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Conserved domains on  [gi|493865687|ref|WP_006812366|]
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MULTISPECIES: acyl-CoA thioesterase YigI [Gammaproteobacteria]

Protein Classification

thioesterase family protein( domain architecture ID 10793604)

thioesterase family protein similar to Escherichia coli protein YigI

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11688 PRK11688
thioesterase family protein;
4-155 3.24e-99

thioesterase family protein;


:

Pssm-ID: 183276  Cd Length: 154  Bit Score: 281.73  E-value: 3.24e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   4 TLTAEETLKLVGEIFVYHMPFNRALGLELERYEKDFAQLSFNNQPMMVGNWAQSILHGGVIASALDVAAGLVCVGSTLTR 83
Cdd:PRK11688   3 VLTQEEALKLVGEIFVYHMPFNRLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493865687  84 HDTINEDELRQRLSRMGTIDLRVDYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMVG 155
Cdd:PRK11688  83 HEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQGVHIASGTATYLVG 154
 
Name Accession Description Interval E-value
PRK11688 PRK11688
thioesterase family protein;
4-155 3.24e-99

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 281.73  E-value: 3.24e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   4 TLTAEETLKLVGEIFVYHMPFNRALGLELERYEKDFAQLSFNNQPMMVGNWAQSILHGGVIASALDVAAGLVCVGSTLTR 83
Cdd:PRK11688   3 VLTQEEALKLVGEIFVYHMPFNRLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493865687  84 HDTINEDELRQRLSRMGTIDLRVDYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMVG 155
Cdd:PRK11688  83 HEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQGVHIASGTATYLVG 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-154 2.41e-27

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 99.25  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  16 EIFVYHMPFNRALGLELERYEKDFAQLSFNNQPMMVGNWaqSILHGGVIASALDVAAGLVCvgstltrHDTINEDElrqr 95
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAA-------NSALPPGR---- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  96 lsRMGTIDLRVDYLRPGR-GNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:COG2050   76 --RAVTIELNINFLRPARlGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-154 7.36e-24

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: 89.54  E-value: 7.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  27 ALGLELERYEKDFAQLSFNNQPMMVGnwAQSILHGGVIASALDVAAGLVCVGSTltrhdtinedelrQRLSRMGTIDLRV 106
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLN--PGGIVHGGAIATLADTAGGLAALSAL-------------PPGALAVTVDLNV 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493865687 107 DYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:cd03443   66 NYLRPARGGDLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 58-146 5.65e-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: 55.34  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   58 ILHGGVIASALDVAAGLVCVGSTLTRHDtinedelrqrlsrMGTIDLRVDYLRPGR-GNRFTCTSSLLRAGNKVAVARVE 136
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAARRLGGSQQV-------------VVVVELSIDFLRPARlGDRLTVEARVVRLGRTSAVVEVE 69

                          90
                  ....*....|
gi 493865687  137 LHNEEQVYIA 146
Cdd:pfam03061  70 VRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 23-154 9.20e-11

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: 55.81  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   23 PFNRALGLELERYEKDFAQLSFNNQPMMVgNWAQSiLHGGVIASALDVAAGLVCvgsTLTRHDTINedelrqrlsrMGTI 102
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTL-QPFGS-LHGGVSAALADTAGSAAG---YLCNSGGQA----------VVGL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 493865687  103 DLRVDYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:TIGR00369  66 ELNANHLRPAREGKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
PRK11688 PRK11688
thioesterase family protein;
4-155 3.24e-99

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 281.73  E-value: 3.24e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   4 TLTAEETLKLVGEIFVYHMPFNRALGLELERYEKDFAQLSFNNQPMMVGNWAQSILHGGVIASALDVAAGLVCVGSTLTR 83
Cdd:PRK11688   3 VLTQEEALKLVGEIFVYHMPFNRLLGLELERLEPDFVELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILAR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493865687  84 HDTINEDELRQRLSRMGTIDLRVDYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMVG 155
Cdd:PRK11688  83 HEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTATSSVLRAGNKVAVARMELHNEQGVHIASGTATYLVG 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 16-154 2.41e-27

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 99.25  E-value: 2.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  16 EIFVYHMPFNRALGLELERYEKDFAQLSFNNQPMMVGNWaqSILHGGVIASALDVAAGLVCvgstltrHDTINEDElrqr 95
Cdd:COG2050    9 EGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPP--GTVHGGALAALADSAAGLAA-------NSALPPGR---- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  96 lsRMGTIDLRVDYLRPGR-GNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:COG2050   76 --RAVTIELNINFLRPARlGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAV 133
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-154 7.36e-24

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: 89.54  E-value: 7.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  27 ALGLELERYEKDFAQLSFNNQPMMVGnwAQSILHGGVIASALDVAAGLVCVGSTltrhdtinedelrQRLSRMGTIDLRV 106
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLN--PGGIVHGGAIATLADTAGGLAALSAL-------------PPGALAVTVDLNV 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493865687 107 DYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:cd03443   66 NYLRPARGGDLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 58-146 5.65e-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: 55.34  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   58 ILHGGVIASALDVAAGLVCVGSTLTRHDtinedelrqrlsrMGTIDLRVDYLRPGR-GNRFTCTSSLLRAGNKVAVARVE 136
Cdd:pfam03061   3 VVHGGVYLALADEAAGAAARRLGGSQQV-------------VVVVELSIDFLRPARlGDRLTVEARVVRLGRTSAVVEVE 69

                          90
                  ....*....|
gi 493865687  137 LHNEEQVYIA 146
Cdd:pfam03061  70 VRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 23-154 9.20e-11

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: 55.81  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   23 PFNRALGLELERYEKDFAQLSFNNQPMMVgNWAQSiLHGGVIASALDVAAGLVCvgsTLTRHDTINedelrqrlsrMGTI 102
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTL-QPFGS-LHGGVSAALADTAGSAAG---YLCNSGGQA----------VVGL 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 493865687  103 DLRVDYLRPGRGNRFTCTSSLLRAGNKVAVARVELHNEEQVYIASATATYMV 154
Cdd:TIGR00369  66 ELNANHLRPAREGKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 58-153 8.31e-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: 50.17  E-value: 8.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687  58 ILHGGVIASALDVAAGLVCVGSTLTRHDTInedelrqrlsrmgTIDLRVDYLRPGR-GNRFTCTSSLLRAGNKVAVARVE 136
Cdd:cd03440   17 IVHGGLLLALADEAAGAAAARLGGRGLGAV-------------TLSLDVRFLRPVRpGDTLTVEAEVVRVGRSSVTVEVE 83

                         90
                 ....*....|....*..
gi 493865687 137 LHNEEQVYIASATATYM 153
Cdd:cd03440   84 VRNEDGKLVATATATFV 100
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 52-153 6.55e-05

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463937 [Multi-domain]  Cd Length: 246  Bit Score: 41.55  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493865687   52 GNWAQ-SILHGGVIASALDVAAGLVCVGSTLTRhdtinedelrqrlsrmgtidLRVDYLRPGRGNRFTCTSSLLRAGNKV 130
Cdd:pfam13622   3 PPWSPgRAPHGGYVAALLLRAAERTVPPDPLHS--------------------LHVDFLRPVPPGPVTIRVEVVRDGRSF 62

                          90       100
                  ....*....|....*....|...
gi 493865687  131 AVARVELHNEEQVyIASATATYM 153
Cdd:pfam13622  63 STRRVELSQDGRV-VVTATATFG 84
 
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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