|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-404 |
3.10e-132 |
|
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: 385.60 E-value: 3.10e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPRIDRSVGHVA-----EDMTEGLHPSQVRMLDRVTVMAnyaan 78
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAgevkdFDPEEYLDRKELRRMDRFTQYA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 79 qalgaaaLDASRQA--------------ECGVFIGTGIGGVSTLCESVEAYHGVVPKR--PLLVvPAVMPQAIAAQIAQG 142
Cdd:COG0304 76 -------LAAAREAladagldldevdpdRTGVIIGSGIGGLDTLEEAYRALLEKGPRRvsPFFV-PMMMPNMAAGHVSIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 143 LQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGyCRPFSHKRTG 222
Cdd:COG0304 148 FGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKA-SRPFDKDRDG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 223 FALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTL 300
Cdd:COG0304 227 FVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPdgEGAARAMRAALKDAGLSPEDIDYINAHGTSTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 301 VGDRIETAAIKQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLP 380
Cdd:COG0304 307 LGDAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK 386
|
410 420
....*....|....*....|....
gi 2751072858 381 dLRLAISNSFGMGGNNAVLAFRKV 404
Cdd:COG0304 387 -IDYALSNSFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4-401 |
1.90e-128 |
|
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: 375.72 E-value: 1.90e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPRIDRSVGHVA-----EDMTEGLHPSQVRMLDRVTVMANYAAN 78
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAgevpdFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 79 QALGAAALDASRQA--ECGVFIGTGIGGVSTLCESVEAYHGVVPKRPL-LVVPAVMPQAIAAQIAQGLQSTAEAQTYATA 155
Cdd:cd00834 81 EALADAGLDPEELDpeRIGVVIGSGIGGLATIEEAYRALLEKGPRRVSpFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 156 CSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGyCRPFSHKRTGFALAEGAAMLVLE 235
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKA-SRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 236 SADHARARNAAVIAEICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQV 313
Cdd:cd00834 240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPdgEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 314 FGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPdLRLAISNSFGMG 393
Cdd:cd00834 320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNSFGFG 398
|
....*...
gi 2751072858 394 GNNAVLAF 401
Cdd:cd00834 399 GHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
4-405 |
4.13e-100 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 303.63 E-value: 4.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRkhPDPRIDRS------VGHV-AEDMTEGLHPSQVRMLDRVTVMANYA 76
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIG--PITHFDTSdlavkiAGEVkDFNPDDYMSRKEARRMDRFIQYGIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 77 ANQALGAAALDASRQAEC--GVFIGTGIGGVSTLCESVEAYHGVVPKR--PLLVvPAVMPQAIAAQIAQGLQSTAEAQTY 152
Cdd:PRK07314 80 AKQAVEDAGLEITEENADriGVIIGSGIGGLETIEEQHITLLEKGPRRvsPFFV-PMAIINMAAGHVSIRYGAKGPNHSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 153 ATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCA---EPAAGqtgyCRPFSHKRTGFALAEGA 229
Cdd:PRK07314 159 VTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrndDPERA----SRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 230 AMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIET 307
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPdgEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 308 AAIKQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLpDLRLAIS 387
Cdd:PRK07314 315 QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARER-KIDYALS 393
|
410
....*....|....*...
gi 2751072858 388 NSFGMGGNNAVLAFRKVA 405
Cdd:PRK07314 394 NSFGFGGTNASLVFKRYE 411
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-404 |
1.49e-84 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 264.25 E-value: 1.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 13 VASPVGGSAQSTFDALNAGVCGIRK---HPDPRIDRSVGHVAEDMTEGLHPSQVRML-----------------DRVTVM 72
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKlteFPKFLPDCIPEQKALENLVAAMPCQIAAEvdqsefdpsdfaptkreSRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 73 ANYAANQALGAAALDASR---QAECGVFIGTGIGGVSTLCESVEAYHGVVPKR--PLLVvPAVMPQAIAAQIAQGLQSTA 147
Cdd:PTZ00050 81 AMAAAREALADAKLDILSekdQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRvsPYFI-PKILGNMAAGLVAIKHKLKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 148 EAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCaepaagqTGY-------CRPFSHKR 220
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALC-------TKYnddpqraSRPFDKDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 221 TGFALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGG-LAAADVGYINAHAT 297
Cdd:PTZ00050 233 AGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPdgRGARRCMENALKDGAnININDVDYVNAHAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 298 GTLVGDRIETAAIKQVFGAH-ASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAE-G 375
Cdd:PTZ00050 313 STPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGkT 392
|
410 420
....*....|....*....|....*....
gi 2751072858 376 ARRLPDLRLAISNSFGMGGNNAVLAFRKV 404
Cdd:PTZ00050 393 AHPLQSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-403 |
2.10e-81 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 256.08 E-value: 2.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 1 MTHRQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPD-------PRIDRSVGHVAEDMTEGLHPSQV------RMLD 67
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDfpvgdlaTKIGGQVPDLAEDAEAGFDPDRYldpkdqRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 68 R---VTVMANYAANQALGAAALDASRQAECGVFIGTGIGGVSTLCESVEAYHGVVPKR--PLlVVPAVMPQAIAAQIAQG 142
Cdd:PRK06333 81 RfilFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRlsPF-TIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 143 LQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGYCRPFSHKRTG 222
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 223 FALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPV--RPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTL 300
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTagPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 301 VGDRIETAAIKQVFGaHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCD-LDYVAEGARRL 379
Cdd:PRK06333 320 VGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPM 398
|
410 420
....*....|....*....|....
gi 2751072858 380 PdLRLAISNSFGMGGNNAVLAFRK 403
Cdd:PRK06333 399 D-MDYALSNGFGFGGVNASILFRR 421
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-403 |
3.07e-78 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 247.72 E-value: 3.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 6 VVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPRID------RSVGHVAEDMTEGLHPSQVRMLDRVTVMANYAANQ 79
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEefdlpvRIGGHLLEEFDHQLTRVELRRMSYLQRMSTVLGRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 80 ALGAAALDASRQAECGVFIGTGIGGVSTLCESVE-----AYHGVVPkrplLVVPAVMPQAIAAQIAQGLQSTAEAQTYAT 154
Cdd:PRK07910 94 VWENAGSPEVDTNRLMVSIGTGLGSAEELVFAYDdmrarGLRAVSP----LAVQMYMPNGPAAAVGLERHAKAGVITPVS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 155 ACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGYCRPFSHKRTGFALAEGAAMLVL 234
Cdd:PRK07910 170 ACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 235 ESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQ--ALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQ 312
Cdd:PRK07910 250 ETEEHAKARGANILARIMGASITSDGFHMVAPDPNGEraGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 313 VFGAHASSlpVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRlPDLRLAISNSFGM 392
Cdd:PRK07910 330 ALGGHRPA--VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP-GNYRYAINNSFGF 406
|
410
....*....|.
gi 2751072858 393 GGNNAVLAFRK 403
Cdd:PRK07910 407 GGHNVALAFGR 417
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-401 |
6.94e-73 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 234.30 E-value: 6.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 2 THRQVVITAVGVASPVGGSAQSTFDALNAGVCGIR---------KHPDPRIDRSV-----GHVAEDMTEGLHPSQVRMLD 67
Cdd:PLN02836 4 PTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRaltqddlkmKSEDEETQLYTldqlpSRVAALVPRGTGPGDFDEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 68 RVTVMANYAANQALGAAALDASRQAE-----------CGVFIGtgiGGVSTLCESVEAYHGVVPKRPLLVVPAVMPQ--- 133
Cdd:PLN02836 84 WLNSRSSSRFIGYALCAADEALSDARwlpsedeakerTGVSIG---GGIGSITDILEAAQLICEKRLRRLSPFFVPRili 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 134 ---AIAAQIAQGLQSTAEAQTyaTACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQT 210
Cdd:PLN02836 161 nmaAGHVSIRYGFQGPNHAAV--TACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNSCPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 211 GYCRPFSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRP--DPRGQALAMFRCLVDGGLAAAD 288
Cdd:PLN02836 239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPheDGRGAVLAMTRALQQSGLHPNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 289 VGYINAHATGTLVGDRIETAAIKQVFGAHASS--LPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQ 366
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*
gi 2751072858 367 CDLDYVAEGARRLPDLRLAISNSFGMGGNNAVLAF 401
Cdd:PLN02836 399 FDDGFVPLTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4-404 |
4.17e-72 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 231.55 E-value: 4.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRK--HPDPRiDRSVGHVAE----DMTEGLHPSQVRMLDRVTVMANYAA 77
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKitLFDAS-DFPVQIAGEitdfDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAALDASR--QAECGVFIGTGIGGVSTLCESVEAYHGVVPKRpllVVPAVMPQAIA------AQIAQGLQSTAEA 149
Cdd:PRK08439 81 REAMKDAGFLPEEldAERFGVSSASGIGGLPNIEKNSIICFEKGPRK---ISPFFIPSALVnmlggfISIEHGLKGPNLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 150 QTyaTACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCA---EPAAGQtgycRPFSHKRTGFALA 226
Cdd:PRK08439 158 SV--TACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrndDPKKAS----RPFDKDRDGFVMG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 227 EGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQALAMFRCLVDGGlaAADVGYINAHATGTLVGDRIE 306
Cdd:PRK08439 232 EGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 307 TAAIKQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLpDLRLAI 386
Cdd:PRK08439 310 TAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKA-ELNVVM 388
|
410
....*....|....*...
gi 2751072858 387 SNSFGMGGNNAVLAFRKV 404
Cdd:PRK08439 389 SNSFGFGGTNGVVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-404 |
7.91e-62 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 204.85 E-value: 7.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 1 MTHRQVVITAVGVASPVGGSAQSTFDALNAGVCGIR--KHPDPRI--DRSVGHVAE-DMTEGLHPSQVRMLDRVTVMANY 75
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVniEHFDTTNfsTRFAGLVKDfNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 76 AANQALGAAALDASRQ--AECGVFIGTGIGGVstlcESVEAYH-GVVPKRPLLVVPAVMPQAIAAQIA------QGLQST 146
Cdd:PRK08722 81 AGIQALDDSGLEVTEEnaHRIGVAIGSGIGGL----GLIEAGHqALVEKGPRKVSPFFVPSTIVNMIAgnlsimRGLRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 147 AEAqtYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGyCRPFSHKRTGFALA 226
Cdd:PRK08722 157 NIA--ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKA-SRPWDKDRDGFVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 227 EGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQ--ALAMFRCLVDGGLAAADVGYINAHATGTLVGDR 304
Cdd:PRK08722 234 DGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSggALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 305 IETAAIKQVFG-AHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPDLR 383
Cdd:PRK08722 314 AEIKGIKRALGeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESME 393
|
410 420
....*....|....*....|.
gi 2751072858 384 LAISNSFGMGGNNAVLAFRKV 404
Cdd:PRK08722 394 YAICNSFGFGGTNGSLIFKKM 414
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4-402 |
7.05e-56 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 189.04 E-value: 7.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPD----PRIDRSVGHVAEDMTEGLHPS--QVRMLDRVTVMANYAA 77
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwdryDGLNTRLAAPIDDFELPAHYTrkKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAAL--DAS-RQAECGVFIGTGIGgvSTlcESVEAYHGVVPKRPLLVVPA-----VMPQAIAAQIAQGLQSTAEA 149
Cdd:PRK09116 82 ELALEDAGLlgDPIlTDGRMGIAYGSSTG--ST--DPIGAFGTMLLEGSMSGITAttyvrMMPHTTAVNVGLFFGLKGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 150 QTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESmFSPALMAAWVQLHVLCAEPAAGQTGyCRPFSHKRTGFALAEGA 229
Cdd:PRK09116 158 IPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELT-PRPFDANRDGLVIGEGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 230 AMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAA 309
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 310 IKQVFGAhasSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQC-DLDYVAEGARRLpDLRLAISN 388
Cdd:PRK09116 316 TAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREI-DTEYVMSN 391
|
410
....*....|....
gi 2751072858 389 SFGMGGNNAVLAFR 402
Cdd:PRK09116 392 NFAFGGINTSLIFK 405
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
6-403 |
9.29e-56 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 187.95 E-value: 9.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 6 VVITAVGVASPVGGSAQStFDALNAGVCGIRKH-PDPRI-DRSVGHVAEdmteglHPSQVRMLDRVTVMAnyaanqALGA 83
Cdd:PRK05952 4 VVVTGIGLVSALGDLEQS-WQRLLQGKSGIKLHqPFPELpPLPLGLIGN------QPSSLEDLTKTVVTA------ALKD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 84 AALDASrQAECGVFIGTGIG-------GVSTLCESVEAYHGVVPKRPLLvvpAVMPQAIAAQIAQGLQSTAEAQTYATAC 156
Cdd:PRK05952 71 AGLTPP-LTDCGVVIGSSRGcqgqwekLARQMYQGDDSPDEELDLENWL---DTLPHQAAIAAARQIGTQGPVLAPMAAC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 157 SAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLcaepaaGQTGyCRPFSHKRTGFALAEGAAMLVLES 236
Cdd:PRK05952 147 ATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGAL------AKTG-AYPFDRQREGLVLGEGGAILVLES 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 237 ADHARARNAAVIAEICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVF 314
Cdd:PRK05952 220 AELAQKRGAKIYGQILGFGLTCDAYHMSAPEPdgKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 315 GahaSSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESgdPQCDLDYVAEGarRLPDLRLAISNSFGMGG 394
Cdd:PRK05952 300 P---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFVRQA--QQSPLQNVLCLSFGFGG 372
|
....*....
gi 2751072858 395 NNAVLAFRK 403
Cdd:PRK05952 373 QNAAIALGK 381
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
94-397 |
2.10e-53 |
|
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: 183.14 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 94 CGVFIGTGIGGVSTLCESVEAYHgvvpkrPLLVVPAVMPQAIAAQIAQGLQSTAEAQTYATACSAGAVAIGEAYRRIRDG 173
Cdd:cd00833 114 TGVFVGASSSDYLELLARDPDEI------DAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 174 YLDVAIAGGSESMFSPALMAAWVQLHVLCAepaagqTGYCRPFSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICG 253
Cdd:cd00833 188 ECDLALVGGVNLILSPDMFVGFSKAGMLSP------DGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 254 YGVSNDGT--HPVRPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVFGAH---ASSLPVSSIKG 328
Cdd:cd00833 262 SAVNQDGRtkGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSrsaDQPLLIGSVKS 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2751072858 329 AIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLD----YVAEGARRLPD---LRLAISNSFGMGGNNA 397
Cdd:cd00833 342 NIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEARPWPApagPRRAGVSSFGFGGTNA 417
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
134-401 |
1.07e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 175.97 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 134 AIAAQIAQGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPAlmaAWVQLHVLCA-----EPAAG 208
Cdd:PRK06501 153 SIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAE---ALIRFSLLSAlstqnDPPEK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 209 QTgycRPFSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQAL--AMFRCLVDGGLAA 286
Cdd:PRK06501 230 AS---KPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAigAIRAALADAGLTP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 287 ADVGYINAHATGTLVGDRIETAAIKQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQ 366
Cdd:PRK06501 307 EQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPA 386
|
250 260 270
....*....|....*....|....*....|....*
gi 2751072858 367 CDLDYVAEGARRLPdLRLAISNSFGMGGNNAVLAF 401
Cdd:PRK06501 387 IPLDVVPNVARDAR-VTAVLSNSFGFGGQNASLVL 420
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
87-403 |
2.85e-49 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 169.91 E-value: 2.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 87 DASRQAECGVFIGTGIGGVSTLCESVEAYHGVVPKR-PLLVVPAVMPQAIAAQIAQGLQSTAEAQTYATACSAGAVAIGE 165
Cdd:PRK14691 21 NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRlSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 166 AYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQTGYCRPFSHKRTGFALAEGAAMLVLESADHARARNA 245
Cdd:PRK14691 101 AVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 246 AVIAEICGYGVSNDGTHPVR--PDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVFGaHASSLPV 323
Cdd:PRK14691 181 KPLAEIVGYGTSADAYHMTSgaEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFG-ESNALAI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 324 SSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPDLRLAISNSFGMGGNNAVLAFRK 403
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
4-401 |
5.61e-48 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 171.31 E-value: 5.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKhpDPRID------RSVGHVAEDMTEG-LHPSQVRMLDR-----VTV 71
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISE--IERFDcsqfptRIAGEIKSFSTDGwVAPKLSKRMDKfmlylLTA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 72 MANYAANQALGAAALDASRQAECGVFIGTGIGGVSTLCESVEAYHGVVPKRPLLVVPAVMPQAIAAQIAQGLQSTAEAQT 151
Cdd:PLN02787 207 GKKALADGGITEDVMKELDKTKCGVLIGSAMGGMKVFNDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 152 YATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLcAEPAAGQTGYCRPFSHKRTGFALAEGAAM 231
Cdd:PLN02787 287 ISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRAL-SQRNDDPTKASRPWDMNRDGFVMGEGAGV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 232 LVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQA--LAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAA 309
Cdd:PLN02787 366 LLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGviLCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 310 IKQVFGAHaSSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPDLRLAISNS 389
Cdd:PLN02787 446 LMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVALSNS 524
|
410
....*....|..
gi 2751072858 390 FGMGGNNAVLAF 401
Cdd:PLN02787 525 FGFGGHNSSILF 536
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
6-401 |
1.16e-47 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 166.94 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 6 VVITAVGVASPVGGSAQSTFDALNAGVC-GIRKHPDPRIDRS--VGHVAEDMTEGLHPSQVRMLDR-----VTVMANYAA 77
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRAsGMRPCDFWLVDLPtwVGEVVGVELPALPAALAAFDCRnnrlaLLALQQIEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAALDASRqaeCGVFIGTGIGGVStlcESVEAYHGVVPKRPLLvvPAVM------PQAIAAQIAQGLQSTAEAQT 151
Cdd:PRK09185 84 AVEAAIARYGADR---IGVVLGTSTSGIL---EGELAYRRRDPAHGAL--PADYhyaqqeLGSLADFLRAYLGLSGPAYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 152 YATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM-------FSpalmaawvQLHVLCAEPaagqtgyCRPFSHKRTGFA 224
Cdd:PRK09185 156 ISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLcrltlngFN--------SLESLSPQP-------CRPFSANRDGIN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 225 LAEGAAMLVLEsadhaRARNAAVIaeICGYGVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTLVG 302
Cdd:PRK09185 221 IGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPegLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 303 DRIETAAIKQVFGAHassLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPdL 382
Cdd:PRK09185 294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALA-I 369
|
410
....*....|....*....
gi 2751072858 383 RLAISNSFGMGGNNAVLAF 401
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLIF 388
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-399 |
1.46e-47 |
|
"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: 167.23 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTF---DALNAGVCGIRKHPDPRI--DRSV-GHVAEDMTEGLHPSQVRMLDRVTVMANYAA 77
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVEefwEALREGRSGIAPVARLKSrfDRGVaGQIPTGDIPGWDAKRTGIVDRTTLLALVAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAALDASRQ---AECGVFIGTGIGGVSTLcesVEAYHGVVPKRPLLVVPAVMPQ--AIAAQIAQGLQSTA-EAQT 151
Cdd:cd00828 81 EEALADAGITDPYEvhpSEVGVVVGSGMGGLRFL---RRGGKLDARAVNPYVSPKWMLSpnTVAGWVNILLLSSHgPIKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 152 YATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESmFSPALMAAWVQLHVLCAEPAAGQTGYcRPFSHKRTGFALAEGAAM 231
Cdd:cd00828 158 PVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMS-RPFDETRDGFVEAEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 232 LVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDP-RGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAI 310
Cdd:cd00828 236 LVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGgKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 311 KQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPD-LRLAISNS 389
Cdd:cd00828 316 AEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLkVRAALVNA 395
|
410
....*....|
gi 2751072858 390 FGMGGNNAVL 399
Cdd:cd00828 396 FGFGGSNAAL 405
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-403 |
8.42e-45 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 159.81 E-value: 8.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 5 QVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPriDRSVG-HVAEDMTEGLHPSQVRMLDRVTVMANYAA------ 77
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRP--GRQVPdDAGAGLASAFIGAELDSLALPERLDAKLLrrasls 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAALDASRQAECGVFIGTGIGGVS-----TLCESVEAYHGVVpKRPLLVVPA----VMPQAIAAQIAQGLQSTAE 148
Cdd:PRK07103 81 AQAALAAAREAWRDAALGPVDPDRIGLVVggsnlQQREQALVHETYR-DRPAFLRPSyglsFMDTDLVGLCSEQFGIRGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 149 AQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAEPAAGQ-TGYCRPFSHKRTGFALAE 227
Cdd:PRK07103 160 GFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRFADEpEAACRPFDQDRDGFIYGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 228 GAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIET 307
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 308 AAIkqvFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTL-FFESGDPQCdlDYVAEGARRLpDLRLAI 386
Cdd:PRK07103 320 AAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRnLDEPIDERF--RWVGSTAESA-RIRYAL 393
|
410
....*....|....*..
gi 2751072858 387 SNSFGMGGNNAVLAFRK 403
Cdd:PRK07103 394 SLSFGFGGINTALVLER 410
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-405 |
3.01e-40 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 147.51 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPRIDRSVGHVAEDMTegLHPSQV------RMLDRVTVMANYAA 77
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK--LDPTGLidrkvmRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 78 NQALGAAALDASRQA--ECGVFIGTGIGGVSTLCESVEAYHGvvPKRPLLVVPAVMPQAIAaqiaqglqSTAEAqTYAT- 154
Cdd:PRK07967 80 EQAIADAGLSEEQVSnpRTGLIAGSGGGSTRNQVEAADAMRG--PRGPKRVGPYAVTKAMA--------STVSA-CLATp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 155 ------------ACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMfspalmaAWvQLHVLCAEPAAGQTGY-------CRP 215
Cdd:PRK07967 149 fkikgvnysissACATSAHCIGNAVEQIQLGKQDIVFAGGGEEL-------DW-EMSCLFDAMGALSTKYndtpekaSRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 216 FSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHPVRPDPRGQALAMFRCL--VDGglaaaDVGYIN 293
Cdd:PRK07967 221 YDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALatVDT-----PIDYIN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 294 AHATGTLVGDRIETAAIKQVFGAHASslPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQ-CDLDYV 372
Cdd:PRK07967 296 THGTSTPVGDVKELGAIREVFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIV 373
|
410 420 430
....*....|....*....|....*....|...
gi 2751072858 373 AEGARRLPdLRLAISNSFGMGGNNAVLAFRKVA 405
Cdd:PRK07967 374 TETTDNAE-LTTVMSNSFGFGGTNATLVFRRYK 405
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
154-397 |
5.00e-39 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 149.25 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 154 TACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAepaagqTGYCRPFSHKRTGFALAEGAAMLV 233
Cdd:COG3321 172 TACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSP------DGRCRAFDADADGYVRGEGVGVVV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 234 LESADHARARNAAVIAEICGYGVSNDG-----ThpvRPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETA 308
Cdd:COG3321 246 LKRLSDALRDGDRIYAVIRGSAVNQDGrsnglT---APNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 309 AIKQVFGAHAS---SLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLD----YVAEGARRLPD 381
Cdd:COG3321 323 ALTAAFGQGRPadqPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPWPA 402
|
250
....*....|....*....
gi 2751072858 382 ---LRLAISNSFGMGGNNA 397
Cdd:COG3321 403 gggPRRAGVSSFGFGGTNA 421
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
95-400 |
2.98e-32 |
|
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: 124.29 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 95 GVFIGTGIGGVSTLCESVEAYHGVVPkrplLVVPAVMPQAIAAQIAQGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGY 174
Cdd:cd00825 39 GVVVGTGGGSPRFQVFGADAMRAVGP----YVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 175 LDVAIAGGSESMFSPALMAAWVQLhvlcaePAAGQTGYCRPFSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICGY 254
Cdd:cd00825 115 QDIVLAGGSEELAAPMDCEFDAMG------ALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 255 GVSNDGTHPVRPDP--RGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVFGAHasSLPVSSIKGAIGH 332
Cdd:cd00825 189 AATIDGAGMGAFAPsaEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDK--SPAVSATKAMTGN 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2751072858 333 TIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRlpdLRLAISNSFGMGGNNAVLA 400
Cdd:cd00825 267 LSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRE---LRTALLNGFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
249-361 |
3.53e-31 |
|
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: 114.97 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 249 AEICGYGVSNDGTHPV--RPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVFGAHA--SSLPVS 324
Cdd:pfam02801 2 AVIKGSAVNHDGRHNGltAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkQPLAIG 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 2751072858 325 SIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFE 361
Cdd:pfam02801 82 SVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4-399 |
7.82e-30 |
|
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: 119.00 E-value: 7.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGI----RKHPDPRIDRSVGHVAE-DMTEGLHPSQVRMLDRVTVMANYAAN 78
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLgpitRFDPSGYPARLAGEVPDfDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 79 QALGAAALDASRQAE--CGVFIGTGIGGVSTLCESVEAYHGVVPKRpllvVPAVmpQAIA-------AQIAQGLQSTAEA 149
Cdd:cd00832 81 WALADAGVDPAALPPydMGVVTASAAGGFEFGQRELQKLWSKGPRH----VSAY--QSFAwfyavntGQISIRHGMRGPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 150 QTYATACSAGAVAIGEAYRRIRDGyLDVAIAGGSESMFSPALMAAWVQLHVLC--AEPAAGQtgycRPFSHKRTGFALAE 227
Cdd:cd00832 155 GVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLStsDDPARAY----LPFDAAAAGYVPGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 228 GAAMLVLESADHARARNAAVIAEICGYGVSNDGThPVRPDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIET 307
Cdd:cd00832 230 GGAILVLEDAAAARERGARVYGEIAGYAATFDPP-PGSGRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 308 AAIKQVFGAHAssLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLDYVAEGARRLPdLRLAIS 387
Cdd:cd00832 309 AALAAVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAA-LRTALV 385
|
410
....*....|..
gi 2751072858 388 NSFGMGGNNAVL 399
Cdd:cd00832 386 LARGRGGFNSAL 397
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-240 |
1.10e-26 |
|
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: 106.95 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 4 RQVVITAVGVASPVGGSAQSTFDALNAGVCGIRKHPDPRIDRS---------VGHVA------------EDMTEGLHPSQ 62
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRWDPDklydppsriAGKIYtkwgglddifdfDPLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 63 VRMLDRVTVMAnyaanqalgaaaLDASRQA--------------ECGVFIGTGIGGVSTLCESVEAyhgVVPKRPLLVVP 128
Cdd:pfam00109 81 AERMDPQQRLL------------LEAAWEAledagitpdsldgsRTGVFIGSGIGDYAALLLLDED---GGPRRGSPFAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 129 AVMPQAIAAQIAQGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAepaag 208
Cdd:pfam00109 146 GTMPSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP----- 220
|
250 260 270
....*....|....*....|....*....|..
gi 2751072858 209 qTGYCRPFSHKRTGFALAEGAAMLVLESADHA 240
Cdd:pfam00109 221 -DGPCKAFDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
154-397 |
1.85e-24 |
|
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: 102.02 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 154 TACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQLHVLCAepaagqTGYCRPFSHKRTGFALAEGAAMLV 233
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSP------DGRCKTFDASADGYVRGEGVGVVV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 234 LESADHARARNAAVIAEICGYGVSNDG-----THpvrPDPRGQalamfrclvdgglaaadvgyinahatgtlvgdrieta 308
Cdd:smart00825 169 LKRLSDALRDGDPILAVIRGSAVNQDGrsngiTA---PSGPAQ------------------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 309 aikqvfgahassLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPTLFFESGDPQCDLD----YVAEGARRLPD--- 381
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPpgr 276
|
250
....*....|....*.
gi 2751072858 382 LRLAISNSFGMGGNNA 397
Cdd:smart00825 277 PRRAGVSSFGFGGTNA 292
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
128-396 |
5.11e-22 |
|
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: 98.92 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 128 PAVMPQAIAAQIAQ-----GLQSTAEAqtyatACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQlhvlc 202
Cdd:TIGR02813 178 PGSLGNVISGRIANrfdlgGMNCVVDA-----ACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSK----- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 203 aEPAAGQTGYCRPFSHKRTGFALAEGAAMLVLESADHARARNAAVIAEICGYGVSNDGTHP--VRPDPRGQALAMFRCLV 280
Cdd:TIGR02813 248 -TPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKsiYAPRPEGQAKALKRAYD 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 281 DGGLAAADVGYINAHATGTLVGDRIETAAIKQVFG---AHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQGIVPPT 357
Cdd:TIGR02813 327 DAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPT 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2751072858 358 LFFESGDPQCDLD----YVAEGAR----RLPDL-RLAISNSFGMGGNN 396
Cdd:TIGR02813 407 INVDQPNPKLDIEnspfYLNTETRpwmqREDGTpRRAGISSFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
104-399 |
7.83e-16 |
|
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: 76.71 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 104 GVSTLCESVEAYHGVVPKRPLLVVPAVMP----QAIAAQIAQGLQ-STAEAQTYATACSAGAVAIGEAYRRIRDGYLDVA 178
Cdd:cd00327 11 GFEAAEQAIADAGLSKGPIVGVIVGTTGGsgefSGAAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 179 IAGGSESmfspalmaawvqlhvlcaepaagqtgycrpfshkrtgFALAEGAAMLVLESADHARARNAAVIAEICGYGVSN 258
Cdd:cd00327 91 LAGGSEE-------------------------------------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 259 DGTHPVR-PDPRGQALAMFRCLVDGGLAAADVGYINAHATGTLVGDRIETAAIKQVFGAHasSLPVSSIKGAIGHTIGAA 337
Cdd:cd00327 134 DGASMVPaVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2751072858 338 GAIEAAVTAMALQQGIVPPTlffesgdpqcdldyvaegarrLPDLRLAISNSFGMGGNNAVL 399
Cdd:cd00327 212 GLAILDELLLMLEHEFIPPT---------------------PREPRTVLLLGFGLGGTNAAV 252
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
157-356 |
1.00e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 50.34 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 157 SAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAW--VQLH-------VLCAEPAAGqtgycrpfshkrTGFALAE 227
Cdd:PRK06519 176 SAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYelGGLLlkggwapVWSRGGEDG------------GGFILGS 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 228 GAAMLVLESADHARARNAAVIAEICgyGVSNDGThpvRPDPRGQALAMFRCLVDGGLAAADVGYINAhATGTLvgdriET 307
Cdd:PRK06519 244 GGAFLVLESREHAEARGARPYARIS--GVESDRA---RRAPGDLEASLERLLKPAGGLAAPTAVISG-ATGAH-----PA 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2751072858 308 AAIKQVFGAHASSLPVSSIKGAIGHTIGAAGAIEAAVTAMALQQG-IVPP 356
Cdd:PRK06519 313 TAEEKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGaLFPP 362
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
126-195 |
4.20e-05 |
|
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: 45.16 E-value: 4.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2751072858 126 VVPAVMPQAIAAQIA--QGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMfSPALMAAW 195
Cdd:cd00751 52 VLQAGEGQNPARQAAllAGLPESVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESM-SRAPYLLP 122
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
126-186 |
3.65e-04 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 42.30 E-value: 3.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2751072858 126 VVPAVMPQA--------IAAQIAqGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM 186
Cdd:PRK09052 58 IVGCAMPEAeqglnvarIGALLA-GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESM 125
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
126-186 |
5.00e-04 |
|
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: 41.98 E-value: 5.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2751072858 126 VVPAVMPQAIAAQIAQ--GLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM 186
Cdd:COG0183 56 VLQAGQGQNPARQAALlaGLPESVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESM 118
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
126-186 |
1.49e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 39.98 E-value: 1.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2751072858 126 VVPAVMPQAIA--AQIAQGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM 186
Cdd:pfam00108 53 VLQAGEGQNPArqAALKAGIPDSAPAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
126-186 |
1.64e-03 |
|
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: 40.29 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2751072858 126 VVPAVMPQAIAAQIA--QGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM 186
Cdd:TIGR01930 51 VLQAGEQQNIARQAAllAGLPESVPAYTVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESM 113
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
142-186 |
4.50e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 38.78 E-value: 4.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2751072858 142 GLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM 186
Cdd:PRK09050 76 GLPVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESM 120
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
123-201 |
5.14e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 38.84 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 123 PLLVVPAVMPQAIAAQIAQ----------GLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESM-FSPAL 191
Cdd:PRK06366 45 PALVQEVIMGNVIQAGVGQnpagqaayhaGLPFGVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMsNAPFL 124
|
90
....*....|...
gi 2751072858 192 MAA---WVQLHVL 201
Cdd:PRK06366 125 LPSdlrWGPKHLL 137
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
125-228 |
5.32e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 38.58 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072858 125 LVVPAVMPQA-----IAAQIA--QGLQSTAEAQTYATACSAGAVAIGEAYRRIRDGYLDVAIAGGSESMFSPALMAAWVQ 197
Cdd:PRK07661 52 LIIGCAMPEAeqglnMARNIGalAGLPYTVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVR 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2751072858 198 LHVLCAEPA--------------AGQTGYCR----PF---SHKRTGFALAEG 228
Cdd:PRK07661 132 PNPRLVEAApeyymgmghtaeqvAVKYGISRedqdAFavrSHQRAAKALAEG 183
|
|
| |
