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Conserved domains on  [gi|937421208|gb|ALI27207|]
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Putative esterase [Mycolicibacterium fortuitum]

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 ...
 12-133 4.24e-30

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 105.41  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  12 GFDTELGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIWLSEngGGTVVGVNNNTDFLRAIGSG 91
Cdd:COG2050   16 PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPP--GRRAVTIELNINFLRPARLG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 937421208  92 -TVTAISQPIHRGRRQQLWLITITDENDKLVARGQVRLQNIPE 133
Cdd:COG2050   94 dRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-133 4.24e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 105.41  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  12 GFDTELGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIWLSEngGGTVVGVNNNTDFLRAIGSG 91
Cdd:COG2050   16 PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPP--GRRAVTIELNINFLRPARLG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 937421208  92 -TVTAISQPIHRGRRQQLWLITITDENDKLVARGQVRLQNIPE 133
Cdd:COG2050   94 dRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 17-125 3.24e-28

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: 99.55  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSghIWLSENGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLA--ALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100
                 ....*....|....*....|....*....
gi 937421208  97 SQPIHRGRRQQLWLITITDENDKLVARGQ 125
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 17-122 5.50e-22

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: 83.93  E-value: 5.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIWLSenGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNS--GGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 937421208   97 SQPIHRGRRQQLWLITITDENDKLVA 122
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
17-119 1.32e-17

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 73.48  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGhiWLSENGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100
                 ....*....|....*....|...
gi 937421208  97 SQPIHRGRRQQLWLITITDENDK 119
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-122 4.59e-12

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: 57.26  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   44 GIVHGGVYCSIVESLASVsgHIWLSENGGGTVVGVNNNTDFLRAIGSG-TVTAISQPIHRGRRQQLWLITITDENDKLVA 122
Cdd:pfam03061   2 GVVHGGVYLALADEAAGA--AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 12-133 4.24e-30

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 105.41  E-value: 4.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  12 GFDTELGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIWLSEngGGTVVGVNNNTDFLRAIGSG 91
Cdd:COG2050   16 PFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPP--GRRAVTIELNINFLRPARLG 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 937421208  92 -TVTAISQPIHRGRRQQLWLITITDENDKLVARGQVRLQNIPE 133
Cdd:COG2050   94 dRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 17-125 3.24e-28

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: 99.55  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSghIWLSENGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLA--ALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100
                 ....*....|....*....|....*....
gi 937421208  97 SQPIHRGRRQQLWLITITDENDKLVARGQ 125
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 17-122 5.50e-22

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: 83.93  E-value: 5.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIWLSenGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGYLCNS--GGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 937421208   97 SQPIHRGRRQQLWLITITDENDKLVA 122
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
17-119 1.32e-17

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 73.48  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  17 LGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGhiWLSENGGGTVVGVNNNTDFLRAIGSGTVTAI 96
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100
                 ....*....|....*....|...
gi 937421208  97 SQPIHRGRRQQLWLITITDENDK 119
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGR 124
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
1-120 2.08e-12

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 60.02  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   1 MTTDSTERLGKG-FDTELGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGhiWLSENGGGTVVGVN 79
Cdd:PRK10293   7 ITLEALNAMGEGnMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAG--YLCTEGEQKVVGLE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 937421208  80 NNTDFLRAIGSGTVTAISQPIHRGRRQQLWLITITDENDKL 120
Cdd:PRK10293  85 INANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRL 125
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-122 4.59e-12

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: 57.26  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   44 GIVHGGVYCSIVESLASVsgHIWLSENGGGTVVGVNNNTDFLRAIGSG-TVTAISQPIHRGRRQQLWLITITDENDKLVA 122
Cdd:pfam03061   2 GVVHGGVYLALADEAAGA--AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-128 4.98e-11

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: 55.56  E-value: 4.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208  30 RAQLTIHDKLLQPWGIVHGGVYCSIVESLASVsgHIWLSENGGGTVVGVNNNTDFLRAIGSG-TVTAISQPIHRGRRQQL 108
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGA--AAARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|
gi 937421208 109 WLITITDENDKLVARGQVRL 128
Cdd:cd03440   80 VEVEVRNEDGKLVATATATF 99
PLN02322 PLN02322
acyl-CoA thioesterase
 2-132 7.07e-09

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 50.83  E-value: 7.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   2 TTDSTERLGKGFDTeLGLTYLELTPDGGRAQLTIHDKLLQPWGIVHGGVYCSIVESLASVSGHIwlsENGGGTVVGVNNN 81
Cdd:PLN02322   2 ASSNTKAIDPPLHM-LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHM---ASGFKRVAGIQLS 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 937421208  82 TDFLRAIGSGT-VTAISQPIHRGRRQQLWLITI--TDENDK----LVARGQVRLQ-NIP 132
Cdd:PLN02322  78 INHLKSADLGDlVFAEATPVSTGKTIQVWEVKLwkTTDKDKankiLISSSRVTLIcNLP 136
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 17-128 4.84e-03

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: 34.93  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937421208   17 LGLTYLELTPdgGRAQLTIHD--KLLQPWGIVHGGVYCSIVESLASV-------SGHIWLSEngGGTVvgvnnntDFLrA 87
Cdd:pfam14539  18 IGPRITELRP--GRCEVRLPKrrRVRNHIGTVHAIAICNLAELAMGLmaeaslpDTHRWIPK--GMTV-------DYL-A 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 937421208   88 IGSGTVTAISQ--PIHRGRRQQLWL-ITITDENDKLVARGQVRL 128
Cdd:pfam14539  86 KATGDLTAVAEldPEDWGEKGDLPVpVEVRDDAGTEVVRATITL 129
 
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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