|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
9-417 |
1.29e-173 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 491.15 E-value: 1.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIP-FELNlSPFSKRILKNTPRFGRLGLIAAD 86
Cdd:COG0304 2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASgLPVRIAGEVKdFDPE-EYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 87 EALKMAfGDDLSELDKHyppfsR-GVIFGTGWGGADALAQNSLSYNTEGFA--SPLTNILSMNNVGSAIMSMNWNLRGYQ 163
Cdd:COG0304 81 EALADA-GLDLDEVDPD-----RtGVIIGSGIGGLDTLEEAYRALLEKGPRrvSPFFVPMMMPNMAAGHVSIRFGLKGPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 164 NTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEGAA 243
Cdd:COG0304 155 YTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 244 VLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETE 321
Cdd:COG0304 235 VLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLspEDIDYINAHGTSTPLGDAAETK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 322 MLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVLNV 401
Cdd:COG0304 315 AIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSN 393
|
410
....*....|....*.
gi 2468800260 402 NYGFGGSNSALIFERY 417
Cdd:COG0304 394 SFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-414 |
4.28e-173 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 489.74 E-value: 4.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPFELNLSPFSKRILKNTPRFGRLGLIAAD 86
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASgFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 87 EALKMAFGDDlseldKHYPPFSRGVIFGTGWGGADALAQNSLSYNTEG--FASPLTNILSMNNVGSAIMSMNWNLRGYQN 164
Cdd:cd00834 81 EALADAGLDP-----EELDPERIGVVIGSGIGGLATIEEAYRALLEKGprRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 165 TPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEGAAV 244
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 245 LCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL--VDYVNAHGTSTQLNDFNETEM 322
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPedIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 323 LKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVLNVN 402
Cdd:cd00834 316 IKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNS 394
|
410
....*....|..
gi 2468800260 403 YGFGGSNSALIF 414
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
8-414 |
7.10e-138 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 400.32 E-value: 7.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPfelNLSP---FSKRILKNTPRFGRLGLI 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASdLPVKIAGEVK---DFDPedyIDKKEARRMDRFIQYALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 84 AADEALKMAfGDDLSELDKhyppfSR-GVIFGTGWGGADALAQNSLSYNTEGF--ASPLTNILSMNNVGSAIMSMNWNLR 160
Cdd:TIGR03150 78 AAKEAVEDS-GLDIEEEDA-----ERvGVIIGSGIGGLETIEEQHIVLLEKGPrrVSPFFIPMSIINMAAGQISIRYGAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 161 GYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSE 240
Cdd:TIGR03150 152 GPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 241 GAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFN 318
Cdd:TIGR03150 232 GAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGInpEDVDYINAHGTSTPLGDKA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 319 ETEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSV 398
Cdd:TIGR03150 312 ETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYA 390
|
410
....*....|....*.
gi 2468800260 399 LNVNYGFGGSNSALIF 414
Cdd:TIGR03150 391 LSNSFGFGGTNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
7-418 |
3.16e-136 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 396.47 E-value: 3.16e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 7 RQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPfELNLSPF-SKRILKNTPRFGRLGLIA 84
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSdLAVKIAGEVK-DFNPDDYmSRKEARRMDRFIQYGIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 85 ADEALKMAfGDDLSELDKhyppfSR-GVIFGTGWGGADALAQNSLSYNTEGFA--SPLTNILSMNNVGSAIMSMNWNLRG 161
Cdd:PRK07314 80 AKQAVEDA-GLEITEENA-----DRiGVIIGSGIGGLETIEEQHITLLEKGPRrvSPFFVPMAIINMAAGHVSIRYGAKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 162 YQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEG 241
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 242 AAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNE 319
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGInpEDIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 320 TEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVL 399
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERK-IDYAL 392
|
410
....*....|....*....
gi 2468800260 400 NVNYGFGGSNSALIFERYK 418
Cdd:PRK07314 393 SNSFGFGGTNASLVFKRYE 411
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
261-374 |
3.79e-35 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 125.76 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 261 LAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETEMLKMVFGDSVYS--LPI 336
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVdpEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2468800260 337 SSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLN 374
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
169-415 |
9.00e-15 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 74.29 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGeSLNSDLNIW-SIDILNALSKEQEnvetaCCPFDRNRNGFVLSEGAAVLCL 247
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGV-NLILSPDTFvGLSRAGMLSPDGR-----CKTFDASADGYVRGEGVGVVVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 248 EKYETALTRGATILAEVTGYGNCSDAYDV--TTPapdcggryhavkyalkqadielvdyvNAHGtstQlndfnetemlkm 325
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSNgiTAP--------------------------SGPA---Q------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 326 vfgdsvysLPISSTKSYTGHLIAAAGaLESIlsIK---SIETNIIPATIHLNNPDPGCNLD----YVPNKHRQVENIQSV 398
Cdd:smart00825 209 --------LLIGSVKSNIGHLEAAAG-VAGL--IKvvlALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGRP 277
|
250 260
....*....|....*....|
gi 2468800260 399 LNV---NYGFGGSNSALIFE 415
Cdd:smart00825 278 RRAgvsSFGFGGTNAHVILE 297
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
9-417 |
1.29e-173 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 491.15 E-value: 1.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIP-FELNlSPFSKRILKNTPRFGRLGLIAAD 86
Cdd:COG0304 2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASgLPVRIAGEVKdFDPE-EYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 87 EALKMAfGDDLSELDKHyppfsR-GVIFGTGWGGADALAQNSLSYNTEGFA--SPLTNILSMNNVGSAIMSMNWNLRGYQ 163
Cdd:COG0304 81 EALADA-GLDLDEVDPD-----RtGVIIGSGIGGLDTLEEAYRALLEKGPRrvSPFFVPMMMPNMAAGHVSIRFGLKGPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 164 NTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEGAA 243
Cdd:COG0304 155 YTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 244 VLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETE 321
Cdd:COG0304 235 VLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLspEDIDYINAHGTSTPLGDAAETK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 322 MLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVLNV 401
Cdd:COG0304 315 AIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSN 393
|
410
....*....|....*.
gi 2468800260 402 NYGFGGSNSALIFERY 417
Cdd:COG0304 394 SFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
8-414 |
4.28e-173 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 489.74 E-value: 4.28e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPFELNLSPFSKRILKNTPRFGRLGLIAAD 86
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASgFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 87 EALKMAFGDDlseldKHYPPFSRGVIFGTGWGGADALAQNSLSYNTEG--FASPLTNILSMNNVGSAIMSMNWNLRGYQN 164
Cdd:cd00834 81 EALADAGLDP-----EELDPERIGVVIGSGIGGLATIEEAYRALLEKGprRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 165 TPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEGAAV 244
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 245 LCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL--VDYVNAHGTSTQLNDFNETEM 322
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPedIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 323 LKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVLNVN 402
Cdd:cd00834 316 IKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNS 394
|
410
....*....|..
gi 2468800260 403 YGFGGSNSALIF 414
Cdd:cd00834 395 FGFGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
8-414 |
7.10e-138 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 400.32 E-value: 7.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPfelNLSP---FSKRILKNTPRFGRLGLI 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASdLPVKIAGEVK---DFDPedyIDKKEARRMDRFIQYALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 84 AADEALKMAfGDDLSELDKhyppfSR-GVIFGTGWGGADALAQNSLSYNTEGF--ASPLTNILSMNNVGSAIMSMNWNLR 160
Cdd:TIGR03150 78 AAKEAVEDS-GLDIEEEDA-----ERvGVIIGSGIGGLETIEEQHIVLLEKGPrrVSPFFIPMSIINMAAGQISIRYGAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 161 GYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSE 240
Cdd:TIGR03150 152 GPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 241 GAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFN 318
Cdd:TIGR03150 232 GAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGInpEDVDYINAHGTSTPLGDKA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 319 ETEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSV 398
Cdd:TIGR03150 312 ETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYA 390
|
410
....*....|....*.
gi 2468800260 399 LNVNYGFGGSNSALIF 414
Cdd:TIGR03150 391 LSNSFGFGGTNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
7-418 |
3.16e-136 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 396.47 E-value: 3.16e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 7 RQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPfELNLSPF-SKRILKNTPRFGRLGLIA 84
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSdLAVKIAGEVK-DFNPDDYmSRKEARRMDRFIQYGIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 85 ADEALKMAfGDDLSELDKhyppfSR-GVIFGTGWGGADALAQNSLSYNTEGFA--SPLTNILSMNNVGSAIMSMNWNLRG 161
Cdd:PRK07314 80 AKQAVEDA-GLEITEENA-----DRiGVIIGSGIGGLETIEEQHITLLEKGPRrvSPFFVPMAIINMAAGHVSIRYGAKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 162 YQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEG 241
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 242 AAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNE 319
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGInpEDIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 320 TEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVL 399
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERK-IDYAL 392
|
410
....*....|....*....
gi 2468800260 400 NVNYGFGGSNSALIFERYK 418
Cdd:PRK07314 393 SNSFGFGGTNASLVFKRYE 411
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
8-417 |
1.13e-108 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 325.92 E-value: 1.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDdsiTAKFFGKIPFEL-NLSP---FSKRILKNTPRFGRLGLI 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFD---ASDFPVQIAGEItDFDPtevMDPKEVKKADRFIQLGLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 84 AADEALKMAfGDDLSELDKHyppfSRGVIFGTGWGGADALAQNSLSYNTEG--------FASPLTNILSmnnvgsAIMSM 155
Cdd:PRK08439 79 AAREAMKDA-GFLPEELDAE----RFGVSSASGIGGLPNIEKNSIICFEKGprkispffIPSALVNMLG------GFISI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 156 NWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNG 235
Cdd:PRK08439 148 EHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 236 FVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDcgGRYHAVKYALKQADIELVDYVNAHGTSTQLN 315
Cdd:PRK08439 228 FVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPKIDYINAHGTSTPYN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 316 DFNETEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnI 395
Cdd:PRK08439 306 DKNETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAE-L 384
|
410 420
....*....|....*....|..
gi 2468800260 396 QSVLNVNYGFGGSNSALIFERY 417
Cdd:PRK08439 385 NVVMSNSFGFGGTNGVVIFKKV 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
5-418 |
4.04e-107 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 322.72 E-value: 4.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 5 NSRQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKY-EYSDDSITAKFFGKIPF-----ELNLSP---FSKRILKNTP 75
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLtDFPVGDLATKIGGQVPDlaedaEAGFDPdryLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 76 RFGRLGLIAADEALKMAFGDDLSELDKHyppfSRGVIFGTGWGGADALAQNSLSYNTEGF--ASPLTNILSMNNVGSAIM 153
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLEDRE----RTATIIGSGVGGFPAIAEAVRTLDSRGPrrLSPFTIPSFLTNMAAGHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 154 SMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESlnsdlniwSIDILN--------ALSKE-QENVET 224
Cdd:PRK06333 157 SIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEA--------AIDRVSlagfaaarALSTRfNDAPEQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 225 ACCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELV 302
Cdd:PRK06333 229 ASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIppEEV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 303 DYVNAHGTSTQLNDFNETEMLKMVFGdSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCN- 381
Cdd:PRK06333 309 QHLNAHATSTPVGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEg 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 2468800260 382 LDYVPNKHRQVEnIQSVLNVNYGFGGSNSALIFERYK 418
Cdd:PRK06333 388 LDVVANKARPMD-MDYALSNGFGFGGVNASILFRRWE 423
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
17-417 |
1.37e-101 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 308.16 E-value: 1.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 17 AVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDSITAKFFGKIPFELNLSPFSKRI----------------LKNTPRFGRL 80
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVAAMPCQIaaevdqsefdpsdfapTKRESRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 81 GLIAADEALKMAFGDDLSELDKHyppfSRGVIFGTGWGGADALAQNSLSYNTEGFA--SPLTNILSMNNVGSAIMSMNWN 158
Cdd:PTZ00050 81 AMAAAREALADAKLDILSEKDQE----RIGVNIGSGIGSLADLTDEMKTLYEKGHSrvSPYFIPKILGNMAAGLVAIKHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 159 LRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALS-KEQENVETACCPFDRNRNGFV 237
Cdd:PTZ00050 157 LKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtKYNDDPQRASRPFDKDRAGFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 238 LSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQ-ADIEL--VDYVNAHGTSTQL 314
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANINIndVDYVNAHATSTPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 315 NDFNETEMLKMVFGDS-VYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQ-V 392
Cdd:PTZ00050 317 GDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHpL 396
|
410 420
....*....|....*....|....*
gi 2468800260 393 ENIQSVLNVNYGFGGSNSALIFERY 417
Cdd:PTZ00050 397 QSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
9-414 |
3.80e-89 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 277.06 E-value: 3.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSD---------------DSITAKFFGKIPFELNLSPFSKRIL-- 71
Cdd:PLN02836 7 RVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDlkmksedeetqlytlDQLPSRVAALVPRGTGPGDFDEELWln 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 72 -KNTPRFGRLGLIAADEALKMAFGDDLSELDKHyppfSRGVIFGTGWGG------ADALAQNSLSYNTEGFASPltNILS 144
Cdd:PLN02836 87 sRSSSRFIGYALCAADEALSDARWLPSEDEAKE----RTGVSIGGGIGSitdileAAQLICEKRLRRLSPFFVP--RILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 145 mnNVGSAIMSMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALS-KEQENVE 223
Cdd:PLN02836 161 --NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStKFNSCPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 224 TACCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL-- 301
Cdd:PLN02836 239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPnq 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 302 VDYVNAHGTSTQLNDFNETEMLKMVFGDSVYS--LPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPG 379
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*
gi 2468800260 380 CNLDYVPNKHRQVENIQSVLNVNYGFGGSNSALIF 414
Cdd:PLN02836 399 FDDGFVPLTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
6-416 |
1.11e-83 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 262.25 E-value: 1.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 6 SRQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDSITAKFFGKIPFELNLSPF-SKRILKNTPRFGRLGLIA 84
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYmSKKDARKMDLFIQYGIAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 85 ADEALKMAfGDDLSELDKHyppfSRGVIFGTGWGGADALAQNSLSYNTEG--FASPLTNILSMNNVGSAIMSMNWNLRGY 162
Cdd:PRK08722 82 GIQALDDS-GLEVTEENAH----RIGVAIGSGIGGLGLIEAGHQALVEKGprKVSPFFVPSTIVNMIAGNLSIMRGLRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 163 QNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSEGA 242
Cdd:PRK08722 157 NIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 243 AVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNET 320
Cdd:PRK08722 237 GMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVtgEQIGYVNAHGTSTPAGDVAEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 321 EMLKMVFGDS-VYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVENIQSVL 399
Cdd:PRK08722 317 KGIKRALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAI 396
|
410
....*....|....*..
gi 2468800260 400 NVNYGFGGSNSALIFER 416
Cdd:PRK08722 397 CNSFGFGGTNGSLIFKK 413
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
8-414 |
1.01e-78 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 249.13 E-value: 1.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSD--DSITAKFFGKIP-FELNlSPFSKRILKNTPRFGRLGLIA 84
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDryDGLNTRLAAPIDdFELP-AHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 85 ADEALKMA-FGDDLSELDKhyppfSRGVIFGTGWGGAD---ALAQNSLSYNTEGFASPlTNILSMNNVGSAIMSMNWNLR 160
Cdd:PRK09116 81 SELALEDAgLLGDPILTDG-----RMGIAYGSSTGSTDpigAFGTMLLEGSMSGITAT-TYVRMMPHTTAVNVGLFFGLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 161 GYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLnSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVLSE 240
Cdd:PRK09116 155 GRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEEL-CPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 241 GAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRyhAVKYALKQADI--ELVDYVNAHGTSTQLNDFN 318
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLapEDIGYVNAHGTATDRGDIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 319 ETEMLKMVFGDSVyslPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGC-NLDYVPNKHRQVENiQS 397
Cdd:PRK09116 312 ESQATAAVFGARM---PISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDT-EY 387
|
410
....*....|....*..
gi 2468800260 398 VLNVNYGFGGSNSALIF 414
Cdd:PRK09116 388 VMSNNFAFGGINTSLIF 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
7-418 |
3.92e-76 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 243.00 E-value: 3.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 7 RQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKY-EYSDDSITAKFFGKIPFeLNLSPFSKrilknTPRFGRLGLIAA 85
Cdd:PRK06501 10 RPIVAVTGMGVVTSLGQGKADNWAALTAGESGIHTItRFPTEGLRTRIAGTVDF-LPESPFGA-----SALSEALARLAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 86 DEALKMA------FGDDL------SELD----------------------------KHYPPFSRGVIFGTGwggADALAQ 125
Cdd:PRK06501 84 EEALAQAgigkgdFPGPLflaappVELEwparfalaaavgdndapsydrllraargGRFDALHERFQFGSI---ADRLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 126 NslsYNTEGfaSPLTniLSmnnvgsaimsmnwnlrgyqntpvSACATGGIAIGDAVEIIRSGRAE--MMIAGGGeSLNSD 203
Cdd:PRK06501 161 R---FGTRG--LPIS--LS-----------------------TACASGATAIQLGVEAIRRGETDraLCIATDG-SVSAE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 204 LNIwSIDILNALSKEQENVETACCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDC 283
Cdd:PRK06501 210 ALI-RFSLLSALSTQNDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 284 GGRYHAVKYALKQA--DIELVDYVNAHGTSTQLNDFNETEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKS 361
Cdd:PRK06501 289 SPAIGAIRAALADAglTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLT 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2468800260 362 IETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnIQSVLNVNYGFGGSNSALIFERYK 418
Cdd:PRK06501 369 IQTGRLPPTINYDNPDPAIPLDVVPNVARDAR-VTAVLSNSFGFGGQNASLVLTAEP 424
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
8-418 |
2.98e-68 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 221.85 E-value: 2.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKY-EYSDDSITAKFFGKIpfELNLSPF-SKRILkntpRFGRLGLIAA 85
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSpEFAEMGMRSQVWGNV--KLDPTGLiDRKVM----RFMGDASAYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 86 DEALKMAFGDdlSELDKHYPPFSR-GVIFGTGWG-------GADALAQNSLSYNTEGFASPLTnilsMNNVGSAIMSMNW 157
Cdd:PRK07967 76 YLAMEQAIAD--AGLSEEQVSNPRtGLIAGSGGGstrnqveAADAMRGPRGPKRVGPYAVTKA----MASTVSACLATPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 158 NLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNsdlniWSI----DILNALS-KEQENVETACCPFDRN 232
Cdd:PRK07967 150 KIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELD-----WEMsclfDAMGALStKYNDTPEKASRAYDAN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 233 RNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTtpAPDCGGRYHAVKYALKQADIElVDYVNAHGTST 312
Cdd:PRK07967 225 RDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMV--APSGEGAVRCMQMALATVDTP-IDYINTHGTST 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 313 QLNDFNETEMLKMVFGDSVysLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDP---GCNldyVPNKH 389
Cdd:PRK07967 302 PVGDVKELGAIREVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPqaaGMP---IVTET 376
|
410 420
....*....|....*....|....*....
gi 2468800260 390 RQVENIQSVLNVNYGFGGSNSALIFERYK 418
Cdd:PRK07967 377 TDNAELTTVMSNSFGFGGTNATLVFRRYK 405
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
8-412 |
3.30e-68 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 221.93 E-value: 3.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 8 QRVVVTGYGAVTSLGQN---VEEIWKAIMDYKIGYSKYEYSDDSITAKFFGKIPFElnlsPFSKRILKNT---PRFGRLG 81
Cdd:cd00828 1 SRVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLKSRFDRGVAGQIPTG----DIPGWDAKRTgivDRTTLLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 82 LIAADEALKMAFGDDLSELDkhypPFSRGVIFGTGWGGADAL--AQNSLSYNTEGFASPLtNILSMNNVGSAIMSMNWNL 159
Cdd:cd00828 77 LVATEEALADAGITDPYEVH----PSEVGVVVGSGMGGLRFLrrGGKLDARAVNPYVSPK-WMLSPNTVAGWVNILLLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 160 RGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDIlNALSKEQENVETACCPFDRNRNGFVLS 239
Cdd:cd00828 152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANM-GALSTAEEEPEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 240 EGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDcGGRYHAVKYALKQA--DIELVDYVNAHGTSTQLNDF 317
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGG-KGIARAIRTALAKAglSLDDLDVISAHGTSTPANDV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 318 NETEMLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQ-VENIQ 396
Cdd:cd00828 310 AESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlNLKVR 389
|
410
....*....|....*.
gi 2468800260 397 SVLNVNYGFGGSNSAL 412
Cdd:cd00828 390 AALVNAFGFGGSNAAL 405
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
7-418 |
3.29e-67 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 222.93 E-value: 3.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 7 RQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPFELNLSPFSKRILKNTPRFGRLGLIAA 85
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSqFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 86 DEALKMA--FGDDLSELDKhyppfSR-GVIFGTGWGGA----DALAQNSLSYNTegfASPLTNILSMNNVGSAIMSMNWN 158
Cdd:PLN02787 208 KKALADGgiTEDVMKELDK-----TKcGVLIGSAMGGMkvfnDAIEALRISYRK---MNPFCVPFATTNMGSAMLAMDLG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 159 LRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKEQENVETACCPFDRNRNGFVL 238
Cdd:PLN02787 280 WMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVM 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 239 SEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLND 316
Cdd:PLN02787 360 GEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVskEDVNYINAHATSTKAGD 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 317 FNETEMLKMVFGDSVySLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVENIQ 396
Cdd:PLN02787 440 LKEYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIK 518
|
410 420
....*....|....*....|..
gi 2468800260 397 SVLNVNYGFGGSNSALIFERYK 418
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFAPYK 540
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
91-417 |
7.81e-67 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 216.13 E-value: 7.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 91 MAFGDDLSELDKHYPPFSRGVIFGTGWGGADALAQNSLSYNTEG--FASPLTNILSMNNVGSAIMSMNWNLRGYQNTPVS 168
Cdd:PRK14691 10 ITFHPSLTHADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGpkRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKE-QENVETACCPFDRNRNGFVLSEGAAVLCL 247
Cdd:PRK14691 90 ACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 248 EKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETEMLKM 325
Cdd:PRK14691 170 EELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGItpEQVQHLNAHATSTPVGDLGEINAIKH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 326 VFGDSvYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVENIQSVLNVNYGF 405
Cdd:PRK14691 250 LFGES-NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGF 328
|
330
....*....|..
gi 2468800260 406 GGSNSALIFERY 417
Cdd:PRK14691 329 AGVNASILLKRW 340
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
9-412 |
1.13e-65 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 214.53 E-value: 1.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGqNVEEIWKAIMDYKIGYSKYEysddsitakffgkiPFElNLSPFSKRILKNTPRF-GRLGLIAADE 87
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQ--------------PFP-ELPPLPLGLIGNQPSSlEDLTKTVVTA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 88 ALKMAfgddlseldKHYPPF-SRGVIFGT--GWGGA--DALAQNSLSYNTEGFASPLTNILSMNNVGSAIMSMNwnLRGY 162
Cdd:PRK05952 67 ALKDA---------GLTPPLtDCGVVIGSsrGCQGQweKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAAR--QIGT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 163 QNT---PVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKeqenveTACCPFDRNRNGFVLS 239
Cdd:PRK05952 136 QGPvlaPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 240 EGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL--VDYVNAHGTSTQLNDF 317
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPedIDYIHAHGTATRLNDQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 318 NETEMLKMVFGDSVyslPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDpgCNLDYVPNKHRQveNIQS 397
Cdd:PRK05952 290 REANLIQALFPHRV---AVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFVRQAQQS--PLQN 362
|
410
....*....|....*
gi 2468800260 398 VLNVNYGFGGSNSAL 412
Cdd:PRK05952 363 VLCLSFGFGGQNAAI 377
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
10-417 |
4.10e-65 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 214.21 E-value: 4.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 10 VVVTGYGAVTSLGQNVEEIWKAIMDykiGYSKYEYSDDSITAKF-----FG---KIPFELNLSPFSKRilkNTPRFGRLG 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLD---GQSGIRTLDDPFVEEFdlpvrIGghlLEEFDHQLTRVELR---RMSYLQRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 82 LIAADEALKMAFGDDLSeldkhypPFSRGVIFGTGWGGADALAQNSLSYNTEGF--ASPLTNILSMNNVGSAIMSMNWNL 159
Cdd:PRK07910 88 TVLGRRVWENAGSPEVD-------TNRLMVSIGTGLGSAEELVFAYDDMRARGLraVSPLAVQMYMPNGPAAAVGLERHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 160 RGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNA-LSKEQENVETACCPFDRNRNGFVL 238
Cdd:PRK07910 161 KAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 239 SEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL--VDYVNAHGTSTQLND 316
Cdd:PRK07910 241 GEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPgdIDHVNAHATGTSVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 317 FNETEMLKMVFGD---SVYslpisSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQvE 393
Cdd:PRK07910 321 VAEGKAINNALGGhrpAVY-----APKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP-G 394
|
410 420
....*....|....*....|....
gi 2468800260 394 NIQSVLNVNYGFGGSNSALIFERY 417
Cdd:PRK07910 395 NYRYAINNSFGFGGHNVALAFGRY 418
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
7-416 |
1.06e-49 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 173.29 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 7 RQRVVVTGYGAVTSLGQNVEEIWKAIMDYKIGY--------SKYEYSDDSITAKFFG-KIPFELNLSPFSKRILKNTPRF 77
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrQVPDDAGAGLASAFIGaELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 78 GRLGLIAADEALKMAFGDDlseldkhYPPFSRGVIFGtgwggADALAQNSL-----SY-NTEGFASPlTNILS-MNNVGS 150
Cdd:PRK07103 81 AQAALAAAREAWRDAALGP-------VDPDRIGLVVG-----GSNLQQREQalvheTYrDRPAFLRP-SYGLSfMDTDLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 151 AIMSMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESlnsDLNIWSIDILNAL-----SKEQENVETA 225
Cdd:PRK07103 148 GLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALM---DLSYWECQALRSLgamgsDRFADEPEAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 226 CCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYdvTTPAPDCGGRYHAVKYALKQADI--ELVD 303
Cdd:PRK07103 225 CRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDAN--RGPDPSLEGEMRVIRAALRRAGLgpEDID 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 304 YVNAHGTSTQLNDfnETEmLKMVFGDSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNP-DPGCNl 382
Cdd:PRK07103 303 YVNPHGTGSPLGD--ETE-LAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFR- 378
|
410 420 430
....*....|....*....|....*....|....
gi 2468800260 383 dYVpNKHRQVENIQSVLNVNYGFGGSNSALIFER 416
Cdd:PRK07103 379 -WV-GSTAESARIRYALSLSFGFGGINTALVLER 410
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
168-416 |
1.22e-45 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 161.93 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 168 SACATGGIAIGDAVEIIRSGRAEMMIAGGGESLnSDLNIWSIDILNALSKEQenvetaCCPFDRNRNGFVLSEGAAVLCL 247
Cdd:PRK09185 158 TACSSSAKVFASARRLLEAGLCDAAIVGGVDSL-CRLTLNGFNSLESLSPQP------CRPFSANRDGINIGEAAAFFLL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 248 EKyetalTRGATILaeVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADIEL--VDYVNAHGTSTQLNDFNETEMLKM 325
Cdd:PRK09185 231 ER-----EDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPadIGYINLHGTATPLNDAMESRAVAA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 326 VFGDSVyslPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKhRQVENIQSVLNVNYGF 405
Cdd:PRK09185 304 VFGDGV---PCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVEN-AQALAIRYVLSNSFAF 379
|
250
....*....|.
gi 2468800260 406 GGSNSALIFER 416
Cdd:PRK09185 380 GGNNCSLIFGR 390
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
51-413 |
4.96e-44 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 158.49 E-value: 4.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 51 AKFFGKIPFELNLSpfskrilknTPRFgRLGLIAADEALKMAFGDDLSELDKHyppfsRGVIFGTGWGGADALAQNSLSY 130
Cdd:cd00833 71 AAFFGISPREAEAM---------DPQQ-RLLLEVAWEALEDAGYSPESLAGSR-----TGVFVGASSSDYLELLARDPDE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 131 ntegfASPLTNILSMNNVGSAIMSMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGeSLNSDLNIW-SI 209
Cdd:cd00833 136 -----IDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGV-NLILSPDMFvGF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 210 DILNALSKEqenveTACCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYD--VTTPAPDcgGRY 287
Cdd:cd00833 210 SKAGMLSPD-----GRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTkgITAPSGE--AQA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 288 HAVKYALKQADIEL--VDYVNAHGTSTQLNDFNETEMLKMVFG---DSVYSLPISSTKSYTGHLIAAAGALESILSIKSI 362
Cdd:cd00833 283 ALIRRAYARAGVDPsdIDYVEAHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLAL 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2468800260 363 ETNIIPATIHLNNPDPGCNLD----YVP--NKHRQVENIQSVLNVN-YGFGGSNSALI 413
Cdd:cd00833 363 EHGVIPPNLHFETPNPKIDFEesplRVPteARPWPAPAGPRRAGVSsFGFGGTNAHVI 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
76-413 |
1.01e-42 |
|
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: 152.79 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 76 RFGRLGLIAADEALKMAfgddlsELDKHYPPFSR-GVIFGTGWG-------GADALAQNSLSYNTEGFASPLT-NILSMN 146
Cdd:cd00825 10 YVSILGFEAAERAIADA------GLSREYQKNPIvGVVVGTGGGsprfqvfGADAMRAVGPYVVTKAMFPGASgQIATPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 147 NVGSAIMSMNwnlrgyqntpvSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLnsdlnIWSIDILNALSKEQENVETAC 226
Cdd:cd00825 84 GIHGPAYDVS-----------AACAGSLHALSLAADAVQNGKQDIVLAGGSEEL-----AAPMDCEFDAMGALSTPEKAS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 227 CPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDY 304
Cdd:cd00825 148 RTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLtvWDIDY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 305 VNAHGTSTQLNDFNETEMLKMVFGDsvYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPgcNLDY 384
Cdd:cd00825 228 LVAHGTGTPIGDVKELKLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLN 303
|
330 340
....*....|....*....|....*....
gi 2468800260 385 VPNKHRQVEnIQSVLNVNYGFGGSNSALI 413
Cdd:cd00825 304 IVTETTPRE-LRTALLNGFGLGGTNATLV 331
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
9-413 |
4.40e-40 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 147.51 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYSKYEYSDDS-ITAKFFGKIPFELNLSPFSKRILKNTPRFGRLGLIAADE 87
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSgYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAADW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 88 ALKMAfGDDLSELdkhyPPFSRGVIFGTGWGGADaLAQNSL-SYNTEG--FASPLTNILSMNNVGSAIMSMNWNLRGyqn 164
Cdd:cd00832 82 ALADA-GVDPAAL----PPYDMGVVTASAAGGFE-FGQRELqKLWSKGprHVSAYQSFAWFYAVNTGQISIRHGMRG--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 165 tPVSACAT---GGI-AIGDAVEIIRSGrAEMMIAGGGESLNSDLNiWSIDILNALSKEQENVETACCPFDRNRNGFVLSE 240
Cdd:cd00832 153 -PSGVVVAeqaGGLdALAQARRLVRRG-TPLVVSGGVDSALCPWG-WVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 241 GAAVLCLEKYETALTRGATILAEVTGYGNCSDaydvttPAPDCG---GRYHAVKYALKQADI--ELVDYVNAHGTSTQLN 315
Cdd:cd00832 230 GGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPGSGrppGLARAIRLALADAGLtpEDVDVVFADAAGVPEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 316 DFNETEMLKMVFGDsvYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDPGCNLDYVPNKHRQVEnI 395
Cdd:cd00832 304 DRAEAAALAAVFGP--RGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAA-L 380
|
410
....*....|....*...
gi 2468800260 396 QSVLNVNYGFGGSNSALI 413
Cdd:cd00832 381 RTALVLARGRGGFNSALV 398
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
261-374 |
3.79e-35 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 125.76 E-value: 3.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 261 LAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETEMLKMVFGDSVYS--LPI 336
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVdpEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2468800260 337 SSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLN 374
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
9-253 |
1.96e-31 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 120.43 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 9 RVVVTGYGAVTSLGQNVEEIWKAIMDYKIGYS--------KYEYSDDSitAKFFGKIP-----------FELNLSPFSKR 69
Cdd:pfam00109 2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISeipadrwdPDKLYDPP--SRIAGKIYtkwgglddifdFDPLFFGISPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 70 ILKNTPRFGRLGLIAADEALKMAfGDDLSELDKhyppfSR-GVIFGTGWGGADALaQNSLSYNTEGFASPLTnILSMNNV 148
Cdd:pfam00109 80 EAERMDPQQRLLLEAAWEALEDA-GITPDSLDG-----SRtGVFIGSGIGDYAAL-LLLDEDGGPRRGSPFA-VGTMPSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 149 GSAIMSMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKeqenvETACCP 228
Cdd:pfam00109 152 IAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP-----DGPCKA 226
|
250 260
....*....|....*....|....*
gi 2468800260 229 FDRNRNGFVLSEGAAVLCLEKYETA 253
Cdd:pfam00109 227 FDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
79-417 |
2.58e-24 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 106.11 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 79 RLGLIAADEALkmafgddlsElDKHYPP--FSR---GVIFGTGWGG-ADALAQNSlsynteGFASPLTNILSMNNVGSAI 152
Cdd:COG3321 93 RLLLEVAWEAL---------E-DAGYDPesLAGsrtGVFVGASSNDyALLLLADP------EAIDAYALTGNAKSVLAGR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 153 MSMNWNLRGyqntP-VS---ACATGGIAIGDAVEIIRSGRAEMMIAGGgeslnsdlniwsIDILN------------ALS 216
Cdd:COG3321 157 ISYKLDLRG----PsVTvdtACSSSLVAVHLACQSLRSGECDLALAGG------------VNLMLtpesfilfskggMLS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 217 KEQEnvetaCCPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYG-NcSD----AYdvTTPAPDcgGRYHAVK 291
Cdd:COG3321 221 PDGR-----CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAvN-QDgrsnGL--TAPNGP--AQAAVIR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 292 YALKQADIEL--VDYVNAHGTSTQLNDFNETEMLKMVFG---DSVYSLPISSTKSYTGHLIAAAGA--LesilsIK---S 361
Cdd:COG3321 291 RALADAGVDPatVDYVEAHGTGTPLGDPIEAAALTAAFGqgrPADQPCAIGSVKSNIGHLEAAAGVagL-----IKavlA 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468800260 362 IETNIIPATIHLNNPDPGCNLD----YVPNKHR--QVENIQSVLNVN-YGFGGSNSALIFERY 417
Cdd:COG3321 366 LRHGVLPPTLHFETPNPHIDFEnspfYVNTELRpwPAGGGPRRAGVSsFGFGGTNAHVVLEEA 428
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
144-418 |
9.35e-23 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 101.24 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 144 SMNNVGSAIMSMNWNLRGYQNTPVSACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNSDLNIWSIDILNALSKeQENVE 223
Cdd:TIGR02813 180 SLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTT-NEDIQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 224 taccPFDRNRNGFVLSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCGGRYHAVKYALKQA--DIEL 301
Cdd:TIGR02813 259 ----PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAgfAPHT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 302 VDYVNAHGTSTQLNDFNETEMLKMVFG---DSVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATIHLNNPDP 378
Cdd:TIGR02813 335 CGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNP 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2468800260 379 GCNLD----YVPNKHR----QVENIQSVLNV-NYGFGGSNSALIFERYK 418
Cdd:TIGR02813 415 KLDIEnspfYLNTETRpwmqREDGTPRRAGIsSFGFGGTNFHMVLEEYS 463
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
168-413 |
3.43e-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: 94.82 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 168 SACATGGIAIGDAVEIIRSGRAEMMIAGGGESlnsdlniwsidilnalskeqenvetaccpfdrnrngFVLSEGAAVLCL 247
Cdd:cd00327 66 QACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGAAAAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 248 EKYETALTRGATILAEVTGYGNCSD-AYDVTTPAPDcgGRYHAVKYALKQADI--ELVDYVNAHGTSTQLNDFNETEMLK 324
Cdd:cd00327 110 ESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGE--GLARAARKALEGAGLtpSDIDYVEAHGTGTPIGDAVELALGL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 325 MVFGdsVYSLPISSTKSYTGHLIAAAGALESILSIKSIETNIIPATihlnnPDPGcnldyvpnkhrqveniQSVLNVNYG 404
Cdd:cd00327 188 DPDG--VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----PREP----------------RTVLLLGFG 244
|
....*....
gi 2468800260 405 FGGSNSALI 413
Cdd:cd00327 245 LGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
169-415 |
9.00e-15 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 74.29 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGeSLNSDLNIW-SIDILNALSKEQEnvetaCCPFDRNRNGFVLSEGAAVLCL 247
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGV-NLILSPDTFvGLSRAGMLSPDGR-----CKTFDASADGYVRGEGVGVVVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 248 EKYETALTRGATILAEVTGYGNCSDAYDV--TTPapdcggryhavkyalkqadielvdyvNAHGtstQlndfnetemlkm 325
Cdd:smart00825 170 KRLSDALRDGDPILAVIRGSAVNQDGRSNgiTAP--------------------------SGPA---Q------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468800260 326 vfgdsvysLPISSTKSYTGHLIAAAGaLESIlsIK---SIETNIIPATIHLNNPDPGCNLD----YVPNKHRQVENIQSV 398
Cdd:smart00825 209 --------LLIGSVKSNIGHLEAAAG-VAGL--IKvvlALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGRP 277
|
250 260
....*....|....*....|
gi 2468800260 399 LNV---NYGFGGSNSALIFE 415
Cdd:smart00825 278 RRAgvsSFGFGGTNAHVILE 297
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
169-200 |
3.31e-04 |
|
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: 41.90 E-value: 3.31e-04
10 20 30
....*....|....*....|....*....|..
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGESL 200
Cdd:pfam00108 84 VCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
238-304 |
3.93e-04 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 42.39 E-value: 3.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468800260 238 LSEGAAVLCLEKYETALTRGATILAEVTGYGNCSDAYDVTTPAPDCggryhAVKYALKQADIEL--VDY 304
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPAL-----AIPKALKHAGLEAsqVDY 313
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
169-199 |
1.49e-03 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 40.43 E-value: 1.49e-03
10 20 30
....*....|....*....|....*....|.
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGES 199
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
169-216 |
5.60e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 38.72 E-value: 5.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2468800260 169 ACATGGIAIGDAVEIIRSGRAEMMIAGGGESLNsdlNIWSIDILNALS 216
Cdd:PRK06064 84 ACASGGAALRQAYLAVASGEADVVLAAGVEKMT---DVPTPDATEAIA 128
|
|
|