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Conserved domains on  [gi|37927801|pdb|1Q4S|A]
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Chain A, Thioesterase

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 ...
 27-150 3.56e-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: 3.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       27 EQTLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATeATVAVVHEKGMMAVGQSNHTSFFRPVKE 106
Cdd:COG2050  14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAG-LAANSALPPGRRAVTIELNINFLRPARL 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1Q4S_A      107 G-HVRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAVRPRR 150
Cdd:COG2050  93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 27-150 3.56e-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: 3.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       27 EQTLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATeATVAVVHEKGMMAVGQSNHTSFFRPVKE 106
Cdd:COG2050  14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAG-LAANSALPPGRRAVTIELNINFLRPARL 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1Q4S_A      107 G-HVRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAVRPRR 150
Cdd:COG2050  93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 33-146 2.50e-25

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: 93.01  E-value: 2.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       33 TVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATeATVAVVHEKGMMAVGQSNHTSFFRPVKEGHVRAE 112
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGG-LAALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                        90       100       110
                ....*....|....*....|....*....|....
1Q4S_A      113 AVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 29-146 2.94e-16

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: 70.07  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A         29 TLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVAVVHEkGMMAVGQSNHTSFFRPVKEGH 108
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSG-GQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
1Q4S_A        109 VRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
27-146 3.98e-12

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 59.61  E-value: 3.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A        27 EQTLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVAVVHEkGMMAVGQSNHTSFFRPVKE 106
Cdd:PRK10254  17 DNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRD-GQCVVGTELNATHHRPVSE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
1Q4S_A       107 GHVRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:PRK10254  96 GKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAV 135
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 61-138 2.49e-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: 2.49e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1Q4S_A         61 GLVHGGAYCALAEMLATEAtVAVVHEKGMMAVGQSNHTSFFRPVKEG-HVRAEAVRIHAGSTTWFWDVSLRDDAGRLCA 138
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAA-ARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 27-150 3.56e-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: 3.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       27 EQTLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATeATVAVVHEKGMMAVGQSNHTSFFRPVKE 106
Cdd:COG2050  14 ANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAG-LAANSALPPGRRAVTIELNINFLRPARL 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1Q4S_A      107 G-HVRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAVRPRR 150
Cdd:COG2050  93 GdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 33-146 2.50e-25

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: 93.01  E-value: 2.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       33 TVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATeATVAVVHEKGMMAVGQSNHTSFFRPVKEGHVRAE 112
Cdd:cd03443   1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGG-LAALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                        90       100       110
                ....*....|....*....|....*....|....
1Q4S_A      113 AVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:cd03443  80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 29-146 2.94e-16

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: 70.07  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A         29 TLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVAVVHEkGMMAVGQSNHTSFFRPVKEGH 108
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSG-GQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
1Q4S_A        109 VRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PRK10254 PRK10254
proofreading thioesterase EntH;
27-146 3.98e-12

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 59.61  E-value: 3.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A        27 EQTLDGTVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVAVVHEkGMMAVGQSNHTSFFRPVKE 106
Cdd:PRK10254  17 DNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRD-GQCVVGTELNATHHRPVSE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
1Q4S_A       107 GHVRAEAVRIHAGSTTWFWDVSLRDDAGRLCAVSSMSIAV 146
Cdd:PRK10254  96 GKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAV 135
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 61-138 2.49e-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: 2.49e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1Q4S_A         61 GLVHGGAYCALAEMLATEAtVAVVHEKGMMAVGQSNHTSFFRPVKEG-HVRAEAVRIHAGSTTWFWDVSLRDDAGRLCA 138
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAA-ARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 46-145 1.48e-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: 52.09  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A       46 ATASVEVTDTLRQRWGLVHGGAYCALAEMLATEAtVAVVHEKGMMAVGQSNHTSFFRPVKEGH-VRAEAVRIHAGSTTWF 124
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAA-AARLGGRGLGAVTLSLDVRFLRPVRPGDtLTVEAEVVRVGRSSVT 79

                        90       100
                ....*....|....*....|.
1Q4S_A      125 WDVSLRDDAGRLCAVSSMSIA 145
Cdd:cd03440  80 VEVEVRNEDGKLVATATATFV 100
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
48-146 1.77e-08

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 50.01  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A        48 ASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVaVVHEKGMMAVGQSNHTSFFRPVKEGHVRAEAVRIHAGSTTWFWDV 127
Cdd:PRK10293  38 ATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGY-LCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQI 116

                         90
                 ....*....|....*....
1Q4S_A       128 SLRDDAGRLCAVSSMSIAV 146
Cdd:PRK10293 117 EIFDEKGRLCCSSRLTTAI 135
PLN02322 PLN02322
acyl-CoA thioesterase
 33-141 1.89e-05

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 42.36  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1Q4S_A        33 TVGFVIDEMTPERATASVEVTDTLRQRWGLVHGGAYCALAEMLATEATVAVVHEKGMMAVGQS-NHtsffrpVKEGH--- 108
Cdd:PLN02322  15 MLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQLSiNH------LKSADlgd 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
1Q4S_A       109 -VRAEAVRIHAGSTTWFWDVSL-----RDDAGRLCAVSS 141
Cdd:PLN02322  89 lVFAEATPVSTGKTIQVWEVKLwkttdKDKANKILISSS 127
 
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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