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Conserved domains on  [gi|496946998|ref|WP_009416779|]
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MULTISPECIES: PaaI family thioesterase [Capnocytophaga]

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 ...
 1-132 1.66e-37

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998   1 MNKqDLQQKWDTLPENNLMRLWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFlLHRKPNEQIR 80
Cdd:COG2050    1 MSD-PLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496946998  81 GIELSANHLRSGKIGDTLFATAKCINAGRTLQLWEINITNQDNKLISYCKFT 132
Cdd:COG2050   79 TIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGT 130
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-132 1.66e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998   1 MNKqDLQQKWDTLPENNLMRLWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFlLHRKPNEQIR 80
Cdd:COG2050    1 MSD-PLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496946998  81 GIELSANHLRSGKIGDTLFATAKCINAGRTLQLWEINITNQDNKLISYCKFT 132
Cdd:COG2050   79 TIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGT 130
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-126 4.37e-31

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: 107.26  E-value: 4.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  21 LWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFlLHRKPNEQIRGIELSANHLRSGKIGDtLFA 100
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAAL-SALPPGALAVTVDLNVNYLRPARGGD-LTA 78

                         90       100
                 ....*....|....*....|....*.
gi 496946998 101 TAKCINAGRTLQLWEINITNQDNKLI 126
Cdd:cd03443   79 RARVVKLGRRLAVVEVEVTDEDGKLV 104
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 24-133 1.37e-28

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: 100.88  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998   24 MEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLhrKPNEQIR-GIELSANHLRSGKiGDTLFATA 102
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC--NSGGQAVvGLELNANHLRPAR-EGKVRAIA 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 496946998  103 KCINAGRTLQLWEINITNQDNKLISYCKFTT 133
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEIVDEQGRLCALSRGTT 115
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 49-126 2.30e-19

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: 76.14  E-value: 2.30e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496946998   49 GVLHGGATLALAETAGSVAAFLLHRKPnEQIRGIELSANHLRSGKIGDTLFATAKCINAGRTLQLWEINITNQDNKLI 126
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
11-133 1.64e-18

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 75.82  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  11 DTLPENNLMRLWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLhRKPNEQIRGIELSANHLR 90
Cdd:PRK10293  13 NAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLC-TEGEQKVVGLEINANHVR 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496946998  91 SGKIGdTLFATAKCINAGRTLQLWEINITNQDNKLISYCKFTT 133
Cdd:PRK10293  92 SAREG-RVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTT 133
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-132 1.66e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 124.28  E-value: 1.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998   1 MNKqDLQQKWDTLPENNLMRLWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFlLHRKPNEQIR 80
Cdd:COG2050    1 MSD-PLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAAN-SALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496946998  81 GIELSANHLRSGKIGDTLFATAKCINAGRTLQLWEINITNQDNKLISYCKFT 132
Cdd:COG2050   79 TIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGT 130
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-126 4.37e-31

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: 107.26  E-value: 4.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  21 LWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFlLHRKPNEQIRGIELSANHLRSGKIGDtLFA 100
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAAL-SALPPGALAVTVDLNVNYLRPARGGD-LTA 78

                         90       100
                 ....*....|....*....|....*.
gi 496946998 101 TAKCINAGRTLQLWEINITNQDNKLI 126
Cdd:cd03443   79 RARVVKLGRRLAVVEVEVTDEDGKLV 104
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 24-133 1.37e-28

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: 100.88  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998   24 MEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLhrKPNEQIR-GIELSANHLRSGKiGDTLFATA 102
Cdd:TIGR00369   8 IEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLC--NSGGQAVvGLELNANHLRPAR-EGKVRAIA 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 496946998  103 KCINAGRTLQLWEINITNQDNKLISYCKFTT 133
Cdd:TIGR00369  85 QVVHLGRQTGVAEIEIVDEQGRLCALSRGTT 115
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 49-126 2.30e-19

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: 76.14  E-value: 2.30e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496946998   49 GVLHGGATLALAETAGSVAAFLLHRKPnEQIRGIELSANHLRSGKIGDTLFATAKCINAGRTLQLWEINITNQDNKLI 126
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAAARRLGGSQ-QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
11-133 1.64e-18

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 75.82  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  11 DTLPENNLMRLWQMEIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLhRKPNEQIRGIELSANHLR 90
Cdd:PRK10293  13 NAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLC-TEGEQKVVGLEINANHVR 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 496946998  91 SGKIGdTLFATAKCINAGRTLQLWEINITNQDNKLISYCKFTT 133
Cdd:PRK10293  92 SAREG-RVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTT 133
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 34-132 8.88e-17

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: 70.20  E-value: 8.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  34 LVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLHRkPNEQIRGIELSANHLRSGKIGDTLFATAKCINAGRTLQL 113
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVT 79

                         90
                 ....*....|....*....
gi 496946998 114 WEINITNQDNKLISYCKFT 132
Cdd:cd03440   80 VEVEVRNEDGKLVATATAT 98
PRK10254 PRK10254
proofreading thioesterase EntH;
29-133 1.09e-16

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 71.17  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  29 VGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLLHRKpNEQIRGIELSANHLRSGKIGdTLFATAKCINAG 108
Cdd:PRK10254  31 LGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFLMTRD-GQCVVGTELNATHHRPVSEG-KVRGVCQPLHLG 108

                         90       100
                 ....*....|....*....|....*
gi 496946998 109 RTLQLWEINITNQDNKLISYCKFTT 133
Cdd:PRK10254 109 RQNQSWEIVVFDEQGRRCCTCRLGT 133
PLN02322 PLN02322
acyl-CoA thioesterase
 25-134 1.05e-14

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 66.24  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496946998  25 EIAEVGEDYLVMTMPVTDKVTQIDGVLHGGATLALAETAGSVAAFLlhRKPNEQIRGIELSANHLRSGKIGDTLFATAKC 104
Cdd:PLN02322  19 EFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHM--ASGFKRVAGIQLSINHLKSADLGDLVFAEATP 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496946998 105 INAGRTLQLWEINI--TNQDNK----LISYCKFTTI 134
Cdd:PLN02322  97 VSTGKTIQVWEVKLwkTTDKDKankiLISSSRVTLI 132
 
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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