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Conserved domains on  [gi|1002248007|ref|XP_015628176|]
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1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1 [Oryza sativa Japonica Group]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 6-164 6.51e-70

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.


The actual alignment was detected with superfamily member PLN02322:

Pssm-ID: 469797  Cd Length: 154  Bit Score: 208.38  E-value: 6.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007   6 SSSSraprpKTEELDAALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGYSRVAGVQ 85
Cdd:PLN02322    1 SASS-----NTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002248007  86 LSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDPSTKEKGAQISESRVTLLCNLPVPESVKNAGEALKKYSKL 164
Cdd:PLN02322   76 LSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 6-164 6.51e-70

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 208.38  E-value: 6.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007   6 SSSSraprpKTEELDAALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGYSRVAGVQ 85
Cdd:PLN02322    1 SASS-----NTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002248007  86 LSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDPSTKEKGAQISESRVTLLCNLPVPESVKNAGEALKKYSKL 164
Cdd:PLN02322   76 LSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 20-121 3.99e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.15  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  20 DAALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGY-SRVAGVQLSINHFRSAALGD 98
Cdd:COG2050    15 NPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRPARLGD 94

                          90       100
                  ....*....|....*....|...
gi 1002248007  99 TVLVRAAPLHVGRSTQVWAVKLW 121
Cdd:COG2050    95 RLTAEARVVRRGRRLAVVEVEVT 117
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-140 1.91e-20

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: 81.06  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  25 AMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASG-YSRVAGVQLSINHFRSAALGDtVLVR 103
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGD-LTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002248007 104 AAPLHVGRSTQVWAVKLWkldpstKEKGAQISESRVT 140
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT------DEDGKLVATARGT 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 52-125 6.20e-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: 65.74  E-value: 6.20e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002248007  52 FKVLHGGVSALIAEGLASMGA-HMASGYSRVAGVQLSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDP 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAArRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-116 5.88e-13

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 61.59  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  21 AALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASM-GAHMASGYSRVAGVQLSINHFRSaALGDT 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAaGYLCNSGGQAVVGLELNANHLRP-AREGK 79

                          90
                  ....*....|....*..
gi 1002248007 100 VLVRAAPLHVGRSTQVW 116
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVA 96
 
Name Accession Description Interval E-value
PLN02322 PLN02322
acyl-CoA thioesterase
 6-164 6.51e-70

acyl-CoA thioesterase


Pssm-ID: 177956  Cd Length: 154  Bit Score: 208.38  E-value: 6.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007   6 SSSSraprpKTEELDAALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGYSRVAGVQ 85
Cdd:PLN02322    1 SASS-----NTKAIDPPLHMLGFEFDELSPTRVTGRLPVSPMCCQPFKVLHGGVSALIAESLASLGAHMASGFKRVAGIQ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002248007  86 LSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDPSTKEKGAQISESRVTLLCNLPVPESVKNAGEALKKYSKL 164
Cdd:PLN02322   76 LSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTDKDKANKILISSSRVTLICNLPIPDNAKDAANMLRMQAKL 154
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 20-121 3.99e-22

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 86.15  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  20 DAALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGY-SRVAGVQLSINHFRSAALGD 98
Cdd:COG2050    15 NPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPgRRAVTIELNINFLRPARLGD 94

                          90       100
                  ....*....|....*....|...
gi 1002248007  99 TVLVRAAPLHVGRSTQVWAVKLW 121
Cdd:COG2050    95 RLTAEARVVRRGRRLAVVEVEVT 117
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 25-140 1.91e-20

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: 81.06  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  25 AMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASG-YSRVAGVQLSINHFRSAALGDtVLVR 103
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSALPpGALAVTVDLNVNYLRPARGGD-LTAR 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1002248007 104 AAPLHVGRSTQVWAVKLWkldpstKEKGAQISESRVT 140
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVT------DEDGKLVATARGT 110
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 52-125 6.20e-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: 65.74  E-value: 6.20e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002248007  52 FKVLHGGVSALIAEGLASMGA-HMASGYSRVAGVQLSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDP 125
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAArRLGGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 21-116 5.88e-13

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 61.59  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  21 AALHAMGFEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASM-GAHMASGYSRVAGVQLSINHFRSaALGDT 99
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSAaGYLCNSGGQAVVGLELNANHLRP-AREGK 79

                          90
                  ....*....|....*..
gi 1002248007 100 VLVRAAPLHVGRSTQVW 116
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVA 96
PRK10293 PRK10293
1,4-dihydroxy-2-naphthoyl-CoA hydrolase;
22-140 5.77e-11

1,4-dihydroxy-2-naphthoyl-CoA hydrolase;


Pssm-ID: 182360  Cd Length: 136  Bit Score: 56.94  E-value: 5.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  22 ALHAMG---------FEIERVSPAEVTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMAS-GYSRVAGVQLSINHF 91
Cdd:PRK10293   11 ALNAMGegnmvglldIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTeGEQKVVGLEINANHV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1002248007  92 RSAALGDTVLVrAAPLHVGRSTQVWAVKLWkldpstKEKGAQISESRVT 140
Cdd:PRK10293   91 RSAREGRVRGV-CKPLHLGSRHQVWQIEIF------DEKGRLCCSSRLT 132
PRK10254 PRK10254
proofreading thioesterase EntH;
50-118 1.05e-10

proofreading thioesterase EntH;


Pssm-ID: 182337  Cd Length: 137  Bit Score: 56.53  E-value: 1.05e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  50 QPFKVLHGGVSALIAEGLASM-GAHMASGYSRVAGVQLSINHFRSAALGdTVLVRAAPLHVGRSTQVWAV 118
Cdd:PRK10254   48 QPFGLLHGGASAALAETLGSMaGFLMTRDGQCVVGTELNATHHRPVSEG-KVRGVCQPLHLGRQNQSWEI 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 38-124 3.00e-09

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: 51.71  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  38 VTGRLLVTPTCCQPFKVLHGGVSALIAEGLASMGAHMASGY-SRVAGVQLSINHFRSAALGDTVLVRAAPLHVGRSTQVW 116
Cdd:cd03440     1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRgLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80


                  ....*...
gi 1002248007 117 AVKLWKLD 124
Cdd:cd03440    81 EVEVRNED 88
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 52-143 9.58e-03

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: 34.12  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002248007  52 FKVLHGGVSALIAEGLASMGAHMASGYSRVAgVQLSINHFRSAALGDTVLVRAAPLHVGRSTQVWAVKLWKLDpstkekG 131
Cdd:cd00586    24 LRYFEEAREEFLRELGLGYDELEEQGLGLVV-VELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFRED------G 96

                          90
                  ....*....|..
gi 1002248007 132 AQISESRVTLLC 143
Cdd:cd00586    97 ELLATAETVLVC 108
 
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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