NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488050389|ref|WP_002121786|]
View 

MULTISPECIES: thioesterase family protein [Acinetobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
52-163 7.73e-41

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 PRK11688:

Pssm-ID: 469797  Cd Length: 154  Bit Score: 134.20  E-value: 7.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  52 EGYIEMQPNLIGNLAFQILHGGVAATLLDSIGGIVAMEHLYRRSTPETLTETIKQVSRLATVDMRVDYLAPGRGKYFIAR 131
Cdd:PRK11688  40 ELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILARHEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTAT 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488050389 132 AEVLRLGRKGCTMRMTMVNDEDKAIAAGIASY 163
Cdd:PRK11688 120 SSVLRAGNKVAVARMELHNEQGVHIASGTATY 151
 
Name Accession Description Interval E-value
PRK11688 PRK11688
thioesterase family protein;
52-163 7.73e-41

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 134.20  E-value: 7.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  52 EGYIEMQPNLIGNLAFQILHGGVAATLLDSIGGIVAMEHLYRRSTPETLTETIKQVSRLATVDMRVDYLAPGRGKYFIAR 131
Cdd:PRK11688  40 ELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILARHEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTAT 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488050389 132 AEVLRLGRKGCTMRMTMVNDEDKAIAAGIASY 163
Cdd:PRK11688 120 SSVLRAGNKVAVARMELHNEQGVHIASGTATY 151
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
21-164 1.29e-21

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.61  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  21 TVVLNQLCKAFNSSPFFKHSGM-IMRVVDGHIEGYIEMQPNLIGNlaFQILHGGVAATLLDSIGGIVAMEHLyrrstpet 99
Cdd:COG2050    2 SDPLERLEGFLAANPFAELLGIeLVEVEPGRAVLRLPVRPEHLNP--PGTVHGGALAALADSAAGLAANSAL-------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488050389 100 ltetiKQVSRLATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAAGIASYA 164
Cdd:COG2050   72 -----PPGRRAVTIELNINFLRPARlGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
45-164 6.21e-21

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: 82.22  E-value: 6.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  45 RVVDGHIEGYIEMQPNLIGnlAFQILHGGVAATLLDSIGGIVAMEHLYRRSTPetltetikqvsrlATVDMRVDYLAPGR 124
Cdd:cd03443    8 EVGPGRVVLRLPVRPRHLN--PGGIVHGGAIATLADTAGGLAALSALPPGALA-------------VTVDLNVNYLRPAR 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488050389 125 GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAAGIASYA 164
Cdd:cd03443   73 GGDLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFA 112
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
67-157 5.35e-10

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: 53.03  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389   67 FQILHGGVAATLLDSIGGIVAMEHLYRRSTPetltetikqvsrlATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMR 145
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVV-------------VVVELSIDFLRPARlGDRLTVEARVVRLGRTSAVVE 67
                          90
                  ....*....|..
gi 488050389  146 MTMVNDEDKAIA 157
Cdd:pfam03061  68 VEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
35-157 7.80e-10

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: 53.50  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389   35 PFFKHSGM-IMRVVDGHIEGYIEMQPNLIGNlaFQILHGGVAATLLDSIGGIVAMEhlyrrSTPETLTetikqvsrLATV 113
Cdd:TIGR00369   1 PLVSFLGIeIEELGDGFLEATMPVDERTLQP--FGSLHGGVSAALADTAGSAAGYL-----CNSGGQA--------VVGL 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 488050389  114 DMRVDYLAPGRGKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIA 157
Cdd:TIGR00369  66 ELNANHLRPAREGKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
 
Name Accession Description Interval E-value
PRK11688 PRK11688
thioesterase family protein;
52-163 7.73e-41

thioesterase family protein;


Pssm-ID: 183276  Cd Length: 154  Bit Score: 134.20  E-value: 7.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  52 EGYIEMQPNLIGNLAFQILHGGVAATLLDSIGGIVAMEHLYRRSTPETLTETIKQVSRLATVDMRVDYLAPGRGKYFIAR 131
Cdd:PRK11688  40 ELSFKMQPELVGNIAQSILHGGVIASVLDVAGGLVCVGGILARHEDISEEELRQRLSRLGTIDLRVDYLRPGRGERFTAT 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488050389 132 AEVLRLGRKGCTMRMTMVNDEDKAIAAGIASY 163
Cdd:PRK11688 120 SSVLRAGNKVAVARMELHNEQGVHIASGTATY 151
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
21-164 1.29e-21

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 84.61  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  21 TVVLNQLCKAFNSSPFFKHSGM-IMRVVDGHIEGYIEMQPNLIGNlaFQILHGGVAATLLDSIGGIVAMEHLyrrstpet 99
Cdd:COG2050    2 SDPLERLEGFLAANPFAELLGIeLVEVEPGRAVLRLPVRPEHLNP--PGTVHGGALAALADSAAGLAANSAL-------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488050389 100 ltetiKQVSRLATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAAGIASYA 164
Cdd:COG2050   72 -----PPGRRAVTIELNINFLRPARlGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFA 132
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
45-164 6.21e-21

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: 82.22  E-value: 6.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  45 RVVDGHIEGYIEMQPNLIGnlAFQILHGGVAATLLDSIGGIVAMEHLYRRSTPetltetikqvsrlATVDMRVDYLAPGR 124
Cdd:cd03443    8 EVGPGRVVLRLPVRPRHLN--PGGIVHGGAIATLADTAGGLAALSALPPGALA-------------VTVDLNVNYLRPAR 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488050389 125 GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAAGIASYA 164
Cdd:cd03443   73 GGDLTARARVVKLGRRLAVVEVEVTDEDGKLVATARGTFA 112
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
67-157 5.35e-10

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: 53.03  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389   67 FQILHGGVAATLLDSIGGIVAMEHLYRRSTPetltetikqvsrlATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMR 145
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQQVV-------------VVVELSIDFLRPARlGDRLTVEARVVRLGRTSAVVE 67
                          90
                  ....*....|..
gi 488050389  146 MTMVNDEDKAIA 157
Cdd:pfam03061  68 VEVRDEDGRLVA 79
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
35-157 7.80e-10

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: 53.50  E-value: 7.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389   35 PFFKHSGM-IMRVVDGHIEGYIEMQPNLIGNlaFQILHGGVAATLLDSIGGIVAMEhlyrrSTPETLTetikqvsrLATV 113
Cdd:TIGR00369   1 PLVSFLGIeIEELGDGFLEATMPVDERTLQP--FGSLHGGVSAALADTAGSAAGYL-----CNSGGQA--------VVGL 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 488050389  114 DMRVDYLAPGRGKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIA 157
Cdd:TIGR00369  66 ELNANHLRPAREGKVRAIAQVVHLGRQTGVAEIEIVDEQGRLCA 109
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
66-164 1.21e-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: 52.48  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389  66 AFQILHGGVAATLLDSIGGIVAMEHLYRRStpetltetikqvsRLATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTM 144
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGGRGL-------------GAVTLSLDVRFLRPVRpGDTLTVEAEVVRVGRSSVTV 80
                         90       100
                 ....*....|....*....|
gi 488050389 145 RMTMVNDEDKAIAAGIASYA 164
Cdd:cd03440   81 EVEVRNEDGKLVATATATFV 100
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
110-158 6.19e-04

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 37.96  E-value: 6.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488050389 110 LATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAA 158
Cdd:COG0824   57 LVVVEAEIDYLRPARyGDELTVETRVVRLGGSSLTFEYEIFRADDGELLA 106
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
110-165 1.59e-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: 36.43  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488050389 110 LATVDMRVDYLAPGR-GKYFIARAEVLRLGRKGCTMRMTMVNDEDKAIAAGIASYAY 165
Cdd:cd00586   52 LVVVELEIDYLRPLRlGDRLTVETRVLRLGRKSFTFEQEIFREDGELLATAETVLVC 108
4HBT_3 pfam13622
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
71-164 7.79e-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: 35.39  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488050389   71 HGG-VAATLLdsiggiVAMEhlyRRSTPETLtetikqVSrlatvdMRVDYLAPGRGKYFIARAEVLRLGRKGCTMRMTMV 149
Cdd:pfam13622  12 HGGyVAALLL------RAAE---RTVPPDPL------HS------LHVDFLRPVPPGPVTIRVEVVRDGRSFSTRRVELS 70
                          90
                  ....*....|....*
gi 488050389  150 NDeDKAIAAGIASYA 164
Cdd:pfam13622  71 QD-GRVVVTATATFG 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH