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Conserved domains on  [gi|390616406|gb|AFM17556|]
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hypothetical protein Mycch_2795 [Mycolicibacterium chubuense NBB4]

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 ...
 1-128 4.48e-31

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


:

Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.72  E-value: 4.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   1 MTTELPAGLG----NGFDTELGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVV 76
Cdd:COG2050    1 MSDPLERLEGflaaNPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLA--ANSALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 390616406  77 GVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTITDDTDRVVARGQVRL 128
Cdd:COG2050   79 TIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-128 4.48e-31

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.72  E-value: 4.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   1 MTTELPAGLG----NGFDTELGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVV 76
Cdd:COG2050    1 MSDPLERLEGflaaNPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLA--ANSALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 390616406  77 GVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTITDDTDRVVARGQVRL 128
Cdd:COG2050   79 TIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 17-125 7.63e-29

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: 101.48  E-value: 7.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVVGVNNNTDFLRAIKSGTVTAT 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLA--ALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100
                 ....*....|....*....|....*....
gi 390616406  97 STPIHRGRRQQLWLVTITDDTDRVVARGQ 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 1.62e-19

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: 77.77  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGQvwLSENGDGHVVGVNNNTDFLRAIKSGTVTAT 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY--LCNSGGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 390616406   97 STPIHRGRRQQLWLVTITDDTDRVVA 122
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
4-119 7.82e-13

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 61.16  E-value: 7.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   4 ELPAGLGNGFDTELGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGqvWLSENGDGHVVGVNNNTD 83
Cdd:PRK10254  11 ELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNAT 88

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 390616406  84 FLRAIKSGTVTATSTPIHRGRRQQLWLVTITDDTDR 119
Cdd:PRK10254  89 HHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-122 1.05e-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: 56.49  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   44 GIVHGGVYCSVIESMASVSgqVWLSENGDGHVVGVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTITDDTDRVVA 122
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAA--ARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-128 4.48e-31

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 107.72  E-value: 4.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   1 MTTELPAGLG----NGFDTELGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVV 76
Cdd:COG2050    1 MSDPLERLEGflaaNPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLA--ANSALPPGRRAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 390616406  77 GVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTITDDTDRVVARGQVRL 128
Cdd:COG2050   79 TIELNINFLRPARLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTF 131
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 17-125 7.63e-29

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: 101.48  E-value: 7.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVVGVNNNTDFLRAIKSGTVTAT 96
Cdd:cd03443    2 LGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLA--ALSALPPGALAVTVDLNVNYLRPARGGDLTAR 79

                         90       100
                 ....*....|....*....|....*....
gi 390616406  97 STPIHRGRRQQLWLVTITDDTDRVVARGQ 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 1.62e-19

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: 77.77  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGQvwLSENGDGHVVGVNNNTDFLRAIKSGTVTAT 96
Cdd:TIGR00369   6 LGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY--LCNSGGQAVVGLELNANHLRPAREGKVRAI 83

                          90       100
                  ....*....|....*....|....*.
gi 390616406   97 STPIHRGRRQQLWLVTITDDTDRVVA 122
Cdd:TIGR00369  84 AQVVHLGRQTGVAEIEIVDEQGRLCA 109
PRK10254 PRK10254
proofreading thioesterase EntH;
4-119 7.82e-13

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 61.16  E-value: 7.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   4 ELPAGLGNGFDTELGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGqvWLSENGDGHVVGVNNNTD 83
Cdd:PRK10254  11 ELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAG--FLMTRDGQCVVGTELNAT 88

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 390616406  84 FLRAIKSGTVTATSTPIHRGRRQQLWLVTITDDTDR 119
Cdd:PRK10254  89 HHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGR 124
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 44-122 1.05e-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: 56.49  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   44 GIVHGGVYCSVIESMASVSgqVWLSENGDGHVVGVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTITDDTDRVVA 122
Cdd:pfam03061   2 GVVHGGVYLALADEAAGAA--ARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
17-120 1.17e-11

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 58.10  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGqvWLSENGDGHVVGVNNNTDFLRAIKSGTVTAT 96
Cdd:PRK10293  24 LDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAG--YLCTEGEQKVVGLEINANHVRSAREGRVRGV 101

                         90       100
                 ....*....|....*....|....
gi 390616406  97 STPIHRGRRQQLWLVTITDDTDRV 120
Cdd:PRK10293 102 CKPLHLGSRHQVWQIEIFDEKGRL 125
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 30-128 4.27e-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: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  30 RARLTITDKLLQPWGIVHGGVYCSVIESMASVSgqVWLSENGDGHVVGVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQL 108
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAA--AARLGGRGLGAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                         90       100
                 ....*....|....*....|
gi 390616406 109 WLVTITDDTDRVVARGQVRL 128
Cdd:cd03440   80 VEVEVRNEDGKLVATATATF 99
PLN02322 PLN02322
acyl-CoA thioesterase
 17-119 1.10e-10

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 55.84  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  17 LGLEYLEMTPDGGRARLTITDKLLQPWGIVHGGVYCSVIESMASVSGQVwlsENGDGHVVGVNNNTDFLRAIKSGT-VTA 95
Cdd:PLN02322  16 LGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHM---ASGFKRVAGIQLSINHLKSADLGDlVFA 92

                         90       100
                 ....*....|....*....|....
gi 390616406  96 TSTPIHRGRRQQLWLVTITDDTDR 119
Cdd:PLN02322  93 EATPVSTGKTIQVWEVKLWKTTDK 116
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 27-128 5.09e-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: 37.62  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406   27 DGGRARLTITD--KLLQPWGIVHGGVYCSVIESmasVSGQVWLSENGDGHVVGVNN-NTDFLRAIKSG-TVTATSTPIHR 102
Cdd:pfam14539  26 RPGRCEVRLPKrrRVRNHIGTVHAIAICNLAEL---AMGLMAEASLPDTHRWIPKGmTVDYLAKATGDlTAVAELDPEDW 102

                          90       100
                  ....*....|....*....|....*..
gi 390616406  103 GRRQQLWL-VTITDDTDRVVARGQVRL 128
Cdd:pfam14539 103 GEKGDLPVpVEVRDDAGTEVVRATITL 129
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 83-134 2.61e-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: 36.16  E-value: 2.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 390616406   83 DFLRAIKSGTVTATSTPIHRGRRQQLWLVTITDDtDRVVARGQVRLQNLTGE 134
Cdd:pfam13622  39 DFLRPVPPGPVTIRVEVVRDGRSFSTRRVELSQD-GRVVVTATATFGRLRSS 89
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 42-128 2.89e-03

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: 34.89  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390616406  42 PWGIVHGGVYCSVIES-----MASVS-GQVWLSENGDGHVVgVNNNTDFLRAIKSG-TVTATSTPIHRGRRQQLWLVTIT 114
Cdd:cd00586   14 AAGHVNNARYLRYFEEareefLRELGlGYDELEEQGLGLVV-VELEIDYLRPLRLGdRLTVETRVLRLGRKSFTFEQEIF 92

                         90
                 ....*....|....
gi 390616406 115 DDTDRVVARGQVRL 128
Cdd:cd00586   93 REDGELLATAETVL 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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