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Conserved domains on  [gi|488414423|ref|WP_002483808|]
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MULTISPECIES: hotdog fold thioesterase [Staphylococcus]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 3-120 2.99e-31

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.


The actual alignment was detected with superfamily member TIGR00369:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 117  Bit Score: 107.43  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423    3 NMLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGT 82
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488414423   83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
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 ...
 3-120 2.99e-31

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: 107.43  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423    3 NMLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGT 82
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488414423   83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-125 3.89e-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: 3.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   4 MLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEG-T 82
Cdd:COG2050   17 FAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGL-AANSALPPGRRAVTIELNINFLRPARLGdR 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488414423  83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAIKPLKR 125
Cdd:COG2050   96 LTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 7-120 1.65e-30

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: 105.33  E-value: 1.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   7 ALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMGAAYLIDTEKYVpLGLEMNGNHIGSTTEGTIYAT 86
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALA-VTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488414423  87 ATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-120 6.89e-24

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 89.30  E-value: 6.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   3 NMLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGT 82
Cdd:PRK10293  19 NMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSV-AGYLCTEGEQKVVGLEINANHVRSAREGR 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488414423  83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:PRK10293  98 VRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAI 135
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 34-112 1.27e-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: 58.81  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   34 FGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEG-TIYATATIIHEGKTTQVWNIDIKDDTDRLIC 112
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA-AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
Name Accession Description Interval E-value
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 3-120 2.99e-31

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: 107.43  E-value: 2.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423    3 NMLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGT 82
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSA-AGYLCNSGGQAVVGLELNANHLRPAREGK 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488414423   83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 4-125 3.89e-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: 3.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   4 MLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEG-T 82
Cdd:COG2050   17 FAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGL-AANSALPPGRRAVTIELNINFLRPARLGdR 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488414423  83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAIKPLKR 125
Cdd:COG2050   96 LTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPKRP 138
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 7-120 1.65e-30

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: 105.33  E-value: 1.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   7 ALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMGAAYLIDTEKYVpLGLEMNGNHIGSTTEGTIYAT 86
Cdd:cd03443    1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALA-VTVDLNVNYLRPARGGDLTAR 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488414423  87 ATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:cd03443   80 ARVVKLGRRLAVVEVEVTDEDGKLVATARGTFAV 113
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
3-120 6.89e-24

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


Pssm-ID: 182360  Cd Length: 136  Bit Score: 89.30  E-value: 6.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   3 NMLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGT 82
Cdd:PRK10293  19 NMVGLLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSV-AGYLCTEGEQKVVGLEINANHVRSAREGR 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488414423  83 IYATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:PRK10293  98 VRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAI 135
PRK10254 PRK10254
proofreading thioesterase EntH;
4-120 7.94e-19

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 76.18  E-value: 7.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   4 MLDALDIKVEKQERGLMVMSMPVTDKVKQPFGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEGTI 83
Cdd:PRK10254  20 MVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSM-AGFLMTRDGQCVVGTELNATHHRPVSEGKV 98

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488414423  84 YATATIIHEGKTTQVWNIDIKDDTDRLICVMRGTIAI 120
Cdd:PRK10254  99 RGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAV 135
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 34-112 1.27e-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: 58.81  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423   34 FGYLHGGASLALGESACSMgAAYLIDTEKYVPLGLEMNGNHIGSTTEG-TIYATATIIHEGKTTQVWNIDIKDDTDRLIC 112
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGA-AARRLGGSQQVVVVVELSIDFLRPARLGdRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PLN02322 PLN02322
acyl-CoA thioesterase
 24-109 1.06e-11

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 58.15  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423  24 MPVTDKVKQPFGYLHGGASLALGESACSMGaAYLIDTEKYVPlGLEMNGNHIGSTTEGT-IYATATIIHEGKTTQVWNID 102
Cdd:PLN02322  32 LPVSPMCCQPFKVLHGGVSALIAESLASLG-AHMASGFKRVA-GIQLSINHLKSADLGDlVFAEATPVSTGKTIQVWEVK 109


                 ....*..
gi 488414423 103 IKDDTDR 109
Cdd:PLN02322 110 LWKTTDK 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 21-119 6.75e-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: 49.78  E-value: 6.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488414423  21 VMSMPVTDKVKQPFGYLHGGASLALGESACSMGAAYLIDTEKYVPLgLEMNGNHIGSTTEG-TIYATATIIHEGKTTQVW 99
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVT-LSLDVRFLRPVRPGdTLTVEAEVVRVGRSSVTV 80

                         90       100
                 ....*....|....*....|
gi 488414423 100 NIDIKDDTDRLICVMRGTIA 119
Cdd:cd03440   81 EVEVRNEDGKLVATATATFV 100
 
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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