|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-390 |
1.48e-121 |
|
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: 358.00 E-value: 1.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 1 MDVFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVPLKNEElaDLLNLPRVKEYSRTTLLGLAA 78
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSriAGEVPDFDPE--DYLDRKELRRMDRFAQFALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 79 AAEALEDSGI---ERDGLRIGFISATSVGGMDVSELFYREYHKDKNRGK----LRQLIGHDCGASTQfmcERLGIKDFAT 151
Cdd:cd00834 79 AEEALADAGLdpeELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVspffVPMALPNMAAGQVA---IRLGLRGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLC-RFTVNGFSSLGILDREL------CRPFDKSRSGLNLGEGAGY 224
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNddpekaSRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 225 LLLCSDKVKTARR---YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVA 301
Cdd:cd00834 236 LVLESLEHAKARGakiYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 302 MKRLFGENV--PPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRCIKrdnLKAVMT 376
Cdd:cd00834 316 IKRVFGEHAkkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDldyVPNEAREAP---IRYALS 392
|
410
....*....|....
gi 1309054216 377 NSFGFGGNCTSLVF 390
Cdd:cd00834 393 NSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-390 |
2.56e-117 |
|
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: 347.08 E-value: 2.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 2 DVFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVplKNEELADLLNLPRVKEYSRTTLLGLAAA 79
Cdd:COG0304 2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVriAGEV--KDFDPEEYLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 80 AEALEDSGIERDGL---RIGFISATSVGGMDVSELFYREYHKdKNRGKLR-----QLIGHDCGAstqFMCERLGIKDFAT 151
Cdd:COG0304 80 REALADAGLDLDEVdpdRTGVIIGSGIGGLDTLEEAYRALLE-KGPRRVSpffvpMMMPNMAAG---HVSIRFGLKGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLGILDR------ELCRPFDKSRSGLNLGEGAGY 224
Cdd:COG0304 156 TVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAaITPLGLAGFDALGALSTrnddpeKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 225 LLLCSD---KVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVA 301
Cdd:COG0304 236 LVLEELehaKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 302 MKRLFGENV--PPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRciKRDnLKAVMT 376
Cdd:COG0304 316 IKRVFGDHAykVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDldyVPNEAR--EAK-IDYALS 392
|
410
....*....|....
gi 1309054216 377 NSFGFGGNCTSLVF 390
Cdd:COG0304 393 NSFGFGGHNASLVF 406
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-394 |
1.20e-95 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 291.36 E-value: 1.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 1 MDVFIGGLGCITALGKGTNAQLERLASGR-SGLGELTLFETSHQATVGEV-----PLKNEELAD-------LLNL----- 62
Cdd:PRK09185 2 TPVYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDLPTWVGEVvgvelPALPAALAAfdcrnnrLALLalqqi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 63 -PRVKEYsrttllglaaaaealedsgIERDGL-RIGFISATSVGGMDVSELFYReyHKDKNRGKL------RQligHDCG 134
Cdd:PRK09185 82 ePAVEAA-------------------IARYGAdRIGVVLGTSTSGILEGELAYR--RRDPAHGALpadyhyAQ---QELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 135 ASTQFMCERLGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTVNGFSSLGILDRELCRPFDKSRS 214
Cdd:PRK09185 138 SLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 215 GLNLGEGAGYLLLCSDKVKTARrygkVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNN 294
Cdd:PRK09185 218 GINIGEAAAFFLLEREDDAAVA----LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 295 DASEGVAMKRLFGENVpPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNfTAKIEEAD-----VTPETRCIKRd 369
Cdd:PRK09185 294 DAMESRAVAAVFGDGV-PCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWN-TGQPDPALpplylVENAQALAIR- 370
|
410 420
....*....|....*....|....*
gi 1309054216 370 nlkAVMTNSFGFGGNCTSLVFESAK 394
Cdd:PRK09185 371 ---YVLSNSFAFGGNNCSLIFGRAD 392
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-390 |
4.76e-86 |
|
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: 267.04 E-value: 4.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVplKNEELADLLNLPRVKEYSRTTLLGLAAAA 80
Cdd:TIGR03150 3 VVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVkiAGEV--KDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 81 EALEDSGI---ERDGLRIGFISATSVGGMDVSELFYREYHkdkNRGKLR--------QLIGhdcGASTQfMCERLGIKDF 149
Cdd:TIGR03150 81 EAVEDSGLdieEEDAERVGVIIGSGIGGLETIEEQHIVLL---EKGPRRvspffipmSIIN---MAAGQ-ISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLGILDR------ELCRPFDKSRSGLNLGEGA 222
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTrnddpeKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 223 GYLLLCS---DKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEG 299
Cdd:TIGR03150 234 GVLVLEElehAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 300 VAMKRLFGENVP--PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRCIKrdnLKAV 374
Cdd:TIGR03150 314 KAIKKVFGDHAYklAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDldyVPNEAREAK---IDYA 390
|
410
....*....|....*.
gi 1309054216 375 MTNSFGFGGNCTSLVF 390
Cdd:TIGR03150 391 LSNSFGFGGTNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3-390 |
7.40e-78 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 246.24 E-value: 7.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVplKNEELADLLNLPRVKEYSRTTLLGLAAAA 80
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVkiAGEV--KDFNPDDYMSRKEARRMDRFIQYGIAAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 81 EALEDSGI---ERDGLRIGFISATSVGGMDVSELFYREYHkdkNRGKLR--------QLIGhdcGASTQfMCERLGIKDF 149
Cdd:PRK07314 82 QAVEDAGLeitEENADRIGVIIGSGIGGLETIEEQHITLL---EKGPRRvspffvpmAIIN---MAAGH-VSIRYGAKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLgildREL----------CRPFDKSRSGLNL 218
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFAAA----RALstrnddperaSRPFDKDRDGFVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 219 GEGAGYLLLCS---DKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNND 295
Cdd:PRK07314 231 GEGAGILVLEElehAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 296 ASEGVAMKRLFGENVP--PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRciKRDn 370
Cdd:PRK07314 311 KAETQAIKRVFGEHAYkvAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDldyVPNEAR--ERK- 387
|
410 420
....*....|....*....|
gi 1309054216 371 LKAVMTNSFGFGGNCTSLVF 390
Cdd:PRK07314 388 IDYALSNSFGFGGTNASLVF 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-390 |
1.38e-65 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 214.56 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 11 ITALGKGTNAQLERLASGRSGLGELTLFE----------TSHQATVGEVP------LKNEELADLLNLPRVKEySRTTLL 74
Cdd:PTZ00050 2 VTPLGVGAESTWEALIAGKSGIRKLTEFPkflpdcipeqKALENLVAAMPcqiaaeVDQSEFDPSDFAPTKRE-SRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 75 GLAAAAEALEDSGI----ERDGLRIGFISATSVGGM----DVSELFYREYHKDKNRGKLRQLIGHdcgASTQFMCERLGI 146
Cdd:PTZ00050 81 AMAAAREALADAKLdilsEKDQERIGVNIGSGIGSLadltDEMKTLYEKGHSRVSPYFIPKILGN---MAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 147 KDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGT-DSLCRFTVNGFSSL-----GILDR--ELCRPFDKSRSGLNL 218
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTeASITPVSFAGFSRMralctKYNDDpqRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 219 GEGAGYLLLCSD---KVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPG-DIGYINVHGTGTQNN 294
Cdd:PTZ00050 238 GEGAGILVLEELehaLRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINInDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 295 DASEGVAMKRLFGENVPP---FSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEADV--TPETRCIKRD 369
Cdd:PTZ00050 318 DKIELKAIKKVFGDSGAPklyVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLnlVQGKTAHPLQ 397
|
410 420
....*....|....*....|.
gi 1309054216 370 NLKAVMTNSFGFGGNCTSLVF 390
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLF 418
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-390 |
1.02e-60 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 201.50 E-value: 1.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVplKNEELADLLNLPRVKEYSRTTLLGLAAAA 80
Cdd:PRK08439 4 VVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVqiAGEI--TDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 81 EALEDSGI---ERDGLRIGFISATSVGGMDVSElfyreyhkdKN------RGKLR--------QLIGHDCGastqFMCER 143
Cdd:PRK08439 82 EAMKDAGFlpeELDAERFGVSSASGIGGLPNIE---------KNsiicfeKGPRKispffipsALVNMLGG----FISIE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 144 LGIKDFATTINTACSSANNAIMLGTRMIKAGMLD-VVIAGGTDSLCRFTVNGFSSLGILD------RELCRPFDKSRSGL 216
Cdd:PRK08439 149 HGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADkMLVVGAESAICPVGIGGFAAMKALStrnddpKKASRPFDKDRDGF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 217 NLGEGAGYLLL---CSDKVKTARRYGKVTGYANANDAFHQTASSStgDGAYLAMKGALEQSGSEPgdIGYINVHGTGTQN 293
Cdd:PRK08439 229 VMGEGAGALVLeeyESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 294 NDASEGVAMKRLFG--ENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEADVTPETRCIKRDNL 371
Cdd:PRK08439 305 NDKNETAALKELFGskEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAEL 384
|
410
....*....|....*....
gi 1309054216 372 KAVMTNSFGFGGNCTSLVF 390
Cdd:PRK08439 385 NVVMSNSFGFGGTNGVVIF 403
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
3-390 |
5.46e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 200.22 E-value: 5.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETS-HQATV-GEVPLKNEELADLLNLPRV------KEYSRTTLL 74
Cdd:PRK06333 6 IVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGdLATKIgGQVPDLAEDAEAGFDPDRYldpkdqRKMDRFILF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 75 GLAAAAEALEDSGI----ERDGLRIGFISATSVGGMDVSELFYReyhKDKNRGKLR-------QLIGHDCGASTQFmceR 143
Cdd:PRK06333 86 AMAAAKEALAQAGWdpdtLEDRERTATIIGSGVGGFPAIAEAVR---TLDSRGPRRlspftipSFLTNMAAGHVSI---R 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 144 LGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFS-----SLGILDR--ELCRPFDKSRSG 215
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAaIDRVSLAGFAaaralSTRFNDApeQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 216 LNLGEGAGYLLLCSDKVKTARR---YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQ 292
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGappLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 293 NNDASEGVAMKRLFG-ENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD----VTPETRcik 367
Cdd:PRK06333 320 VGDLGEVAAIKKVFGhVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgldvVANKAR--- 396
|
410 420
....*....|....*....|...
gi 1309054216 368 RDNLKAVMTNSFGFGGNCTSLVF 390
Cdd:PRK06333 397 PMDMDYALSNGFGFGGVNASILF 419
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-393 |
1.07e-59 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 199.63 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTL--------FETSHQATVGEVPLK---------NEELADLLNLPRV 65
Cdd:PLN02836 8 VVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQddlkmkseDEETQLYTLDQLPSRvaalvprgtGPGDFDEELWLNS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 66 KEYSRTTLLGLAAAAEALEDS--------GIERDGLRIGfisatsvGGM----DVSELFYREYHKDKNRGKL----RQLI 129
Cdd:PLN02836 88 RSSSRFIGYALCAADEALSDArwlpsedeAKERTGVSIG-------GGIgsitDILEAAQLICEKRLRRLSPffvpRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 130 GHDCGASTQfmceRLGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTD-SLCRFTVNGFSSLGILD------ 202
Cdd:PLN02836 161 NMAAGHVSI----RYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTEsSIDALSIAGFSRSRALStkfnsc 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 203 -RELCRPFDKSRSGLNLGEGAGYLLLCS---DKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEP 278
Cdd:PLN02836 237 pTEASRPFDCDRDGFVIGEGAGVLVLEElehAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 279 GDIGYINVHGTGTQNNDASEGVAMKRLFGENVP----PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTA-- 352
Cdd:PLN02836 317 NQVDYVNAHATSTPLGDAVEARAIKTVFSEHATsgglAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERpd 396
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1309054216 353 KIEEADVTPETRcIKRDNLKAVMTNSFGFGGNCTSLVFESA 393
Cdd:PLN02836 397 PIFDDGFVPLTA-SKAMLIRAALSNSFGFGGTNASLLFTSP 436
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
3-390 |
1.15e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 188.69 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVplkneelaDLLNLPRVKEYSRTTLLGLAAAA 80
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTriAGTV--------DFLPESPFGASALSEALARLAAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 81 EALEDSGIERDGLRIGFISATSVGGMDVSELF-------------YREYHKDKNRGKLRQLigHDcgaSTQF------MC 141
Cdd:PRK06501 85 EALAQAGIGKGDFPGPLFLAAPPVELEWPARFalaaavgdndapsYDRLLRAARGGRFDAL--HE---RFQFgsiadrLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 142 ERLGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTD------SLCRFTVngFSSLGILD---RELCRPFDKS 212
Cdd:PRK06501 160 DRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgsvsaeALIRFSL--LSALSTQNdppEKASKPFSKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 213 RSGLNLGEGAGYLLLCSDKVKTARR---YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGT 289
Cdd:PRK06501 238 RDGFVMAEGAGALVLESLESAVARGakiLGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 290 GTQNNDASEGVAMKRLFGENVP--PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFT---AKIeEADVTPETr 364
Cdd:PRK06501 318 STPENDKMEYLGLSAVFGERLAsiPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDnpdPAI-PLDVVPNV- 395
|
410 420
....*....|....*....|....*..
gi 1309054216 365 ciKRD-NLKAVMTNSFGFGGNCTSLVF 390
Cdd:PRK06501 396 --ARDaRVTAVLSNSFGFGGQNASLVL 420
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
156-383 |
9.53e-53 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 179.86 E-value: 9.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 156 ACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLGILDRELCRPFDKSRSGLNLGEGAGYLLLCSDKV-- 232
Cdd:PRK05952 145 ACATGLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELaq 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 233 -KTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKRLFGENVp 311
Cdd:PRK05952 225 kRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPHRV- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 312 PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWP---------NLNFtakIEEAdvtpetrciKRDNLKAVMTNSFGFG 382
Cdd:PRK05952 304 AVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPcvglqepefDLNF---VRQA---------QQSPLQNVLCLSFGFG 371
|
.
gi 1309054216 383 G 383
Cdd:PRK05952 372 G 372
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-389 |
5.15e-45 |
|
"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: 160.30 E-value: 5.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 5 IGGLGCITALGKGTNAQLE---RLASGRSGLGELTLFETSHQATV-GEVPLKNEELADLlnlPRVKEYSRTTLLGLAAAA 80
Cdd:cd00828 5 ITGIGVVSPHGEGCDEVEEfweALREGRSGIAPVARLKSRFDRGVaGQIPTGDIPGWDA---KRTGIVDRTTLLALVATE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 81 EALEDSGIERDGL----RIGFISATSVGGMDVSELFYREYHKDKNRGKLRQLIGHDCGASTQFMCERLGIKDFATTINTA 156
Cdd:cd00828 82 EALADAGITDPYEvhpsEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNILLLSSHGPIKTPVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 157 CSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTVNGFSSLGIL------DRELCRPFDKSRSGLNLGEGAGYLLLCSD 230
Cdd:cd00828 162 CATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALstaeeePEEMSRPFDETRDGFVEAEGAGVLVLERA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 231 KV---KTARRYGKVTGYANANDAFHQTASSsTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKRLFG 307
Cdd:cd00828 242 ELalaRGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 308 E--NVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNftakIEEADVTPETRCI------KRDNLKAVMTNSF 379
Cdd:cd00828 321 AlgAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTAN----LDDVDPDVEHLSVvglsrdLNLKVRAALVNAF 396
|
410
....*....|
gi 1309054216 380 GFGGNCTSLV 389
Cdd:cd00828 397 GFGGSNAALV 406
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
155-390 |
1.75e-44 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 159.13 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 155 TACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLGIL------DRE-LCRPFDKSRSGLNLGEGAGYLL 226
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETrIEAVPIAGFAQMRIVmstnndDPAgACRPFDKDRDGFVFGEGGALMV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 227 LCSD---KVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMK 303
Cdd:PRK07910 249 IETEehaKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAIN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 304 RLFGENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRcikRDNLKAVMTNSFG 380
Cdd:PRK07910 329 NALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDldvVAGEPR---PGNYRYAINNSFG 405
|
250
....*....|
gi 1309054216 381 FGGNCTSLVF 390
Cdd:PRK07910 406 FGGHNVALAF 415
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
145-390 |
2.91e-44 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 158.23 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 145 GIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTVNGFSSLGILDR-----ELC-RPFDKSRSGLNL 218
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTrndapELTpRPFDANRDGLVI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 219 GEGAGYLLLCS---DKVKTARRYGKVTGYANANDAFHQTasSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNND 295
Cdd:PRK09116 232 GEGAGTLVLEElehAKARGATIYAEIVGFGTNSDGAHVT--QPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGD 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 296 ASEGVAMKRLFGENVpPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTakieeadvTPETRCIKRDNLKA-- 373
Cdd:PRK09116 310 IAESQATAAVFGARM-PISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLT--------QVDPACGALDYIMGea 380
|
250 260
....*....|....*....|....
gi 1309054216 374 -------VMTNSFGFGGNCTSLVF 390
Cdd:PRK09116 381 reidteyVMSNNFAFGGINTSLIF 404
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3-390 |
7.59e-44 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 157.14 E-value: 7.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLF-ETSHQATV-GEVPLKNEELADllnlPRVKEY-SRTTLLGLAAA 79
Cdd:PRK07967 4 VVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFaEMGMRSQVwGNVKLDPTGLID----RKVMRFmGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 80 AEALEDSGIERD---GLRIGFI-------SATSVGGMDVSelfyREYHKDKNRGKLRQLIGHDCGAS----TQFMcerlg 145
Cdd:PRK07967 80 EQAIADAGLSEEqvsNPRTGLIagsgggsTRNQVEAADAM----RGPRGPKRVGPYAVTKAMASTVSaclaTPFK----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 146 IKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTVNGFSSLGILDREL-------CRPFDKSRSGLNL 218
Cdd:PRK07967 151 IKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKYndtpekaSRAYDANRDGFVI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 219 GEGAGYLL---LCSDKVKTARRYGKVTGYANANDAFHQTASSstGDGAYLAMKGALEQSGsepGDIGYINVHGTGTQNND 295
Cdd:PRK07967 231 AGGGGVVVveeLEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMALATVD---TPIDYINTHGTSTPVGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 296 ASEGVAMKRLFGENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEE-ADVTPETRCIKRDNLKAV 374
Cdd:PRK07967 306 VKELGAIREVFGDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTV 385
|
410
....*....|....*.
gi 1309054216 375 MTNSFGFGGNCTSLVF 390
Cdd:PRK07967 386 MSNSFGFGGTNATLVF 401
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
2-392 |
6.73e-43 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 154.42 E-value: 6.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 2 DVFIGGLGCITALGKGTNAQLERLASGRSGLGELTLF---ETSHQATVGEVPLKNEELADLLNLPRVKEY-----SRTTL 73
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPgrqVPDDAGAGLASAFIGAELDSLALPERLDAKllrraSLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 74 LGLAAAAEALEDSGIER-DGLRIGFIsatsVGGMDVSELFYREYHkDKNRGKLRQLighDCGASTQFM--------CERL 144
Cdd:PRK07103 83 AALAAAREAWRDAALGPvDPDRIGLV----VGGSNLQQREQALVH-ETYRDRPAFL---RPSYGLSFMdtdlvglcSEQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 145 GIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGtdSLCRFT---VNGFSSLGILDRE--------LCRPFDKSR 213
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVG--ALMDLSyweCQALRSLGAMGSDrfadepeaACRPFDQDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 214 SGLNLGEGAGYLLLCSDKV---KTARRYGKVTGYANANDAFHQTASSSTGDGAylAMKGALEQSGSEPGDIGYINVHGTG 290
Cdd:PRK07103 233 DGFIYGEACGAVVLESAESarrRGARPYAKLLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPEDIDYVNPHGTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 291 TQNNDASEgvaMKRLFGENV--PPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEA----DVTPETR 364
Cdd:PRK07103 311 SPLGDETE---LAALFASGLahAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDERfrwvGSTAESA 387
|
410 420
....*....|....*....|....*...
gi 1309054216 365 CIKRdnlkaVMTNSFGFGGNCTSLVFES 392
Cdd:PRK07103 388 RIRY-----ALSLSFGFGGINTALVLER 410
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-391 |
3.00e-42 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 152.85 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQATVGEVPLKNEELADLLNLPRVKEYSRTTLLGLAAAAEA 82
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGIQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 83 LEDSGI---ERDGLRIGFISATSVGGMDVSELFYREYHKDKNRGK---------LRQLIGHdcgastqfMCERLGIKDFA 150
Cdd:PRK08722 86 LDDSGLevtEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVspffvpstiVNMIAGN--------LSIMRGLRGPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 151 TTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTD-SLCRFTVNGFSSLGILD------RELCRPFDKSRSGLNLGEGAG 223
Cdd:PRK08722 158 IAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEkASTPLGMAGFGAAKALStrndepQKASRPWDKDRDGFVLGDGAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 224 YLLLCS---DKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGV 300
Cdd:PRK08722 238 MMVLEEyehAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 301 AMKRLFGENVPP---FSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIE--EADVTPETrCIKRDNLKAVM 375
Cdd:PRK08722 318 GIKRALGEAGSKqvlVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEglDIDLVPHT-ARKVESMEYAI 396
|
410
....*....|....*.
gi 1309054216 376 TNSFGFGGNCTSLVFE 391
Cdd:PRK08722 397 CNSFGFGGTNGSLIFK 412
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-390 |
1.63e-38 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 145.12 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQAT--VGEVPLKNEE--LADLL--NLPRVKEYSRTTLLGL 76
Cdd:PLN02787 131 VVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTriAGEIKSFSTDgwVAPKLskRMDKFMLYLLTAGKKA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 77 AAAAEALEDSGIERDGLRIGFISATSVGGM----DVSELFYREYHK---------DKNRGklrqlighdcgasTQFMCER 143
Cdd:PLN02787 211 LADGGITEDVMKELDKTKCGVLIGSAMGGMkvfnDAIEALRISYRKmnpfcvpfaTTNMG-------------SAMLAMD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 144 LGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS-LCRFTVNGFSSLGILDR------ELCRPFDKSRSGL 216
Cdd:PLN02787 278 LGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAaIIPIGLGGFVACRALSQrnddptKASRPWDMNRDGF 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 217 NLGEGAGYLLLCS---DKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQN 293
Cdd:PLN02787 358 VMGEGAGVLLLEElehAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 294 NDASEGVAMKRLFGENvPPF--SSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD----VTPETRcik 367
Cdd:PLN02787 438 GDLKEYQALMRCFGQN-PELrvNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDtkvlVGPKKE--- 513
|
410 420
....*....|....*....|...
gi 1309054216 368 RDNLKAVMTNSFGFGGNCTSLVF 390
Cdd:PLN02787 514 RLDIKVALSNSFGFGGHNSSILF 536
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
155-391 |
3.19e-38 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 140.63 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 155 TACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLC-RFTVNGFSSLGILD-------RELCRPFDKSRSGLNLGEGAGYLL 226
Cdd:PRK14691 89 TACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIdTVSLAGFAAARALSthfnstpEKASRPFDTARDGFVMGEGAGLLI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 227 ---LCSDKVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMK 303
Cdd:PRK14691 169 ieeLEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 304 RLFGE-NVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNftakIEEADVTPETRCIKRDN-----LKAVMTN 377
Cdd:PRK14691 249 HLFGEsNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLN----LENPDPAAKGLNIIAGNaqphdMTYALSN 324
|
250
....*....|....
gi 1309054216 378 SFGFGGNCTSLVFE 391
Cdd:PRK14691 325 GFGFAGVNASILLK 338
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
152-385 |
2.30e-36 |
|
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: 137.30 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTVN-GFSSLGILDRE-LCRPFDKSRSGLNLGEGAGYLLLCs 229
Cdd:cd00833 165 TVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFvGFSKAGMLSPDgRCRPFDADADGYVRGEGVGVVVLK- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 230 dKVKTARR-----YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKR 304
Cdd:cd00833 244 -RLSDALRdgdriYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 305 LFGENVPPFS-----STKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTA-----KIEEADVTPETRCI---KRDNL 371
Cdd:cd00833 323 VFGGSRSADQplligSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETpnpkiDFEESPLRVPTEARpwpAPAGP 402
|
250
....*....|....*
gi 1309054216 372 KAVMTNSFGFGG-NC 385
Cdd:cd00833 403 RRAGVSSFGFGGtNA 417
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
238-351 |
1.29e-33 |
|
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: 121.52 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 238 YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKRLFGENVP----PF 313
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1309054216 314 SSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFT 351
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
143-389 |
4.46e-28 |
|
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: 112.73 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 143 RLGIKDFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCR--FTVNGFSSLGILDRELCRPFDKSRSGLNLGE 220
Cdd:cd00825 82 PLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAApmDCEFDAMGALSTPEKASRTFDAAADGFVFGD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 221 GAGYLLLCSD---KVKTARRYGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDAS 297
Cdd:cd00825 162 GAGALVVEELehaLARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 298 EGVAMKRLFGENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD-VTPETRcikRDNLKAVMT 376
Cdd:cd00825 242 ELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLnIVTETT---PRELRTALL 318
|
250
....*....|...
gi 1309054216 377 NSFGFGGNCTSLV 389
Cdd:cd00825 319 NGFGLGGTNATLV 331
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
152-383 |
9.73e-22 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 97.64 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGMLDVVIAGGTD-SLCRFTVNGFSSLGILDRE-LCRPFDKSRSGLNLGEGAGYLLL-- 227
Cdd:COG3321 169 TVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLSPDgRCRAFDADADGYVRGEGVGVVVLkr 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 228 CSDkvktARR-----YGKVTGYANANDAfhqtASSS-T---GDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASE 298
Cdd:COG3321 249 LSD----ALRdgdriYAVIRGSAVNQDG----RSNGlTapnGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 299 GVAMKRLFGENVPP-----FSSTKGYTGHTLGAAgGVESVF-AVLSLFHGYIWPNLNFTA---KIEEAD----VTPETRC 365
Cdd:COG3321 321 AAALTAAFGQGRPAdqpcaIGSVKSNIGHLEAAA-GVAGLIkAVLALRHGVLPPTLHFETpnpHIDFENspfyVNTELRP 399
|
250 260
....*....|....*....|.
gi 1309054216 366 IKRDNLK---AVmtNSFGFGG 383
Cdd:COG3321 400 WPAGGGPrraGV--SSFGFGG 418
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
150-389 |
2.22e-17 |
|
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: 80.95 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRftvngfsslgildrelcrpfdksrsglnlGEGAGYLLLCS 229
Cdd:cd00327 61 AYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVF-----------------------------GDGAAAAVVES 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 230 D---KVKTARRYGKVTGYA-NANDAFHQTASSstGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKRL 305
Cdd:cd00327 112 EehaLRRGAHPQAEIVSTAaTFDGASMVPAVS--GEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 306 FGENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPnlnftakieeadvtpetrciKRDNLKAVMTNSFGFGGNC 385
Cdd:cd00327 190 DGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP--------------------TPREPRTVLLLGFGLGGTN 249
|
....
gi 1309054216 386 TSLV 389
Cdd:cd00327 250 AAVV 253
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-389 |
2.37e-17 |
|
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: 82.79 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 3 VFIGGLGCITALGKGTNAQLERLASGRSGLGELTLFETSHQ-ATV-GEVPlkneELADLLNLPR--VKEYSRTTLLGLAA 78
Cdd:cd00832 3 AVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYpARLaGEVP----DFDAAEHLPGrlLPQTDRMTRLALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 79 AAEALEDSGIER---DGLRIGFISATSVGGMDVSElfyREYHKDKNRGKLR----QLIGHDCGASTQFMCERLGIKDFAT 151
Cdd:cd00832 79 ADWALADAGVDPaalPPYDMGVVTASAAGGFEFGQ---RELQKLWSKGPRHvsayQSFAWFYAVNTGQISIRHGMRGPSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGmLDVVIAGGTDS-LCRFTVNGFSSLGILDR-----ELCRPFDKSRSGLNLGEGAGYL 225
Cdd:cd00832 156 VVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSaLCPWGWVAQLSSGRLSTsddpaRAYLPFDAAAAGYVPGEGGAIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 226 LL---CSDKVKTARRYGKVTGYANAndaFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAM 302
Cdd:cd00832 235 VLedaAAARERGARVYGEIAGYAAT---FDPPPGSGRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAAL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 303 KRLFGENVPPFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTAKIEEAD---VTPETRCIKrdnLKAVMTNSF 379
Cdd:cd00832 312 AAVFGPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGldlVTGRPRPAA---LRTALVLAR 388
|
410
....*....|
gi 1309054216 380 GFGGNCTSLV 389
Cdd:cd00832 389 GRGGFNSALV 398
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
153-391 |
3.35e-17 |
|
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: 83.90 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 153 INTACSSANNAIMLGTRMIKAGMLDVVIAGG--TDSlCRFTVNGFSSL-GILDRELCRPFDKSRSGLNLGEGAGYLLLcs 229
Cdd:TIGR02813 202 VDAACAGSLAAIRMALSELLEGRSEMMITGGvcTDN-SPFMYMSFSKTpAFTTNEDIQPFDIDSKGMMIGEGIGMMAL-- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 230 DKVKTARR-----YGKVTGYANANDAFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVHGTGTQNNDASEGVAMKR 304
Cdd:TIGR02813 279 KRLEDAERdgdriYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVS 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 305 LFGENVP-----PFSSTKGYTGHTLGAAGGVESVFAVLSLFHGYIWPNLNFTA-----KIEEAD--VTPETR-CIKR--D 369
Cdd:TIGR02813 359 VFSQDNDqkqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQpnpklDIENSPfyLNTETRpWMQRedG 438
|
250 260
....*....|....*....|..
gi 1309054216 370 NLKAVMTNSFGFGGNCTSLVFE 391
Cdd:TIGR02813 439 TPRRAGISSFGFGGTNFHMVLE 460
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
85-229 |
4.31e-14 |
|
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: 71.51 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 85 DSGI---ERDGLRIGFISATSVGGmdvselfYREYHKDKNRGKLRQLIGHDCGASTQFMCER----LGIKDFATTINTAC 157
Cdd:pfam00109 101 DAGItpdSLDGSRTGVFIGSGIGD-------YAALLLLDEDGGPRRGSPFAVGTMPSVIAGRisyfLGLRGPSVTVDTAC 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309054216 158 SSANNAIMLGTRMIKAGMLDVVIAGGTD-SLCRFTVNGFSSLGILDR-ELCRPFDKSRSGLNLGEGAGYLLLCS 229
Cdd:pfam00109 174 SSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPdGPCKAFDPFADGFVRGEGVGAVVLKR 247
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
148-385 |
1.14e-12 |
|
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: 68.12 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 148 DFATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLC--RFTVnGFSSLGILDRE-LCRPFDKSRSGLNLGEGAGY 224
Cdd:smart00825 88 DYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILspDTFV-GLSRAGMLSPDgRCKTFDASADGYVRGEGVGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 225 LLLC--SDkvktARRygkvtgyananDafhqtassstGDgaylamkgaleqsgsepgdigyiNVH----GTGTQNNDASE 298
Cdd:smart00825 167 VVLKrlSD----ALR-----------D----------GD-----------------------PILavirGSAVNQDGRSN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 299 GVAMKrlfgeNVP---PFSSTKGYTGHTLGAAgGVESVF-AVLSLFHGYIWPNLNFTA---KIEEAD-----VTPETRCI 366
Cdd:smart00825 199 GITAP-----SGPaqlLIGSVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETpnpHIDLEEsplrvPTELTPWP 272
|
250 260
....*....|....*....|
gi 1309054216 367 KRDNLKAVMTNSFGFGG-NC 385
Cdd:smart00825 273 PPGRPRRAGVSSFGFGGtNA 292
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
150-186 |
8.02e-09 |
|
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: 57.00 E-value: 8.02e-09
10 20 30
....*....|....*....|....*....|....*..
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS 186
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
150-186 |
1.24e-08 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 56.33 E-value: 1.24e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS 186
Cdd:cd00751 77 ATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES 113
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
150-189 |
2.34e-07 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 52.23 E-value: 2.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCR 189
Cdd:TIGR01930 76 AYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSR 115
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
150-186 |
1.32e-06 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 50.15 E-value: 1.32e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDS 186
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQES 117
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
150-187 |
5.15e-06 |
|
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: 47.68 E-value: 5.15e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSL 187
Cdd:pfam00108 78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
134-287 |
9.12e-06 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 47.26 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 134 GASTQFMCERLGIKD-FATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTD--SLCRFTVNGFSSLGILDRELCRPFD 210
Cdd:cd00829 53 SFPGALIAEYLGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEkmSDVPTGDEAGGRASDLEWEGPEPPG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 211 ---------------KSRSGLN-------------------------------------------------LGEGAGYLL 226
Cdd:cd00829 133 gltppalyalaarryMHRYGTTredlakvavknhrnaarnpyaqfrkpitvedvlnsrmiadplrlldccpVSDGAAAVV 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309054216 227 LCSDKV--KTARRYGKVTGYANAND--AFHQTASSSTGDGAYLAMKGALEQSGSEPGDIGYINVH 287
Cdd:cd00829 213 LASEERarELTDRPVWILGVGAASDtpSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELY 277
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| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
150-187 |
3.57e-05 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 45.47 E-value: 3.57e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSL 187
Cdd:PLN02644 80 CTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESM 117
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| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
150-189 |
1.05e-04 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 44.17 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1309054216 150 ATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCR 189
Cdd:PRK09050 83 GTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSR 122
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
140-277 |
1.27e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 40.62 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054216 140 MCERLGIKD-FATTINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSLCRFTvngfsslGILDRELCRPFdksrsglnl 218
Cdd:PRK12879 96 VQARLGIPNaAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAERLSKVT-------DYTDRTTCILF--------- 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309054216 219 GEGAGYLLLcsdkVKTARRYGKVTGYANAN----DAFHQTASSSTGDGAYLAMKGALEQSGSE 277
Cdd:PRK12879 160 GDGAGAVVL----EATENEPGFIDYVLGTDgdggDILYRTGLGTTMDRDALSGDGYIVQNGRE 218
|
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| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
152-187 |
1.79e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 40.08 E-value: 1.79e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1309054216 152 TINTACSSANNAIMLGTRMIKAGMLDVVIAGGTDSL 187
Cdd:PRK08235 83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESM 118
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
142-191 |
8.58e-03 |
|
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: 37.78 E-value: 8.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1309054216 142 ERLGIKD-FATTINTACSSANNAIMLGTRMIKAGMLD--VVIagGTDSLCRFT 191
Cdd:COG0332 96 HKLGAKNaAAFDINAACSGFVYALSVAAALIRSGQAKnvLVV--GAETLSRIV 146
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