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Conserved domains on  [gi|446593921|ref|WP_000671267|]
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MULTISPECIES: PaaI family thioesterase [Streptococcus]

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 ...
 13-126 5.21e-29

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.33  E-value: 5.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  13 NYEIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAIST---GYEAVTLQSNINYLRAGRLDDLLTVIGT 89
Cdd:COG2050   22 GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446593921  90 CVHNGRTTKVVDVHIKNQKGEMVTTAIFTMFVTGERK 126
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 13-126 5.21e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.33  E-value: 5.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  13 NYEIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAIST---GYEAVTLQSNINYLRAGRLDDLLTVIGT 89
Cdd:COG2050   22 GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446593921  90 CVHNGRTTKVVDVHIKNQKGEMVTTAIFTMFVTGERK 126
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 14-121 1.37e-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: 95.32  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  14 YEIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAISTGYE---AVTLQSNINYLRAGRLDDlLTVIGTC 90
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgalAVTVDLNVNYLRPARGGD-LTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446593921  91 VHNGRTTKVVDVHIKNQKGEMVTTAIFTMFV 121
Cdd:cd03443   83 VKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 38-110 2.86e-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: 65.35  E-value: 2.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446593921   38 YGNAHGGYLFTLCDQVSGLVAISTG---YEAVTLQSNINYLRAGRLDDLLTVIGTCVHNGRTTKVVDVHIKNQKGE 110
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGgsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 15-115 5.86e-14

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: 63.13  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921   15 EIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCD---QVSGLVAISTGYEAVTLQSNINYLRAGRlDDLLTVIGTCV 91
Cdd:TIGR00369   9 EIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADtagSAAGYLCNSGGQAVVGLELNANHLRPAR-EGKVRAIAQVV 87

                          90       100
                  ....*....|....*....|....
gi 446593921   92 HNGRTTKVVDVHIKNQKGEMVTTA 115
Cdd:TIGR00369  88 HLGRQTGVAEIEIVDEQGRLCALS 111
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 13-126 5.21e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 102.33  E-value: 5.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  13 NYEIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAIST---GYEAVTLQSNINYLRAGRLDDLLTVIGT 89
Cdd:COG2050   22 GIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVTIELNINFLRPARLGDRLTAEAR 101

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446593921  90 CVHNGRTTKVVDVHIKNQKGEMVTTAIFTMFVTGERK 126
Cdd:COG2050  102 VVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 14-121 1.37e-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: 95.32  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  14 YEIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAISTGYE---AVTLQSNINYLRAGRLDDlLTVIGTC 90
Cdd:cd03443    4 IRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPgalAVTVDLNVNYLRPARGGD-LTARARV 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446593921  91 VHNGRTTKVVDVHIKNQKGEMVTTAIFTMFV 121
Cdd:cd03443   83 VKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 24-119 8.42e-16

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: 67.50  E-value: 8.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  24 VTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAISTGYE---AVTLQSNINYLRAGRLDDLLTVIGTCVHNGRTTKVV 100
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRglgAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*....
gi 446593921 101 DVHIKNQKGEMVTTAIFTM 119
Cdd:cd03440   81 EVEVRNEDGKLVATATATF 99
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 38-110 2.86e-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: 65.35  E-value: 2.86e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446593921   38 YGNAHGGYLFTLCDQVSGLVAISTG---YEAVTLQSNINYLRAGRLDDLLTVIGTCVHNGRTTKVVDVHIKNQKGE 110
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGgsqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGR 76
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 15-115 5.86e-14

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: 63.13  E-value: 5.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921   15 EIENWEEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCD---QVSGLVAISTGYEAVTLQSNINYLRAGRlDDLLTVIGTCV 91
Cdd:TIGR00369   9 EIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADtagSAAGYLCNSGGQAVVGLELNANHLRPAR-EGKVRAIAQVV 87

                          90       100
                  ....*....|....*....|....
gi 446593921   92 HNGRTTKVVDVHIKNQKGEMVTTA 115
Cdd:TIGR00369  88 HLGRQTGVAEIEIVDEQGRLCALS 111
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 20-119 8.66e-09

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: 49.87  E-value: 8.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  20 EEGQVTLTTKVVDSSLNYYGNAHGGYLFTLCDQVSGLVAIS-TGYEAVTLQ-SNINYLRAGRLDDLLTVIGTCVHNGRT- 96
Cdd:cd03442    4 EDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRhAGGRVVTASvDRIDFLKPVRVGDVVELSARVVYTGRTs 83

                         90       100
                 ....*....|....*....|....*..
gi 446593921  97 ----TKVVDVHIKNQKGEMVTTAIFTM 119
Cdd:cd03442   84 mevgVEVEAEDPLTGERRLVTSAYFTF 110
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 36-121 4.75e-04

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 37.24  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921   36 NYYGNAHGGYLFTLCDQVSGLVAIST---GYEAVTLQSNINYLRAGRLDdlLTVIGTCVHNGRTTK---VVDVHIKNQKG 109
Cdd:pfam14539  42 NHIGTVHAIAICNLAELAMGLMAEASlpdTHRWIPKGMTVDYLAKATGD--LTAVAELDPEDWGEKgdlPVPVEVRDDAG 119

                          90
                  ....*....|..
gi 446593921  110 EMVTTAIFTMFV 121
Cdd:pfam14539 120 TEVVRATITLWV 131
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 25-119 5.11e-04

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 36.82  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446593921  25 TLTTKVVDSSLNYYGNAHGGYLFTLCDQV----------SGLVAISTGYEAVTLQSNINYLRAGRLDDLLTVIGTCVHNG 94
Cdd:cd00586    2 TLEIRVRFGDTDAAGHVNNARYLRYFEEAreeflrelglGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLG 81

                         90       100
                 ....*....|....*....|....*
gi 446593921  95 RTTKVVDVHIKNQKGEMVTTAIFTM 119
Cdd:cd00586   82 RKSFTFEQEIFREDGELLATAETVL 106
 
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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