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Conserved domains on  [gi|1232154020|gb|OYU86828|]
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MAG: acyl-CoA thioesterase [Bradyrhizobiaceae bacterium PARB1]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10787832)

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

CATH:  3.10.129.10
EC:  3.1.2.-
Gene Ontology:  GO:0016790|GO:0016787
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
12-124 6.90e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 150.72  E-value: 6.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  12 VRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVN 91
Cdd:COG1607     7 LTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232154020  92 VEVTAETLVTGQRRRAMHGSFEMIAVDDSGRPR 124
Cdd:COG1607    87 VEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPR 119
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
12-124 6.90e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 150.72  E-value: 6.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  12 VRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVN 91
Cdd:COG1607     7 LTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232154020  92 VEVTAETLVTGQRRRAMHGSFEMIAVDDSGRPR 124
Cdd:COG1607    87 VEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPR 119
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 11-124 4.27e-39

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: 127.69  E-value: 4.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  11 PVRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTV 90
Cdd:cd03442     7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232154020  91 NVEVTAETLVTGQRRRAMHGSFEMIAVDDSGRPR 124
Cdd:cd03442    87 GVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPR 120
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
17-126 8.64e-14

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 63.34  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  17 LVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVNVEVTA 96
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232154020  97 ETLVT---GQRRRAMHGSFEMIAVDDSGRPRGV 126
Cdd:PRK10694   97 KKVASepiGQRYKATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-102 3.24e-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: 58.04  E-value: 3.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232154020  26 YGTLFGGNALSLMGKAAFVAATRHAR-CAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVNVEVTAETLVTG 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
12-124 6.90e-48

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 150.72  E-value: 6.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  12 VRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVN 91
Cdd:COG1607     7 LTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGRTSMEVG 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232154020  92 VEVTAETLVTGQRRRAMHGSFEMIAVDDSGRPR 124
Cdd:COG1607    87 VEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPR 119
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 11-124 4.27e-39

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: 127.69  E-value: 4.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  11 PVRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTV 90
Cdd:cd03442     7 ELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTGRTSMEV 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232154020  91 NVEVTAETLVTGQRRRAMHGSFEMIAVDDSGRPR 124
Cdd:cd03442    87 GVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPR 120
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
17-126 8.64e-14

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 63.34  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  17 LVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVNVEVTA 96
Cdd:PRK10694   17 LAMPADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWV 96

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232154020  97 ETLVT---GQRRRAMHGSFEMIAVDDSGRPRGV 126
Cdd:PRK10694   97 KKVASepiGQRYKATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 26-102 3.24e-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: 58.04  E-value: 3.24e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232154020  26 YGTLFGGNALSLMGKAAFVAATRHAR-CAVVMASTDHVQFETPVQVGELAELTSWVSRIGRSSMTVNVEVTAETLVTG 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 12-98 3.52e-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: 50.55  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  12 VRFVELVFPDQANHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTD-HVQFETPVQVGELAELTSWVSRIGRSSMTV 90
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80


                  ....*...
gi 1232154020  91 NVEVTAET 98
Cdd:cd03440    81 EVEVRNED 88
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-124 1.31e-05

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: 41.81  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020   1 MSPEAALQSEPVRFVELvfpDQANHygtLFGGNALSLMGKAAF---------VAATRHARCAVVMASTdHVQFETPVQVG 71
Cdd:COG0824     1 MTLFTFETPIRVRFGDT---DAMGH---VNNANYLRYFEEARTeflralglsYAELEEEGIGLVVVEA-EIDYLRPARYG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1232154020  72 ELAELTSWVSRIGRSSMTVNVEVTAEtlvtGQRRRAMHGSFEMIAVD-DSGRPR 124
Cdd:COG0824    74 DELTVETRVVRLGGSSLTFEYEIFRA----DDGELLATGETVLVFVDlETGRPV 123
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 20-97 1.81e-04

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 38.77  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  20 PDQANHYGTLFGGnAL-----SLMGKAAFVAATRHARCAVVMASTDHVQfetPVQVGELAELTSWVSRIGRSSMTVNVEV 94
Cdd:COG2050    41 PEHLNPPGTVHGG-ALaaladSAAGLAANSALPPGRRAVTIELNINFLR---PARLGDRLTAEARVVRRGRRLAVVEVEV 116


                  ...
gi 1232154020  95 TAE 97
Cdd:COG2050   117 TDE 119
PLN02647 PLN02647
acyl-CoA thioesterase
 20-96 7.50e-04

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 38.23  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  20 PDQANHYGTLFGGnalSLMGKA---AFVAATRHARCAVVMASTDHVQFETPVQVGELAELTSWV--SRIGRSSMT-VNVE 93
Cdd:PLN02647  299 PQQRNIHGRIFGG---FLMRRAfelAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVlyTELENSEQPlINVE 375


                  ...
gi 1232154020  94 VTA 96
Cdd:PLN02647  376 VVA 378
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 11-118 8.06e-04

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: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  11 PVRFVELvfpDQANH-----YGTLFGGNALSLMGKAAFVAATRHAR-CAVVMASTdHVQFETPVQVGELAELTSWVSRIG 84
Cdd:cd00586     6 RVRFGDT---DAAGHvnnarYLRYFEEAREEFLRELGLGYDELEEQgLGLVVVEL-EIDYLRPLRLGDRLTVETRVLRLG 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232154020  85 RSSMTVNVEVTAETlvtgqRRRAMHGSFEMIAVD 118
Cdd:cd00586    82 RKSFTFEQEIFRED-----GELLATAETVLVCVD 110
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 15-98 3.08e-03

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: 34.84  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232154020  15 VELVFPDQA---NHYGTLFGGNALSLMGKAAFVAATRHARCAVVMASTD-HVQFETPVQVGELaELTSWVSRIGRSSMTV 90
Cdd:cd03443    14 VVLRLPVRPrhlNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDL-TARARVVKLGRRLAVV 92


                  ....*...
gi 1232154020  91 NVEVTAET 98
Cdd:cd03443    93 EVEVTDED 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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