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Conserved domains on  [gi|2279651087|ref|WP_256329669|]
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PaaI family thioesterase [Variovorax sp. YR634]

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 ...
 1-139 3.01e-18

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 75.36  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087   1 MEEPIDPFENLAAAGwrrirtagAFMSTAGPLWTRREGTSWVYAVWSTDAHLNPAGVVHGGLLATLTDHAISTVAWEAAS 80
Cdd:COG2050     1 MSDPLERLEGFLAAN--------PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279651087  81 R-MPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQL-QAAGQEVLVAQALMKV 139
Cdd:COG2050    73 PgRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVtDEDGKLVATATGTFAV 133
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-139 3.01e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 75.36  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087   1 MEEPIDPFENLAAAGwrrirtagAFMSTAGPLWTRREGTSWVYAVWSTDAHLNPAGVVHGGLLATLTDHAISTVAWEAAS 80
Cdd:COG2050     1 MSDPLERLEGFLAAN--------PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279651087  81 R-MPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQL-QAAGQEVLVAQALMKV 139
Cdd:COG2050    73 PgRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVtDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 48-139 5.02e-17

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: 71.43  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087  48 TDAHLNPAGVVHGGLLATLTDHAISTVAWEAASR-MPCVTVQLDTQFLAPVAAGVLVeARAQLVRRTSSLLFMRGQL-QA 125
Cdd:cd03443    21 RPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgALAVTVDLNVNYLRPARGGDLT-ARARVVKLGRRLAVVEVEVtDE 99

                          90
                  ....*....|....
gi 2279651087 126 AGQEVLVAQALMKV 139
Cdd:cd03443   100 DGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-132 1.60e-09

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: 51.10  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651087  56 GVVHGGLLATLTDHAISTVAWEAA-SRMPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQLQAAGQEVLV 132
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGgSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 51-114 7.87e-04

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: 36.94  E-value: 7.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279651087  51 HLNPAGVVHGGLLATLTDHAISTVAWEAASR-MPCVTVQLDTQFLAPVAAGVLVeARAQLVRRTS 114
Cdd:TIGR00369  28 TLQPFGSLHGGVSAALADTAGSAAGYLCNSGgQAVVGLELNANHLRPAREGKVR-AIAQVVHLGR 91
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-139 3.01e-18

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 75.36  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087   1 MEEPIDPFENLAAAGwrrirtagAFMSTAGPLWTRREGTSWVYAVWSTDAHLNPAGVVHGGLLATLTDHAISTVAWEAAS 80
Cdd:COG2050     1 MSDPLERLEGFLAAN--------PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2279651087  81 R-MPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQL-QAAGQEVLVAQALMKV 139
Cdd:COG2050    73 PgRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVtDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 48-139 5.02e-17

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: 71.43  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087  48 TDAHLNPAGVVHGGLLATLTDHAISTVAWEAASR-MPCVTVQLDTQFLAPVAAGVLVeARAQLVRRTSSLLFMRGQL-QA 125
Cdd:cd03443    21 RPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgALAVTVDLNVNYLRPARGGDLT-ARARVVKLGRRLAVVEVEVtDE 99

                          90
                  ....*....|....
gi 2279651087 126 AGQEVLVAQALMKV 139
Cdd:cd03443   100 DGKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 48-132 9.20e-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: 52.48  E-value: 9.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2279651087  48 TDAHLNPAGVVHGGLLATLTDHAISTVAWEAA-SRMPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQLQAA 126
Cdd:cd03440     8 TPEDIDGGGIVHGGLLLALADEAAGAAAARLGgRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNE 87


                  ....*.
gi 2279651087 127 GQEVLV 132
Cdd:cd03440    88 DGKLVA 93
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
50-114 1.15e-09

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 53.26  E-value: 1.15e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651087  50 AHLNPAGVVHGGLLATLTDHAISTVAWEAAsRMPCVTVQLDT-QFLAPVAAGVLVEARAQLVR--RTS 114
Cdd:COG1607    16 EDTNHHGTLFGGWLLSWMDEAAAIAAARHA-RGRVVTASVDSvDFLRPVRVGDIVELYARVVRvgRTS 82
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 56-132 1.60e-09

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: 51.10  E-value: 1.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2279651087  56 GVVHGGLLATLTDHAISTVAWEAA-SRMPCVTVQLDTQFLAPVAAGVLVEARAQLVRRTSSLLFMRGQLQAAGQEVLV 132
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGgSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 49-114 1.43e-05

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: 41.79  E-value: 1.43e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2279651087  49 DAHLNPAGVVHGGLLATLTDHAISTVAWEAASRmPCVTVQLD-TQFLAPVAAGVLVEARAQLVR--RTS 114
Cdd:cd03442    16 PEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG-RVVTASVDrIDFLKPVRVGDVVELSARVVYtgRTS 83
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 51-114 7.87e-04

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: 36.94  E-value: 7.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2279651087  51 HLNPAGVVHGGLLATLTDHAISTVAWEAASR-MPCVTVQLDTQFLAPVAAGVLVeARAQLVRRTS 114
Cdd:TIGR00369  28 TLQPFGSLHGGVSAALADTAGSAAGYLCNSGgQAVVGLELNANHLRPAREGKVR-AIAQVVHLGR 91
 
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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