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Conserved domains on  [gi|746786167|ref|WP_039698556|]
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PaaI family thioesterase [Sulfolobus islandicus]

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 ...
 1-135 8.96e-33

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 112.34  E-value: 8.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   1 MEDPKIIEEIFKNADHVFRYVGAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFT-VNDGVDQVTQ 79
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746786167  80 ELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSWYILRKK 135
Cdd:COG2050   81 ELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-135 8.96e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 112.34  E-value: 8.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   1 MEDPKIIEEIFKNADHVFRYVGAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFT-VNDGVDQVTQ 79
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746786167  80 ELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSWYILRKK 135
Cdd:COG2050   81 ELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 22-131 9.40e-32

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: 108.80  E-value: 9.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167  22 GAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFT-VNDGVDQVTQELKVNFLQPMYKGPFRVEGKV 100
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSaLPPGALAVTVDLNVNYLRPARGGDLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 746786167 101 LRKGSTVIVVEIEFRDAEGNLGAKALGSWYI 131
Cdd:cd03443   83 VKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-131 3.60e-19

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: 77.00  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   18 FRYVGAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFTVN-DGVDQVTQELKVNFLQPMYKGPFRV 96
Cdd:TIGR00369   3 VSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNsGGQAVVGLELNANHLRPAREGKVRA 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 746786167   97 EGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSWYI 131
Cdd:TIGR00369  83 IAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 47-123 2.18e-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: 2.18e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746786167   47 GNVLHGGIIMTAIDFTGGLAAFTVNDG-VDQVTQELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVVEIEFRDAEGNLGA 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK11688 PRK11688
thioesterase family protein;
4-132 8.37e-10

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 53.70  E-value: 8.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   4 PKIIEEIFKNADHVFRY-------VGAKVLLLEQGRAVVEIPFKEELTrrGNV----LHGGIIMTAIDFTGGLAAFT--- 69
Cdd:PRK11688   3 VLTQEEALKLVGEIFVYhmpfnrlLGLELERLEPDFVELSFKMQPELV--GNIaqsiLHGGVIASVLDVAGGLVCVGgil 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746786167  70 ---VNDGVDQV--------TQELKVNFLQPMYKGPFRVEGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSwYIL 132
Cdd:PRK11688  81 arhEDISEEELrqrlsrlgTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQGVHIASGTAT-YLV 153
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-135 8.96e-33

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 112.34  E-value: 8.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   1 MEDPKIIEEIFKNADHVFRYVGAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFT-VNDGVDQVTQ 79
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSaLPPGRRAVTI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 746786167  80 ELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSWYILRKK 135
Cdd:COG2050   81 ELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 22-131 9.40e-32

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: 108.80  E-value: 9.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167  22 GAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFT-VNDGVDQVTQELKVNFLQPMYKGPFRVEGKV 100
Cdd:cd03443    3 GIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSaLPPGALAVTVDLNVNYLRPARGGDLTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 746786167 101 LRKGSTVIVVEIEFRDAEGNLGAKALGSWYI 131
Cdd:cd03443   83 VKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-131 3.60e-19

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: 77.00  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   18 FRYVGAKVLLLEQGRAVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFTVN-DGVDQVTQELKVNFLQPMYKGPFRV 96
Cdd:TIGR00369   3 VSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNsGGQAVVGLELNANHLRPAREGKVRA 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 746786167   97 EGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSWYI 131
Cdd:TIGR00369  83 IAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 47-123 2.18e-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: 2.18e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 746786167   47 GNVLHGGIIMTAIDFTGGLAAFTVNDG-VDQVTQELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVVEIEFRDAEGNLGA 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 33-129 4.09e-11

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: 55.94  E-value: 4.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167  33 AVVEIPFKEELTRRGNVLHGGIIMTAIDFTGGLAAFTV-NDGVDQVTQELKVNFLQPMYKG-PFRVEGKVLRKGSTVIVV 110
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLgGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*....
gi 746786167 111 EIEFRDAEGNLGAKALGSW 129
Cdd:cd03440   81 EVEVRNEDGKLVATATATF 99
PRK11688 PRK11688
thioesterase family protein;
4-132 8.37e-10

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 53.70  E-value: 8.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 746786167   4 PKIIEEIFKNADHVFRY-------VGAKVLLLEQGRAVVEIPFKEELTrrGNV----LHGGIIMTAIDFTGGLAAFT--- 69
Cdd:PRK11688   3 VLTQEEALKLVGEIFVYhmpfnrlLGLELERLEPDFVELSFKMQPELV--GNIaqsiLHGGVIASVLDVAGGLVCVGgil 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 746786167  70 ---VNDGVDQV--------TQELKVNFLQPMYKGPFRVEGKVLRKGSTVIVVEIEFRDAEGNLGAKALGSwYIL 132
Cdd:PRK11688  81 arhEDISEEELrqrlsrlgTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQGVHIASGTAT-YLV 153
 
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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