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Conserved domains on  [gi|15596791|ref|NP_250285|]
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hypothetical protein PA1594 [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 ...
 22-145 3.44e-26

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 95.78  E-value: 3.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  22 LVELIPYAKLLGIECLRLGDD-MVFRLPANKDNIGNPtlPAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLR 100
Cdd:COG2050  11 FLAANPFAELLGIELVEVEPGrAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLR 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15596791 101 AGHFRDT-YAQCQVWRQGRRVANVAINAWQtTQGEPIATARAHFKV 145
Cdd:COG2050  89 PARLGDRlTAEARVVRRGRRLAVVEVEVTD-EDGKLVATATGTFAV 133
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 22-145 3.44e-26

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 95.78  E-value: 3.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  22 LVELIPYAKLLGIECLRLGDD-MVFRLPANKDNIGNPtlPAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLR 100
Cdd:COG2050  11 FLAANPFAELLGIELVEVEPGrAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLR 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15596791 101 AGHFRDT-YAQCQVWRQGRRVANVAINAWQtTQGEPIATARAHFKV 145
Cdd:COG2050  89 PARLGDRlTAEARVVRRGRRLAVVEVEVTD-EDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 31-145 4.07e-22

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: 84.53  E-value: 4.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  31 LLGIECLRLGDD-MVFRLPANKDniGNPTLPAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLRAGHFRDTYA 109
Cdd:cd03443   1 LLGIRVVEVGPGrVVLRLPVRPR--HLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTA 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15596791 110 QCQVWRQGRRVANVAINAWQtTQGEPIATARAHFKV 145
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTD-EDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 62-136 2.24e-13

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: 61.12  E-value: 2.24e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596791    62 IHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLRAGHFRDT-YAQCQVWRQGRRVANVAINAWQTTQGEPI 136
Cdd:pfam03061   4 VHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRlTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK11688 PRK11688
thioesterase family protein;
1-141 4.37e-09

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 51.77  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791    1 MSPTSLEQLVRDArrnndyspLVELIPYAKLLGIECLRLGDDMV-FRLPANKDNIGNPTLPAIHGGVIA-------GFme 72
Cdd:PRK11688   4 LTQEEALKLVGEI--------FVYHMPFNRLLGLELERLEPDFVeLSFKMQPELVGNIAQSILHGGVIAsvldvagGL-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791   73 hAAMLHLLT-FMSIP------HLPKI--IDFSIDYLRAGHFRDTYAQCQVWRQGRRVANVAI---NAwqttQGEPIATAR 140
Cdd:PRK11688  74 -VCVGGILArHEDISeeelrqRLSRLgtIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMelhNE----QGVHIASGT 148


                 .
gi 15596791  141 A 141
Cdd:PRK11688 149 A 149
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 27-140 4.32e-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: 40.41  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791    27 PYAKLLGIECLRLGDD-MVFRLPANKDNIGNPTLpaIHGGVIAGFMEHAAMlhLLTFMSIPHLPKI--IDFSIDYLRAGH 103
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGfLEATMPVDERTLQPFGS--LHGGVSAALADTAGS--AAGYLCNSGGQAVvgLELNANHLRPAR 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15596791   104 FRDTYAQCQVWRQGRRVAnVAINAWQTTQGEPIATAR 140
Cdd:TIGR00369  77 EGKVRAIAQVVHLGRQTG-VAEIEIVDEQGRLCALSR 112
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 22-145 3.44e-26

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 95.78  E-value: 3.44e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  22 LVELIPYAKLLGIECLRLGDD-MVFRLPANKDNIGNPtlPAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLR 100
Cdd:COG2050  11 FLAANPFAELLGIELVEVEPGrAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLR 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15596791 101 AGHFRDT-YAQCQVWRQGRRVANVAINAWQtTQGEPIATARAHFKV 145
Cdd:COG2050  89 PARLGDRlTAEARVVRRGRRLAVVEVEVTD-EDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 31-145 4.07e-22

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: 84.53  E-value: 4.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  31 LLGIECLRLGDD-MVFRLPANKDniGNPTLPAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLRAGHFRDTYA 109
Cdd:cd03443   1 LLGIRVVEVGPGrVVLRLPVRPR--HLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTA 78

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15596791 110 QCQVWRQGRRVANVAINAWQtTQGEPIATARAHFKV 145
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTD-EDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 62-136 2.24e-13

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: 61.12  E-value: 2.24e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596791    62 IHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLRAGHFRDT-YAQCQVWRQGRRVANVAINAWQTTQGEPI 136
Cdd:pfam03061   4 VHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGDRlTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK11688 PRK11688
thioesterase family protein;
1-141 4.37e-09

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 51.77  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791    1 MSPTSLEQLVRDArrnndyspLVELIPYAKLLGIECLRLGDDMV-FRLPANKDNIGNPTLPAIHGGVIA-------GFme 72
Cdd:PRK11688   4 LTQEEALKLVGEI--------FVYHMPFNRLLGLELERLEPDFVeLSFKMQPELVGNIAQSILHGGVIAsvldvagGL-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791   73 hAAMLHLLT-FMSIP------HLPKI--IDFSIDYLRAGHFRDTYAQCQVWRQGRRVANVAI---NAwqttQGEPIATAR 140
Cdd:PRK11688  74 -VCVGGILArHEDISeeelrqRLSRLgtIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMelhNE----QGVHIASGT 148


                 .
gi 15596791  141 A 141
Cdd:PRK11688 149 A 149
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 60-143 1.88e-08

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: 49.01  E-value: 1.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  60 PAIHGGVIAGFMEHAAMLHLLTFMSIPHLPKIIDFSIDYLRAGHFRDT-YAQCQVWRQGRRVANVAINAWQTTqGEPIAT 138
Cdd:cd03440  16 GIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTlTVEAEVVRVGRSSVTVEVEVRNED-GKLVAT 94


                ....*
gi 15596791 139 ARAHF 143
Cdd:cd03440  95 ATATF 99
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 60-141 1.42e-05

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 43.09  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791    60 PAIHGGVIAGFMEHAAMLHlltfmsiPHLPKIIDFSIDYLRAGHFRDTYAQCQVWRQGRRVANVAINAWQttQGEPIATA 139
Cdd:pfam13622   9 RAPHGGYVAALLLRAAERT-------VPPDPLHSLHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQ--DGRVVVTA 79


                  ..
gi 15596791   140 RA 141
Cdd:pfam13622  80 TA 81
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 27-140 4.32e-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: 40.41  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791    27 PYAKLLGIECLRLGDD-MVFRLPANKDNIGNPTLpaIHGGVIAGFMEHAAMlhLLTFMSIPHLPKI--IDFSIDYLRAGH 103
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGfLEATMPVDERTLQPFGS--LHGGVSAALADTAGS--AAGYLCNSGGQAVvgLELNANHLRPAR 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15596791   104 FRDTYAQCQVWRQGRRVAnVAINAWQTTQGEPIATAR 140
Cdd:TIGR00369  77 EGKVRAIAQVVHLGRQTG-VAEIEIVDEQGRLCALSR 112
Thioesterase_II cd00556
Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases ...
 57-145 7.19e-03

Thioesterase II (TEII) is thought to regenerate misprimed nonribosomal peptide synthetases (NRPSs) as well as modular polyketide synthases (PKSs) by hydrolyzing acetyl groups bound to the peptidyl carrier protein (PCP) and acyl carrier protein (ACP) domains, respectively. TEII has two tandem asymmetric hot dog folds that are structurally similar to one found in PaaI thioesterase, 4-hydroxybenzoyl-CoA thioesterase (4HBT) and beta-hydroxydecanoyl-ACP dehydratase and thus, the TEII monomer is equivalent to the homodimeric form of the latter three enzymes. Human TEII is expressed in T cells and has been shown to bind the product of the HIV-1 Nef gene.


Pssm-ID: 238311 [Multi-domain]  Cd Length: 99  Bit Score: 34.24  E-value: 7.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  57 PTLPAIHGGVIAGFMEHAAMLHLLTF----MSIPHlpkiiDFSIDYLRAGhFRDTYAQCQVW--RQGRRVANVAINAWQT 130
Cdd:cd00556  12 PDDRRVFGGQLAAQSDLAALRTVPRPhgasGFASL-----DHHIYFHRPG-DADEWLLYEVEslRDGRSRALRRGRAYQR 85

                        90
                ....*....|....*
gi 15596791 131 TqGEPIATARAHFKV 145
Cdd:cd00556  86 D-GKLVASATQSFLV 99
TesB COG1946
Acyl-CoA thioesterase [Lipid transport and metabolism];
31-148 9.50e-03

Acyl-CoA thioesterase [Lipid transport and metabolism];


Pssm-ID: 441549 [Multi-domain]  Cd Length: 273  Bit Score: 34.85  E-value: 9.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596791  31 LLGIEclRLGDDmVFRLPANKDNignpTLPAIHGGVIAGFMEHAAMLHLltfmsiPHLPKIIDFSIDYLRAGHFRD--TY 108
Cdd:COG1946   8 LLDLE--RLEDG-LFRGEISPDQ----GLRRVFGGQVAAQALRAARRTV------PEDRPPHSLHAYFLRPGDPDGpiEY 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15596791 109 aQCQVWRQGRRVANVAINAWQttQGEPIATARAHFKVDEP 148
Cdd:COG1946  75 -EVERLRDGRSFSTRRVTAIQ--GGRVIFTATASFGVPEE 111
 
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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