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Conserved domains on  [gi|1133513669|ref|WP_075992207|]
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MULTISPECIES: PaaI family thioesterase [Sphingobacterium]

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 ...
 31-153 2.82e-28

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 101.56  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  31 PISKTLGINIIEAGLGTATVQINTTKElHSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFE-D 109
Cdd:COG2050    16 PFAELLGIELVEVEPGRAVLRLPVRPE-HLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLgD 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1133513669 110 ILTAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTVMTLRGDK 153
Cdd:COG2050    95 RLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-153 2.82e-28

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 101.56  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  31 PISKTLGINIIEAGLGTATVQINTTKElHSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFE-D 109
Cdd:COG2050    16 PFAELLGIELVEVEPGRAVLRLPVRPE-HLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLgD 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1133513669 110 ILTAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTVMTLRGDK 153
Cdd:COG2050    95 RLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 35-147 1.81e-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: 96.09  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  35 TLGINIIEAGLGTATVQINTTKElHSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFEDILTAK 114
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPR-HLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1133513669 115 ASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTVM 147
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFA 112
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 31-146 1.95e-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: 70.45  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  31 PISKTLGINIIEAGLGTATVQINTTKELHSNQqGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFEDI 110
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPF-GSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1133513669 111 LTAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTV 146
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTT 115
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 63-140 8.05e-13

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: 59.96  E-value: 8.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133513669  63 QGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPV-FEDILTAKASPLHNGKNLNHYRCDIFRSDGKTAA 140
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPArLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-153 2.82e-28

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 101.56  E-value: 2.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  31 PISKTLGINIIEAGLGTATVQINTTKElHSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFE-D 109
Cdd:COG2050    16 PFAELLGIELVEVEPGRAVLRLPVRPE-HLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIELNINFLRPARLgD 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1133513669 110 ILTAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTVMTLRGDK 153
Cdd:COG2050    95 RLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 35-147 1.81e-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: 96.09  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  35 TLGINIIEAGLGTATVQINTTKElHSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFEDILTAK 114
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPR-HLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1133513669 115 ASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTVM 147
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFA 112
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 31-146 1.95e-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: 70.45  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  31 PISKTLGINIIEAGLGTATVQINTTKELHSNQqGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFEDI 110
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPF-GSLHGGVSAALADTAGSAAGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1133513669 111 LTAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTV 146
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTT 115
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 33-146 3.27e-15

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 67.45  E-value: 3.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  33 SKTLGINIIEAGLGTATVQInTTKELHSNQQGTIHGGLLCELADAAIGTAHSTliqEGETFTSVELKINFYRPVFE-DIL 111
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAM-TVRADMLNGHGTAHGGFLFSLADSAFAYACNS---YGDAAVAAQCTIDFLRPGRAgERL 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1133513669 112 TAKASPLHNGKNLNHYRCDIFRSDGKTAAMVTSTV 146
Cdd:TIGR02286  77 EAEAVEVSRGGRTGTYDVEVVNQEGELVALFRGTS 111
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 59-147 1.25e-14

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: 65.57  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  59 HSNQQGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPVFE-DILTAKASPLHNGKNLNHYRCDIFRSDGK 137
Cdd:cd03440    11 DIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPgDTLTVEAEVVRVGRSSVTVEVEVRNEDGK 90

                          90
                  ....*....|
gi 1133513669 138 TAAMVTSTVM 147
Cdd:cd03440    91 LVATATATFV 100
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 63-140 8.05e-13

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: 59.96  E-value: 8.05e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133513669  63 QGTIHGGLLCELADAAIGTAHSTLIQEGETFTSVELKINFYRPV-FEDILTAKASPLHNGKNLNHYRCDIFRSDGKTAA 140
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVVVVVELSIDFLRPArLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
59-148 1.44e-03

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 36.70  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133513669  59 HSNQQGTIHGGLLCELAD--AAI-GTAHStliqEGETFT-SVElKINFYRPVFE-DILTAKASPLHNGKNLNHYRCDIFR 133
Cdd:COG1607    17 DTNHHGTLFGGWLLSWMDeaAAIaAARHA----RGRVVTaSVD-SVDFLRPVRVgDIVELYARVVRVGRTSMEVGVEVWA 91

                          90
                  ....*....|....*..
gi 1133513669 134 SDGKTAA--MVTSTVMT 148
Cdd:COG1607    92 EDLRTGErrLVTEAYFT 108
 
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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