|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl-ACP_TE |
pfam01643 |
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ... |
2-241 |
1.42e-112 |
|
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: 323.15 E-value: 1.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 2 GLTYRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAILEEHNLVWIITEYDIEVVRLPRFAEEITIETE 81
Cdd:pfam01643 1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLSDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 82 ALSYNRLFCYRRFNIYDEAGQELIHMMATFVLMDRDSRKVHAVEPEIVAPYQSDFDKKLIRGPK---YESLEEPFSKDYY 158
Cdd:pfam01643 81 ASSYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKtkpGKPIEESTEKEYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 159 VRFYDLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKINLKYVKEVRPGGVITS----AVERTGLESKHEITSD-GATNA 233
Cdd:pfam01643 161 VRYSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIEIitesAGSEEGLKTLHEIRNStGEEIA 240
|
....*...
gi 2308054732 234 QAIITWQE 241
Cdd:pfam01643 241 QARTDWRK 248
|
|
| FatA |
COG3884 |
Acyl-ACP thioesterase [Lipid transport and metabolism]; |
5-241 |
3.84e-74 |
|
Acyl-ACP thioesterase [Lipid transport and metabolism];
Pssm-ID: 443092 [Multi-domain] Cd Length: 242 Bit Score: 225.21 E-value: 3.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 5 YRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAiLEEHNLVWIITEYDIEVVRLPRFAEEITIETEALS 84
Cdd:COG3884 1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDD-LEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 85 YNRLFCYRRFNIYDEAGQELIHMMATFVLMDRDSRKVHAVEPEIVAPYQSDFDKKLIRG-PKYESLEEP-FSKDYYVRFY 162
Cdd:COG3884 80 YNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRPpRKLKKPEDDeEEKEFTVRYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 163 DLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKINLKYVKEVRPGGVITSAVERTG-LESKHEITSD--GATNAQAIITW 239
Cdd:COG3884 160 DIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEdGRTLHRIVGDddGKELARARIEW 239
|
..
gi 2308054732 240 QE 241
Cdd:COG3884 240 RK 241
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
5-115 |
4.51e-15 |
|
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: 68.79 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 5 YRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAiLEEHNLVWIITEYDIEVVRLPRFAEEITIETEALS 84
Cdd:cd00586 1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDE-LEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79
|
90 100 110
....*....|....*....|....*....|.
gi 2308054732 85 YNRLFCYRRFNIYDEAGQELIHMMATFVLMD 115
Cdd:cd00586 80 LGRKSFTFEQEIFREDGELLATAETVLVCVD 110
|
|
| PLN02370 |
PLN02370 |
acyl-ACP thioesterase |
50-219 |
8.09e-12 |
|
acyl-ACP thioesterase
Pssm-ID: 215210 [Multi-domain] Cd Length: 419 Bit Score: 64.25 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 50 LEEHNLVWIITEYDIEVVRLPRFAEEITIETEALSYNRLFCYRRFNIYD-EAGQELIHMMATFVLMDRDSRKVHAVEPEI 128
Cdd:PLN02370 190 MSKRNLIWVVTRMQVLVDRYPTWGDVVQVDTWVSASGKNGMRRDWLVRDcKTGETLTRASSVWVMMNKLTRRLSKIPEEV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 129 ---VAPYQSDFD-------KKLirgPKYE-SLEEPFSKDYYVRFYDLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKIN 197
Cdd:PLN02370 270 rgeIEPYFLNSDpvvnedsRKL---PKLDdKTADYIRKGLTPRWSDLDVNQHVNNVKYIGWILESAPPPIMESHELAAIT 346
|
170 180
....*....|....*....|....
gi 2308054732 198 LKYVKEVRPGGVITS--AVERTGL 219
Cdd:PLN02370 347 LEYRRECGRDSVLQSltAVSGTGI 370
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl-ACP_TE |
pfam01643 |
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ... |
2-241 |
1.42e-112 |
|
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: 323.15 E-value: 1.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 2 GLTYRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAILEEHNLVWIITEYDIEVVRLPRFAEEITIETE 81
Cdd:pfam01643 1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLSDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 82 ALSYNRLFCYRRFNIYDEAGQELIHMMATFVLMDRDSRKVHAVEPEIVAPYQSDFDKKLIRGPK---YESLEEPFSKDYY 158
Cdd:pfam01643 81 ASSYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKtkpGKPIEESTEKEYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 159 VRFYDLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKINLKYVKEVRPGGVITS----AVERTGLESKHEITSD-GATNA 233
Cdd:pfam01643 161 VRYSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIEIitesAGSEEGLKTLHEIRNStGEEIA 240
|
....*...
gi 2308054732 234 QAIITWQE 241
Cdd:pfam01643 241 QARTDWRK 248
|
|
| FatA |
COG3884 |
Acyl-ACP thioesterase [Lipid transport and metabolism]; |
5-241 |
3.84e-74 |
|
Acyl-ACP thioesterase [Lipid transport and metabolism];
Pssm-ID: 443092 [Multi-domain] Cd Length: 242 Bit Score: 225.21 E-value: 3.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 5 YRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAiLEEHNLVWIITEYDIEVVRLPRFAEEITIETEALS 84
Cdd:COG3884 1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDD-LEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 85 YNRLFCYRRFNIYDEAGQELIHMMATFVLMDRDSRKVHAVEPEIVAPYQSDFDKKLIRG-PKYESLEEP-FSKDYYVRFY 162
Cdd:COG3884 80 YNRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRPpRKLKKPEDDeEEKEFTVRYS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 163 DLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKINLKYVKEVRPGGVITSAVERTG-LESKHEITSD--GATNAQAIITW 239
Cdd:COG3884 160 DIDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEdGRTLHRIVGDddGKELARARIEW 239
|
..
gi 2308054732 240 QE 241
Cdd:COG3884 240 RK 241
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
5-115 |
4.51e-15 |
|
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: 68.79 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 5 YRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGVSDKAiLEEHNLVWIITEYDIEVVRLPRFAEEITIETEALS 84
Cdd:cd00586 1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDE-LEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLR 79
|
90 100 110
....*....|....*....|....*....|.
gi 2308054732 85 YNRLFCYRRFNIYDEAGQELIHMMATFVLMD 115
Cdd:cd00586 80 LGRKSFTFEQEIFREDGELLATAETVLVCVD 110
|
|
| PLN02370 |
PLN02370 |
acyl-ACP thioesterase |
50-219 |
8.09e-12 |
|
acyl-ACP thioesterase
Pssm-ID: 215210 [Multi-domain] Cd Length: 419 Bit Score: 64.25 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 50 LEEHNLVWIITEYDIEVVRLPRFAEEITIETEALSYNRLFCYRRFNIYD-EAGQELIHMMATFVLMDRDSRKVHAVEPEI 128
Cdd:PLN02370 190 MSKRNLIWVVTRMQVLVDRYPTWGDVVQVDTWVSASGKNGMRRDWLVRDcKTGETLTRASSVWVMMNKLTRRLSKIPEEV 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 129 ---VAPYQSDFD-------KKLirgPKYE-SLEEPFSKDYYVRFYDLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKKIN 197
Cdd:PLN02370 270 rgeIEPYFLNSDpvvnedsRKL---PKLDdKTADYIRKGLTPRWSDLDVNQHVNNVKYIGWILESAPPPIMESHELAAIT 346
|
170 180
....*....|....*....|....
gi 2308054732 198 LKYVKEVRPGGVITS--AVERTGL 219
Cdd:PLN02370 347 LEYRRECGRDSVLQSltAVSGTGI 370
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
153-239 |
3.10e-09 |
|
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: 52.99 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 153 FSKDYYVRFYDLDMNGHVNNSKYLDWiFEVMGADFLTQYIP--------------KKINLKYVKEVRPGGVIT-----SA 213
Cdd:cd00586 1 FTLEIRVRFGDTDAAGHVNNARYLRY-FEEAREEFLRELGLgydeleeqglglvvVELEIDYLRPLRLGDRLTvetrvLR 79
|
90 100
....*....|....*....|....*..
gi 2308054732 214 VERTGLESKHEITS-DGATNAQAIITW 239
Cdd:cd00586 80 LGRKSFTFEQEIFReDGELLATAETVL 106
|
|
| FadM |
COG0824 |
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
150-239 |
6.96e-09 |
|
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: 52.98 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 150 EEPFSKDYYVRFYDLDMNGHVNNSKYLDWiFEVMGADFLTQ--------------YIPKKINLKYVKEVRPGGVIT---- 211
Cdd:COG0824 3 LFTFETPIRVRFGDTDAMGHVNNANYLRY-FEEARTEFLRAlglsyaeleeegigLVVVEAEIDYLRPARYGDELTvetr 81
|
90 100 110
....*....|....*....|....*....|.
gi 2308054732 212 -SAVERTGLESKHEIT--SDGATNAQAIITW 239
Cdd:COG0824 82 vVRLGGSSLTFEYEIFraDDGELLATGETVL 112
|
|
| FadM |
COG0824 |
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
41-130 |
6.77e-06 |
|
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: 44.50 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 41 ELGVSDKAiLEEHNLVWIITEYDIEVVRLPRFAEEITIETEALSYNRLFCYRRFNIYDEAGQELI-HMMATFVLMDRDSR 119
Cdd:COG0824 42 ALGLSYAE-LEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADDGELLaTGETVLVFVDLETG 120
|
90
....*....|.
gi 2308054732 120 KVHAVEPEIVA 130
Cdd:COG0824 121 RPVPLPDELRA 131
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
5-112 |
2.30e-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: 39.38 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 5 YRMKMKIPFDMADMNGHIKLPDVILLSLQVSGMQSIELGvsdkaileEHNLVWIITEYDIEVVRLPRFAEEITIETEALS 84
Cdd:cd03440 1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLG--------GRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVR 72
|
90 100
....*....|....*....|....*...
gi 2308054732 85 YNRLFCYRRFNIYDEAGQELIHMMATFV 112
Cdd:cd03440 73 VGRSSVTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
159-222 |
3.76e-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: 38.61 E-value: 3.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 159 VRFYDLDMNGHVNNSKYLDWIFEVMGADFLTQYIPKK------INLKYVKEVRPGGVITSAVERTGLESK 222
Cdd:cd03440 7 VTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLgavtlsLDVRFLRPVRPGDTLTVEAEVVRVGRS 76
|
|
| 4HBT_2 |
pfam13279 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
159-238 |
2.50e-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: 36.93 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308054732 159 VRFYDLDMNGHVNNSKYLDWI-------FEVMG----ADFLTQYIP--KKINLKYVKEVRPGGVIT-----SAVERTGLE 220
Cdd:pfam13279 1 VRPGDIDANGHMNNARYLRYFeeardrfLERLGldlaYREALGIGLilAEAHVRYRRELKLGDELTvetrlIDWDAKRFH 80
|
90
....*....|....*....
gi 2308054732 221 SKHEITS-DGATNAQAIIT 238
Cdd:pfam13279 81 LEHRFLSpDGKLVATAETR 99
|
|
| |
