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Conserved domains on  [gi|1080949426|gb|OFR08566|]
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acyl-CoA thioesterase [Staphylococcus sp. HMSC078E07]

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];
10-155 1.11e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


:

Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 200.02  E-value: 1.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  10 SMSESKSIKTRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGS 89
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080949426  90 SSMEICVQIIIEDVLNKERHLAALSFLTFVALDENGKPTRIPKVYPETKIEKWFYEGAPKRVQRRK 155
Cdd:COG1607    81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 1.11e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 200.02  E-value: 1.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  10 SMSESKSIKTRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGS 89
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080949426  90 SSMEICVQIIIEDVLNKERHLAALSFLTFVALDENGKPTRIPKVYPETKIEKWFYEGAPKRVQRRK 155
Cdd:COG1607    81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 2.66e-48

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: 152.72  E-value: 2.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426   9 KSMSESKSIKTRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAG 88
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1080949426  89 SSSMEICVQIIIEDVLNKERHLAALSFLTFVALDENGKPTRIP 131
Cdd:cd03442    81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
24-131 4.39e-19

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 78.36  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQIIIEDV 103
Cdd:PRK10694   20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1080949426 104 LNK---ERHLAALSFLTFVALDENGKPTRIP 131
Cdd:PRK10694  100 ASEpigQRYKATEALFTYVAVDPEGKPRALP 130
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 5.18e-15

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: 66.51  E-value: 5.18e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080949426  30 HHTMFGGSLMANIDEIAAITAMKHANA-QVVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQIIIED 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
 
Name Accession Description Interval E-value
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
10-155 1.11e-66

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 200.02  E-value: 1.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  10 SMSESKSIKTRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGS 89
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDEAAAIAAARHARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1080949426  90 SSMEICVQIIIEDVLNKERHLAALSFLTFVALDENGKPTRIPKVYPETKIEKWFYEGAPKRVQRRK 155
Cdd:COG1607    81 TSMEVGVEVWAEDLRTGERRLVTEAYFTFVAVDEDGKPRPVPPLIPETEEEKRLFEEALRRRELRL 146
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 9-131 2.66e-48

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: 152.72  E-value: 2.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426   9 KSMSESKSIKTRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAG 88
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDELAGIAAYRHAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1080949426  89 SSSMEICVQIIIEDVLNKERHLAALSFLTFVALDENGKPTRIP 131
Cdd:cd03442    81 RTSMEVGVEVEAEDPLTGERRLVTSAYFTFVALDEDGKPRPVP 123
PRK10694 PRK10694
acyl-CoA thioester hydrolase YciA;
24-131 4.39e-19

acyl-CoA thioester hydrolase YciA;


Pssm-ID: 236736 [Multi-domain]  Cd Length: 133  Bit Score: 78.36  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQIIIEDV 103
Cdd:PRK10694   20 PADTNANGDIFGGWLMSQMDIGGAILAKEIAHGRVVTVRVEGMTFLRPVAVGDVVCCYARCVKTGTTSISINIEVWVKKV 99

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1080949426 104 LNK---ERHLAALSFLTFVALDENGKPTRIP 131
Cdd:PRK10694  100 ASEpigQRYKATEALFTYVAVDPEGKPRALP 130
PLN02647 PLN02647
acyl-CoA thioesterase
 36-166 2.09e-15

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 72.90  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  36 GSLMANIDEIAAITAMKHANAQ--------VVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQII--IEDVLN 105
Cdd:PLN02647  114 GKLLEDLDALAGTISVKHCSDDdsttrpllLVTASVDKIVLKKPIRVDVDLKIVGAVTWVGRSSMEIQLEVIqpTKDESN 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080949426 106 KERHLAALSFLTFVALD-ENGKPTRIPKVYPETKIEKWFYEGAPKRVQRRKERREESKKTIE 166
Cdd:PLN02647  194 TSDSVALTANFTFVARDsKTGKSAPVNRLSPETEEEKLLFEEAEARNKLRKKKRGEQKREFE 255
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 30-102 5.18e-15

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: 66.51  E-value: 5.18e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080949426  30 HHTMFGGSLMANIDEIAAITAMKHANA-QVVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQIIIED 102
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSqQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 19-119 2.90e-13

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: 62.49  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  19 TRQVFPQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSYEAMVSYAGSSSMEICVQ 97
Cdd:cd03440     4 RLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSlDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVE 83

                          90       100
                  ....*....|....*....|..
gi 1080949426  98 IIiedvlNKERHLAALSFLTFV 119
Cdd:cd03440    84 VR-----NEDGKLVATATATFV 100
PLN02647 PLN02647
acyl-CoA thioesterase
 24-140 2.04e-06

acyl-CoA thioesterase


Pssm-ID: 215349 [Multi-domain]  Cd Length: 437  Bit Score: 46.71  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  24 PQDTNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTDSVDFLRPIKTGDITSYEAMVSYAGSSSMEiCVQIIIEDV 103
Cdd:PLN02647  299 PQQRNIHGRIFGGFLMRRAFELAFSTAYAFAGLRPYFLEVDHVDFLRPVDVGDFLRFKSCVLYTELENSE-QPLINVEVV 377

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1080949426 104 LNKERHLAALS------FLTFVALDENGKPT--RIPKVYPETKIE 140
Cdd:PLN02647  378 AHVTRPELRSSevsntfYFTFTVRPEAAMKNgfKIRNVVPATEEE 422
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 27-111 2.48e-06

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: 44.09  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  27 TNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSyEAMVSYAGSSSmeICVQIIIEDvlN 105
Cdd:cd03443    25 LNPGGIVHGGAIATLADTAGGLAALSALPPGALAVTVDlNVNYLRPARGGDLTA-RARVVKLGRRL--AVVEVEVTD--E 99


                  ....*.
gi 1080949426 106 KERHLA 111
Cdd:cd03443   100 DGKLVA 105
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 27-124 3.49e-06

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 44.55  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  27 TNHHHTMFGGSLMANIDEIAAITAMKHANAQVVTASTD-SVDFLRPIKTGDITSYEAMVSYAGSSSMEICVqiiieDVLN 105
Cdd:COG2050    44 LNPPGTVHGGALAALADSAAGLAANSALPPGRRAVTIElNINFLRPARLGDRLTAEARVVRRGRRLAVVEV-----EVTD 118

                          90
                  ....*....|....*....
gi 1080949426 106 KERHLAALSFLTFVALDEN 124
Cdd:COG2050   119 EDGKLVATATGTFAVLPKR 137
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 11-143 9.17e-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: 40.65  E-value: 9.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  11 MSESKSIKTRQVFPQDT------NHHH--TMFGGSLMANIDEIA-AITAMKHANAQVVTASTdSVDFLRPIKTGDITSYE 81
Cdd:COG0824     1 MTLFTFETPIRVRFGDTdamghvNNANylRYFEEARTEFLRALGlSYAELEEEGIGLVVVEA-EIDYLRPARYGDELTVE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1080949426  82 AMVSYAGSSSMEICVQIIIEDvlnkERHLAALSFLTFVALD-ENGKPTRIPKVYPEtKIEKWF 143
Cdd:COG0824    80 TRVVRLGGSSLTFEYEIFRAD----DGELLATGETVLVFVDlETGRPVPLPDELRA-ALEALL 137
YiiD_C pfam09500
Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed ...
 28-121 2.52e-04

Putative thioesterase (yiiD_Cterm); This entry consists of a broadly distributed uncharacterized domain often found as a standalone protein. The member from Shewanella oneidensis is described from crystallography work as a putative thioesterase because it belongs to the HotDog clan of enzymes. About half of the members of this family are fused to an Acetyltransf_1 domain pfam00583.


Pssm-ID: 430649  Cd Length: 144  Bit Score: 39.16  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080949426  28 NHHHTMFGGSLMAnideIAAITA-------MKHA--NAQVVTASTDsVDFLRPIK---------------TGDITSYEAm 83
Cdd:pfam09500  41 NHHGTMFAGSIYT----LATLTGwgllwllLKEAglEGDIVLADGN-IRYLKPVTgdptarvslptpeawSGFLSRLAR- 114

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1080949426  84 vsyAGSSSMEICVQIIIEDVLnkerhlaALSFL-TFVAL 121
Cdd:pfam09500 115 ---GGKARITLEVEIYSGGEL-------AAEFTgRYVVL 143
 
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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