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Conserved domains on  [gi|757600349|ref|WP_042847983|]
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MULTISPECIES: acyl-CoA thioesterase [Providencia]

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];
12-132 6.42e-54

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 166.12  E-value: 6.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  12 KIEQSISRVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGR 91
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 757600349  92 TSLTVNVSIFLEDMYSEGREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPV 121
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
12-132 6.42e-54

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 166.12  E-value: 6.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  12 KIEQSISRVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGR 91
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 757600349  92 TSLTVNVSIFLEDMYSEGREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 11-132 1.60e-40

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: 131.54  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  11 QKIEQSISRVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVG 90
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 757600349  91 RTSLTVNVSIFLEDMYSEGREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
26-132 3.12e-16

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 69.89  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  26 PTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLEDM 105
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|
gi 757600349 106 YSE---GREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 32-104 1.92e-13

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: 61.12  E-value: 1.92e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757600349   32 HSTLFGGTALAWMDEVSFITATRF-SRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLED 104
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLgGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
12-132 6.42e-54

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 166.12  E-value: 6.42e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  12 KIEQSISRVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGR 91
Cdd:COG1607    1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 757600349  92 TSLTVNVSIFLEDMYSEGREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:COG1607   81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPV 121
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 11-132 1.60e-40

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: 131.54  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  11 QKIEQSISRVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVG 90
Cdd:cd03442    1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 757600349  91 RTSLTVNVSIFLEDMYSEGREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:cd03442   81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPV 122
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
26-132 3.12e-16

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 69.89  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  26 PTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLEDM 105
Cdd:PRK10694  20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                         90       100       110
                 ....*....|....*....|....*....|
gi 757600349 106 YSE---GREEVIHGQFNFVAIDDNGKPTPL 132
Cdd:PRK10694 100 ASEpigQRYKATEALFTYVAVDPEGKPRAL 129
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 32-104 1.92e-13

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: 61.12  E-value: 1.92e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757600349   32 HSTLFGGTALAWMDEVSFITATRF-SRKRLVTVSTEKINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLED 104
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLgGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 19-121 3.13e-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: 53.25  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  19 RVSKVVFPTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTE-KINFTHPIPSGTIVELVGKVIRVGRTSLTVN 97
Cdd:cd03440    2 VLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVE 81

                         90       100
                 ....*....|....*....|....
gi 757600349  98 VSIfledmYSEGREEVIHGQFNFV 121
Cdd:cd03440   82 VEV-----RNEDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 26-124 7.46e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 50.71  E-value: 7.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  26 PTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTE-KINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLED 104
Cdd:COG2050   41 PEHLNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDED 120

                         90       100
                 ....*....|....*....|
gi 757600349 105 mysegREEVIHGQFNFVAID 124
Cdd:COG2050  121 -----GKLVATATGTFAVLP 135
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 26-104 7.10e-07

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: 44.86  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600349  26 PTTTNHHSTLFGGTALAWMDEVSFITATRFSRKRLVTVSTE-KINFTHPIPSGTiVELVGKVIRVGRTSLTVNVSIFLED 104
Cdd:cd03443   22 PRHLNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGD-LTARARVVKLGRRLAVVEVEVTDED 100
PLN02647 PLN02647
acyl-CoA thioesterase
 60-132 1.23e-03

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 37.46  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757600349  60 LVTVSTEKINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLEDMYSEGREE--VIHGQFNFVAID-DNGKPTPL 132
Cdd:PLN02647 144 LVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIQPTKDESNTSDsvALTANFTFVARDsKTGKSAPV 219
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 60-132 1.40e-03

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: 36.41  E-value: 1.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757600349  60 LVTVSTEkINFTHPIPSGTIVELVGKVIRVGRTSLTVNVSIFLEDmyseGREEVIHGQFNFVAID-DNGKPTPL 132
Cdd:COG0824   57 LVVVEAE-IDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRAD----DGELLATGETVLVFVDlETGRPVPL 125
 
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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