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Conserved domains on  [gi|1790796305|gb|QHC04254|]
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hotdog fold thioesterase [Anoxybacillus sp. PDR2]

Protein Classification

hotdog fold thioesterase( domain architecture ID 10794535)

hotdog fold thioesterase similar to Bacillus subtilis putative esterase ComA2 and to thioesterase PaaI that functions in the aerobic phenylacetate degradation pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 10-127 6.80e-44

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: 139.40  E-value: 6.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  10 TLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVRPVRSGT 89
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY-LCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1790796305  90 VTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAI 127
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 10-127 6.80e-44

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: 139.40  E-value: 6.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  10 TLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVRPVRSGT 89
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY-LCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1790796305  90 VTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAI 127
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 6-130 5.46e-39

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 127.75  E-value: 5.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305   6 MGKGTLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYALVDQDtESVAGLEINANHVRPV 85
Cdd:COG2050    12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPG-RRAVTIELNINFLRPA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1790796305  86 RSG-TVTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAIIKK 130
Cdd:COG2050    91 RLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PRK10254 PRK10254
proofreading thioesterase EntH;
4-128 9.04e-36

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 119.71  E-value: 9.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305   4 NEMGKGTLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVR 83
Cdd:PRK10254   13 NATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGF-LMTRDGQCVVGTELNATHHR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1790796305  84 PVRSGTVTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAII 128
Cdd:PRK10254   92 PVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 14-127 9.83e-35

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: 116.12  E-value: 9.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  14 ALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYALVDQDtESVAGLEINANHVRPVRSGTVTAT 93
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPG-ALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1790796305  94 GTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAI 127
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-119 3.87e-16

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: 67.67  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  41 FGLLHGGASVALAETVASLGAYALVDqDTESVAGLEINANHVRPVRSG-TVTATGTVLHRGRTTMVWDIRIVDDQQRLVC 119
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 10-127 6.80e-44

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: 139.40  E-value: 6.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  10 TLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVRPVRSGT 89
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAAGY-LCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1790796305  90 VTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAI 127
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 6-130 5.46e-39

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 127.75  E-value: 5.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305   6 MGKGTLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYALVDQDtESVAGLEINANHVRPV 85
Cdd:COG2050    12 LAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPG-RRAVTIELNINFLRPA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1790796305  86 RSG-TVTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAIIKK 130
Cdd:COG2050    91 RLGdRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PRK10254 PRK10254
proofreading thioesterase EntH;
4-128 9.04e-36

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 119.71  E-value: 9.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305   4 NEMGKGTLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVR 83
Cdd:PRK10254   13 NATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGF-LMTRDGQCVVGTELNATHHR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1790796305  84 PVRSGTVTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAII 128
Cdd:PRK10254   92 PVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVL 136
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
4-128 3.52e-35

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 118.19  E-value: 3.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305   4 NEMGKGTLLEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYaLVDQDTESVAGLEINANHVR 83
Cdd:PRK10293   13 NAMGEGNMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGY-LCTEGEQKVVGLEINANHVR 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1790796305  84 PVRSGTVTATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAII 128
Cdd:PRK10293   92 SAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 14-127 9.83e-35

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: 116.12  E-value: 9.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  14 ALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYALVDQDtESVAGLEINANHVRPVRSGTVTAT 93
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPG-ALAVTVDLNVNYLRPARGGDLTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1790796305  94 GTVLHRGRTTMVWDIRIVDDQQRLVCVSRCTIAI 127
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PLN02322 PLN02322
acyl-CoA thioesterase
 12-125 7.70e-18

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 74.33  E-value: 7.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  12 LEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYalVDQDTESVAGLEINANHVRPVRSGT-V 90
Cdd:PLN02322   13 LHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAH--MASGFKRVAGIQLSINHLKSADLGDlV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1790796305  91 TATGTVLHRGRTTMVWDIRIVDDQQR------LVCVSRCTI 125
Cdd:PLN02322   91 FAEATPVSTGKTIQVWEVKLWKTTDKdkankiLISSSRVTL 131
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-119 3.87e-16

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: 67.67  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  41 FGLLHGGASVALAETVASLGAYALVDqDTESVAGLEINANHVRPVRSG-TVTATGTVLHRGRTTMVWDIRIVDDQQRLVC 119
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGG-SQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 12-124 1.87e-12

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: 59.36  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  12 LEALGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVAslgAYALVDQDTESVAgLEINANHVRPVRSG-TV 90
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAF---AYACNSYGDAAVA-AQCTIDFLRPGRAGeRL 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1790796305  91 TATGTVLHRGRTTMVWDIRIVDDQQRLVCVSRCT 124
Cdd:TIGR02286  77 EAEAVEVSRGGRTGTYDVEVVNQEGELVALFRGT 110
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 27-126 2.51e-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: 55.94  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1790796305  27 VVATMPVDHRTHQPFGLLHGGASVALAETVASLGAYALVDQDTeSVAGLEINANHVRPVRSG-TVTATGTVLHRGRTTMV 105
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGL-GAVTLSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVT 79

                          90       100
                  ....*....|....*....|.
gi 1790796305 106 WDIRIVDDQQRLVCVSRCTIA 126
Cdd:cd03440    80 VEVEVRNEDGKLVATATATFV 100
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 15-59 1.10e-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: 36.47  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1790796305  15 LGIEITEIGHGRVVATMPVDHRTHQPFGLLHGGASVALAETVASL 59
Cdd:pfam14539  18 IGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAMGL 62
 
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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