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Conserved domains on  [gi|15596790|ref|NP_250284|]
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hypothetical protein PA1593 [Pseudomonas aeruginosa PAO1]

Protein Classification

PaaI family thioesterase( domain architecture ID 10005230)

PaaI family thioesterase is a hotdog fold thioesterase similar to Escherichia coli PaaI, a thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016836|GO:0047617
PubMed:  15307895|16061252
TCDB:  9.B.371

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
1-141 1.59e-30

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.34  E-value: 1.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790   1 MSENplLERARRFLSALRHCQVLGLTVEAADEKGLTLRLPYSQAIIGNPesGVVHGGAITTLMDTTCGISTVCVLPDFEI 80
Cdd:COG2050   1 MSDP--LERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRR 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596790  81 CPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDpGQPIAHVVGAFMRMGG 141
Cdd:COG2050  77 AVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDED-GKLVATATGTFAVLPK 136
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
1-141 1.59e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.34  E-value: 1.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790   1 MSENplLERARRFLSALRHCQVLGLTVEAADEKGLTLRLPYSQAIIGNPesGVVHGGAITTLMDTTCGISTVCVLPDFEI 80
Cdd:COG2050   1 MSDP--LERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRR 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596790  81 CPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDpGQPIAHVVGAFMRMGG 141
Cdd:COG2050  77 AVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDED-GKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
23-138 8.83e-24

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: 89.15  E-value: 8.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790  23 LGLTVEAADEKGLTLRLPYSQaiIGNPESGVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPAePHKDVYG 102
Cdd:cd03443   2 LGIRVVEVGPGRVVLRLPVRP--RHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPA-RGGDLTA 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15596790 103 FAECYRVTPNVIFTRGFAYQDDpGQPIAHVVGAFMR 138
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTDED-GKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
52-129 3.04e-10

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: 53.41  E-value: 3.04e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596790    52 GVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDPGQPI 129
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK11688 PRK11688
thioesterase family protein;
21-93 3.55e-09

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 52.16  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790   21 QVLGLTVEAADEKGLTLRLPYSQAIIGNPESGVVHGGAITTLMDTTCGIstVCV------LPD---------FEICPTLD 85
Cdd:PRK11688  25 RLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVAGGL--VCVggilarHEDiseeelrqrLSRLGTID 102

                 ....*...
gi 15596790   86 LRIDYMHP 93
Cdd:PRK11688 103 LRVDYLRP 110
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
21-94 1.66e-05

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 41.95  E-value: 1.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596790    21 QVLGLTVEAADEKGLTLRLPYSQAIIgNPEsGVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPA 94
Cdd:TIGR00369   4 SFLGIEIEELGDGFLEATMPVDERTL-QPF-GSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPA 75
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
1-141 1.59e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.34  E-value: 1.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790   1 MSENplLERARRFLSALRHCQVLGLTVEAADEKGLTLRLPYSQAIIGNPesGVVHGGAITTLMDTTCGISTVCVLPDFEI 80
Cdd:COG2050   1 MSDP--LERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRR 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596790  81 CPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDpGQPIAHVVGAFMRMGG 141
Cdd:COG2050  77 AVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDED-GKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
23-138 8.83e-24

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: 89.15  E-value: 8.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790  23 LGLTVEAADEKGLTLRLPYSQaiIGNPESGVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPAePHKDVYG 102
Cdd:cd03443   2 LGIRVVEVGPGRVVLRLPVRP--RHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPA-RGGDLTA 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15596790 103 FAECYRVTPNVIFTRGFAYQDDpGQPIAHVVGAFMR 138
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTDED-GKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
52-129 3.04e-10

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: 53.41  E-value: 3.04e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596790    52 GVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDPGQPI 129
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
52-137 3.26e-09

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: 51.32  E-value: 3.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790  52 GVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPAEPHKDVYGFAECYRVTPNVIFTRGFAYQDDpGQPIAH 131
Cdd:cd03440  16 GIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNED-GKLVAT 94

                ....*.
gi 15596790 132 VVGAFM 137
Cdd:cd03440  95 ATATFV 100
PRK11688 PRK11688
thioesterase family protein;
21-93 3.55e-09

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 52.16  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596790   21 QVLGLTVEAADEKGLTLRLPYSQAIIGNPESGVVHGGAITTLMDTTCGIstVCV------LPD---------FEICPTLD 85
Cdd:PRK11688  25 RLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVAGGL--VCVggilarHEDiseeelrqrLSRLGTID 102

                 ....*...
gi 15596790   86 LRIDYMHP 93
Cdd:PRK11688 103 LRVDYLRP 110
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
21-94 1.66e-05

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 41.95  E-value: 1.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596790    21 QVLGLTVEAADEKGLTLRLPYSQAIIgNPEsGVVHGGAITTLMDTTCGISTVCVLPDFEICPTLDLRIDYMHPA 94
Cdd:TIGR00369   4 SFLGIEIEELGDGFLEATMPVDERTL-QPF-GSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPA 75
 
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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