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Conserved domains on  [gi|1781406437|dbj|GED95519|]
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putative acyl-CoA thioester hydrolase [Lentilactobacillus buchneri subsp. silagei]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 1903523)

acyl-CoA thioesterase catalyzes the hydrolysis of acyl-CoA esters to the free fatty acid and CoA; belongs to the Hotdog fold superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciA super family cl43465
Acyl-CoA hydrolase [Lipid transport and metabolism];
17-162 3.39e-15

Acyl-CoA hydrolase [Lipid transport and metabolism];


The actual alignment was detected with superfamily member COG1607:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 68.67  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  17 KCSDTRAIHESYVFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGNlsFVTAGYDHVQFLSPARPNEILTCISYVTGS 96
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGR--VVTASVDSVDFLRPVRVGDIVELYARVVRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  97 SKR----AVEVFTKFLTTDTKTKdVQVAFMAFCTLIVTNEISEIhfPELVGESAEEKYLLATYDDRLKER 162
Cdd:COG1607    79 GRTsmevGVEVWAEDLRTGERRL-VTEAYFTFVAVDEDGKPRPV--PPLIPETEEEKRLFEEALRRRELR 145
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
17-162 3.39e-15

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 68.67  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  17 KCSDTRAIHESYVFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGNlsFVTAGYDHVQFLSPARPNEILTCISYVTGS 96
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGR--VVTASVDSVDFLRPVRVGDIVELYARVVRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  97 SKR----AVEVFTKFLTTDTKTKdVQVAFMAFCTLIVTNEISEIhfPELVGESAEEKYLLATYDDRLKER 162
Cdd:COG1607    79 GRTsmevGVEVWAEDLRTGERRL-VTEAYFTFVAVDEDGKPRPV--PPLIPETEEEKRLFEEALRRRELR 145
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 29-120 5.58e-09

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 51.80  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  29 VFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGnlSFVTAGYDHVQFLSPARPNEILTCISYVTGSSKRAVEVFTKFL 108
Cdd:cd03442    14 VLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG--RVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVGVEVE 91

                          90
                  ....*....|..
gi 1781406437 109 TTDTKTKDVQVA 120
Cdd:cd03442    92 AEDPLTGERRLV 103
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-103 5.51e-03

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: 34.54  E-value: 5.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1781406437  41 FGGETLRILDANAGLAGVKFLPGNLSFVTAGyDHVQFLSPARPNEILTCISYVTGSSKRAVEV 103
Cdd:pfam03061   5 HGGVYLALADEAAGAAARRLGGSQQVVVVVE-LSIDFLRPARLGDRLTVEARVVRLGRTSAVV 66
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
17-162 3.39e-15

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 68.67  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  17 KCSDTRAIHESYVFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGNlsFVTAGYDHVQFLSPARPNEILTCISYVTGS 96
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGR--VVTASVDSVDFLRPVRVGDIVELYARVVRV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  97 SKR----AVEVFTKFLTTDTKTKdVQVAFMAFCTLIVTNEISEIhfPELVGESAEEKYLLATYDDRLKER 162
Cdd:COG1607    79 GRTsmevGVEVWAEDLRTGERRL-VTEAYFTFVAVDEDGKPRPV--PPLIPETEEEKRLFEEALRRRELR 145
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 29-120 5.58e-09

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 51.80  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  29 VFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGnlSFVTAGYDHVQFLSPARPNEILTCISYVTGSSKRAVEVFTKFL 108
Cdd:cd03442    14 VLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGG--RVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEVGVEVE 91

                          90
                  ....*....|..
gi 1781406437 109 TTDTKTKDVQVA 120
Cdd:cd03442    92 AEDPLTGERRLV 103
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 29-114 8.53e-07

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: 45.16  E-value: 8.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1781406437  29 VFPAQLNNNRIQFGGETLRILDANAGLAGVKFLPGNLSFVTAGYdHVQFLSPARPNEILTCISYVTGSSKRAVEVFTKFL 108
Cdd:cd03440     7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSL-DVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVR 85


                  ....*.
gi 1781406437 109 TTDTKT 114
Cdd:cd03440    86 NEDGKL 91
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 41-103 5.51e-03

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: 34.54  E-value: 5.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1781406437  41 FGGETLRILDANAGLAGVKFLPGNLSFVTAGyDHVQFLSPARPNEILTCISYVTGSSKRAVEV 103
Cdd:pfam03061   5 HGGVYLALADEAAGAAARRLGGSQQVVVVVE-LSIDFLRPARLGDRLTVEARVVRLGRTSAVV 66
 
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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