|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3-409 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 701.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 3 LNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAA 82
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 83 QEAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINT 162
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 163 ACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST-TEDPTRASIPFDKDRNGFVMGEGSGMLVLE 241
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 242 SLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAV 321
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 322 LG---KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGG 398
Cdd:PRK07314 321 FGehaYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|.
gi 2038653373 399 HNAVLAFKRWE 409
Cdd:PRK07314 401 TNASLVFKRYE 411
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
4-406 |
0e+00 |
|
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: 633.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQ 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 84 EAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINTA 163
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 164 CSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST-TEDPTRASIPFDKDRNGFVMGEGSGMLVLES 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 243 LEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVL 322
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 323 G---KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGH 399
Cdd:TIGR03150 321 GdhaYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 2038653373 400 NAVLAFK 406
Cdd:TIGR03150 401 NASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-408 |
0e+00 |
|
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: 616.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQ 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 84 EAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINTA 163
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 164 CSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTT-EDPTRASIPFDKDRNGFVMGEGSGMLVLES 242
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRnDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 243 LEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVL 322
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 323 G---KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGH 399
Cdd:COG0304 321 GdhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 2038653373 400 NAVLAFKRW 408
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4-405 |
0e+00 |
|
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: 601.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQ 83
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 84 EAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINTA 163
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 164 CSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTT-EDPTRASIPFDKDRNGFVMGEGSGMLVLES 242
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRnDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 243 LEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVL 322
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 323 G---KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGH 399
Cdd:cd00834 321 GehaKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 2038653373 400 NAVLAF 405
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-409 |
1.28e-166 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 473.72 E-value: 1.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 1 MKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQD--------FPFDKYFVKKDTNRFD 72
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 73 NYSLYALYAAQEAVNHANLDVEAL-NRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRF 151
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLeDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 152 GANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTT--EDPTRASIPFDKDRNGF 229
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfnDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 230 VMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPA 309
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 310 NEKGESGAIVAVLG--KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEA-NVVYGQGLEKEI 386
Cdd:PRK06333 321 GDLGEVAAIKKVFGhvSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGlDVVANKARPMDM 400
|
410 420
....*....|....*....|...
gi 2038653373 387 PYAISNTFGFGGHNAVLAFKRWE 409
Cdd:PRK06333 401 DYALSNGFGFGGVNASILFRRWE 423
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-407 |
1.35e-146 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 422.95 E-value: 1.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 13 VTSPIGNTPEEFWNSLATGKIGIGGITKFDHS--DFDVHNAAE----------IQDFPFDKYFVKKD---TNRFDNYSLY 77
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpDCIPEQKALenlvaampcqIAAEVDQSEFDPSDfapTKRESRATHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 78 ALYAAQEAVNHANLDVEA-LNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGV 156
Cdd:PTZ00050 81 AMAAAREALADAKLDILSeKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 157 CKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTT--EDPTRASIPFDKDRNGFVMGEG 234
Cdd:PTZ00050 161 SGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKynDDPQRASRPFDKDRAGFVMGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 235 SGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEE-AEISPEQVAYVNAHGTSTPANEKG 313
Cdd:PTZ00050 241 AGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIGDKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 314 ESGAIVAVLG----KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGL--EKEIP 387
Cdd:PTZ00050 321 ELKAIKKVFGdsgaPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQSID 400
|
410 420
....*....|....*....|
gi 2038653373 388 YAISNTFGFGGHNAVLAFKR 407
Cdd:PTZ00050 401 AVLSTSFGFGGVNTALLFTK 420
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-407 |
1.34e-131 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 384.08 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 1 MKlnRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALY 80
Cdd:PRK08439 1 MK--RVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 81 AAQEAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSI 160
Cdd:PRK08439 79 AAREAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 161 NTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST-TEDPTRASIPFDKDRNGFVMGEGSGMLV 239
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGAGALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 240 LESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEgqGAIKAIKLALEEAEISPeqVAYVNAHGTSTPANEKGESGAIV 319
Cdd:PRK08439 239 LEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 320 AVLGKEV---PVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGF 396
Cdd:PRK08439 315 ELFGSKEkvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGF 394
|
410
....*....|.
gi 2038653373 397 GGHNAVLAFKR 407
Cdd:PRK08439 395 GGTNGVVIFKK 405
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
5-405 |
8.39e-120 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 355.25 E-value: 8.39e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 5 RVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGIT----KFDHSDFDVHNAAEIQ----------------DFPFDKYFV 64
Cdd:PLN02836 7 RVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTqddlKMKSEDEETQLYTLDQlpsrvaalvprgtgpgDFDEELWLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 65 KKDTNRFdnySLYALYAAQEAVNHAN-LDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMA 143
Cdd:PLN02836 87 SRSSSRF---IGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 144 SGNVAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST--TEDPTRASIP 221
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASRP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 222 FDKDRNGFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVN 301
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 302 AHGTSTPANEKGESGAIVAVLGKEVP-----VSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANV 376
Cdd:PLN02836 324 AHATSTPLGDAVEARAIKTVFSEHATsgglaFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGF 403
|
410 420 430
....*....|....*....|....*....|.
gi 2038653373 377 VyGQGLEKEIPY--AISNTFGFGGHNAVLAF 405
Cdd:PLN02836 404 V-PLTASKAMLIraALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-405 |
1.05e-118 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 355.83 E-value: 1.05e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 1 MKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALY 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 81 AAQEAVNHANLDVEA---LNRDRFGVIVASGIGGIKEIEDQV--LRLHEKgpkRVKPMTLPKALPNMASGNVAMRFGANG 155
Cdd:PLN02787 206 AGKKALADGGITEDVmkeLDKTKCGVLIGSAMGGMKVFNDAIeaLRISYR---KMNPFCVPFATTNMGSAMLAMDLGWMG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 156 VCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST-TEDPTRASIPFDKDRNGFVMGEG 234
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGEG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 235 SGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGE 314
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 315 SGAIVAVLGK--EVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEK-EIPYAIS 391
Cdd:PLN02787 443 YQALMRCFGQnpELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALS 522
|
410
....*....|....
gi 2038653373 392 NTFGFGGHNAVLAF 405
Cdd:PLN02787 523 NSFGFGGHNSSILF 536
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-407 |
3.17e-118 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 350.46 E-value: 3.17e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 1 MKLNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALY 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 81 AAQEAVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSI 160
Cdd:PRK08722 81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 161 NTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST-TEDPTRASIPFDKDRNGFVMGEGSGMLV 239
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 240 LESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIV 319
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 320 AVLG----KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKE-IPYAISNTF 394
Cdd:PRK08722 321 RALGeagsKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSF 400
|
410
....*....|...
gi 2038653373 395 GFGGHNAVLAFKR 407
Cdd:PRK08722 401 GFGGTNGSLIFKK 413
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
5-406 |
1.29e-96 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 294.59 E-value: 1.29e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 5 RVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFD-HSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQ 83
Cdd:PRK09116 3 RVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 84 EAVNHANL-DVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINT 162
Cdd:PRK09116 83 LALEDAGLlGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPTSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 163 ACSSSNDAIGDAFRSIKFGFQDVMLVGGTEAsITPFAIAGFQALTALSTTED-PTRASIPFDKDRNGFVMGEGSGMLVLE 241
Cdd:PRK09116 163 ACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDaPELTPRPFDANRDGLVIGEGAGTLVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 242 SLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGaiKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAV 321
Cdd:PRK09116 242 ELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 322 LGKEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVS------DYIEanvvyGQGLEKEIPYAISNTFG 395
Cdd:PRK09116 320 FGARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDpacgalDYIM-----GEAREIDTEYVMSNNFA 394
|
410
....*....|.
gi 2038653373 396 FGGHNAVLAFK 406
Cdd:PRK09116 395 FGGINTSLIFK 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
5-409 |
2.57e-93 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 286.18 E-value: 2.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 5 RVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDkyFVKKDTNRF-DNYSLYALYAAQ 83
Cdd:PRK07967 3 RVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTG--LIDRKVMRFmGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 84 EAVNHANLDVEALNRDRFGVIVASGIGGIKEIED--QVLRlHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSIN 161
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEaaDAMR-GPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 162 TACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAgFQALTALST--TEDPTRASIPFDKDRNGFVMGEGSGMLV 239
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDGFVIAGGGGVVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 240 LESLEHAEKRGATILAEVVGYGNTCDAYHMTSphPEGQGAIKAIKLALEEAEISpeqVAYVNAHGTSTPANEKGESGAIV 319
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVDTP---IDYINTHGTSTPVGDVKELGAIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 320 AVLGKEVP-VSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEA-NVVYGQGLEKEIPYAISNTFGFG 397
Cdd:PRK07967 314 EVFGDKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGmPIVTETTDNAELTTVMSNSFGFG 393
|
410
....*....|..
gi 2038653373 398 GHNAVLAFKRWE 409
Cdd:PRK07967 394 GTNATLVFRRYK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
98-408 |
4.92e-91 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 278.54 E-value: 4.92e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 98 RDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINTACSSSNDAIGDAFRS 177
Cdd:PRK14691 25 QERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 178 IKFGFQDVMLVGGTEASITPFAIAGFQALTALST--TEDPTRASIPFDKDRNGFVMGEGSGMLVLESLEHAEKRGATILA 255
Cdd:PRK14691 105 IRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 256 EVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVLGKE--VPVSSTKS 333
Cdd:PRK14691 185 EIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESnaLAITSTKS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038653373 334 FTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEA-NVVYGQGLEKEIPYAISNTFGFGGHNAVLAFKRW 408
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGlNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-408 |
2.94e-87 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 271.22 E-value: 2.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 6 VVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDV------HNAAEiqdfpFDKYFVKKDTNRFDNYSLYAL 79
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFDLpvriggHLLEE-----FDHQLTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 80 YAAQEAVNHA-NLDVEAlnrDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGAN-GVC 157
Cdd:PRK07910 89 VLGRRVWENAgSPEVDT---NRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKaGVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 158 KSInTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTA-LSTT-EDPTRASIPFDKDRNGFVMGEGS 235
Cdd:PRK07910 166 TPV-SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNnDDPAGACRPFDKDRDGFVFGEGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 236 GMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGES 315
Cdd:PRK07910 245 ALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 316 GAIVAVLGKEVP-VSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTF 394
Cdd:PRK07910 325 KAINNALGGHRPaVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSF 404
|
410
....*....|....
gi 2038653373 395 GFGGHNAVLAFKRW 408
Cdd:PRK07910 405 GFGGHNVALAFGRY 418
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-403 |
3.04e-87 |
|
"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: 270.85 E-value: 3.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGN---TPEEFWNSLATGKIGIGGITKFdHSDFDVHNAAEIQDFPFDKYFVKKdTNRFDNYSLYALY 80
Cdd:cd00828 1 SRVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWDAKR-TGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 81 AAQEAVNHANL-DVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKalPNMASGNVAMRF-GANGVCK 158
Cdd:cd00828 79 ATEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLS--PNTVAGWVNILLlSSHGPIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 159 SINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEAsITPFAIAGFQALTALSTTED-PTRASIPFDKDRNGFVMGEGSGM 237
Cdd:cd00828 157 TPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDGFVEAEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 238 LVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPeGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGA 317
Cdd:cd00828 236 LVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 318 IVAV---LGKEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQG--LEKEIPYAISN 392
Cdd:cd00828 315 IAEVagaLGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSrdLNLKVRAALVN 394
|
410
....*....|.
gi 2038653373 393 TFGFGGHNAVL 403
Cdd:cd00828 395 AFGFGGSNAAL 405
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
6-407 |
3.95e-85 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 265.73 E-value: 3.95e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 6 VVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIqDFPFDKYFVKKD-TNRFdnyslyALYAAQE 84
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DFLPESPFGASAlSEAL------ARLAAEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 85 AVNHANLDVEALNRDRFgvIVASGIggikEIE-DQVLRLHEKGPKRVKPmTLPKALPNMASG----------------NV 147
Cdd:PRK06501 86 ALAQAGIGKGDFPGPLF--LAAPPV----ELEwPARFALAAAVGDNDAP-SYDRLLRAARGGrfdalherfqfgsiadRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 148 AMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTTED-PTRASIPFDKDR 226
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDpPEKASKPFSKDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 227 NGFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTS 306
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 307 TPANEKGESGAIVAVLG---KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLE 383
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGerlASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARD 398
|
410 420
....*....|....*....|....
gi 2038653373 384 KEIPYAISNTFGFGGHNAVLAFKR 407
Cdd:PRK06501 399 ARVTAVLSNSFGFGGQNASLVLTA 422
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
4-407 |
1.34e-78 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 247.83 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIG---------------IGGITKFDH-------SDFDVHNaaeiqdfpfdk 61
Cdd:PRK09185 2 TPVYISAFGATSALGRGLDAILAALRAGRASgmrpcdfwlvdlptwVGEVVGVELpalpaalAAFDCRN----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 62 yfvkkdtNRFdnySLYALYAAQEAVNHAnldVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPkrvkpmTLPKAL-- 139
Cdd:PRK09185 71 -------NRL---ALLALQQIEPAVEAA---IARYGADRIGVVLGTSTSGILEGELAYRRRDPAHG------ALPADYhy 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 140 PNMASGN----VAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEaSITPFAIAGFQALTALSTTedP 215
Cdd:PRK09185 132 AQQELGSladfLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVD-SLCRLTLNGFNSLESLSPQ--P 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 216 TRasiPFDKDRNGFVMGEGSGMLVLEslehAEKRGATILAevvGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPE 295
Cdd:PRK09185 209 CR---PFSANRDGINIGEAAAFFLLE----REDDAAVALL---GVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 296 QVAYVNAHGTSTPANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEAN 375
Cdd:PRK09185 279 DIGYINLHGTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPL 358
|
410 420 430
....*....|....*....|....*....|..
gi 2038653373 376 VVYGQGLEKEIPYAISNTFGFGGHNAVLAFKR 407
Cdd:PRK09185 359 YLVENAQALAIRYVLSNSFAFGGNNCSLIFGR 390
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
5-407 |
7.36e-76 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 240.72 E-value: 7.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 5 RVVVTGYGVTSPIGNTpEEFWNSLATGKIGIGGITKFdhSDFDVHNAAEIQDFPFDKYFVKKDTnrfdnyslyalyaAQE 84
Cdd:PRK05952 3 KVVVTGIGLVSALGDL-EQSWQRLLQGKSGIKLHQPF--PELPPLPLGLIGNQPSSLEDLTKTV-------------VTA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 85 AVNHANLDveALNRDrFGVIVAS--GIGGIKEiedQVLRLHEKGPKRVKPMTLPK----ALPNMASGNVAMRFGANGVCK 158
Cdd:PRK05952 67 ALKDAGLT--PPLTD-CGVVIGSsrGCQGQWE---KLARQMYQGDDSPDEELDLEnwldTLPHQAAIAAARQIGTQGPVL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 159 SINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTTedptrASIPFDKDRNGFVMGEGSGML 238
Cdd:PRK05952 141 APMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKT-----GAYPFDRQREGLVLGEGGAIL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 239 VLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAI 318
Cdd:PRK05952 216 VLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 319 VAVLGKEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEvSDYiEANVVYgQGLEKEIPYAISNTFGFGG 398
Cdd:PRK05952 296 QALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE-PEF-DLNFVR-QAQQSPLQNVLCLSFGFGG 372
|
....*....
gi 2038653373 399 HNAVLAFKR 407
Cdd:PRK05952 373 QNAAIALGK 381
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
5-403 |
2.69e-72 |
|
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: 231.87 E-value: 2.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 5 RVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDFDVHNAAEIQDFPFDKYFVKKDTNRFDNYSLYALYAAQE 84
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAADW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 85 AVNHANLDVEALNRDRFGVIVASGIGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGANGVCKSINTAC 164
Cdd:cd00832 82 ALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAEQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 165 SSSNDAIGDAFRSIKFGfQDVMLVGGTEASITPFAIAGFQALTALSTTEDPTRASIPFDKDRNGFVMGEGSGMLVLESLE 244
Cdd:cd00832 162 AGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVLEDAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 245 HAEKRGATILAEVVGYGNTCDAyhmtSPHP-EGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVLG 323
Cdd:cd00832 241 AARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 324 KE-VPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYGQGLEKEIPYAISNTFGFGGHNAV 402
Cdd:cd00832 317 PRgVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGFNSA 396
|
.
gi 2038653373 403 L 403
Cdd:cd00832 397 L 397
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
3-407 |
1.78e-68 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 222.21 E-value: 1.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 3 LNRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITKFDHSDF--------DVHNAAEIQDFPfDKYFVKKDTNRFDNY 74
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPddagaglaSAFIGAELDSLA-LPERLDAKLLRRASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 75 SL-YALYAAQEAVNHANLDveALNRDRFGVIVasgiGGIKEIEDQVLRLHEKGPKRVKPMTLPKALPNMAS---GNVAMR 150
Cdd:PRK07103 80 SAqAALAAAREAWRDAALG--PVDPDRIGLVV----GGSNLQQREQALVHETYRDRPAFLRPSYGLSFMDTdlvGLCSEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 151 FGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALST---TEDPTRASIPFDKDRN 227
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSdrfADEPEAACRPFDQDRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 228 GFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQgaIKAIKLALEEAEISPEQVAYVNAHGTST 307
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 308 PANEKGESGAIVAVLGKEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDyIEANVVYGQGLEKEIP 387
Cdd:PRK07103 312 PLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPID-ERFRWVGSTAESARIR 390
|
410 420
....*....|....*....|
gi 2038653373 388 YAISNTFGFGGHNAVLAFKR 407
Cdd:PRK07103 391 YALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-401 |
4.17e-60 |
|
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: 200.86 E-value: 4.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGITK--FDHSDFDVHNAAEIQDFPFDKYFVK---KDTNRFDNYS--- 75
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEdrWDADGYYPDPGKPGKTYTRRGGFLDdvdAFDAAFFGISpre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 76 --------LYALYAAQEAVNHANLDVEALNRDRFGVIVASGiggikeiEDQVLRLHEKGPKRVKPMTLPKALPNMASGNV 147
Cdd:cd00833 81 aeamdpqqRLLLEVAWEALEDAGYSPESLAGSRTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLANRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 148 AMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSttedPTRASIPFDKDRN 227
Cdd:cd00833 154 SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----PDGRCRPFDADAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 228 GFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAY--HMTSPHPEGQgaIKAIKLALEEAEISPEQVAYVNAHGT 305
Cdd:cd00833 230 GYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYVEAHGT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 306 STPANEKGESGAIVAVLGKE------VPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIEANVVYG 379
Cdd:cd00833 308 GTPLGDPIEVEALAKVFGGSrsadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPL 387
|
410 420 430
....*....|....*....|....*....|.
gi 2038653373 380 QGLEKEIPY---------AISNtFGFGGHNA 401
Cdd:cd00833 388 RVPTEARPWpapagprraGVSS-FGFGGTNA 417
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
75-404 |
5.92e-59 |
|
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: 195.16 E-value: 5.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 75 SLYALYAAQEAVNHANLDVEALNRDRFGVIVASGIGGikeieDQVLRLHEKGPKRVKPMTLPKALPNMASGNVAMRFGAN 154
Cdd:cd00825 12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 155 GVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAgFQALTALSTtedPTRASIPFDKDRNGFVMGEG 234
Cdd:cd00825 87 GPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCE-FDAMGALST---PEKASRTFDAAADGFVFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 235 SGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGE 314
Cdd:cd00825 163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 315 SGAIVAVLG-KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDyiEANVVYGQGLEKEIPYAISNT 393
Cdd:cd00825 243 LKLLRSEFGdKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALLNG 320
|
330
....*....|.
gi 2038653373 394 FGFGGHNAVLA 404
Cdd:cd00825 321 FGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-246 |
1.48e-53 |
|
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: 178.60 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIGIGGI--TKFDHSDF-----------DVHNAAEIQDFPFDKYFVK---KD 67
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLFFGispRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 68 TNRFDNYSLYALYAAQEAVNHANLDVEALNRDRFGVIVASGIGgikEIEDQVLRLHEKGPKRVKPMTLPkALPNMASGNV 147
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIG---DYAALLLLDEDGGPRRGSPFAVG-TMPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 148 AMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALtALSTTEDPTRAsipFDKDRN 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAA-GMLSPDGPCKA---FDPFAD 232
|
250
....*....|....*....
gi 2038653373 228 GFVMGEGSGMLVLESLEHA 246
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
19-373 |
4.04e-42 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 158.50 E-value: 4.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 19 NTPEEFWNSLATGKIGIGGITK--FDHSDFDVHNAAEIqdfpfDKYFVK-----KDTNRFD----NYS-----------L 76
Cdd:COG3321 19 DDPEEFWRNLRAGRDAITEVPAdrWDADAYYDPDPDAP-----GKTYVRwggflDDVDEFDalffGISpreaeamdpqqR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 77 YALYAAQEAVNHANLDVEALNRDRFGVIVASGIGgikeieDQVLRLHEkGPKRVKPMTLPKALPNMASGNVAMRFGANGV 156
Cdd:COG3321 94 LLLEVAWEALEDAGYDPESLAGSRTGVFVGASSN------DYALLLLA-DPEAIDAYALTGNAKSVLAGRISYKLDLRGP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 157 CKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTTEDpTRAsipFDKDRNGFVMGEGSG 236
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGR-CRA---FDADADGYVRGEGVG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 237 MLVLESLEHAEKRGATILAeVV--------GYGNTcdayhMTSPHPEGQgaIKAIKLALEEAEISPEQVAYVNAHGTSTP 308
Cdd:COG3321 243 VVVLKRLSDALRDGDRIYA-VIrgsavnqdGRSNG-----LTAPNGPAQ--AAVIRRALADAGVDPATVDYVEAHGTGTP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038653373 309 AnekG---ESGAIVAVLGKE------VPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYIE 373
Cdd:COG3321 315 L---GdpiEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
254-364 |
1.50e-37 |
|
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: 132.31 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 254 LAEVVGYGNTCDAYHMTSPHPEGQGAIKAIKLALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVLGKE-----VPV 328
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2038653373 329 SSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAG 364
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
72-400 |
7.91e-34 |
|
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: 134.36 E-value: 7.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 72 DNYSLYALYAAQEAVNHANLDvEALNRDRFGVIVASGiGGIKEIEDQVLRLHEKGPKRV--------------------- 130
Cdd:TIGR02813 91 DISQLLSLVVAKEVLNDAGLP-DGYDRDKIGITLGVG-GGQKQSSSLNARLQYPVLKKVfkasgvededsemlikkfqdq 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 131 ----KPMTLPKALPNMASGNVAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQAL 206
Cdd:TIGR02813 169 yihwEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKT 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 207 TALSTTEDPTrasiPFDKDRNGFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMT--SPHPEGQGaiKAIK 284
Cdd:TIGR02813 249 PAFTTNEDIQ----PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQA--KALK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 285 LALEEAEISPEQVAYVNAHGTSTPANEKGESGAIVAVLGKE------VPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNF 358
Cdd:TIGR02813 323 RAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKV 402
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2038653373 359 VPMTAGTS------EVSD---YIEANVVYGQGLEKEIP-YAISNTFGFGGHN 400
Cdd:TIGR02813 403 LPPTINVDqpnpklDIENspfYLNTETRPWMQREDGTPrRAGISSFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
143-403 |
3.27e-30 |
|
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: 116.77 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 143 ASGNVAMRFG-ANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEAsitpfaiagfqaltalsttedptrasip 221
Cdd:cd00327 46 AAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 222 fdkdrngFVMGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDAYHMTsPHPEGQGAIKAIKLALEEAEISPEQVAYVN 301
Cdd:cd00327 98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 302 AHGTSTPANEKGESGAIVAVLG-KEVPVSSTKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTagtsevsdyieanvvyGQ 380
Cdd:cd00327 170 AHGTGTPIGDAVELALGLDPDGvRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------PR 233
|
250 260
....*....|....*....|...
gi 2038653373 381 GLEKeipyAISNTFGFGGHNAVL 403
Cdd:cd00327 234 EPRT----VLLLGFGLGGTNAAV 252
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
19-401 |
8.53e-21 |
|
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: 91.62 E-value: 8.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 19 NTPEEFWNSLATGkigIGGITKFDHSDFDVHNA-AEIQD-----FpfdkyfvkkdtnrfdnyslyaLYAAQEAVNHANLD 92
Cdd:smart00825 14 DDPEEFWDLLLAG---LDDVDLFDAAFFGISPReAEAMDpqqrlL---------------------LEVAWEALEDAGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 93 VEALNRDRFGVIVASGiggikeiedqvlrlhekgpkrvkpmtlpkalpnmaSGNVAMrfgangvckSINTACSSSNDAIG 172
Cdd:smart00825 70 PESLRGSRTGVFVGVS-----------------------------------SSDYSV---------TVDTACSSSLVALH 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 173 DAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSttedPTRASIPFDKDRNGFVMGEGSGMLVLESLEHAEKRGAT 252
Cdd:smart00825 106 LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 253 ILAEVVGYGNTCDAYH--MTSPHPEGQGAIkaiklaleeaeispeqvayvnahgtstpanekgesgaivavlgkevpvSS 330
Cdd:smart00825 182 ILAVIRGSAVNQDGRSngITAPSGPAQLLI------------------------------------------------GS 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 331 TKSFTGHLLGAAGAVEAIVTIEAMRHNFVPMTAGTSEVSDYI---EANVVYGQGL----EKEIPY--AISNtFGFGGHNA 401
Cdd:smart00825 214 VKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIdleESPLRVPTELtpwpPPGRPRraGVSS-FGFGGTNA 292
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
4-259 |
1.89e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 71.14 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 4 NRVVVTGYGVTSPIGNTPEEFWNSLATGKIG-IGGITKFdhSDFDVHNAAEIQdfpFDKYFVKK-DTNRFDNYSLYALYA 81
Cdd:PRK06519 6 NDVVITGIGLVSSLGEGLDAHWNALSAGRPQpNVDTETF--APYPVHPLPEID---WSQQIPKRgDQRQMETWQRLGTYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 82 AQEAVNHANL--DVEALnrDRFGVIVASGiGGIKEI-------------EDQVLRLHEKGPKRVKPmTLPKA-LPNMASG 145
Cdd:PRK06519 81 AGLALDDAGIkgNEELL--STMDMIVAAG-GGERDIavdtailnearkrNDRGVLLNERLMTELRP-TLFLAqLSNLLAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 146 NVAMRFGANGVCKSINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTTE-DPTRASIPFDK 224
Cdd:PRK06519 157 NISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGwAPVWSRGGEDG 236
|
250 260 270
....*....|....*....|....*....|....*
gi 2038653373 225 DrnGFVMGEGSGMLVLESLEHAEKRGATILAEVVG 259
Cdd:PRK06519 237 G--GFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
159-300 |
1.11e-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: 47.09 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 159 SINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTE---------------------------------------------- 192
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVEsmsrapyllpkarrggrlglntldgmlddgltdpftglsmgitaen 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 193 ---------------------------------ASITPFAIAGFQALTALSTTEDPtRASIPFDK--------DRNGFV- 230
Cdd:cd00751 159 vaekygisreeqdefalrshqraaaaqeagrfkDEIVPVEVPGRKGPVVVDRDEGP-RPDTTLEKlaklkpafKKDGTVt 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038653373 231 ------MGEGSGMLVLESLEHAEKRGATILAEVVGYGNT-CDAYHMtsphpeGQGAIKAIKLALEEAEISPEQVAYV 300
Cdd:cd00751 238 agnasgINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAgVDPAIM------GIGPVPAIPKALKRAGLTLDDIDLI 308
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
159-300 |
2.13e-05 |
|
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: 46.21 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 159 SINTACSSSNDAIGDAFRSIKFGFQDVMLVGGTE---------------------------------------------- 192
Cdd:COG0183 83 TVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVEsmsrapmllpkarwgyrmnaklvdpminpgltdpytglsmgetaen 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 193 ---------------------------------ASITPFAIAGFQALTALSTTEDP----TRASIP-----FDKDrnGFV 230
Cdd:COG0183 163 vaerygisreeqdafalrshqraaaaiaagrfdDEIVPVEVPDRKGEVVVDRDEGPrpdtTLEKLAklkpaFKKD--GTV 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038653373 231 -------MGEGSGMLVLESLEHAEKRGATILAEVVGYGNT-CDAYHMtsphpeGQGAIKAIKLALEEAEISPEQVAYV 300
Cdd:COG0183 241 tagnasgINDGAAALLLMSEEAAKELGLKPLARIVAYAVAgVDPEIM------GIGPVPATRKALARAGLTLDDIDLI 312
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
169-300 |
3.71e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 45.40 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 169 DAIGDAFRSIKFGFQDVMLVGGTEASITPFAIAGFQALTALSTTEDPtrasipfdkdrNGFVMGEGSGMLVLESLEHAEK 248
Cdd:PRK06147 138 VALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFIPGEAAAAVLLGRPAGGEA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2038653373 249 RGATILAevVGYGNTCDAYHMTSPHP-EGQGAIKAIKLALEEAEISPEQVAYV 300
Cdd:PRK06147 207 PGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
234-297 |
5.41e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 45.14 E-value: 5.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038653373 234 GSGMLVLESLEHAEKRGATILAEVVGYGNT-CDAYHMtsphpeGQGAIKAIKLALEEAEISPEQV 297
Cdd:PRK05790 253 GAAAVVVMSEAKAKELGLTPLARIVSYAVAgVDPAIM------GIGPVPAIRKALEKAGWSLADL 311
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
231-344 |
8.68e-04 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 41.23 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038653373 231 MGEGSGMLVLESLEHAEKRGATILAEVVGYGNTCDA--YHMTSPHpegqgaiKAIKLALEEAEISPEQVAY--VN-AHGT 305
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQApeLFTTAPA-------LAIPKALKHAGLEASQVDYyeINeAFSV 322
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2038653373 306 STPANEK--GESGAIVAVLGKEVPVsstksftGHLLGAAGA 344
Cdd:PLN02644 323 VALANQKllGLDPEKVNVHGGAVSL-------GHPIGCSGA 356
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
160-192 |
6.28e-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: 38.05 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|...
gi 2038653373 160 INTACSSSNDAIGDAFRSIKFGFQDVMLVGGTE 192
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVE 113
|
|
| |
