|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl-ACP_TE |
pfam01643 |
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ... |
9-251 |
4.83e-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: 321.99 E-value: 4.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 9 GKKHTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGR-DAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQ 87
Cdd:pfam01643 1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLsDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 88 AMSYNKYFCYRNFWVHDEEGNECVFVKSTFVLMDQKNRKISSVLPEIIAPFDSEKITKIYRHEK---IEKVTEGNFLPYR 164
Cdd:pfam01643 81 ASSYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKtkpGKPIEESTEKEYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 165 VRFFDIDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKFDKEVEYGQEVESHYEIVEQENQLKTRHEIRID-GQTYC 243
Cdd:pfam01643 161 VRYSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIEIITESAGSEEGLKTLHEIRNStGEEIA 240
|
....*...
gi 514564565 244 EANIDWTN 251
Cdd:pfam01643 241 QARTDWRK 248
|
|
| FatA |
COG3884 |
Acyl-ACP thioesterase [Lipid transport and metabolism]; |
12-249 |
3.55e-82 |
|
Acyl-ACP thioesterase [Lipid transport and metabolism];
Pssm-ID: 443092 [Multi-domain] Cd Length: 242 Bit Score: 246.02 E-value: 3.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:COG3884 1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFVKSTFVLMDQKNRKISSVLPEIIAPFDSEKITKIYRH-EKIEKVTEGNF-LPYRVRFFD 169
Cdd:COG3884 81 NRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRPpRKLKKPEDDEEeKEFTVRYSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 170 IDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKFDKEVEYGQEVESHYEIVEQEnqlKTRHEIRID--GQTYCEANI 247
Cdd:COG3884 161 IDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEDG---RTLHRIVGDddGKELARARI 237
|
..
gi 514564565 248 DW 249
Cdd:COG3884 238 EW 239
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
12-121 |
3.78e-18 |
|
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: 77.26 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:cd00586 1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80
|
90 100 110
....*....|....*....|....*....|
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFVKSTFVLMD 121
Cdd:cd00586 81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
|
|
| PLN02370 |
PLN02370 |
acyl-ACP thioesterase |
61-209 |
6.43e-12 |
|
acyl-ACP thioesterase
Pssm-ID: 215210 [Multi-domain] Cd Length: 419 Bit Score: 64.64 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 61 LGWVITNYEIEIHRLPKVGEKVAITTQAMSYNKYFCYRNFWVHD-EEGNECVFVKSTFVLMDQKNRKISSVLPEI---IA 136
Cdd:PLN02370 195 LIWVVTRMQVLVDRYPTWGDVVQVDTWVSASGKNGMRRDWLVRDcKTGETLTRASSVWVMMNKLTRRLSKIPEEVrgeIE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 137 PF----------DSEKITKIyrHEKIEKVTEGNFLPyrvRFFDIDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKF 206
Cdd:PLN02370 275 PYflnsdpvvneDSRKLPKL--DDKTADYIRKGLTP---RWSDLDVNQHVNNVKYIGWILESAPPPIMESHELAAITLEY 349
|
...
gi 514564565 207 DKE 209
Cdd:PLN02370 350 RRE 352
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Acyl-ACP_TE |
pfam01643 |
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ... |
9-251 |
4.83e-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: 321.99 E-value: 4.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 9 GKKHTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGR-DAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQ 87
Cdd:pfam01643 1 GLVFKRKYDVRFYESDFNGTAKLPALMNLLQDIAADQSEELGLsDDGFFKDYNLVWVVYRYEIDIERLPEFGDMIEIETW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 88 AMSYNKYFCYRNFWVHDEEGNECVFVKSTFVLMDQKNRKISSVLPEIIAPFDSEKITKIYRHEK---IEKVTEGNFLPYR 164
Cdd:pfam01643 81 ASSYNKFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAPYQSESIEKLIRGPKtkpGKPIEESTEKEYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 165 VRFFDIDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKFDKEVEYGQEVESHYEIVEQENQLKTRHEIRID-GQTYC 243
Cdd:pfam01643 161 VRYSDIDMNQHVNNVKYLEWILEVLPLDFLDTHEPKKITLKYEKEVQYGDDIEIITESAGSEEGLKTLHEIRNStGEEIA 240
|
....*...
gi 514564565 244 EANIDWTN 251
Cdd:pfam01643 241 QARTDWRK 248
|
|
| FatA |
COG3884 |
Acyl-ACP thioesterase [Lipid transport and metabolism]; |
12-249 |
3.55e-82 |
|
Acyl-ACP thioesterase [Lipid transport and metabolism];
Pssm-ID: 443092 [Multi-domain] Cd Length: 242 Bit Score: 246.02 E-value: 3.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:COG3884 1 YEKEYRVRYYEVDFNGRLRLPALLNYLQDAATEHAEALGFGIDDLEEKGLAWVLSRYQIEIDRYPRWGEKITVETWPSGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFVKSTFVLMDQKNRKISSVLPEIIAPFDSEKITKIYRH-EKIEKVTEGNF-LPYRVRFFD 169
Cdd:COG3884 81 NRFFAYRDFRILDEDGELLARATSIWVLIDLETRRPVRIPDEILEPYGLEEERALPRPpRKLKKPEDDEEeKEFTVRYSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 170 IDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKFDKEVEYGQEVESHYEIVEQEnqlKTRHEIRID--GQTYCEANI 247
Cdd:COG3884 161 IDTNGHVNNARYLEWALDALPLEFLKNHRLKRLEINYLKEVRLGDTVEVRSARDEDG---RTLHRIVGDddGKELARARI 237
|
..
gi 514564565 248 DW 249
Cdd:COG3884 238 EW 239
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
12-121 |
3.78e-18 |
|
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: 77.26 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:cd00586 1 FTLEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRELGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRL 80
|
90 100 110
....*....|....*....|....*....|
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFVKSTFVLMD 121
Cdd:cd00586 81 GRKSFTFEQEIFREDGELLATAETVLVCVD 110
|
|
| PLN02370 |
PLN02370 |
acyl-ACP thioesterase |
61-209 |
6.43e-12 |
|
acyl-ACP thioesterase
Pssm-ID: 215210 [Multi-domain] Cd Length: 419 Bit Score: 64.64 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 61 LGWVITNYEIEIHRLPKVGEKVAITTQAMSYNKYFCYRNFWVHD-EEGNECVFVKSTFVLMDQKNRKISSVLPEI---IA 136
Cdd:PLN02370 195 LIWVVTRMQVLVDRYPTWGDVVQVDTWVSASGKNGMRRDWLVRDcKTGETLTRASSVWVMMNKLTRRLSKIPEEVrgeIE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 137 PF----------DSEKITKIyrHEKIEKVTEGNFLPyrvRFFDIDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILVKF 206
Cdd:PLN02370 275 PYflnsdpvvneDSRKLPKL--DDKTADYIRKGLTP---RWSDLDVNQHVNNVKYIGWILESAPPPIMESHELAAITLEY 349
|
...
gi 514564565 207 DKE 209
Cdd:PLN02370 350 RRE 352
|
|
| FadM |
COG0824 |
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
160-249 |
2.31e-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: 54.13 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 160 FLPYRVRFFDIDGNQHVNNAIYFNW-------LLDVLGYDFLTTHQPKKILV------KFDKEVEYGQEVESHYEIVE-Q 225
Cdd:COG0824 7 ETPIRVRFGDTDAMGHVNNANYLRYfeearteFLRALGLSYAELEEEGIGLVvveaeiDYLRPARYGDELTVETRVVRlG 86
|
90 100
....*....|....*....|....*.
gi 514564565 226 ENQLKTRHEIR--IDGQTYCEANIDW 249
Cdd:COG0824 87 GSSLTFEYEIFraDDGELLATGETVL 112
|
|
| 4HBT |
cd00586 |
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ... |
161-249 |
3.01e-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: 53.38 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 161 LPYRVRFFDIDGNQHVNNAIYFNWLLDV-------LGYDFLTTHQPKKILV------KFDKEVEYGQEVESHYEIVEQEN 227
Cdd:cd00586 3 LEIRVRFGDTDAAGHVNNARYLRYFEEAreeflreLGLGYDELEEQGLGLVvveleiDYLRPLRLGDRLTVETRVLRLGR 82
|
90 100
....*....|....*....|....
gi 514564565 228 -QLKTRHEIRI-DGQTYCEANIDW 249
Cdd:cd00586 83 kSFTFEQEIFReDGELLATAETVL 106
|
|
| 4HBT_2 |
pfam13279 |
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ... |
22-138 |
3.42e-08 |
|
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: 50.80 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 22 DGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSYNKYFCYRNFW 101
Cdd:pfam13279 5 DIDANGHMNNARYLRYFEEARDRFLERLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 514564565 102 VHDEEGNECVFVKSTFVLMDQKNRKISSVLPEIIAPF 138
Cdd:pfam13279 85 FLSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
|
|
| FadM |
COG0824 |
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ... |
12-140 |
2.89e-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: 42.58 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIKVSEEQTELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:COG0824 6 FETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLRALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFV-KSTFVLMDQKNRKISSVLPEIIAPFDS 140
Cdd:COG0824 86 GGSSLTFEYEIFRADDGELLATgETVLVFVDLETGRPVPLPDELRAALEA 135
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
12-118 |
1.34e-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: 40.15 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 12 HTSSYEVAYYDGDFTGAMKIPALLAVVIkvseeqtELLGRDAAYVAQFGLGWVITNYEIEIHRLPKVGEKVAITTQAMSY 91
Cdd:cd03440 1 FVLRLTVTPEDIDGGGIVHGGLLLALAD-------EAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV 73
|
90 100
....*....|....*....|....*..
gi 514564565 92 NKYFCYRNFWVHDEEGNECVFVKSTFV 118
Cdd:cd03440 74 GRSSVTVEVEVRNEDGKLVATATATFV 100
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
161-249 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514564565 161 LPYRVRFFDIDGNQHVNNAIYFNWLLDVLGYDFLTTHQPKKILV------KFDKEVEYGQEVESHYEIVEQENQLKT-RH 233
Cdd:cd03440 3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVtlsldvRFLRPVRPGDTLTVEAEVVRVGRSSVTvEV 82
|
90
....*....|....*..
gi 514564565 234 EIRI-DGQTYCEANIDW 249
Cdd:cd03440 83 EVRNeDGKLVATATATF 99
|
|
| |
