NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15597997|ref|NP_251491|]
View 

hypothetical protein PA2801 [Pseudomonas aeruginosa PAO1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 8-134 2.94e-33

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: 113.45  E-value: 2.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLEGAAE---GPVVLqSLH-TYLKPVVHPATVVVELYAGR 83
Cdd:COG0824   6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEegiGLVVV-EAEiDYLRPARYGDELTVETRVVR 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597997  84 LGTSSLVLEHRLHTLEDPQgTYGEGHCKLVWVRHAENRSTPVPDSIRAAIA 134
Cdd:COG0824  85 LGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGRPVPLPDELRAALE 134
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 8-134 2.94e-33

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: 113.45  E-value: 2.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLEGAAE---GPVVLqSLH-TYLKPVVHPATVVVELYAGR 83
Cdd:COG0824   6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEegiGLVVV-EAEiDYLRPARYGDELTVETRVVR 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597997  84 LGTSSLVLEHRLHTLEDPQgTYGEGHCKLVWVRHAENRSTPVPDSIRAAIA 134
Cdd:COG0824  85 LGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-115 1.30e-25

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: 93.05  E-value: 1.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLEGAAE---GPVVLQSLHTYLKPVVHPATVVVELYAGRL 84
Cdd:cd00586   1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEqglGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 15597997  85 GTSSLVLEHRLHtleDPQGT-YGEGHCKLVWV 115
Cdd:cd00586  81 GRKSFTFEQEIF---REDGElLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-133 7.94e-19

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: 76.22  E-value: 7.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997    14 VRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLE--GAAEGPVVLQSLH-TYLKPVVHPATVVVELYAGRLGTSSLV 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAyrEALGIGLILAEAHvRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15597997    91 LEHRLHTLEdpQGTYGEGHCKLVWVRHAENRSTPVPDSIRAAI 133
Cdd:pfam13279  81 LEHRFLSPD--GKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 14-95 9.84e-09

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 49.72  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997    14 VRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGI---DLEGAAEGPVVLQSLHTYLKPVVHPATVVVELYAGRLGTSSLV 90
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFpqsVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFV 83


                  ....*
gi 15597997    91 LEHRL 95
Cdd:TIGR00051  84 FSQEI 88
 
Name Accession Description Interval E-value
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 8-134 2.94e-33

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: 113.45  E-value: 2.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLEGAAE---GPVVLqSLH-TYLKPVVHPATVVVELYAGR 83
Cdd:COG0824   6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEegiGLVVV-EAEiDYLRPARYGDELTVETRVVR 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597997  84 LGTSSLVLEHRLHTLEDPQgTYGEGHCKLVWVRHAENRSTPVPDSIRAAIA 134
Cdd:COG0824  85 LGGSSLTFEYEIFRADDGE-LLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 8-115 1.30e-25

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: 93.05  E-value: 1.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLEGAAE---GPVVLQSLHTYLKPVVHPATVVVELYAGRL 84
Cdd:cd00586   1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEqglGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 15597997  85 GTSSLVLEHRLHtleDPQGT-YGEGHCKLVWV 115
Cdd:cd00586  81 GRKSFTFEQEIF---REDGElLATAETVLVCV 109
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 14-133 7.94e-19

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: 76.22  E-value: 7.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997    14 VRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDLE--GAAEGPVVLQSLH-TYLKPVVHPATVVVELYAGRLGTSSLV 90
Cdd:pfam13279   1 VRPGDIDANGHMNNARYLRYFEEARDRFLERLGLDLAyrEALGIGLILAEAHvRYRRELKLGDELTVETRLIDWDAKRFH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15597997    91 LEHRLHTLEdpQGTYGEGHCKLVWVRHAENRSTPVPDSIRAAI 133
Cdd:pfam13279  81 LEHRFLSPD--GKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 22-100 1.80e-10

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: 53.41  E-value: 1.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597997    22 YGHVNNTLYFQYLEEARVAWFETLGidleGAAEGPVVLQSLHTYLKPVVHPATVVVELYAGRLGTSSLVLEHRLHTLED 100
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLG----GSQQVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDG 75
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 8-100 3.52e-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: 50.55  E-value: 3.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGIDlegaaEGPVVLQSLH-TYLKPVVHPATVVVELYAGRLGT 86
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGR-----GLGAVTLSLDvRFLRPVRPGDTLTVEAEVVRVGR 75

                        90
                ....*....|....
gi 15597997  87 SSLVLEHRLHTLED 100
Cdd:cd03440  76 SSVTVEVEVRNEDG 89
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 14-95 9.84e-09

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 49.72  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597997    14 VRWGDMDSYGHVNNTLYFQYLEEARVAWFETLGI---DLEGAAEGPVVLQSLHTYLKPVVHPATVVVELYAGRLGTSSLV 90
Cdd:TIGR00051   4 VYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFpqsVLRAEGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFV 83


                  ....*
gi 15597997    91 LEHRL 95
Cdd:TIGR00051  84 FSQEI 88
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
8-37 3.44e-05

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 41.47  E-value: 3.44e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 15597997   8 HTAHIPVRWGDMDSYGHVNNTLYFQYLEEA 37
Cdd:COG3884 150 EEKEFTVRYSDIDTNGHVNNARYLEWALDA 179
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 12-37 8.24e-04

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: 37.72  E-value: 8.24e-04
                          10        20
                  ....*....|....*....|....*.
gi 15597997    12 IPVRWGDMDSYGHVNNTLYFQYLEEA 37
Cdd:pfam01643 159 YHVRYSDIDMNQHVNNVKYLEWILEV 184
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH