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Conserved domains on  [gi|378804927|gb|AFC49062|]
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hypothetical protein OCO_26990 [Mycobacterium intracellulare MOTT-02]

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 ...
 1-139 1.51e-29

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 104.25  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   1 MPEPQETIIPPHFSAPFDREIGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLatRGGGNVV 80
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL--PPGRRAV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  81 GVNNNTDFLRSIGSGM-VYGRVEPIHRGRSQQLWLVTITDDDDRVVARGQVRLQNLELRE 139
Cdd:COG2050   79 TIELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-139 1.51e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 104.25  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   1 MPEPQETIIPPHFSAPFDREIGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLatRGGGNVV 80
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL--PPGRRAV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  81 GVNNNTDFLRSIGSGM-VYGRVEPIHRGRSQQLWLVTITDDDDRVVARGQVRLQNLELRE 139
Cdd:COG2050   79 TIELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-129 9.35e-25

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: 91.08  E-value: 9.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLatrgggnVVGVNNNT-----DFLRSIGSG 95
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAL-------PPGALAVTvdlnvNYLRPARGG 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 378804927  96 MVYGRVEPIHRGRSQQLWLVTITDDDDRVVARGQ 129
Cdd:cd03443   75 DLTARARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-126 1.41e-15

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: 67.76  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYtwLATRGGGNVVGVNNNTDFLRSIGSGMVYGR 100
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY--LCNSGGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 378804927  101 VEPIHRGRSQQLWLVTITDDDDRVVA 126
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
21-123 2.14e-13

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 62.70  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAytWLATRGGGNVVGVNNNTDFLRSIGSGMVYGR 100
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100
                 ....*....|....*....|...
gi 378804927 101 VEPIHRGRSQQLWLVTITDDDDR 123
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 47-126 1.10e-09

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: 51.49  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   47 MGLVHGGVYCSMIESMASVAAYTWLatRGGGNVVGVNNNTDFLRSIGSG-MVYGRVEPIHRGRSQQLWLVTITDDDDRVV 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG--GSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78


                  .
gi 378804927  126 A 126
Cdd:pfam03061  79 A 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-139 1.51e-29

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 104.25  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   1 MPEPQETIIPPHFSAPFDREIGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLatRGGGNVV 80
Cdd:COG2050    1 MSDPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAL--PPGRRAV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  81 GVNNNTDFLRSIGSGM-VYGRVEPIHRGRSQQLWLVTITDDDDRVVARGQVRLQNLELRE 139
Cdd:COG2050   79 TIELNINFLRPARLGDrLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-129 9.35e-25

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: 91.08  E-value: 9.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLatrgggnVVGVNNNT-----DFLRSIGSG 95
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAL-------PPGALAVTvdlnvNYLRPARGG 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 378804927  96 MVYGRVEPIHRGRSQQLWLVTITDDDDRVVARGQ 129
Cdd:cd03443   75 DLTARARVVKLGRRLAVVEVEVTDEDGKLVATAR 108
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-126 1.41e-15

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: 67.76  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYtwLATRGGGNVVGVNNNTDFLRSIGSGMVYGR 100
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY--LCNSGGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 378804927  101 VEPIHRGRSQQLWLVTITDDDDRVVA 126
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
21-123 2.14e-13

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 62.70  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAytWLATRGGGNVVGVNNNTDFLRSIGSGMVYGR 100
Cdd:PRK10254  24 LGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNATHHRPVSEGKVRGV 101

                         90       100
                 ....*....|....*....|...
gi 378804927 101 VEPIHRGRSQQLWLVTITDDDDR 123
Cdd:PRK10254 102 CQPLHLGRQNQSWEIVVFDEQGR 124
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
21-124 5.69e-10

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 53.86  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYtwLATRGGGNVVGVNNNTDFLRSIGSGMVYGR 100
Cdd:PRK10293  24 LDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGY--LCTEGEQKVVGLEINANHVRSAREGRVRGV 101

                         90       100
                 ....*....|....*....|....
gi 378804927 101 VEPIHRGRSQQLWLVTITDDDDRV 124
Cdd:PRK10293 102 CKPLHLGSRHQVWQIEIFDEKGRL 125
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 47-126 1.10e-09

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: 51.49  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   47 MGLVHGGVYCSMIESMASVAAYTWLatRGGGNVVGVNNNTDFLRSIGSG-MVYGRVEPIHRGRSQQLWLVTITDDDDRVV 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG--GSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78


                  .
gi 378804927  126 A 126
Cdd:pfam03061  79 A 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 33-132 3.30e-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: 50.94  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  33 ARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYTWLATRggGNVVGVNNNTDFLRSIGSG-MVYGRVEPIHRGRSQQ 111
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRG--LGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSV 78

                         90       100
                 ....*....|....*....|.
gi 378804927 112 LWLVTITDDDDRVVARGQVRL 132
Cdd:cd03440   79 TVEVEVRNEDGKLVATATATF 99
PLN02322 PLN02322
acyl-CoA thioesterase
 21-123 1.41e-08

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 50.45  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927  21 IGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIESMASVAAYtwLATrGGGNVVGVNNNTDFLRSIGSG-MVYG 99
Cdd:PLN02322  16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAH--MAS-GFKRVAGIQLSINHLKSADLGdLVFA 92

                         90       100
                 ....*....|....*....|....*.
gi 378804927 100 RVEPIHRGRSQQLWLVTI--TDDDDR 123
Cdd:PLN02322  93 EATPVSTGKTIQVWEVKLwkTTDKDK 118
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 13-132 1.23e-07

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: 47.25  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   13 FSAPFDREIGLQFTELSPDGARAQLEVTPKLLQPMGLVHGGVYCSMIES------MASV-AAYTWLATrgggnvvgvNNN 85
Cdd:pfam14539  10 RKAPYFGTIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELamglmaEASLpDTHRWIPK---------GMT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 378804927   86 TDFLRSIGSGMV-YGRVEPIHRGRSQQLWL-VTITDDDDRVVARGQVRL 132
Cdd:pfam14539  81 VDYLAKATGDLTaVAELDPEDWGEKGDLPVpVEVRDDAGTEVVRATITL 129
PRK11688 PRK11688
thioesterase family protein;
16-74 2.86e-05

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 41.37  E-value: 2.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378804927  16 PFDREIGLQFTELSPDGARAQLEVTPKL----LQpmGLVHGGVYCSMIESMASVAAYTWLATR 74
Cdd:PRK11688  22 PFNRLLGLELERLEPDFVELSFKMQPELvgniAQ--SILHGGVIASVLDVAGGLVCVGGILAR 82
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 46-136 1.61e-03

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: 36.93  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378804927   46 PMGLVHGGVycsmiesMASVAAytWLATRGGGNVVGVNNNTDFLRSIGSGMVYGRVEPIHRGRSQQLWLVTITdDDDRVV 125
Cdd:pfam13622   7 PGRAPHGGY-------VAALLL--RAAERTVPPDPLHSLHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELS-QDGRVV 76

                          90
                  ....*....|.
gi 378804927  126 ARGQVRLQNLE 136
Cdd:pfam13622  77 VTATATFGRLR 87
 
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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