCkvTEARFVFVAID- 100
Cdd:COG0824    42 ALGLSYAELEEEGIGLVVVEAeIDYLRPARYGDELTVETRVVRLGGSSLTFEYE--IFRADDGELL--ATGETVLVFVDl 117

                          90
                  ....*....|
gi 1799464207 101 EARRPRAISA 110
Cdd:COG0824   118 ETGRPVPLPD 127
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 6-90 4.05e-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: 44.86  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   6 NPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVD-AMQFHRPVVVGDeVSVYARLVRVGRTSMTIEVEswCRDRHGE 84
Cdd:cd03443    26 NPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGD-LTARARVVKLGRRLAVVEVE--VTDEDGK 102


                  ....*.
gi 1799464207  85 QLCKVT 90
Cdd:cd03443   103 LVATAR 108
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-90 7.68e-07

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 44.49  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   3 ADANPYGDIF--GGWLMSqmdMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARL--VRVGRTSMTIEVESWC 78
Cdd:COG2030    43 AAATGFGGRIahGMLTLS---LASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVleKRESKSRGIVTLRTTV 119

                          90
                  ....*....|..
gi 1799464207  79 RDRHGEQLCKVT 90
Cdd:COG2030   120 TNQDGEVVLTGE 131
PLN02647 PLN02647
acyl-CoA thioesterase
 6-100 2.84e-06

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 44.39  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   6 NPYGDIFGGWLMSQMDMAAGLVAARHAKGR--------AVTIAVDAMQFHRPVVVGDEVSVYARLVRVGRTSMTI--EVE 75
Cdd:PLN02647  106 NPWNEVRIGKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIqlEVI 185

                          90       100
                  ....*....|....*....|....*
gi 1799464207  76 SWCRDRHGEQLCKVTEARFVFVAID 100
Cdd:PLN02647  186 QPTKDESNTSDSVALTANFTFVARD 210
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 23-100 4.74e-06

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: 41.82  E-value: 4.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799464207  23 AAGLVAARHAKGRAVTIAVDA-MQFHRPVVVGDEVSVYARLVRVGRTSMTIEVEswCRDRHGEQLCkvtEARFVFVAID 100
Cdd:cd00586    37 ELGLGYDELEEQGLGLVVVELeIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQE--IFREDGELLA---TAETVLVCVD 110
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 3-91 2.35e-03

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 34.93  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799464207   3 ADANPYGDIF--GGWLMSqmdMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGDEVSVYARLV--RVGRTSMTIEVESWC 78
Cdd:cd03441    35 AKAAGFGGRIahGMLTLS---LASGLLVQWLPGTDGANLGSQSVRFLAPVFPGDTLRVEVEVLgkRPSKGRGVVTVRTEA 111

                          90
                  ....*....|...
gi 1799464207  79 RDRHGEQLCKVTE 91
Cdd:cd03441   112 RNQGGEVVLSGEA 124
PLN02647 PLN02647
acyl-CoA thioesterase
 2-54 4.32e-03

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 35.15  E-value: 4.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1799464207   2 PADANPYGDIFGGWLMSQMDMAAGLVAARHAKGRAVTIAVDAMQFHRPVVVGD 54
Cdd:PLN02647  299 PQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGD 351
 
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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