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Conserved domains on  [gi|302326255|gb|ADL25456|]
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conserved hypothetical protein [Fibrobacter succinogenes subsp. succinogenes S85]

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 ...
 30-161 1.23e-25

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: 94.96  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  30 NPMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTW 108
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSyAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302326255 109 VAGYSKVASVRKCRFERVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQ 161
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 30-161 1.23e-25

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: 94.96  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  30 NPMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTW 108
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSyAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302326255 109 VAGYSKVASVRKCRFERVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQ 161
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 34-143 1.07e-16

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: 71.10  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  34 FEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTWVAGY 112
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGyDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 302326255 113 SKVASVRKCRFERvSDGKVVFESETQWVLMD 143
Cdd:cd00586   81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 31-161 1.85e-12

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: 62.75  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255   31 PMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGATD--VMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTW 108
Cdd:pfam01643   1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLSDdgFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 302326255  109 VAGYSKVASVRKCRFeRVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQ 161
Cdd:pfam01643  81 ASSYNKFFCYRRFRV-YDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQ 132
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 30-161 1.23e-25

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: 94.96  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  30 NPMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTW 108
Cdd:COG0824    2 TLFTFETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSyAELEEEGIGLVVVEAEIDYLRPARYGDELTVETR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302326255 109 VAGYSKVASVRKCRFERVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQ 161
Cdd:COG0824   82 VVRLGGSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
34-162 1.09e-19

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 82.31  E-value: 1.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  34 FEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTWVAGY 112
Cdd:COG3884    1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGiDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSGY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 302326255 113 SKVASVRkcRFE-RVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQV 162
Cdd:COG3884   81 NRFFAYR--DFRiLDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGL 129
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 34-143 1.07e-16

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: 71.10  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  34 FEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGAT-DVMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTWVAGY 112
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGyDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 302326255 113 SKVASVRKCRFERvSDGKVVFESETQWVLMD 143
Cdd:cd00586   81 GRKSFTFEQEIFR-EDGELLATAETVLVCVD 110
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 31-161 1.85e-12

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: 62.75  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255   31 PMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGATD--VMYQFGCGWMIHTQFVEYKNQAFLGDEIRGTTW 108
Cdd:pfam01643   1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLSDdgFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 302326255  109 VAGYSKVASVRKCRFeRVSDGKVVFESETQWVLMDMKKGRPFAIPQEIKDRFQ 161
Cdd:pfam01643  81 ASSYNKFFCYRRFRV-YDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQ 132
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 40-160 9.48e-08

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: 48.11  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255   40 VTPEMIDENKHMNNVWAVQWVqDISIAHSDSVGATDVMYQFGCGWMIHT--QFVEYKNQAFLGDEIRGTTWVAGYSkvAS 117
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYF-EEARDRFLERLGLDLAYREALGIGLILaeAHVRYRRELKLGDELTVETRLIDWD--AK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 302326255  118 VRKCRFERVS-DGKVVFESETQWVLMDMKKGRPFAIPQEIKDRF 160
Cdd:pfam13279  78 RFHLEHRFLSpDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 38-140 8.79e-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: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  38 FKVTPEMIDENKHMNNVWAVQWVQDISIAHSDSVGATdvmyqfGCGWMIHTQFVEYKNQAFLGDEIRGTTWVAGYSKVAS 117
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGR------GLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSV 78

                         90       100
                 ....*....|....*....|...
gi 302326255 118 VRKCRFeRVSDGKVVFESETQWV 140
Cdd:cd03440   79 TVEVEV-RNEDGKLVATATATFV 100
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
30-139 5.02e-06

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 44.94  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302326255  30 NPMKFEKLFKVTPEMIDENKHMNNVWAVQWVQDisiAHSDSVGATDVMYQFgcgwmihtqFVEYKNQAFLGDEIRGTTWV 109
Cdd:COG3884  146 EDDEEEKEFTVRYSDIDTNGHVNNARYLEWALD---ALPLEFLKNHRLKRL---------EINYLKEVRLGDTVEVRSAR 213

                         90       100       110
                 ....*....|....*....|....*....|
gi 302326255 110 AGyskvASVRKCRFERVSDGKVVFESETQW 139
Cdd:COG3884  214 DE----DGRTLHRIVGDDDGKELARARIEW 239
 
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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