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Conserved domains on  [gi|407924434|gb|EKG17484|]
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Thioesterase superfamily [Macrophomina phaseolina MS6]

Protein Classification

hotdog fold domain-containing protein( domain architecture ID 10130798)

hotdog fold domain-containing protein belonging to the hotdog fold superfamily of thioesterases and dehydratases, similar to beta-alanyl-CoA:ammonia lyase that catalyzes the deamination of beta-alanyl-CoA to reversibly form ammonia and acrylyl-CoA

CATH:  3.10.129.10
Gene Ontology:  GO:0016836
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 96-186 9.83e-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: 53.63  E-value: 9.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANmqisvkdpSQPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:cd03440   18 VHGGLLLALADEAAGAAAARL--------GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDG 89

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:cd03440   90 KLVATATATFV 100
 
Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 96-186 9.83e-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: 53.63  E-value: 9.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANmqisvkdpSQPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:cd03440   18 VHGGLLLALADEAAGAAAARL--------GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDG 89

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:cd03440   90 KLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 96-186 5.75e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.25  E-value: 5.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANMQisvkdpsqPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:COG2050   50 VHGGALAALADSAAGLAANSALP--------PGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDG 121

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:COG2050  122 KLVATATGTFA 132
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 96-179 5.72e-06

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: 42.63  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434   96 AHGGFVATMLDETSGRLL--QANMQISVkdpsqprpvwVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDE 173
Cdd:pfam03061   4 VHGGVYLALADEAAGAAArrLGGSQQVV----------VVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*.
gi 407924434  174 HGAVLC 179
Cdd:pfam03061  74 DGRLVA 79
 
Name Accession Description Interval E-value
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 96-186 9.83e-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: 53.63  E-value: 9.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANmqisvkdpSQPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:cd03440   18 VHGGLLLALADEAAGAAAARL--------GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDG 89

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:cd03440   90 KLVATATATFV 100
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 96-186 5.40e-09

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: 51.79  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANMqisvkdpsQPRPVWVTRSTTLEFKRPVPVEnVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:cd03443   31 VHGGAIATLADTAGGLAALSAL--------PPGALAVTVDLNVNYLRPARGG-DLTARARVVKLGRRLAVVEVEVTDEDG 101

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:cd03443  102 KLVATARGTFA 112
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 96-186 5.75e-09

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 52.25  E-value: 5.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLQANMQisvkdpsqPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHG 175
Cdd:COG2050   50 VHGGALAALADSAAGLAANSALP--------PGRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDG 121

                         90
                 ....*....|.
gi 407924434 176 AVLCTSDALFV 186
Cdd:COG2050  122 KLVATATGTFA 132
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 103-186 1.15e-06

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: 45.29  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434 103 TMLDETSGRLLQAnMQISVKDPSQPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHGAVLCTSD 182
Cdd:cd00586   25 RYFEEAREEFLRE-LGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDGELLATAE 103


                 ....
gi 407924434 183 ALFV 186
Cdd:cd00586  104 TVLV 107
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 96-179 5.72e-06

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: 42.63  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434   96 AHGGFVATMLDETSGRLL--QANMQISVkdpsqprpvwVTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDE 173
Cdd:pfam03061   4 VHGGVYLALADEAAGAAArrLGGSQQVV----------VVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDE 73


                  ....*.
gi 407924434  174 HGAVLC 179
Cdd:pfam03061  74 DGRLVA 79
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
93-186 3.98e-05

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 41.79  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  93 KTAAHGGFVATMLdetsgrllqanMQISVKDPSQPRPVWVtRSTTLEFKRPVPVENVVLVRAK-LEKEEEKSCRVVA--- 168
Cdd:COG2030   50 GRIAHGMLTLSLA-----------SGLLVDDLPGTAVANL-GLQEVRFLRPVRVGDTLRARVEvLEKRESKSRGIVTlrt 117

                         90
                 ....*....|....*...
gi 407924434 169 SIEDEHGAVLCTSDALFV 186
Cdd:COG2030  118 TVTNQDGEVVLTGEATVL 135
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 96-183 1.50e-03

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 37.14  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434  96 AHGGFVATMLDETSGRLLqanmqisvkdpsqPRPVWVTRSTTLEFKRPVPVENVVLVRAK-LEKEEEKScRVVAS--IED 172
Cdd:cd03449   48 AHGMLTASLISAVLGTLL-------------PGPGTIYLSQSLRFLRPVFIGDTVTATVTvTEKREDKK-RVTLEtvCTN 113

                         90
                 ....*....|.
gi 407924434 173 EHGAVLCTSDA 183
Cdd:cd03449  114 QNGEVVIEGEA 124
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 82-186 7.21e-03

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: 36.18  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407924434   82 YDIGPGVNTTLKTA-AHGGFVATMLDETSGRLLQANMqisvkdpSQPRPVWVTRSTTLEFKRPVPVENVVLVRAKLEKEE 160
Cdd:pfam01643  13 YESDFNGTAKLPALmNLLQDIAADQSEELGLSDDGFF-------KDYNLVWVVYRYEIDIERLPEFGDMIEIETWASSYN 85

                          90       100
                  ....*....|....*....|....*.
gi 407924434  161 EKSCRVVASIEDEHGAVLCTSDALFV 186
Cdd:pfam01643  86 KFFCYRRFRVYDEKGEKIIEAKSTWV 111
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 132-191 8.19e-03

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: 35.01  E-value: 8.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407924434  132 VTRSTTLEFKRPVPVENVVLVRAKLEKEEEKSCRVVASIEDEHGAVLCT--SDALFVEQRGR 191
Cdd:pfam13279  47 ILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHRFLSPDGKLVATaeTRLVFVDYETR 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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