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Conserved domains on  [gi|1081394526|gb|OFV31051|]
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4-hydroxybenzoyl-CoA thioesterase [Staphylococcus sp. HMSC14D10]

Protein Classification

acyl-CoA thioesterase( domain architecture ID 10002786)

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
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-133 1.52e-41

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: 135.41  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:COG0824     8 TPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1081394526  86 LKSVYCYEVYNE-NGELATTGSTQLICMKSSNFQPIRLDRYFPEWHKVY 133
Cdd:COG0824    88 SSLTFEYEIFRAdDGELLATGETVLVFVDLETGRPVPLPDELRAALEAL 136
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-133 1.52e-41

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: 135.41  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:COG0824     8 TPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1081394526  86 LKSVYCYEVYNE-NGELATTGSTQLICMKSSNFQPIRLDRYFPEWHKVY 133
Cdd:COG0824    88 SSLTFEYEIFRAdDGELLATGETVLVFVDLETGRPVPLPDELRAALEAL 136
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-112 9.83e-36

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: 119.63  E-value: 9.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:cd00586     3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                          90       100
                  ....*....|....*....|....*..
gi 1081394526  86 LKSVYCYEVYNENGELATTGSTQLICM 112
Cdd:cd00586    83 KSFTFEQEIFREDGELLATAETVLVCV 109
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 11-122 1.49e-31

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 109.43  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  11 RYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVY 90
Cdd:TIGR00051   5 YYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFVF 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1081394526  91 CYEVYNENGELATTGSTQLICMKSSNFQPIRL 122
Cdd:TIGR00051  85 SQEIFNEDEALLKAATVIVVCVDPKKQKPVAI 116
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 18-102 1.71e-18

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: 74.60  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  18 MGVIYHGNYATWFEVARTDYIRKLGFSYadmekegIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVYCYEVYNE 97
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ-------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*
gi 1081394526  98 NGELA 102
Cdd:pfam03061  74 DGRLV 78
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 12-122 4.88e-08

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 48.97  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  12 YQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVYC 91
Cdd:PRK10800   11 YEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFT 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1081394526  92 YEVYNENGELATTGSTQLICMKSSNFQPIRL 122
Cdd:PRK10800   91 QRIVNAEGTLLNEAEVLIVCVDPLKMKPRAL 121
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 6-133 1.52e-41

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: 135.41  E-value: 1.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:COG0824     8 TPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1081394526  86 LKSVYCYEVYNE-NGELATTGSTQLICMKSSNFQPIRLDRYFPEWHKVY 133
Cdd:COG0824    88 SSLTFEYEIFRAdDGELLATGETVLVFVDLETGRPVPLPDELRAALEAL 136
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 6-112 9.83e-36

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: 119.63  E-value: 9.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:cd00586     3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                          90       100
                  ....*....|....*....|....*..
gi 1081394526  86 LKSVYCYEVYNENGELATTGSTQLICM 112
Cdd:cd00586    83 KSFTFEQEIFREDGELLATAETVLVCV 109
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 11-122 1.49e-31

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 109.43  E-value: 1.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  11 RYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVY 90
Cdd:TIGR00051   5 YYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFVF 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1081394526  91 CYEVYNENGELATTGSTQLICMKSSNFQPIRL 122
Cdd:TIGR00051  85 SQEIFNEDEALLKAATVIVVCVDPKKQKPVAI 116
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 18-102 1.71e-18

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: 74.60  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  18 MGVIYHGNYATWFEVARTDYIRKLGFSYadmekegIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVYCYEVYNE 97
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ-------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*
gi 1081394526  98 NGELA 102
Cdd:pfam03061  74 DGRLV 78
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 6-107 3.60e-16

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: 69.43  E-value: 3.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526   6 TEIEARYQETDKMGVIYHGNYATWFEVARTDYIRKLGFsyadmekEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSR 85
Cdd:cd03440     3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG-------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGR 75

                          90       100
                  ....*....|....*....|..
gi 1081394526  86 LKSVYCYEVYNENGELATTGST 107
Cdd:cd03440    76 SSVTVEVEVRNEDGKLVATATA 97
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-129 4.29e-15

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 66.98  E-value: 4.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  11 RYQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRlKSVY 90
Cdd:pfam13279   2 RPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDA-KRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1081394526  91 C-YEVYNENGELATTGSTQLICMKSSNFQPIRldryFPEW 129
Cdd:pfam13279  81 LeHRFLSPDGKLVATAETRLVFVDYETRKPAP----IPEE 116
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 12-122 4.88e-08

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 48.97  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  12 YQETDKMGVIYHGNYATWFEVARTDYIRKLGFSYADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLKSVYC 91
Cdd:PRK10800   11 YEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFT 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1081394526  92 YEVYNENGELATTGSTQLICMKSSNFQPIRL 122
Cdd:PRK10800   91 QRIVNAEGTLLNEAEVLIVCVDPLKMKPRAL 121
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 35-156 8.55e-04

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 38.10  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1081394526  35 TDYIRKLGFS-YADMEKEGIISPVVDLQIKYRKSIFYPEKVTIKTWVEQYSRLksvYCY---EVYNENGELATTGSTQLI 110
Cdd:pfam01643  35 ADQSEELGLSdDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETWASSYNKF---FCYrrfRVYDEKGEKIIEAKSTWV 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1081394526 111 CMkssNFQPIRLDRYFPEWHKVYSH--VDKLNQDGKDFE---VTQSSDLEI 156
Cdd:pfam01643 112 LM---DRETRRPHRVPDEIRAPYQSesIEKLIRGPKTKPgkpIEESTEKEY 159
 
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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