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Conserved domains on  [gi|504378081|ref|WP_014565183|]
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acyl-[acyl-carrier-protein] thioesterase [Lactobacillus delbrueckii]

Protein Classification

acyl-[acyl-carrier-protein] thioesterase( domain architecture ID 11467542)

acyl-[acyl-carrier-protein] thioesterase plays an essential role in chain termination during de novo fatty acid synthesis by hydrolyzing an acyl group on a fatty acid

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
3-243 3.33e-68

Acyl-ACP thioesterase [Lipid transport and metabolism];


:

Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 210.19  E-value: 3.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQlAPTLG-GASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVG 81
Cdd:COG3884    1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEH-AEALGfGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  82 YNRFLSYRDFGIEDEAGKDLVIAHSQWVLFDLKSRKLLPSDDKIAEELGAPFLTKIPR-FKKLRPKDDYKDEKVYRAYYY 160
Cdd:COG3884   80 YNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRpPRKLKKPEDDEEEKEFTVRYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 161 DLDSNHHVHNAHYLDWIVDSLPRDFVNSHEPKDLAIKFDKEIKYGDEVVCQVMQETEDsavKTCHAITRQGELMALCEVN 240
Cdd:COG3884  160 DIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEDG---RTLHRIVGDDDGKELARAR 236


                 ....*
gi 504378081 241 --WQK 243
Cdd:COG3884  237 ieWRK 241
 
Name Accession Description Interval E-value
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
3-243 3.33e-68

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 210.19  E-value: 3.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQlAPTLG-GASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVG 81
Cdd:COG3884    1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEH-AEALGfGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  82 YNRFLSYRDFGIEDEAGKDLVIAHSQWVLFDLKSRKLLPSDDKIAEELGAPFLTKIPR-FKKLRPKDDYKDEKVYRAYYY 160
Cdd:COG3884   80 YNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRpPRKLKKPEDDEEEKEFTVRYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 161 DLDSNHHVHNAHYLDWIVDSLPRDFVNSHEPKDLAIKFDKEIKYGDEVVCQVMQETEDsavKTCHAITRQGELMALCEVN 240
Cdd:COG3884  160 DIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEDG---RTLHRIVGDDDGKELARAR 236


                 ....*
gi 504378081 241 --WQK 243
Cdd:COG3884  237 ieWRK 241
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 3-243 1.05e-48

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: 160.60  E-value: 1.05e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081    3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQLApTLG--GASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAV 80
Cdd:pfam01643   4 FKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSE-ELGlsDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETWAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   81 GYNRFLSYRDFGIEDEAGKDLVIAHSQWVLFDLKSRKLLPSDDKIAEELGAPFLTKIPRFKKLRP--KDDYKDEKVYRAY 158
Cdd:pfam01643  83 SYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKTKPgkPIEESTEKEYHVR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  159 YYDLDSNHHVHNAHYLDWIVDSLPRDFVNSHEPKDLAIKFDKEIKYGDEV--VCQvMQETEDSaVKTCHAIT-RQGELMA 235
Cdd:pfam01643 163 YSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIeiITE-SAGSEEG-LKTLHEIRnSTGEEIA 240


                  ....*...
gi 504378081  236 LCEVNWQK 243
Cdd:pfam01643 241 QARTDWRK 248
PLN02370 PLN02370
acyl-ACP thioesterase
 35-221 6.90e-16

acyl-ACP thioesterase


Pssm-ID: 215210 [Multi-domain]  Cd Length: 419  Bit Score: 76.20  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  35 GQLAPTLGGASAMKERGRGWVVTQYEFEFTSLPRAGQKVRV--WTEAVGYNRFlsYRDFGIED-EAGKDLVIAHSQWVLF 111
Cdd:PLN02370 178 GLLGDGFGSTPEMSKRNLIWVVTRMQVLVDRYPTWGDVVQVdtWVSASGKNGM--RRDWLVRDcKTGETLTRASSVWVMM 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 112 DLKSRKLLPSDDKIAEELGAPFLTKIPRF----KKLrPKDDYKDEKVYRA----YYYDLDSNHHVHNAHYLDWIVDSLPR 183
Cdd:PLN02370 256 NKLTRRLSKIPEEVRGEIEPYFLNSDPVVnedsRKL-PKLDDKTADYIRKgltpRWSDLDVNQHVNNVKYIGWILESAPP 334

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504378081 184 DFVNSHEPKDLAIKFDKEIkyGDEVVCQVMQETEDSAV 221
Cdd:PLN02370 335 PIMESHELAAITLEYRREC--GRDSVLQSLTAVSGTGI 370
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-112 1.99e-14

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: 67.25  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQLAPTLGGASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVGY 82
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 504378081  83 NRFLSYRDFGIEDEAGKDLVIAHSQWVLFD 112
Cdd:cd00586   81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 156-176 4.05e-03

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: 36.24  E-value: 4.05e-03
                          10        20
                  ....*....|....*....|.
gi 504378081  156 RAYYYDLDSNHHVHNAHYLDW 176
Cdd:TIGR00051   3 RVYYEDTDAQGIVYHANYLRY 23
 
Name Accession Description Interval E-value
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
3-243 3.33e-68

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 210.19  E-value: 3.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQlAPTLG-GASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVG 81
Cdd:COG3884    1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEH-AEALGfGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  82 YNRFLSYRDFGIEDEAGKDLVIAHSQWVLFDLKSRKLLPSDDKIAEELGAPFLTKIPR-FKKLRPKDDYKDEKVYRAYYY 160
Cdd:COG3884   80 YNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRpPRKLKKPEDDEEEKEFTVRYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 161 DLDSNHHVHNAHYLDWIVDSLPRDFVNSHEPKDLAIKFDKEIKYGDEVVCQVMQETEDsavKTCHAITRQGELMALCEVN 240
Cdd:COG3884  160 DIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEDG---RTLHRIVGDDDGKELARAR 236


                 ....*
gi 504378081 241 --WQK 243
Cdd:COG3884  237 ieWRK 241
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 3-243 1.05e-48

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: 160.60  E-value: 1.05e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081    3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQLApTLG--GASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAV 80
Cdd:pfam01643   4 FKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSE-ELGlsDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETWAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   81 GYNRFLSYRDFGIEDEAGKDLVIAHSQWVLFDLKSRKLLPSDDKIAEELGAPFLTKIPRFKKLRP--KDDYKDEKVYRAY 158
Cdd:pfam01643  83 SYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKTKPgkPIEESTEKEYHVR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  159 YYDLDSNHHVHNAHYLDWIVDSLPRDFVNSHEPKDLAIKFDKEIKYGDEV--VCQvMQETEDSaVKTCHAIT-RQGELMA 235
Cdd:pfam01643 163 YSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIeiITE-SAGSEEG-LKTLHEIRnSTGEEIA 240


                  ....*...
gi 504378081  236 LCEVNWQK 243
Cdd:pfam01643 241 QARTDWRK 248
PLN02370 PLN02370
acyl-ACP thioesterase
 35-221 6.90e-16

acyl-ACP thioesterase


Pssm-ID: 215210 [Multi-domain]  Cd Length: 419  Bit Score: 76.20  E-value: 6.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  35 GQLAPTLGGASAMKERGRGWVVTQYEFEFTSLPRAGQKVRV--WTEAVGYNRFlsYRDFGIED-EAGKDLVIAHSQWVLF 111
Cdd:PLN02370 178 GLLGDGFGSTPEMSKRNLIWVVTRMQVLVDRYPTWGDVVQVdtWVSASGKNGM--RRDWLVRDcKTGETLTRASSVWVMM 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 112 DLKSRKLLPSDDKIAEELGAPFLTKIPRF----KKLrPKDDYKDEKVYRA----YYYDLDSNHHVHNAHYLDWIVDSLPR 183
Cdd:PLN02370 256 NKLTRRLSKIPEEVRGEIEPYFLNSDPVVnedsRKL-PKLDDKTADYIRKgltpRWSDLDVNQHVNNVKYIGWILESAPP 334

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504378081 184 DFVNSHEPKDLAIKFDKEIkyGDEVVCQVMQETEDSAV 221
Cdd:PLN02370 335 PIMESHELAAITLEYRREC--GRDSVLQSLTAVSGTGI 370
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-112 1.99e-14

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: 67.25  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081   3 YYKDYQLEYADCGESGQLKLPRMIDLMMGSSEGQLAPTLGGASAMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVGY 82
Cdd:cd00586    1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 504378081  83 NRFLSYRDFGIEDEAGKDLVIAHSQWVLFD 112
Cdd:cd00586   81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 155-247 2.37e-08

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: 50.68  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 155 YRAYYYDLDSNHHVHNAHYLDWIVDS---------LPRDFVNSHEP----KDLAIKFDKEIKYGDEVVCQV-MQETEDSA 220
Cdd:cd00586    5 IRVRFGDTDAAGHVNNARYLRYFEEAreeflrelgLGYDELEEQGLglvvVELEIDYLRPLRLGDRLTVETrVLRLGRKS 84

                         90       100
                 ....*....|....*....|....*...
gi 504378081 221 VKTCHAITRQ-GELMALCEVNWqkMCFN 247
Cdd:cd00586   85 FTFEQEIFREdGELLATAETVL--VCVD 110
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 152-249 2.34e-07

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: 48.74  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 152 EKVYRAYYYDLDSNHHVHNAHYLDWI----VDSLPRDFVNSHEPK---------DLAIKFDKEIKYGDEVVCQV-MQETE 217
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFeearTEFLRALGLSYAELEeegiglvvvEAEIDYLRPARYGDELTVETrVVRLG 86

                         90       100       110
                 ....*....|....*....|....*....|....
gi 504378081 218 DSAVKTCHAITRQ--GELMALCEVNWqkMCFNRD 249
Cdd:COG0824   87 GSSLTFEYEIFRAddGELLATGETVL--VFVDLE 118
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 46-131 1.34e-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: 43.73  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081  46 AMKERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVGYNRFLSYRDFGIEDEA-GKDLVIAHSQWVLFDLKSRKLLPSDDK 124
Cdd:COG0824   49 ELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADdGELLATGETVLVFVDLETGRPVPLPDE 128


                 ....*..
gi 504378081 125 IAEELGA 131
Cdd:COG0824  129 LRAALEA 135
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 155-241 5.69e-04

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: 38.23  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504378081 155 YRAYYYDLDSNHHVHNAHYLDWIvDSLPRDFVNSHEPK-------DLAIKFDKEIKYGDEVVC--QVMQETEDSAVKTCH 225
Cdd:cd03440    5 LTVTPEDIDGGGIVHGGLLLALA-DEAAGAAAARLGGRglgavtlSLDVRFLRPVRPGDTLTVeaEVVRVGRSSVTVEVE 83

                         90
                 ....*....|....*.
gi 504378081 226 AITRQGELMALCEVNW 241
Cdd:cd03440   84 VRNEDGKLVATATATF 99
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 37-109 3.02e-03

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: 36.30  E-value: 3.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504378081  37 LAPTLGGASAMK--ERGRGWVVTQYEFEFTSLPRAGQKVRVWTEAVGYNRFLSYRDFGIEDEAGKDLVIAHSQWV 109
Cdd:cd03440   26 LADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATFV 100
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 156-176 4.05e-03

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: 36.24  E-value: 4.05e-03
                          10        20
                  ....*....|....*....|.
gi 504378081  156 RAYYYDLDSNHHVHNAHYLDW 176
Cdd:TIGR00051   3 RVYYEDTDAQGIVYHANYLRY 23
 
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.
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