NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15600564|ref|NP_254058|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
9-131 3.50e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 151.49  E-value: 3.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   9 PIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600564  89 SSIRMLVEVWSDDPLSSEWRKVTEAVFVFVAIDGSGRTRPVPP 131
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
9-131 3.50e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 151.49  E-value: 3.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   9 PIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600564  89 SSIRMLVEVWSDDPLSSEWRKVTEAVFVFVAIDGSGRTRPVPP 131
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-130 5.27e-41

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: 132.69  E-value: 5.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   9 PIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600564  89 SSIRMLVEVWSDDPLSSEWRKVTEAVFVFVAIDGSGRTRPVP 130
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
4-131 1.58e-38

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 126.51  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564    4 LEQEDPIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQT 83
Cdd:PRK10694   1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600564   84 LEVGRSSIRMLVEVW----SDDPLSSEWRkVTEAVFVFVAIDGSGRTRPVPP 131
Cdd:PRK10694  81 VKTGTTSISINIEVWvkkvASEPIGQRYK-ATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-102 4.25e-14

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: 62.66  E-value: 4.25e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600564    29 FGDIYGGWLVSQMDLAGTAMASKIAGG-RIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGRSSIRMLVEVWSDDP 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
9-131 3.50e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 151.49  E-value: 3.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   9 PIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:COG1607   1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600564  89 SSIRMLVEVWSDDPLSSEWRKVTEAVFVFVAIDGSGRTRPVPP 131
Cdd:COG1607  81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPP 123
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-130 5.27e-41

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: 132.69  E-value: 5.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   9 PIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:cd03442   2 PMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15600564  89 SSIRMLVEVWSDDPLSSEWRKVTEAVFVFVAIDGSGRTRPVP 130
Cdd:cd03442  82 TSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
4-131 1.58e-38

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 126.51  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564    4 LEQEDPIPQGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMVPVAVGAQLSFYTQT 83
Cdd:PRK10694   1 MSTTHNVPQGELVLRTLAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARC 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15600564   84 LEVGRSSIRMLVEVW----SDDPLSSEWRkVTEAVFVFVAIDGSGRTRPVPP 131
Cdd:PRK10694  81 VKTGTTSISINIEVWvkkvASEPIGQRYK-ATEALFTYVAVDPEGKPRALPV 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 29-102 4.25e-14

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: 62.66  E-value: 4.25e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600564    29 FGDIYGGWLVSQMDLAGTAMASKIAGG-RIATVAIDRMAFMVPVAVGAQLSFYTQTLEVGRSSIRMLVEVWSDDP 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 17-118 2.24e-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: 53.63  E-value: 2.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564  17 LQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAID-RMAFMVPVAVGAQLSFYTQTLEVGRSSIRMLV 95
Cdd:cd03440   3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                        90       100
                ....*....|....*....|...
gi 15600564  96 EVWSDDPlssewRKVTEAVFVFV 118
Cdd:cd03440  83 EVRNEDG-----KLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 2-101 9.86e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 42.24  E-value: 9.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   2 IELEQEDPipqGDLALQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAID-RMAFMVPVAVGAQLSFY 80
Cdd:COG2050  23 IELVEVEP---GRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAE 99

                        90       100
                ....*....|....*....|.
gi 15600564  81 TQTLEVGRSSIRMLVEVWSDD 101
Cdd:COG2050 100 ARVVRRGRRLAVVEVEVTDED 120
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 17-131 5.46e-04

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: 37.57  E-value: 5.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564  17 LQITALPRETNGFGDIYGGWLVSQMDLAGTAM-------ASKIAGGRIATVAID-RMAFMVPVAVGAQLSFYTQTLEVGR 88
Cdd:COG0824   8 TPIRVRFGDTDAMGHVNNANYLRYFEEARTEFlralglsYAELEEEGIGLVVVEaEIDYLRPARYGDELTVETRVVRLGG 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600564  89 SSIRMLVEVWSDDplssEWRKVTEAVFVFVAID-GSGRTRPVPP 131
Cdd:COG0824  88 SSLTFEYEIFRAD----DGELLATGETVLVFVDlETGRPVPLPD 127
PLN02647 PLN02647
acyl-CoA thioesterase
 35-129 2.73e-03

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 36.31  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564   35 GWLVSQMD-LAGTaMASKIAGGR--------IATVAIDRMAFMVPVAVGAQLSFYTQTLEVGRSSIRMLVEV---WSDDP 102
Cdd:PLN02647 114 GKLLEDLDaLAGT-ISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEViqpTKDES 192

                         90       100
                 ....*....|....*....|....*...
gi 15600564  103 LSSEwRKVTEAVFVFVAIDG-SGRTRPV 129
Cdd:PLN02647 193 NTSD-SVALTANFTFVARDSkTGKSAPV 219
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 17-121 2.98e-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: 2.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600564  17 LQITALPRETNGFGDIYGGWLVSQMDLAGTAMASKIAGGRIATVAIDRMAFMV--------PVAVGAQLSFYTQTLEVGR 88
Cdd:cd00586   3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVeleidylrPLRLGDRLTVETRVLRLGR 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 15600564  89 SSIRMLVEVWSDDPlssewRKVTEAVFVFVAID 121
Cdd:cd00586  83 KSFTFEQEIFREDG-----ELLATAETVLVCVD 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH