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Conserved domains on  [gi|15600023|ref|NP_253517|]
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hypothetical protein PA4830 [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 ...
 52-175 4.56e-36

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  52 LPCPPYGELVDFVPIEWSEGRFLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALT 131
Cdd:COG2050  12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPAR 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600023 132 DKvGPVRAEGRVVHLGRSTAVAEGRLYDVDDRLYAVGSTTCLVL 175
Cdd:COG2050  92 LG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVL 134
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 52-175 4.56e-36

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  52 LPCPPYGELVDFVPIEWSEGRFLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALT 131
Cdd:COG2050  12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPAR 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600023 132 DKvGPVRAEGRVVHLGRSTAVAEGRLYDVDDRLYAVGSTTCLVL 175
Cdd:COG2050  92 LG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 60-174 4.94e-35

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: 118.81  E-value: 4.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  60 LVDFVPIEWSEGRFLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALtdKVGPVRA 139
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPA--RGGDLTA 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600023 140 EGRVVHLGRSTAVAEGRLYDVDDRLYAVGSTTCLV 174
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 80-174 1.86e-23

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: 89.33  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023    80 DRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALTDkvGPVRAEGRVVHLGRSTAVAEGRLYD 159
Cdd:TIGR00369  25 DERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPARE--GKVRAIAQVVHLGRQTGVAEIEIVD 102

                          90
                  ....*....|....*
gi 15600023   160 VDDRLYAVGSTTCLV 174
Cdd:TIGR00369 103 EQGRLCALSRGTTAV 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 87-166 6.58e-15

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: 66.12  E-value: 6.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023    87 LGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALtdKVG-PVRAEGRVVHLGRSTAVAEGRLYDVDDRLY 165
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPA--RLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78


                  .
gi 15600023   166 A 166
Cdd:pfam03061  79 A 79
PRK10254 PRK10254
proofreading thioesterase EntH;
80-163 9.06e-06

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 43.44  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023   80 DRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALTDkvGPVRAEGRVVHLGRSTAVAEGRLYD 159
Cdd:PRK10254  43 DTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATHHRPVSE--GKVRGVCQPLHLGRQNQSWEIVVFD 120


                 ....
gi 15600023  160 VDDR 163
Cdd:PRK10254 121 EQGR 124
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 52-175 4.56e-36

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 122.36  E-value: 4.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  52 LPCPPYGELVDFVPIEWSEGRFLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALT 131
Cdd:COG2050  12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPAR 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600023 132 DKvGPVRAEGRVVHLGRSTAVAEGRLYDVDDRLYAVGSTTCLVL 175
Cdd:COG2050  92 LG-DRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVL 134
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 60-174 4.94e-35

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: 118.81  E-value: 4.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  60 LVDFVPIEWSEGRFLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALtdKVGPVRA 139
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPA--RGGDLTA 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15600023 140 EGRVVHLGRSTAVAEGRLYDVDDRLYAVGSTTCLV 174
Cdd:cd03443  79 RARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 80-174 1.86e-23

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: 89.33  E-value: 1.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023    80 DRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALTDkvGPVRAEGRVVHLGRSTAVAEGRLYD 159
Cdd:TIGR00369  25 DERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPARE--GKVRAIAQVVHLGRQTGVAEIEIVD 102

                          90
                  ....*....|....*
gi 15600023   160 VDDRLYAVGSTTCLV 174
Cdd:TIGR00369 103 EQGRLCALSRGTTAV 117
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 87-166 6.58e-15

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: 66.12  E-value: 6.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023    87 LGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALtdKVG-PVRAEGRVVHLGRSTAVAEGRLYDVDDRLY 165
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPA--RLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78


                  .
gi 15600023   166 A 166
Cdd:pfam03061  79 A 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 73-173 2.18e-13

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: 62.88  E-value: 2.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023  73 FLFQGTPDRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALTDKvGPVRAEGRVVHLGRSTAV 152
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPG-DTLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|.
gi 15600023 153 AEGRLYDVDDRLYAVGSTTCL 173
Cdd:cd03440  80 VEVEVRNEDGKLVATATATFV 100
PRK10254 PRK10254
proofreading thioesterase EntH;
80-163 9.06e-06

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 43.44  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023   80 DRRHYNPLGSVHGGYAASLLDSCMGCAIHTRLQAGQGYTTTDLRISYLRALTDkvGPVRAEGRVVHLGRSTAVAEGRLYD 159
Cdd:PRK10254  43 DTRTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQCVVGTELNATHHRPVSE--GKVRGVCQPLHLGRQNQSWEIVVFD 120


                 ....
gi 15600023  160 VDDR 163
Cdd:PRK10254 121 EQGR 124
PRK11688 PRK11688
thioesterase family protein;
91-174 8.09e-04

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 37.90  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600023   91 HGGYAASLLDSCMGCA-------------IHTRLQAGQGYTTTDLRISYLRaltdkvgPVRAE-----GRVVHLGRSTAV 152
Cdd:PRK11688  59 HGGVIASVLDVAGGLVcvggilarhedisEEELRQRLSRLGTIDLRVDYLR-------PGRGErftatSSVLRAGNKVAV 131

                         90       100
                 ....*....|....*....|..
gi 15600023  153 AEGRLYDVDDRLYAVGSTTCLV 174
Cdd:PRK11688 132 ARMELHNEQGVHIASGTATYLV 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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