|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
42-456 |
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: 593.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRgphegqFNEENFVSKSDAKSMSSSTIM 121
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:cd00834 75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
|
410
....*....|....*.
gi 58037235 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
41-454 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 592.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVK------DFNPDDYMSRKEARRMDRFIQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 121 MAVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK07314 75 YGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALS-SNPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStRNDDPERASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 360 NRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390
|
410
....*....|....*
gi 58037235 440 GLTNSFGFGGTNATL 454
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
42-455 |
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: 588.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWhPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:TIGR03150 75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*
gi 58037235 441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
42-456 |
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: 575.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:COG0304 75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*.
gi 58037235 441 LTNSFGFGGTNATLCI 456
Cdd:COG0304 391 LSNSFGFGGHNASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
42-291 |
1.07e-57 |
|
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: 190.54 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKNIPCSVA--AYVPRGP--HEGQFNEENF-VSKSD 111
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGGldDIFDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 112 AKSMSSSTIMAVGAAELALKDSGWHPkREADQVATGVAIGMGMvplEVISETALLFQTKGYNKVSPFFVPKIlINMAAGQ 191
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 192 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNpDPklaCRPFHPER 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231
|
250 260
....*....|....*....|
gi 58037235 272 DGFVMGEGAAVLVLEEHEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
204-452 |
1.07e-30 |
|
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: 120.13 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 204 SVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGAAVL 283
Cdd:smart00825 92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 284 VLEEHEHAVQRGARIYAEILGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspeQisyvnahatstplgdaaenr 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 362 aikrlfrdhacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQEWKAEG- 436
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGr 276
|
250
....*....|....*..
gi 58037235 437 -RCIGLtNSFGFGGTNA 452
Cdd:smart00825 277 pRRAGV-SSFGFGGTNA 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
42-456 |
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: 593.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPRgphegqFNEENFVSKSDAKSMSSSTIM 121
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:cd00834 75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
|
410
....*....|....*.
gi 58037235 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
41-454 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 592.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVK------DFNPDDYMSRKEARRMDRFIQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 121 MAVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK07314 75 YGIAAAKQAVEDAGLEIT-EENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALS-SNPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALStRNDDPERASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 360 NRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07314 314 TQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---Y 390
|
410
....*....|....*
gi 58037235 440 GLTNSFGFGGTNATL 454
Cdd:PRK07314 391 ALSNSFGFGGTNASL 405
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
42-455 |
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: 588.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWhPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:TIGR03150 75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*
gi 58037235 441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
42-456 |
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: 575.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:COG0304 75 ALAAAREALADAGLDLD-EVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*.
gi 58037235 441 LTNSFGFGGTNATLCI 456
Cdd:COG0304 391 LSNSFGFGGHNASLVF 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
42-454 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 523.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK--------------NIPCSVAAYVPRGPHEGQFNEENFV 107
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 108 SksdAKSMSSSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINM 187
Cdd:PLN02836 86 N---SRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 188 AAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACR 265
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 266 PFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYV 345
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 346 NAHATSTPLGDAAENRAIKRLFRDHAC--ALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN 423
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402
|
410 420 430
....*....|....*....|....*....|.
gi 58037235 424 YVPLESQewKAEGRCIGLTNSFGFGGTNATL 454
Cdd:PLN02836 403 FVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
39-454 |
5.23e-175 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 497.21 E-value: 5.23e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 39 MLRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVP--RGPHEGQFNEENFVSKSDAKSMS 116
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlAEDAEAGFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 117 SSTIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRY 196
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 197 KLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGF 274
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 275 VMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPL 354
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 355 GDAAENRAIKRLFrDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFD-LNYVPLESQEWK 433
Cdd:PRK06333 321 GDLGEVAAIKKVF-GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|.
gi 58037235 434 AEgrcIGLTNSFGFGGTNATL 454
Cdd:PRK06333 400 MD---YALSNGFGFGGVNASI 417
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
51-454 |
5.62e-168 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 479.19 E-value: 5.62e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 51 LVTPLGVGTQLVWDRLLRGESGIVSVVGDEYK----------------NIPCSVAAYVPrgphegqfnEENFVSKSDAKS 114
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVD---------QSEFDPSDFAPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 115 MSSS--TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQV 192
Cdd:PTZ00050 72 KRESraTHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 193 SIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPE 270
Cdd:PTZ00050 152 AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 271 RDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAG-VSPEQISYVNAHA 349
Cdd:PTZ00050 232 RAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 350 TSTPLGDAAENRAIKRLFRDHAC-ALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPlE 428
Cdd:PTZ00050 312 TSTPIGDKIELKAIKKVFGDSGApKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQ-G 390
|
410 420
....*....|....*....|....*.
gi 58037235 429 SQEWKAEGRCIGLTNSFGFGGTNATL 454
Cdd:PTZ00050 391 KTAHPLQSIDAVLSTSFGFGGVNTAL 416
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
39-454 |
3.73e-131 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 385.13 E-value: 3.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 39 MLRRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSS 118
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 119 TIMAVGAAELALKDSGWHPKREaDQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKL 198
Cdd:PRK08722 75 IQYGIAAGIQALDDSGLEVTEE-NAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMG 277
Cdd:PRK08722 154 RGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 278 EGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:PRK08722 234 DGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 358 AENRAIKR-LFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQewKAEG 436
Cdd:PRK08722 314 AEIKGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVES 391
|
410
....*....|....*...
gi 58037235 437 RCIGLTNSFGFGGTNATL 454
Cdd:PRK08722 392 MEYAICNSFGFGGTNGSL 409
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
42-451 |
4.75e-122 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 361.74 E-value: 4.75e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTIM 121
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKrEADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:PRK08439 76 GLKAAREAMKDAGFLPE-ELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEGA 280
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPegEGALRCMAAAVKDAGVSPeqISYVNAHATSTPLGDAAEN 360
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 361 RAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcIG 440
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387
|
410
....*....|.
gi 58037235 441 LTNSFGFGGTN 451
Cdd:PRK08439 388 MSNSFGFGGTN 398
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
41-457 |
7.84e-97 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 301.51 E-value: 7.84e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 41 RRRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIK------SFSTDGWVAPKLSKRMDKFML 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 121 MAVGAAELALKDSGWHPK--READQVATGVAIGMGMVPLEVISEtALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKL 198
Cdd:PLN02787 202 YLLTAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGW 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMG 277
Cdd:PLN02787 281 MGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 278 EGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:PLN02787 361 EGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDL 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 358 AENRAIKRLFRDHAcALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNyVPLESQEWKAEGR 437
Cdd:PLN02787 441 KEYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLDIK 518
|
410 420
....*....|....*....|
gi 58037235 438 cIGLTNSFGFGGTNATLCIA 457
Cdd:PLN02787 519 -VALSNSFGFGGHNSSILFA 537
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
136-456 |
7.43e-95 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 289.71 E-value: 7.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 136 HPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHA 215
Cdd:PRK14691 18 HADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 216 VGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGFVMGEGAAVLVLEEHEHAVQ 293
Cdd:PRK14691 98 IGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 294 RGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDhACA 373
Cdd:PRK14691 178 RGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 374 LAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFD-LNYVPLESQewkAEGRCIGLTNSFGFGGTNA 452
Cdd:PRK14691 257 LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---PHDMTYALSNGFGFAGVNA 333
|
....
gi 58037235 453 TLCI 456
Cdd:PRK14691 334 SILL 337
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
42-456 |
1.44e-89 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 278.41 E-value: 1.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVG-DEYKNIPCSVAAYVPrgphegQFNEENFVSKSDAKSMSSSTI 120
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 121 MAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKG 200
Cdd:PRK09116 76 MATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSS-NPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGalRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK09116 235 AGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 360 NRAIKRLFRDHacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEF-DLNYVPLESQEWKAEgrc 438
Cdd:PRK09116 313 SQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTE--- 386
|
410
....*....|....*...
gi 58037235 439 IGLTNSFGFGGTNATLCI 456
Cdd:PRK09116 387 YVMSNNFAFGGINTSLIF 404
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
44-454 |
3.65e-89 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 277.77 E-value: 3.65e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 44 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD--EYKNIPCSVAAYVPRGPHEGQFNEENfvsksdaKSMSSSTIM 121
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPfvEEFDLPVRIGGHLLEEFDHQLTRVEL-------RRMSYLQRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGwhpKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGP 201
Cdd:PRK07910 87 STVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 202 NHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS--NPDPKLACRPFHPERDGFVMGEG 279
Cdd:PRK07910 164 VITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMStnNDDPAGACRPFDKDRDGFVFGEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 280 AAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAE 359
Cdd:PRK07910 244 GALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 360 NRAIKRLFRDHACalAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWKAEgrcI 439
Cdd:PRK07910 324 GKAINNALGGHRP--AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYR---Y 398
|
410
....*....|....*
gi 58037235 440 GLTNSFGFGGTNATL 454
Cdd:PRK07910 399 AINNSFGFGGHNVAL 413
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
42-454 |
1.24e-86 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 270.77 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVsvVGDEYKNI--PCSVAAYVprgphegQFNEENFVSKSDAKSMSSST 119
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVWGNV-------KLDPTGLIDRKVMRFMGDAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 120 IMAVGAAELALKDSGWhpkrEADQVA---TGVAIGMGMVPLEVISETA-LLFQTKGYNKVSPFFVPKILINMAAGQVSIR 195
Cdd:PRK07967 73 AYAYLAMEQAIADAGL----SEEQVSnprTGLIAGSGGGSTRNQVEAAdAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAgFSRARALSS--NPDPKLACRPFHPERDG 273
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITApdPEGEGALRCMAAAVkdAGVSPEqISYVNAHATSTP 353
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVDTP-IDYINTHGTSTP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 354 LGDAAENRAIKRLFRDHACalAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEF-DLNYV--PLESQ 430
Cdd:PRK07967 303 VGDVKELGAIREVFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVteTTDNA 380
|
410 420
....*....|....*....|....
gi 58037235 431 EWKAEgrcigLTNSFGFGGTNATL 454
Cdd:PRK07967 381 ELTTV-----MSNSFGFGGTNATL 399
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
43-458 |
1.90e-82 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 259.21 E-value: 1.90e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 43 RVVITGIGLVTPLGVGTQlVWDRLLRGESGIVSVvgDEYKNIPCSVAAYVPRGPhegqfneenfvsksdaKSMSSSTIMA 122
Cdd:PRK05952 3 KVVVTGIGLVSALGDLEQ-SWQRLLQGKSGIKLH--QPFPELPPLPLGLIGNQP----------------SSLEDLTKTV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 123 VGAAelaLKDSGWHPKrEADqvaTGVAIGMG---------MVPLEVISETALLFQTKGYNKVSpffvpkILINMAAGQVS 193
Cdd:PRK05952 64 VTAA---LKDAGLTPP-LTD---CGVVIGSSrgcqgqwekLARQMYQGDDSPDEELDLENWLD------TLPHQAAIAAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 194 IRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnpdpKLACRPFHPERDG 273
Cdd:PRK05952 131 RQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQREG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTP 353
Cdd:PRK05952 206 LVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 354 LGDAAENRAIKRLFrdhACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctEPEFDLNYV------PL 427
Cdd:PRK05952 286 LNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVrqaqqsPL 360
|
410 420 430
....*....|....*....|....*....|.
gi 58037235 428 ESqewkaegrciGLTNSFGFGGTNATLCIAG 458
Cdd:PRK05952 361 QN----------VLCLSFGFGGQNAAIALGK 381
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
44-458 |
1.17e-81 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 258.41 E-value: 1.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 44 VVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVprgphegqfneeNFVSKSDAKSMSSSTIMAV 123
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFLPESPFGASALSEALAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 124 GAAELALKDSG--------------------WHPKREADQVAtgvaigmgmvPLEVISETALLFQTKGYNKVSPFFvPKI 183
Cdd:PRK06501 81 LAAEEALAQAGigkgdfpgplflaappveleWPARFALAAAV----------GDNDAPSYDRLLRAARGGRFDALH-ERF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 184 LINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPD-PKL 262
Cdd:PRK06501 150 QFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDpPEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 263 ACRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQI 342
Cdd:PRK06501 230 ASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 343 SYVNAHATSTPLGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDL 422
Cdd:PRK06501 310 DYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPL 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 58037235 423 NYVPLESQEwkAEGRCIgLTNSFGFGGTNATLCIAG 458
Cdd:PRK06501 390 DVVPNVARD--ARVTAV-LSNSFGFGGQNASLVLTA 422
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
42-454 |
3.23e-79 |
|
"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: 251.59 E-value: 3.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLV---WDRLLRGESGIvSVVGDEYKNIPCSVAAYVPRGPHEGQFNEENFVsksdaksMSSS 118
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGI-APVARLKSRFDRGVAGQIPTGDIPGWDAKRTGI-------VDRT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 119 TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMvplevISETALLFQTKG-YNKVSPFFVPK--ILINMAAGQVSIR 195
Cdd:cd00828 73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGM-----GGLRFLRRGGKLdARAVNPYVSPKwmLSPNTVAGWVNIL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 196 YKLK-GPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSSNPD-PKLACRPFHPERDG 273
Cdd:cd00828 148 LLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 274 FVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPeGEGALRCMAAAVKDAGVSPEQISYVNAHATSTP 353
Cdd:cd00828 227 FVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 354 LGDAAENRAIKRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVPLESQEWK 433
Cdd:cd00828 306 ANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLN 385
|
410 420
....*....|....*....|.
gi 58037235 434 AEGRCiGLTNSFGFGGTNATL 454
Cdd:cd00828 386 LKVRA-ALVNAFGFGGSNAAL 405
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
198-454 |
3.86e-74 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 237.82 E-value: 3.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 198 LKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSSNPdpklaCRPFHPERDGFVMG 277
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQP-----CRPFSANRDGINIG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 278 EGAAVLVLE-EHEHAVQrgariyaeILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGD 356
Cdd:PRK09185 223 EAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 357 AAENRAIKRLFRDHacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVpLESQEwKAEG 436
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYL-VENAQ-ALAI 369
|
250
....*....|....*...
gi 58037235 437 RCIgLTNSFGFGGTNATL 454
Cdd:PRK09185 370 RYV-LSNSFAFGGNNCSL 386
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
43-452 |
1.85e-73 |
|
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: 237.07 E-value: 1.85e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 43 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYknipcSVAAYVPRG--PHEGQFNEENFVSKSDAKSMSSSTI 120
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRW-----DADGYYPDPgkPGKTYTRRGGFLDDVDAFDAAFFGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 121 MAVGAAEL-------------ALKDSGWHPKREADQvATGVAIGMGMvpleviSETALLfQTKGYNKVSPFFVPKILINM 187
Cdd:cd00833 77 SPREAEAMdpqqrlllevaweALEDAGYSPESLAGS-RTGVFVGASS------SDYLEL-LARDPDEIDAYAATGTSRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 188 AAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPF 267
Cdd:cd00833 149 LANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS--PDGR--CRPF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 268 HPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLS--GDAGHITAPDPEGEGALrcMAAAVKDAGVSPEQISYV 345
Cdd:cd00833 225 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 346 NAHATSTPLGDAAENRAIKRLF---RDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDL 422
Cdd:cd00833 303 EAHGTGTPLGDPIEVEALAKVFggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDF 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 58037235 423 N----YVPLESQEWKAEG--RCIGLtNSFGFGGTNA 452
Cdd:cd00833 383 EesplRVPTEARPWPAPAgpRRAGV-SSFGFGGTNA 417
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
43-457 |
4.08e-61 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 204.49 E-value: 4.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 43 RVVITGIGLVTPLGVGTQLVWDRLLRGESGIvSVVGDEYKNIPCSVAAYVPRGPHEGQFNE---ENFVSKSDAKSMSSST 119
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAF-GVMRRPGRQVPDDAGAGLASAFIGAELDSlalPERLDAKLLRRASLSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 120 IMAVGAAELALKDSGWHPkreADQVATGVAIGMGMVPLEvisETALLFQTkgYNKVSPFFVPK-ILINM---AAGQVSIR 195
Cdd:PRK07103 82 QAALAAAREAWRDAALGP---VDPDRIGLVVGGSNLQQR---EQALVHET--YRDRPAFLRPSyGLSFMdtdLVGLCSEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNP---DPKLACRPFHPERD 272
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfadEPEAACRPFDQDRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 273 GFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEgaLRCMAAAVKDAGVSPEQISYVNAHATST 352
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 353 PLGDAAENRAIKrlfrdhACALA---ISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctEP-EFDLNYVPLE 428
Cdd:PRK07103 312 PLGDETELAALF------ASGLAhawINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD--EPiDERFRWVGST 383
|
410 420
....*....|....*....|....*....
gi 58037235 429 SQEWKAEgrcIGLTNSFGFGGTNATLCIA 457
Cdd:PRK07103 384 AESARIR---YALSLSFGFGGINTALVLE 409
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
42-291 |
1.07e-57 |
|
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: 190.54 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGD-----EYKNIPCSVA--AYVPRGP--HEGQFNEENF-VSKSD 111
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGGldDIFDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 112 AKSMSSSTIMAVGAAELALKDSGWHPkREADQVATGVAIGMGMvplEVISETALLFQTKGYNKVSPFFVPKIlINMAAGQ 191
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 192 VSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNpDPklaCRPFHPER 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231
|
250 260
....*....|....*....|
gi 58037235 272 DGFVMGEGAAVLVLEEHEHA 291
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
119-454 |
2.15e-57 |
|
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: 192.47 E-value: 2.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 119 TIMAVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLFQTKGYNKVSPFFVPkilinmAAGQVSIRYKL 198
Cdd:cd00825 12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 199 KGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnpdPKLACRPFHPERDGFVMGE 278
Cdd:cd00825 86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 279 GAAVLVLEEHEHAVQRGARIYAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAA 358
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 359 ENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDctepEFDLNYVPLESQEWKAEGRC 438
Cdd:cd00825 242 ELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIE----ELDEAGLNIVTETTPRELRT 315
|
330
....*....|....*.
gi 58037235 439 iGLTNSFGFGGTNATL 454
Cdd:cd00825 316 -ALLNGFGLGGTNATL 330
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
129-452 |
8.98e-56 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 200.10 E-value: 8.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 129 ALKDSGWHPKREADQvATGVAIGMGMvplevisETALLFQTKGYNKVSPFFVPKILINMAAGQVSIRYKLKGPNHSVSTA 208
Cdd:COG3321 102 ALEDAGYDPESLAGS-RTGVFVGASS-------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 209 CTTGAHAVgdsfrfiaH--------GDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGA 280
Cdd:COG3321 174 CSSSLVAV--------HlacqslrsGECDLALAGGVNLMLTPESFILFSKGGMLS--PDGR--CRAFDADADGYVRGEGV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 281 AVLVLEEHEHAVQRGARIYAEILGYGLSGDaGH---ITAPDPEGEGALrcMAAAVKDAGVSPEQISYVNAHATSTPLGDA 357
Cdd:COG3321 242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 358 AENRAIKRLFRDHACA---LAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQ 430
Cdd:COG3321 319 IEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELR 398
|
330 340
....*....|....*....|....
gi 58037235 431 EWKAEG--RCIGLtNSFGFGGTNA 452
Cdd:COG3321 399 PWPAGGgpRRAGV-SSFGFGGTNA 421
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
42-454 |
1.30e-54 |
|
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: 187.18 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVGTQLVWDRLLRGESGIVSVVGDEYKNIPCSVAAYVPrGPHEGQFNEENFVSKSDaksmsSSTIM 121
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTD-----RMTRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKREADQ---VATGVAIG---MGMVPLEvisetALLfqTKGYNKVSPFFVPKILINMAAGQVSIR 195
Cdd:cd00832 75 ALAAADWALADAGVDPAALPPYdmgVVTASAAGgfeFGQRELQ-----KLW--SKGPRHVSAYQSFAWFYAVNTGQISIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 196 YKLKGPNHSVSTACTTGAHAVGDSFRFIAHGdADVMVAGGTDSCISPLSLAGFSRARALSSNPDPKLACRPFHPERDGFV 275
Cdd:cd00832 148 HGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 276 MGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDaghitaPDP---EGEGALRCMAAAVKDAGVSPEQISYVNAHATST 352
Cdd:cd00832 227 PGEGGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 353 PLGDAAENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLNYVplesqew 432
Cdd:cd00832 301 PELDRAEAAALAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV------- 371
|
410 420
....*....|....*....|....*.
gi 58037235 433 KAEGRCIGLTNSF----GFGGTNATL 454
Cdd:cd00832 372 TGRPRPAALRTALvlarGRGGFNSAL 397
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
299-414 |
1.10e-47 |
|
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: 159.66 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 299 YAEILGYGLSGDAGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVNAHATSTPLGDAAENRAIKRLFRDHAC--ALAI 376
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 58037235 377 SSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLD 414
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
181-451 |
2.43e-37 |
|
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: 145.92 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 181 PKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDp 260
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 261 klaCRPFHPERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDA--GHITAPDPEGEGalRCMAAAVKDAGVS 338
Cdd:TIGR02813 257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 339 PEQISYVNAHATSTPLGDAAENRAIKRLF---RDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDC 415
Cdd:TIGR02813 332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 58037235 416 TEPEFDLNYVPL----ESQEWKAEG----RCIGLTnSFGFGGTN 451
Cdd:TIGR02813 412 PNPKLDIENSPFylntETRPWMQREdgtpRRAGIS-SFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
188-456 |
2.42e-33 |
|
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: 126.40 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 188 AAGQVSIRYKLK-GPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCisplslagfsraralssnpdpklacrp 266
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 267 fhperdgfVMGEGAAVLVLEEHEHAVQRGARIYAEILGYGLSGDaGHITAPDPEGEGALRCMAAAVKDAGVSPEQISYVN 346
Cdd:cd00327 99 --------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 347 AHATSTPLGDAAENRAIKRLFRDHacALAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTlnldctepefdlnyvp 426
Cdd:cd00327 170 AHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT---------------- 231
|
250 260 270
....*....|....*....|....*....|
gi 58037235 427 lesqewKAEGRCiGLTNSFGFGGTNATLCI 456
Cdd:cd00327 232 ------PREPRT-VLLLGFGLGGTNAAVVL 254
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
204-452 |
1.07e-30 |
|
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: 120.13 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 204 SVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSsnPDPKlaCRPFHPERDGFVMGEGAAVL 283
Cdd:smart00825 92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVGVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 284 VLEEHEHAVQRGARIYAEILGYGL--SGDAGHITAPDPEGegalrcmaaavkdagvspeQisyvnahatstplgdaaenr 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA-------------------Q-------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 362 aikrlfrdhacaLAISSTKGATGHLLGAAGAVEATFTALACYHQKLPPTLNLDCTEPEFDLN----YVPLESQEWKAEG- 436
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGr 276
|
250
....*....|....*..
gi 58037235 437 -RCIGLtNSFGFGGTNA 452
Cdd:smart00825 277 pRRAGV-SSFGFGGTNA 292
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
38-412 |
1.70e-15 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 78.07 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 38 AMLRRRVVITGIGLVTPLGVGTQLVWDRLlrgESGIVSVVGDEYKNIPCSV--------AAYVPRgphegqfneenfvsK 109
Cdd:PRK06519 2 RMQPNDVVITGIGLVSSLGEGLDAHWNAL---SAGRPQPNVDTETFAPYPVhplpeidwSQQIPK--------------R 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 110 SDAKSMSSSTIMAVGAAELALKDSGWhpKREADQVATG---VAIGMGMVPLEVIS----------ETALLFQTKGYNKVS 176
Cdd:PRK06519 65 GDQRQMETWQRLGTYAAGLALDDAGI--KGNEELLSTMdmiVAAGGGERDIAVDTailnearkrnDRGVLLNERLMTELR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 177 PFFVPKILINMAAGQVSIRYKLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSS 256
Cdd:PRK06519 143 PTLFLAQLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 257 NPdpklacrpFHP-------ERDGFVMGEGAAVLVLEEHEHAVQRGARIYAEIlgyglSGDAGHITAPDPegeGAL-RCM 328
Cdd:PRK06519 223 GG--------WAPvwsrggeDGGGFILGSGGAFLVLESREHAEARGARPYARI-----SGVESDRARRAP---GDLeASL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 329 AAAVKDAGVSPEQiSYVNAHATSTPLGDAAEnraikRLFRDHACALAISSTKGATGHLLGAAGAVEATFTALACYHQKLP 408
Cdd:PRK06519 287 ERLLKPAGGLAAP-TAVISGATGAHPATAEE-----KAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALF 360
|
....
gi 58037235 409 PTLN 412
Cdd:PRK06519 361 PPFD 364
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
42-345 |
5.24e-09 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 57.72 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 42 RRVVITGIGLVTPLGVgtqlvwdrllrgesgivsvvgdeykNIPCSVAAYvpRGpHEGQFNEENFVSKSDAKsmssstim 121
Cdd:PRK06147 3 RALAIVGSGMVTAVGL-------------------------DAPSSCAAI--RA-RLDNFQETRFIDPPGGE-------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 122 AVGAAELALKDSGWHPKREADQVATGVAIGMGMVPLEVISETALLfqtkgyNKVSPFFVPKILINMAAG-----QVSIRY 196
Cdd:PRK06147 47 WLIGAPVPLPPPWRGPERLAEMAAPAIAEALEGLPALDASEAPLL------LCVAEEERPGRPPDLEERllrelEARLGL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 197 KLKGPNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSSNPDPklacrpfhperDGFVM 276
Cdd:PRK06147 121 RLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFIP 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037235 277 GEGAAVLVLEEHEHAVQRGARIYAeiLGYGL--SGDAGHITAPdPEGEGALRCMAAAVKDAGVSPEQISYV 345
Cdd:PRK06147 190 GEAAAAVLLGRPAGGEAPGLPLLG--LGLGRepAPVGESEDLP-LRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
201-280 |
5.60e-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: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScispLSLAGFSRARALSSNP-DPKLACRPFHPE----RDGFV 275
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVES----MSRAPMLLPKARWGYRmNAKLVDPMINPGltdpYTGLS 155
|
....*
gi 58037235 276 MGEGA 280
Cdd:COG0183 156 MGETA 160
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
201-280 |
2.56e-03 |
|
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: 39.77 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037235 201 PNHSVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScIS--PLSLAGFSRARALSSNPDPKLACRPFHPERDGFVMGE 278
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVES-MSraPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGI 154
|
..
gi 58037235 279 GA 280
Cdd:cd00751 155 TA 156
|
|
| |
