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Conserved domains on  [gi|428243935|gb|AFZ09721|]
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1,4-dihydroxy-2-naphthoyl-CoA hydrolase [Oscillatoria nigro-viridis PCC 7112]

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 ...
 1-136 3.94e-31

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: 108.45  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   1 MPFTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTP 80
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEE-GIGLVVVEAEIDYLRPARYGDELTVETRV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 428243935  81 KQVTGDEFEIAYQVFSEEvAGRSAAKALTKHVCIDAVSRNRKQLSEDLMQWMRKFE 136
Cdd:COG0824   83 VRLGGSSLTFEYEIFRAD-DGELLATGETVLVFVDLETGRPVPLPDELRAALEALL 137
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-136 3.94e-31

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: 108.45  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   1 MPFTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTP 80
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEE-GIGLVVVEAEIDYLRPARYGDELTVETRV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 428243935  81 KQVTGDEFEIAYQVFSEEvAGRSAAKALTKHVCIDAVSRNRKQLSEDLMQWMRKFE 136
Cdd:COG0824   83 VRLGGSSLTFEYEIFRAD-DGELLATGETVLVFVDLETGRPVPLPDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-115 2.86e-26

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: 94.98  E-value: 2.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   3 FTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLkAFFSNPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQ 82
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGY-DELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 428243935  83 VTGDEFEIAYQVFSEEvaGRSAAKALTKHVCID 115
Cdd:cd00586   80 LGRKSFTFEQEIFRED--GELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 9-132 6.23e-19

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: 76.61  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935    9 VRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFsNPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEF 88
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYRE-ALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 428243935   89 EIAYQVFSEEvaGRSAAKALTKHVCIDAVSRNRKQLSEDLMQWM 132
Cdd:pfam13279  80 HLEHRFLSPD--GKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 9-115 3.50e-12

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: 58.97  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935    9 VRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEF 88
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAE-GVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSF 82

                          90       100
                  ....*....|....*....|....*..
gi 428243935   89 EIAYQVFSEEVAgrSAAKALTKHVCID 115
Cdd:TIGR00051  83 VFSQEIFNEDEA--LLKAATVIVVCVD 107
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 3-115 8.29e-04

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 37.03  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   3 FTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQ 82
Cdd:PRK10800   3 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAE-RVAFVVRKMTVEYYAPARLDDMLEVQSEITS 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 428243935  83 VTGDEFEIAYQVFSEEVAGRSAAKALTkhVCID 115
Cdd:PRK10800  82 MRGTSLTFTQRIVNAEGTLLNEAEVLI--VCVD 112
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 1-136 3.94e-31

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: 108.45  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   1 MPFTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTP 80
Cdd:COG0824    4 FTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEE-GIGLVVVEAEIDYLRPARYGDELTVETRV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 428243935  81 KQVTGDEFEIAYQVFSEEvAGRSAAKALTKHVCIDAVSRNRKQLSEDLMQWMRKFE 136
Cdd:COG0824   83 VRLGGSSLTFEYEIFRAD-DGELLATGETVLVFVDLETGRPVPLPDELRAALEALL 137
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-115 2.86e-26

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: 94.98  E-value: 2.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   3 FTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLkAFFSNPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQ 82
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGY-DELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 428243935  83 VTGDEFEIAYQVFSEEvaGRSAAKALTKHVCID 115
Cdd:cd00586   80 LGRKSFTFEQEIFRED--GELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 9-132 6.23e-19

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: 76.61  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935    9 VRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFsNPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEF 88
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAYRE-ALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 428243935   89 EIAYQVFSEEvaGRSAAKALTKHVCIDAVSRNRKQLSEDLMQWM 132
Cdd:pfam13279  80 HLEHRFLSPD--GKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 9-115 3.50e-12

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: 58.97  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935    9 VRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEF 88
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAE-GVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSF 82

                          90       100
                  ....*....|....*....|....*..
gi 428243935   89 EIAYQVFSEEVAgrSAAKALTKHVCID 115
Cdd:TIGR00051  83 VFSQEIFNEDEA--LLKAATVIVVCVD 107
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 3-112 5.40e-10

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: 52.86  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   3 FTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGInlkaffsnPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQ 82
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGG--------RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVR 72

                         90       100       110
                 ....*....|....*....|....*....|
gi 428243935  83 VTGDEFEIAYQVFSEEvaGRSAAKALTKHV 112
Cdd:cd03440   73 VGRSSVTVEVEVRNED--GKLVATATATFV 100
thio_ybgC TIGR02799
tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical ...
 9-116 2.82e-08

tol-pal system-associated acyl-CoA thioesterase; The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism).


Pssm-ID: 274304  Cd Length: 126  Bit Score: 49.13  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935    9 VRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEF 88
Cdd:TIGR02799   7 VYYEDTDAGGVVYHANYLRFMERARTEWLRALGFEQSALLEETGLVFVVRSMELDYLKPARLDDLLTVTTRVVELKGASL 86

                          90       100
                  ....*....|....*....|....*...
gi 428243935   89 EIAYQVFSEEVAgrsAAKALTKHVCIDA 116
Cdd:TIGR02799  87 VFAQEVRRGDTL---LCEATVEVACVDA 111
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 18-98 3.51e-07

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: 44.94  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   18 GVVYFANVLAMCHEAyeASLAASGINLkaffsnPEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQVTGDEFEIAYQVFSE 97
Cdd:pfam03061   2 GVVHGGVYLALADEA--AGAAARRLGG------SQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  .
gi 428243935   98 E 98
Cdd:pfam03061  74 D 74
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 3-115 8.29e-04

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 37.03  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428243935   3 FTYTRTVRFQDTDAAGVVYFANVLAMCHEAYEASLAASGINLKAFFSNpEVAFPIIHASVDFYRPMFAGDRLIIQLTPKQ 82
Cdd:PRK10800   3 FRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALLAE-RVAFVVRKMTVEYYAPARLDDMLEVQSEITS 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 428243935  83 VTGDEFEIAYQVFSEEVAGRSAAKALTkhVCID 115
Cdd:PRK10800  82 MRGTSLTFTQRIVNAEGTLLNEAEVLI--VCVD 112
 
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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