|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
7-320 |
2.08e-162 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 455.30 E-value: 2.08e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:PRK09352 6 ILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDEtTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGS-TKGLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:PRK09352 86 YAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAyKNVLVIGAEKLSRIVDWTDRSTCVLFGDGAGAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKKLLKEKLAADGTRSSSLTAGYQQNKNPFYSEdsegsyYLQMTGRDIFDFAVRDVANNIQEVMKD-----KPV 239
Cdd:PRK09352 166 VLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPG------YLRMEGREVFKFAVRELAKVAREALEAagltpEDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 240 DYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILME 319
Cdd:PRK09352 240 DWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRG--DLVLLEGFGGGLTWGAALVR 317
|
.
gi 488216404 320 L 320
Cdd:PRK09352 318 W 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
7-320 |
4.95e-144 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 408.73 E-value: 4.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERR-CVTNQETSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:COG0332 5 ILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRiAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGS-TKGLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:COG0332 85 YLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQaKNVLVVGAETLSRIVDWTDRSTCVLFGDGAGAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKK-LLKEKLAADGTRSSSLTAGYQQNKNPFySEDSEGSYYLQMTGRDIFDFAVRDVANNIQEVMKD-----KP 238
Cdd:COG0332 165 VLEASEEGPgILGSVLGSDGSGADLLVVPAGGSRNPP-SPVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKagltlDD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILM 318
Cdd:COG0332 244 IDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPG--DLVLLAGFGAGLTWGAAVL 321
|
..
gi 488216404 319 EL 320
Cdd:COG0332 322 RW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
7-318 |
1.25e-141 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 402.69 E-value: 1.25e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:cd00830 4 ILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGEtTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:cd00830 84 YLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKnVLVVGAETLSRILDWTDRSTAVLFGDGAGAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKK-LLKEKLAADGTRSSSLTAGYQQNKNPFYSEDSEGSyYLQMTGRDIFDFAVRDVANNIQEVMKD---KP-- 238
Cdd:cd00830 164 VLEATEEDPgILDSVLGSDGSGADLLTIPAGGSRSPFEDAEGGDP-YLVMDGREVFKFAVRLMPESIEEALEKaglTPdd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILM 318
Cdd:cd00830 243 IDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKG--DLVLLLGFGAGLTWGAALL 320
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
7-318 |
6.77e-112 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 327.03 E-value: 6.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:TIGR00747 5 ILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDEtSSTMGFEAAKRAIENAGISKDDIDLIIVATTTPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:TIGR00747 85 HAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTvLVVGAEKLSSTLDWTDRGTCVLFGDGAGAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANP-QKKLLKEKLAADGTRSSSL-TAGYQQNKnpfysedSEGSYYLQMTGRDIFDFAVRDVANNIQEVM-----KDK 237
Cdd:TIGR00747 165 VLGESEdPGGIISTHLGADGTQGEALyLPAGGRPT-------SGPSPFITMEGNEVFKHAVRKMGDVVEETLeanglDPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 238 PVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSIL 317
Cdd:TIGR00747 238 DIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPG--DLLLLVAFGGGLTWGAAL 315
|
.
gi 488216404 318 M 318
Cdd:TIGR00747 316 V 316
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
239-320 |
3.75e-34 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 120.30 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKItlGKQQKVIFTGYGGGLTWGSILM 318
Cdd:pfam08541 11 IDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKL--KPGDLVLLVGFGAGLTWGAALL 88
|
..
gi 488216404 319 EL 320
Cdd:pfam08541 89 RW 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
7-320 |
2.08e-162 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 455.30 E-value: 2.08e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:PRK09352 6 ILGTGSYLPERVVTNDDLEKMVDTSDEWIVTRTGIKERRIAAPDEtTSDLATEAAKKALEAAGIDPEDIDLIIVATTTPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGS-TKGLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:PRK09352 86 YAFPSTACLVQARLGAKNAAAFDLSAACSGFVYALSTADQFIRSGAyKNVLVIGAEKLSRIVDWTDRSTCVLFGDGAGAV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKKLLKEKLAADGTRSSSLTAGYQQNKNPFYSEdsegsyYLQMTGRDIFDFAVRDVANNIQEVMKD-----KPV 239
Cdd:PRK09352 166 VLGASEEPGILSTHLGSDGSYGDLLYLPGGGSRGPASPG------YLRMEGREVFKFAVRELAKVAREALEAagltpEDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 240 DYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILME 319
Cdd:PRK09352 240 DWLVPHQANLRIIDATAKKLGLPMEKVVVTVDKYGNTSAASIPLALDEAVRDGRIKRG--DLVLLEGFGGGLTWGAALVR 317
|
.
gi 488216404 320 L 320
Cdd:PRK09352 318 W 318
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
7-320 |
4.95e-144 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 408.73 E-value: 4.95e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERR-CVTNQETSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:COG0332 5 ILGTGSYLPERVVTNDDLEKRLDTSDEWIEERTGIRERRiAAPDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGS-TKGLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:COG0332 85 YLFPSTACLVQHKLGAKNAAAFDINAACSGFVYALSVAAALIRSGQaKNVLVVGAETLSRIVDWTDRSTCVLFGDGAGAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKK-LLKEKLAADGTRSSSLTAGYQQNKNPFySEDSEGSYYLQMTGRDIFDFAVRDVANNIQEVMKD-----KP 238
Cdd:COG0332 165 VLEASEEGPgILGSVLGSDGSGADLLVVPAGGSRNPP-SPVDEGDHYLRMDGREVFKFAVRNLPEVIREALEKagltlDD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILM 318
Cdd:COG0332 244 IDWFIPHQANLRIIEAVAKRLGLPEEKVVVNIDRYGNTSAASIPLALDEALREGRIKPG--DLVLLAGFGAGLTWGAAVL 321
|
..
gi 488216404 319 EL 320
Cdd:COG0332 322 RW 323
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
7-318 |
1.25e-141 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 402.69 E-value: 1.25e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:cd00830 4 ILGIGSYLPERVVTNDELEKRLDTSDEWIRTRTGIRERRIADPGEtTSDLAVEAAKKALEDAGIDADDIDLIIVATSTPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:cd00830 84 YLFPATACLVQARLGAKNAAAFDINAACSGFLYGLSTAAGLIRSGGAKnVLVVGAETLSRILDWTDRSTAVLFGDGAGAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKK-LLKEKLAADGTRSSSLTAGYQQNKNPFYSEDSEGSyYLQMTGRDIFDFAVRDVANNIQEVMKD---KP-- 238
Cdd:cd00830 164 VLEATEEDPgILDSVLGSDGSGADLLTIPAGGSRSPFEDAEGGDP-YLVMDGREVFKFAVRLMPESIEEALEKaglTPdd 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSILM 318
Cdd:cd00830 243 IDWFVPHQANLRIIEAVAKRLGLPEEKVVVNLDRYGNTSAASIPLALDEAIEEGKLKKG--DLVLLLGFGAGLTWGAALL 320
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
1-319 |
3.52e-129 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 371.12 E-value: 3.52e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 1 MEQFGMITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVT-NQETSDLCILVAEKLIKQKNLNPKDLDFILV 79
Cdd:PRK12879 1 MMSYARITGIGTYVPPRVLTNDDLETFIDTSDEWIVQRTGIKERRIAHvEEYTSDLAIKAAERALARAGLDAEDIDLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 80 ATMSPDYTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGS-TKGLVIGGETLSKLIDWSDRTTAVLFG 158
Cdd:PRK12879 81 ATTTPDYLFPSTASQVQARLGIPNAAAFDINAACAGFLYGLETANGLITSGLyKKVLVIGAERLSKVTDYTDRTTCILFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 159 DGAGGILLEANPQK-KLLKEKLAADGTRSSSLtagYQQN-KNPFYSEDSEGSYYLQMTGRDIFDFAVRDVANNIQEV--- 233
Cdd:PRK12879 161 DGAGAVVLEATENEpGFIDYVLGTDGDGGDIL---YRTGlGTTMDRDALSGDGYIVQNGREVFKWAVRTMPKGARQVlek 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 234 --MKDKPVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGL 311
Cdd:PRK12879 238 agLTKDDIDWVIPHQANLRIIESLCEKLGIPMEKTLVSVEYYGNTSAATIPLALDLALEQGKIKPG--DTLLLYGFGAGL 315
|
....*...
gi 488216404 312 TWGSILME 319
Cdd:PRK12879 316 TWAALLVK 323
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
7-318 |
6.77e-112 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 327.03 E-value: 6.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:TIGR00747 5 ILGTGSYLPEKVLTNADLEKMVDTSDEWIVTRTGIKERRIAADDEtSSTMGFEAAKRAIENAGISKDDIDLIIVATTTPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:TIGR00747 85 HAFPSAACMVQAYLGIKGIPAFDLSAACAGFIYALSVAKQYIESGKYKTvLVVGAEKLSSTLDWTDRGTCVLFGDGAGAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANP-QKKLLKEKLAADGTRSSSL-TAGYQQNKnpfysedSEGSYYLQMTGRDIFDFAVRDVANNIQEVM-----KDK 237
Cdd:TIGR00747 165 VLGESEdPGGIISTHLGADGTQGEALyLPAGGRPT-------SGPSPFITMEGNEVFKHAVRKMGDVVEETLeanglDPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 238 PVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGGGLTWGSIL 317
Cdd:TIGR00747 238 DIDWFVPHQANLRIIEALAKRLELDMSQVVKTVHKYGNTSAASIPLALDELLRTGRIKPG--DLLLLVAFGGGLTWGAAL 315
|
.
gi 488216404 318 M 318
Cdd:TIGR00747 316 V 316
|
|
| PLN02326 |
PLN02326 |
3-oxoacyl-[acyl-carrier-protein] synthase III |
5-318 |
1.64e-104 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III
Pssm-ID: 215185 Cd Length: 379 Bit Score: 310.52 E-value: 1.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 5 GMITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQET-SDLCILVAEKLIKQKNLNPKDLDFILVATMS 83
Cdd:PLN02326 48 SKLVGCGSAVPKLLITNDDLSKLVDTSDEWIATRTGIRNRRVLSGDETlTSLAVEAAKKALEMAGVDPEDVDLVLLCTSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 84 PDYTTPSvAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLFGDGAG 162
Cdd:PLN02326 128 PDDLFGS-APQVQAALGCTNALAFDLTAACSGFVLGLVTAARFIRGGGYKNvLVIGADALSRYVDWTDRGTCILFGDGAG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 163 GILLEANP--QKKLLKEKLAADGTRSSSLTAGYQQN------KNPFYSED---SEGSYY-LQMTGRDIFDFAVRDVANNI 230
Cdd:PLN02326 207 AVVLQACDddEDGLLGFDMHSDGNGHKHLHATFKGEdddssgGNTNGVGDfppKKASYScIQMNGKEVFKFAVRCVPQVI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 231 QEVMKD-----KPVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKItlgKQQKVI-F 304
Cdd:PLN02326 287 ESALQKagltaESIDWLLLHQANQRIIDAVAQRLGIPPEKVISNLANYGNTSAASIPLALDEAVRSGKV---KKGDVIaT 363
|
330
....*....|....
gi 488216404 305 TGYGGGLTWGSILM 318
Cdd:PLN02326 364 AGFGAGLTWGSAIV 377
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
7-319 |
1.72e-90 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 272.97 E-value: 1.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCV-TNQETSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:CHL00203 5 ILSTGSSVPNFSVENQQFEDIIETSDHWISTRTGIKKRHLApSSTSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSvAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLFGDGAGGI 164
Cdd:CHL00203 85 DLFGS-ASQLQAEIGATRAVAFDITAACSGFILALVTATQFIQNGSYKNiLVVGADTLSKWIDWSDRKTCILFGDGAGAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKKLLKEKLAADGTRSSSLTAGYQQNKNPFY--SEDSEGSY-YLQMTGRDIFDFAVRDVANNIQEVMKD----- 236
Cdd:CHL00203 164 IIGASYENSILGFKLCTDGKLNSHLQLMNKPVNNQSFgtTKLPQGQYqSISMNGKEVYKFAVFQVPAVIIKCLNAlnisi 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 237 KPVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITlgKQQKVIFTGYGGGLTWGSI 316
Cdd:CHL00203 244 DEVDWFILHQANKRILEAIANRLSVPNSKMITNLEKYGNTSAASIPLALDEAIQNNKIQ--PGQIIVLSGFGAGLTWGAI 321
|
...
gi 488216404 317 LME 319
Cdd:CHL00203 322 VLK 324
|
|
| PRK05963 |
PRK05963 |
beta-ketoacyl-ACP synthase III; |
15-320 |
1.75e-60 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 180328 [Multi-domain] Cd Length: 326 Bit Score: 196.09 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 15 PEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQET-SDLCILVAEKLIKQKNLNPKDLDFILVATMSPDYTTPSVAA 93
Cdd:PRK05963 14 PDRRVENAEIEAQLGLETGWIERRTGIRCRRWAAPDETlSDLAASAGDMALSDAGIERSDIALTLLATSTPDHLLPPSAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 94 QVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKGLVIGGETLSKLIDWSDRTTAVLFGDGAGGILL--EANPQ 171
Cdd:PRK05963 94 LLAHRLGLQNSGAIDLAGACAGFLYALVLADGFVRAQGKPVLVVAANILSRRINMAERASAVLFADAAGAVVLapSAKAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 172 KKLLKEKLAADGTRSS--SLTAGyqQNKNPFYSEDSEGSYYLQMT-GRDIFDFAVRDVANNIQEV-----MKDKPVDYLL 243
Cdd:PRK05963 174 SGVLGSQLISDGSHYDliKIPAG--GSARPFAPERDASEFLMTMQdGRAVFTEAVRMMSGASQNVlasaaMTPQDIDRFF 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216404 244 LHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLdeAVSSGKITLGKQQKVIFTGYGGGLTWGSILMEL 320
Cdd:PRK05963 252 PHQANARIVDKVCETIGIPRAKAASTLETYGNSSAATIPLSL--SLANLEQPLREGERLLFAAAGAGMTGGAVVMRV 326
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
7-316 |
2.93e-47 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 161.83 E-value: 2.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMdtSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFILVATMSPD 85
Cdd:cd00827 4 IEAIGAYLPRYRVDNEELAEGL--GVDPGKYTTGIGQRHMAGDDEdVPTMAVEAARRALERAGIDPDDIGLLIVATESPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 86 YTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLIDWSDRTTAVlFGDGAGGI 164
Cdd:cd00827 82 DKGKSAATYLAELLGLTNAEAFDLKQACYGGTAALQLAANLVESGPWRyALVVASDIASYLLDEGSALEPT-LGDGAAAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 165 LLEANPQKKLLKEK---LAADGTRSSS----LTAGYQQNKNPFYSEDSEGSYylqmTGRDIFDFAVRDVANNIQEVMK-- 235
Cdd:cd00827 161 LVSRNPGILAAGIVsthSTSDPGYDFSpypvMDGGYPKPCKLAYAIRLTAEP----AGRAVFEAAHKLIAKVVRKALDra 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 236 --DKPVDYLLLHQAN-LRIIEKIARKVKMPQEK----FLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYG 308
Cdd:cd00827 237 glSEDIDYFVPHQPNgKKILEAVAKKLGGPPEKasqtRWILLRRVGNMYAASILLGLASLLESGKLKAG--DRVLLFSYG 314
|
....*...
gi 488216404 309 GGLTWGSI 316
Cdd:cd00827 315 SGFTAEAF 322
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
1-319 |
3.05e-44 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 153.84 E-value: 3.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 1 MEQFGMITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQETSDLCILVAEKLIKQKNLNPKDLDFILVA 80
Cdd:PRK07204 1 MKRYISIKGIGTYLPKRKVDSLELDKKLDLPEGWVLKKSGVKTRHFVDGETSSYMGAEAAKKAVEDAKLTLDDIDCIICA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 81 TMSPDYTTPSVAAQVQGKLGATHA-IA-FDISAACSGFVYALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLF 157
Cdd:PRK07204 81 SGTIQQAIPCTASLIQEQLGLQHSgIPcFDINSTCLSFITALDTISYAIECGRYKRvLIISSEISSVGLNWGQNESCILF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 158 GDGAGGILLE-ANPQKKLLKE--KLAADGTRSSSLTAGYQQNKNPFYSEDSEGSYYLQMTGRDIFDFAVRDVANNIQEVM 234
Cdd:PRK07204 161 GDGAAAVVITkGDHSSRILAShmETYSSGAHLSEIRGGGTMIHPREYSEERKEDFLFDMNGRAIFKLSSKYLMKFIDKLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 235 KD-----KPVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVIFTGYGG 309
Cdd:PRK07204 241 MDagytlADIDLIVPHQASGPAMRLIRKKLGVDEERFVTIFEDHGNMIAASIPVALFEAIKQKKVQRG--NKILLLGTSA 318
|
330
....*....|
gi 488216404 310 GLTWGSILME 319
Cdd:PRK07204 319 GLSIGGILLE 328
|
|
| PRK12880 |
PRK12880 |
beta-ketoacyl-ACP synthase III; |
7-315 |
3.12e-39 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 171793 Cd Length: 353 Bit Score: 141.26 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSR----TGIRERR-CVTNQETSDLCILVAEKLIKQKNLNPKDLDFILVAT 81
Cdd:PRK12880 10 ISGICVSVPEHKICIDDELESVFSNDIKTLKRmkkvIGLNTRYiCDENTCVSDLGKHAANTLLQGLNIDKNSLDALIVVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 82 MSPDYTTPSVAAQVQGKLG-ATHAIAFDISAACSGFVYALSMAEKMIRCGSTKGLVIGGETLSKLIDWSDRTTAVLFGDG 160
Cdd:PRK12880 90 QSPDFFMPSTACYLHQLLNlSSKTIAFDLGQACAGYLYGLFVAHSLIQSGLGKILLICGDTLSKFIHPKNMNLAPIFGDG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 161 AGGILLEANPQKKLLKEkLAADGTRSSSLT----------AGYQQNKNPFYSEDSEGSYYLQMTGRDIFDFAVRDVANNI 230
Cdd:PRK12880 170 VSATLIEKTDFNEAFFE-LGSDGKYFDKLIipkgamripkADIFNDDSLMQTEEFRQLENLYMDGANIFNMALECEPKSF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 231 QEVMK-----DKPVDYLLLHQANLRIIEKIARKVKMPQEK---FLtnMDKYGNTSAASIPILLDEavssgkITLGKQQKV 302
Cdd:PRK12880 249 KEILEfskvdEKDIAFHLFHQSNAYLVDCIKEELKLNDDKvpnFI--MEKYANLSACSLPALLCE------LDTPKEFKA 320
|
330
....*....|...
gi 488216404 303 IFTGYGGGLTWGS 315
Cdd:PRK12880 321 SLSAFGAGLSWGS 333
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
239-320 |
3.75e-34 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 120.30 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 239 VDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKItlGKQQKVIFTGYGGGLTWGSILM 318
Cdd:pfam08541 11 IDWFVPHQANLRIIDAVAKRLGLPPEKVVVNLDEYGNTSAASIPLALDEAVEEGKL--KPGDLVLLVGFGAGLTWGAALL 88
|
..
gi 488216404 319 EL 320
Cdd:pfam08541 89 RW 90
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
107-183 |
1.07e-32 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 116.08 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 107 FDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLIDWSDRTTAVLFGDGAGGILLEANPQK--KLLKEKLAADG 183
Cdd:pfam08545 1 FDINAACSGFVYALSTAAALIRSGRAKnVLVIGAETLSKILDWTDRSTAVLFGDGAGAVVLEATDEPgaRILDSVLGSDG 80
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
7-320 |
2.36e-26 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 106.63 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLSKMMDTSDEWISSRTGIRERRCVTNQE-TSDLCILVAEKLIKQKNLNPKDLDFIL-VATMSP 84
Cdd:PRK06840 7 IVGTGVYLPKDVMTAEEIAEKTGIPEEVVIEKFGIYEKPVPGPEDhTSDMAIAAAKPALKQAGVDPAAIDVVIyIGSEHK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 85 DYTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKG--LVIGGETLSKLIDWSDRTTAVLF--GDG 160
Cdd:PRK06840 87 DYPVWSSAPKIQHEIGAKNAWAFDIMAVCASFPIALKVAKDLLYSDPSIEnvLLVGGYRNSDLVDYDNPRTRFMFnfAAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 161 AGGILLEANPQK-KLLKEKLAADGTRSSSLTAGYQQNKNPFYSED-SEGSYYLQMTgrDIFDFAVRDVANNIQ---EVMK 235
Cdd:PRK06840 167 GSAALLKKDAGKnRILGSAIITDGSFSEDVRVPAGGTKQPASPETvENRQHYLDVI--DPESMKERLDEVSIPnflKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 236 D---------KPVDYL-LLH---QANLRIIEKIArkvkMPQEKfLTNMDKYGNTSAASiPIL-LDEAVSSGKITLGkqQK 301
Cdd:PRK06840 245 EalrksgytpKDIDYLaILHmkrSAHIALLEGLG----LTEEQ-AIYLDEYGHLGQLD-QILsLHLALEQGKLKDG--DL 316
|
330
....*....|....*....
gi 488216404 302 VIFTGYGGGLTWGSILMEL 320
Cdd:PRK06840 317 VVLVSAGTGYTWAATVIRW 335
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
88-318 |
3.64e-22 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 95.01 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 88 TPSVAAQVQGKLGAtHAIAFDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLID------------------W 148
Cdd:cd00825 72 FPGASGQIATPLGI-HGPAYDVSAACAGSLHALSLAADAVQNGKQDiVLAGGSEELAAPMDcefdamgalstpekasrtF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 149 SDRTTAVLFGDGAGGILLEANPQkkllkekLAADGTRSSSLTAGYQQNKNPfysedsegsyylqmTGRDIFDFAVRDVAN 228
Cdd:cd00825 151 DAAADGFVFGDGAGALVVEELEH-------ALARGAHIYAEIVGTAATIDG--------------AGMGAFAPSAEGLAR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 229 NIQEVMK-----DKPVDYLLLHQANLRIIEKIARKVKMPQEKFLTN-----MDKYGNTSAASIPILLDEAVSSGKITLGK 298
Cdd:cd00825 210 AAKEALAvagltVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPavsatKAMTGNLSSAAVVLAVDEAVLMLEHGFIP 289
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488216404 299 QQK-----------------------VIFTGYGGGLTWGSILM 318
Cdd:cd00825 290 PSIhieeldeaglnivtettprelrtALLNGFGLGGTNATLVL 332
|
|
| PRK09258 |
PRK09258 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
6-320 |
7.30e-22 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 181732 Cd Length: 338 Bit Score: 94.18 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 6 MITATASVLPEKIITNNDL-SKMMDTSDEW------ISSRTGIRERRC-VTNQETSDLCILVAEKLIKQKNLNPKDLDFI 77
Cdd:PRK09258 7 AILSLAYELAPVVVTSSEIeERLAPLYERLrlppgqLEALTGIRERRWwPEGTQLSDGAIAAGRKALAEAGIDPSDIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 78 LVATMSPDYTTPSVAAQVQGKLG-ATHAIAFDISAACSGFVYALSMAEKMIRCGSTK-GLVIGGETLSKLIDW------S 149
Cdd:PRK09258 87 INTSVCRDYLEPATACRVHHNLGlPKSCANFDVSNACLGFLNGMLDAANMIELGQIDyALVVSGESAREIVEAtidrllA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 150 DRTTAVLF---------GDGAGGILL---EANPQKKLLKEKLAADGTRSSSLTAGYQQnknpFYSEDSEGsyyLQMTGRD 217
Cdd:PRK09258 167 PETTREDFaqsfatltlGSGAAAAVLtrgSLHPRGHRLLGGVTRAATEHHELCQGGRD----GMRTDAVG---LLKEGVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 218 IfdfAVRDVANNIQEV-MKDKPVDYLLLHQANLRIIEKIARKVKMPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITL 296
Cdd:PRK09258 240 L---AVDTWEAFLAQLgWAVEQVDRVICHQVGAAHTRAILKALGIDPEKVFTTFPTLGNMGPASLPITLAMAAEEGFLKP 316
|
330 340
....*....|....*....|....
gi 488216404 297 GkqQKVIFTGYGGGLTwgSILMEL 320
Cdd:PRK09258 317 G--DRVALLGIGSGLN--CSMLEV 336
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
77-318 |
7.48e-22 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 92.51 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 77 ILVATMSPDYTTPSVAAQVQGKLGATHAIAFDISAACSGFVYALSMAEKMIRCGSTKGLVIGGetlsklidwsdrTTAVL 156
Cdd:cd00327 32 VIVGTTGGSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGG------------SEEFV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 157 FGDGAGGILLEAnpqkkllKEKLAADGTRSSSLTAGYQQNknpfysedSEGSYYLQMTGRDifdfavrDVANNIQEVM-- 234
Cdd:cd00327 100 FGDGAAAAVVES-------EEHALRRGAHPQAEIVSTAAT--------FDGASMVPAVSGE-------GLARAARKALeg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 235 ---KDKPVDYLLLHQANLRIIEKIARKVKMPQEKFLTN-----MDKYGNTSAASIPILLDEAVSSGKITLGKQ-----QK 301
Cdd:cd00327 158 aglTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSPavsatLIMTGHPLGAAGLAILDELLLMLEHEFIPPtprepRT 237
|
250
....*....|....*..
gi 488216404 302 VIFTGYGGGLTWGSILM 318
Cdd:cd00327 238 VLLLGFGLGGTNAAVVL 254
|
|
| PRK07515 |
PRK07515 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
41-280 |
2.54e-21 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 236037 Cd Length: 372 Bit Score: 93.02 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 41 IRERrcvTNQETSDLC---ILVAEKLIKQKNLNPKDLDFILVATMSPDYTTPSVAAQVQGKLGAThAIAFDISAACSGFV 117
Cdd:PRK07515 84 IPER---SNDELSIQAemgVAAARQALARAGRTAEDIDAVIVACSNMQRAYPAMAIEIQQALGIE-GFAFDMNVACSSAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 118 YALSMAEKMIRCGSTKG-LVIGGETLSKLIDWSDRTTAVLFGDGAGGILLEAnpqkkllkEKLAADGTR----SSSLTAG 192
Cdd:PRK07515 160 FGIQTAANAIRSGSARRvLVVNPEICSGHLNFRDRDSHFIFGDVATAVIVER--------ADTATSAGGfeilGTRLFTQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 193 YQQN-KNPF--------YSEDSEGSYYLQmTGRDIFDFAVRDVANNIQEVMKD---KPVDY--LLLHQANLRIIEKIARK 258
Cdd:PRK07515 232 FSNNiRNNFgflnradpEGIGARDKLFVQ-EGRKVFKEVCPMVAEHIVEHLAEnglTPADVkrFWLHQANINMNQLIGKK 310
|
250 260
....*....|....*....|....*
gi 488216404 259 V---KMPQEKFLTNMDKYGNTSAAS 280
Cdd:PRK07515 311 VlgrDATPEEAPVILDEYANTSSAG 335
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
7-303 |
3.86e-17 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 81.11 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 7 ITATASVLPEKIITNNDLskmmdtsDEWI------SSRT--------GIRERRCVTNQE------TSDLCILVAEKLIKQ 66
Cdd:PRK06816 5 ITSTGAFLPGEPVSNDEM-------EAYLglingkPSRArriilrnnGIKTRHYALDPEgrpthsNAQMAAEAIRDLLDD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 67 KNLNPKDLDFILVATMSPDYTTPSVAAQVQGKLGAtHAIAFdISAA--CSGFVYALSMAEKMIRCG-STKGLVIGGETLS 143
Cdd:PRK06816 78 AGFSLGDIELLACGTSQPDQLMPGHASMVHGELGA-PPIEV-VSSAgvCAAGMMALKYAYLSVKAGeSRNAVATASELAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 144 KLI------DWSDRTTAV---------------LFGDGAGGILLEANPQKKLLKEKLaaDGTRSSSLT--------AGYQ 194
Cdd:PRK06816 156 RWFrasrfeAEEEKLAELeenpeiafekdflrwMLSDGAGAVLLENKPRPDGLSLRI--DWIDLRSYAgelpvcmyAGAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 195 QNknpfysEDSEGSYYLQMTGRDIFD---FAVR-DVA---NNI----QEVMKD-------KP--VDYLLLHQANLRIIEK 254
Cdd:PRK06816 234 KN------EDGSLKGWSDYPPEEAEAasaLSLKqDVRllnENIvvytIKPLLElvdkrnlDPddIDYFLPHYSSEYFREK 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488216404 255 IARKVK-----MPQEKFLTNMDKYGNTSAASIPILLDEAVSSGKITLGkqQKVI 303
Cdd:PRK06816 308 IVELLAkagfmIPEEKWFTNLATVGNTGSASIYIMLDELLNSGRLKPG--QKIL 359
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
28-312 |
9.46e-11 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 61.86 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 28 MDTSDEW----ISSRTGIRERRCVTNQETSDLCILVAEKLIKQKNLNPKDLDfILVATMSPDYTTPSVAAQVQGKLG-AT 102
Cdd:cd00831 57 LPGGEETyaprPEMSPSLDERNDIALEEARELAEEAARGALDEAGLRPSDID-HLVVNTSTGNPTPSLDAMLINRLGlRP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 103 HAIAFDISA-ACSGFVYALSMAEKMIR-CGSTKGLVIGGETLSKLIDWSDRT----TAVLFGDGAGGILLEANPQ-KKLL 175
Cdd:cd00831 136 DVKRYNLGGmGCSAGAIALDLAKDLLEaNPGARVLVVSTELCSLWYRGPDHRsmlvGNALFGDGAAAVLLSNDPRdRRRE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 176 KEKLAADGTRSSSLTAgyqqnknpfySEDSEGsYYLQMTG------RDIFDFAVRDVANNIQEVMKDKP-------VDYL 242
Cdd:cd00831 216 RPLFELVRAASTLLPD----------SEDAMG-WHLGEEGltfvlsRDVPRLVEKNLERVLRKLLARLGiglfklaFDHW 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488216404 243 LLHQANLRIIEKIARKVKMPQEKfltnMD-------KYGNTSAASIPILLDEAVSSGKitLGKQQKVIFTGYGGGLT 312
Cdd:cd00831 285 CVHPGGRAVLDAVEKALGLSPED----LEasrmvlrRYGNMSSSSVLYVLAYMEAKGR--VKRGDRGLLIAFGPGFT 355
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
154-312 |
3.11e-04 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 41.95 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 154 AVLFGDGAGGILLEANPQ---KKLLKEKLAADGTrsssltagyqqnknpfYSEDSEGSYYLQMTGRDIFDFAVRDV---- 226
Cdd:PLN03168 211 SALFGDGAGVYVVGSDPKpevEKALFEVHWAGET----------------ILPESDGAIDGHLTEAGLIFHLMKDVpgli 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 227 ANNIQEVMKD--KPVD-------YLLLHQANLRIIEKIARKVKMPQEKFLTNMD---KYGNTSAASIPILLDE----AVS 290
Cdd:PLN03168 275 SKNIEKFLNEarKCVGspdwnemFWAVHPGGPAILDQVEAKLKLTKDKMQGSRDilsEFGNMSSASVLFVLDQirqrSVK 354
|
170 180
....*....|....*....|...
gi 488216404 291 SGKITLGKQQKV-IFTGYGGGLT 312
Cdd:PLN03168 355 MGASTLGEGSEFgFFIGFGPGLT 377
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
53-143 |
1.01e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 39.98 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 53 SDLCILVAEKLIKQKNLNPKDLDFILVATMSPDYTTPSVAAQVQGKLGATH-AIAFDISAACSGFVYALSMAEKMIRCG- 130
Cdd:pfam00108 24 VELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDsAPAVTINKVCGSGLKAVYLAAQSIASGd 103
|
90
....*....|...
gi 488216404 131 STKGLVIGGETLS 143
Cdd:pfam00108 104 ADVVLAGGVESMS 116
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
156-318 |
6.56e-03 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 38.16 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 156 LFGDGAGGILLEANPQKKLLKEKLAADGTRSSSLTagyqqnknpfyseDSEGSY--YLQMTG------RDIFDFAVRDVA 227
Cdd:PLN03170 218 LFGDGAAAVIVGADPDERVERPLFQLVSASQTILP-------------DSEGAIdgHLREVGltfhllKDVPGLISKNIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216404 228 NNIQEVMK-----DKPVDYLLLHQANLRIIEKIARKVKMPQEKFLTN---MDKYGNTSAASIPILLDE----AVSSGKIT 295
Cdd:PLN03170 285 RSLEEAFKplgitDYNSIFWVAHPGGPAILDQVEAKVGLEKERMRATrhvLSEYGNMSSACVLFILDEmrkrSAEDGQAT 364
|
170 180
....*....|....*....|....*
gi 488216404 296 LGK--QQKVIFtGYGGGLTWGSILM 318
Cdd:PLN03170 365 TGEgfDWGVLF-GFGPGLTVETVVL 388
|
|
| |
