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Conserved domains on  [gi|2058278636|gb|QWZ07048|]
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PaaI family thioesterase [Nocardioides panacis]

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 ...
 18-131 2.68e-29

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 103.48  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TL 96
Cdd:COG2050    17 FAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGdRL 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2058278636  97 TSTATPLHRGRSQQVWLVETLDPDGKVAARGQVRL 131
Cdd:COG2050    97 TAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 18-131 2.68e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 103.48  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TL 96
Cdd:COG2050    17 FAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGdRL 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2058278636  97 TSTATPLHRGRSQQVWLVETLDPDGKVAARGQVRL 131
Cdd:COG2050    97 TAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-128 1.67e-26

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: 95.70  E-value: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  21 HLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTGTLTSTA 100
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                          90       100
                  ....*....|....*....|....*...
gi 2058278636 101 TPLHRGRSQQVWLVETLDPDGKVAARGQ 128
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-125 4.58e-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: 76.61  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTGTLT 97
Cdd:TIGR00369   2 LVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR 81

                          90       100
                  ....*....|....*....|....*...
gi 2058278636  98 STATPLHRGRSQQVWLVETLDPDGKVAA 125
Cdd:TIGR00369  82 AIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
16-122 7.83e-16

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 68.86  E-value: 7.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  16 GDFVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVgAAVWMGERGK-VVGVNNNTDFYRAVRTG 94
Cdd:PRK10254   18 NTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSM-AGFLMTRDGQcVVGTELNATHHRPVSEG 96

                          90       100
                  ....*....|....*....|....*...
gi 2058278636  95 TLTSTATPLHRGRSQQVWLVETLDPDGK 122
Cdd:PRK10254   97 KVRGVCQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-125 1.56e-11

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: 56.11  E-value: 1.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2058278636  48 YGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TLTSTATPLHRGRSQQVWLVETLDPDGKVAA 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 18-131 2.68e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 103.48  E-value: 2.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TL 96
Cdd:COG2050    17 FAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLGdRL 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2058278636  97 TSTATPLHRGRSQQVWLVETLDPDGKVAARGQVRL 131
Cdd:COG2050    97 TAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-128 1.67e-26

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: 95.70  E-value: 1.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  21 HLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTGTLTSTA 100
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTARA 80

                          90       100
                  ....*....|....*....|....*...
gi 2058278636 101 TPLHRGRSQQVWLVETLDPDGKVAARGQ 128
Cdd:cd03443    81 RVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 18-125 4.58e-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: 76.61  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTGTLT 97
Cdd:TIGR00369   2 LVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGKVR 81

                          90       100
                  ....*....|....*....|....*...
gi 2058278636  98 STATPLHRGRSQQVWLVETLDPDGKVAA 125
Cdd:TIGR00369  82 AIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
16-122 7.83e-16

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 68.86  E-value: 7.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  16 GDFVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVgAAVWMGERGK-VVGVNNNTDFYRAVRTG 94
Cdd:PRK10254   18 NTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSM-AGFLMTRDGQcVVGTELNATHHRPVSEG 96

                          90       100
                  ....*....|....*....|....*...
gi 2058278636  95 TLTSTATPLHRGRSQQVWLVETLDPDGK 122
Cdd:PRK10254   97 KVRGVCQPLHLGRQNQSWEIVVFDEQGR 124
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
16-123 2.91e-13

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 62.34  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  16 GDFVRHLGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTGT 95
Cdd:PRK10293   18 GNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGR 97

                          90       100
                  ....*....|....*....|....*...
gi 2058278636  96 LTSTATPLHRGRSQQVWLVETLDPDGKV 123
Cdd:PRK10293   98 VRGVCKPLHLGSRHQVWQIEIFDEKGRL 125
PLN02322 PLN02322
acyl-CoA thioesterase
 22-115 3.50e-13

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 62.39  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  22 LGVEFGEVTGDRVTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERgKVVGVNNNTDFYRAVRTGTLT-STA 100
Cdd:PLN02322   16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFK-RVAGIQLSINHLKSADLGDLVfAEA 94

                          90
                  ....*....|....*
gi 2058278636 101 TPLHRGRSQQVWLVE 115
Cdd:PLN02322   95 TPVSTGKTIQVWEVK 109
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-125 1.56e-11

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: 56.11  E-value: 1.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2058278636  48 YGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TLTSTATPLHRGRSQQVWLVETLDPDGKVAA 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 34-131 2.82e-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: 53.63  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  34 VTATWTAKPDLHQPYGIVHGGVHCSVIETLASVGAAVWMGERGKVVGVNNNTDFYRAVRTG-TLTSTATPLHRGRSQQVW 112
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVTV 80

                          90
                  ....*....|....*....
gi 2058278636 113 LVETLDPDGKVAARGQVRL 131
Cdd:cd03440    81 EVEVRNEDGKLVATATATF 99
PRK11688 PRK11688
thioesterase family protein;
18-75 3.88e-03

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 35.21  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058278636  18 FVRHLGVEFGEVTGDRVTATWTAKPDL--HQPYGIVHGGVHCSVIETLASVGAAVWMGER 75
Cdd:PRK11688   23 FNRLLGLELERLEPDFVELSFKMQPELvgNIAQSILHGGVIASVLDVAGGLVCVGGILAR 82
 
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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