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Conserved domains on  [gi|15596185|ref|NP_249679|]
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hypothetical protein PA0988 [Pseudomonas aeruginosa PAO1]

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 4.25e-22

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: 84.95  E-value: 4.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   1 MPTPVFIKR-TVLFGDCDPEGIVYTPRFSYFVLEAVQEALGVWlgGPGLRTLLGFRILPPARAFSLEFLHPVTWDDELTM 79
Cdd:COG0824   1 MTLFTFETPiRVRFGDTDAMGHVNNANYLRYFEEARTEFLRAL--GLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596185  80 QVGVSNVGTHSFSFSVEG-RLSPDVVAFTASLTQVCVSPDTREVMEVPAQLRALLA 134
Cdd:COG0824  79 ETRVVRLGGSSLTFEYEIfRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-134 4.25e-22

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: 84.95  E-value: 4.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   1 MPTPVFIKR-TVLFGDCDPEGIVYTPRFSYFVLEAVQEALGVWlgGPGLRTLLGFRILPPARAFSLEFLHPVTWDDELTM 79
Cdd:COG0824   1 MTLFTFETPiRVRFGDTDAMGHVNNANYLRYFEEARTEFLRAL--GLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596185  80 QVGVSNVGTHSFSFSVEG-RLSPDVVAFTASLTQVCVSPDTREVMEVPAQLRALLA 134
Cdd:COG0824  79 ETRVVRLGGSSLTFEYEIfRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 7-116 3.05e-17

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: 71.48  E-value: 3.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   7 IKRTVLFGDCDPEGIVYTPRFSYFVLEAVQEALGVWlgGPGLRTLLGFRILPPARAFSLEFLHPVTWDDELTMQVGVSNV 86
Cdd:cd00586   3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLREL--GLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15596185  87 GTHSFSFSVEGRLSPDVVAFTASLTQVCVS 116
Cdd:cd00586  81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-133 9.80e-10

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: 52.34  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185    11 VLFGDCDPEGIVYTPRFsyfvLEAVQEALGVWLGGPGL--RTLLGFRILPPARAFSLEFLHPVTWDDELTMQVGVsnVGT 88
Cdd:pfam13279   1 VRPGDIDANGHMNNARY----LRYFEEARDRFLERLGLdlAYREALGIGLILAEAHVRYRRELKLGDELTVETRL--IDW 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15596185    89 HSFSFSVEGR-LSPDV-VAFTASLTQVCVSPDTREVMEVPAQLRALL 133
Cdd:pfam13279  75 DAKRFHLEHRfLSPDGkLVATAETRLVFVDYETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 8-119 1.85e-05

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: 41.25  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185     8 KRTVLFGDCDPEGIVYTPRFSYFVLEAVQEalgvwlggpGLRTLlGF--------RILPPARAFSLEFLHPVTWDDELTM 79
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTE---------FLRSL-GFpqsvlraeGVAFVVVNINIEYKKPARLDDVLEI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15596185    80 QVGVSNVGTHSFSFSVEGRLSPDVVAFTASLTQVCVSPDT 119
Cdd:TIGR00051  71 RTQIEELNGFSFVFSQEIFNEDEALLKAATVIVVCVDPKK 110
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-134 4.25e-22

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: 84.95  E-value: 4.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   1 MPTPVFIKR-TVLFGDCDPEGIVYTPRFSYFVLEAVQEALGVWlgGPGLRTLLGFRILPPARAFSLEFLHPVTWDDELTM 79
Cdd:COG0824   1 MTLFTFETPiRVRFGDTDAMGHVNNANYLRYFEEARTEFLRAL--GLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596185  80 QVGVSNVGTHSFSFSVEG-RLSPDVVAFTASLTQVCVSPDTREVMEVPAQLRALLA 134
Cdd:COG0824  79 ETRVVRLGGSSLTFEYEIfRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 7-116 3.05e-17

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: 71.48  E-value: 3.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   7 IKRTVLFGDCDPEGIVYTPRFSYFVLEAVQEALGVWlgGPGLRTLLGFRILPPARAFSLEFLHPVTWDDELTMQVGVSNV 86
Cdd:cd00586   3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLREL--GLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15596185  87 GTHSFSFSVEGRLSPDVVAFTASLTQVCVS 116
Cdd:cd00586  81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-133 9.80e-10

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: 52.34  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185    11 VLFGDCDPEGIVYTPRFsyfvLEAVQEALGVWLGGPGL--RTLLGFRILPPARAFSLEFLHPVTWDDELTMQVGVsnVGT 88
Cdd:pfam13279   1 VRPGDIDANGHMNNARY----LRYFEEARDRFLERLGLdlAYREALGIGLILAEAHVRYRRELKLGDELTVETRL--IDW 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15596185    89 HSFSFSVEGR-LSPDV-VAFTASLTQVCVSPDTREVMEVPAQLRALL 133
Cdd:pfam13279  75 DAKRFHLEHRfLSPDGkLVATAETRLVFVDYETRKPAPIPEELLEAL 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 5-113 4.62e-07

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: 45.16  E-value: 4.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185   5 VFIKRTVLFGDCDPEGIVytprFSYFVLEAVQEALGVWLGGPGLRtllgfRILPPARAFSLEFLHPVTWDDELTMQVGVS 84
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIV----HGGLLLALADEAAGAAAARLGGR-----GLGAVTLSLDVRFLRPVRPGDTLTVEAEVV 71

                        90       100
                ....*....|....*....|....*....
gi 15596185  85 NVGTHSFSFSVEGRLSPDVVAFTASLTQV 113
Cdd:cd03440  72 RVGRSSVTVEVEVRNEDGKLVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-105 1.42e-06

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: 43.40  E-value: 1.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596185    48 LRTLLGFRILPPARAFSLEFLHPVTWDDELTMQVGVSNVGTHSFSFSVEGRLSPDVVA 105
Cdd:pfam03061  21 ARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 8-119 1.85e-05

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: 41.25  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596185     8 KRTVLFGDCDPEGIVYTPRFSYFVLEAVQEalgvwlggpGLRTLlGF--------RILPPARAFSLEFLHPVTWDDELTM 79
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTE---------FLRSL-GFpqsvlraeGVAFVVVNINIEYKKPARLDDVLEI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15596185    80 QVGVSNVGTHSFSFSVEGRLSPDVVAFTASLTQVCVSPDT 119
Cdd:TIGR00051  71 RTQIEELNGFSFVFSQEIFNEDEALLKAATVIVVCVDPKK 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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