|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 588.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150 75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*
gi 8923559 441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
|
|
| 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: 587.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834 75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
|
410
....*....|....*.
gi 8923559 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
42-454 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 585.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK07314 76 GIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK07314 315 QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---YA 391
|
410
....*....|....
gi 8923559 441 LTNSFGFGGTNATL 454
Cdd:PRK07314 392 LSNSFGFGGTNASL 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: 576.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304 75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*.
gi 8923559 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 |
5.45e-56 |
|
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: 186.30 E-value: 5.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGE-----EYKSIPCSVA--AYVPRG--SDEGQFNEQNF-VSKSD 111
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGglDDIFDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 112 IKSMSSPTIMAIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMiplEVVSETALNFQTKGYNKVSPFFVPKIlVNMAAGQ 191
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsDPklaCRPFHPKR 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231
|
250 260
....*....|....*....|
gi 8923559 272 DGFVMGEGAAVLVLEEYEHA 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 |
1.77e-27 |
|
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: 111.27 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 204 AVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSdpklACRPFHPKRDGFVMGEGAAVL 283
Cdd:smart00825 92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 284 VLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstplgdaaenk 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q----------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 362 aikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE 435
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274
|
250
....*....|....*....
gi 8923559 436 --KRFIGLtNSFGFGGTNA 452
Cdd:smart00825 275 grPRRAGV-SSFGFGGTNA 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 588.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVK------DFDPEDYIDKKEARRMDRFIQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWhPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:TIGR03150 75 ALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*
gi 8923559 441 LTNSFGFGGTNATLC 455
Cdd:TIGR03150 391 LSNSFGFGGTNASLV 405
|
|
| 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: 587.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPD------FDPEDYLDRKELRRMDRFAQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:cd00834 75 ALAAAEEALADAGLDPEEL-DPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:cd00834 154 NYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:cd00834 234 GVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:cd00834 314 KAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR---YA 390
|
410
....*....|....*.
gi 8923559 441 LTNSFGFGGTNATLCI 456
Cdd:cd00834 391 LSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
42-454 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 585.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRgsdegqFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKD------FNPDDYMSRKEARRMDRFIQY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK07314 76 GIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK07314 315 QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID---YA 391
|
410
....*....|....
gi 8923559 441 LTNSFGFGGTNATL 454
Cdd:PRK07314 392 LSNSFGFGGTNASL 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: 576.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVK------DFDPEEYLDRKELRRMDRFTQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:COG0304 75 ALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:COG0304 234 GVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:COG0304 314 KAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID---YA 390
|
410
....*....|....*.
gi 8923559 441 LTNSFGFGGTNATLCI 456
Cdd:COG0304 391 LSNSFGFGGHNASLVF 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
41-454 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 532.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK--------------SIPCSVAAYVPRGSDEGQFNEQNF 106
Cdd:PLN02836 5 TRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKmksedeetqlytldQLPSRVAALVPRGTGPGDFDEELW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 107 VSKsdiKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVN 186
Cdd:PLN02836 85 LNS---RSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 187 MAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLAC 264
Cdd:PLN02836 162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 265 RPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISY 344
Cdd:PLN02836 242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 345 INAHATSTPLGDAAENKAIKHLFKDHAY--ALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDL 422
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD 401
|
410 420 430
....*....|....*....|....*....|..
gi 8923559 423 NYVPLKAQewKTEKRFIGLTNSFGFGGTNATL 454
Cdd:PLN02836 402 GFVPLTAS--KAMLIRAALSNSFGFGGTNASL 431
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
41-454 |
3.41e-176 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 499.91 E-value: 3.41e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 41 HRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSD--EGQFNEQNFVSKSDIKSMSSP 118
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDLAEdaEAGFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKL 198
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 199 KGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKRDGFVM 276
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGFVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 277 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 357 AAENKAIKHLFKdHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQEWKTE 435
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401
|
410
....*....|....*....
gi 8923559 436 krfIGLTNSFGFGGTNATL 454
Cdd:PRK06333 402 ---YALSNGFGFGGVNASI 417
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
51-454 |
5.87e-170 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 484.20 E-value: 5.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 51 LVTPLGVGTHLVWDRLIGGESGIVSLVGEEYK----------------SIPCSVAAYVPrgsdegqfNEQNFVSKSDIKS 114
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkalenlvaAMPCQIAAEVD--------QSEFDPSDFAPTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 115 MSSPTI-MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVS 193
Cdd:PTZ00050 73 RESRAThFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 194 IRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKR 271
Cdd:PTZ00050 153 IKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 272 DGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAG-VQPEEISYINAHAT 350
Cdd:PTZ00050 233 AGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHAT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 351 STPLGDAAENKAIKHLFKDH-AYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKA 429
Cdd:PTZ00050 313 STPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKT 392
|
410 420
....*....|....*....|....*
gi 8923559 430 QEWKTEKRfIGLTNSFGFGGTNATL 454
Cdd:PTZ00050 393 AHPLQSID-AVLSTSFGFGGVNTAL 416
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
42-454 |
7.92e-127 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 374.34 E-value: 7.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVK------DFNCEEYMSKKDARKMDLFIQY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08722 78 GIAAGIQALDDSGLE-VTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK08722 157 NIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAEN 360
Cdd:PRK08722 237 GMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKH-LFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQewKTEKRFI 439
Cdd:PRK08722 317 KGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KVESMEY 394
|
410
....*....|....*
gi 8923559 440 GLTNSFGFGGTNATL 454
Cdd:PRK08722 395 AICNSFGFGGTNGSL 409
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
42-451 |
2.15e-124 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 367.52 E-value: 2.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTIM 121
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEIT------DFDPTEVMDPKEVKKADRFIQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGP 201
Cdd:PRK08439 76 GLKAAREAMKDAGFLP-EELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 202 NHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEGA 280
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPegEGALRCMAAALKDAGVqpEEISYINAHATSTPLGDAAEN 360
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGN--PKIDYINAHGTSTPYNDKNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 361 KAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEkrfIG 440
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN---VV 387
|
410
....*....|.
gi 8923559 441 LTNSFGFGGTN 451
Cdd:PRK08439 388 MSNSFGFGGTN 398
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
136-456 |
1.17e-96 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 294.33 E-value: 1.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 136 HPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHA 215
Cdd:PRK14691 18 HADNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 216 VGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST--NSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQ 293
Cdd:PRK14691 98 IGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 294 RRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDhAYA 373
Cdd:PRK14691 178 RGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 374 LAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQewkTEKRFIGLTNSFGFGGTNA 452
Cdd:PRK14691 257 LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---PHDMTYALSNGFGFAGVNA 333
|
....
gi 8923559 453 TLCI 456
Cdd:PRK14691 334 SILL 337
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
42-457 |
2.99e-96 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 299.97 E-value: 2.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGqfneqnFVSKSDIKSMSSPTIM 121
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDG------WVAPKLSKRMDKFMLY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPQ--SEADQVATGVAIGMGMIPLEVVSEtALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLK 199
Cdd:PLN02787 203 LLTAGKKALADGGITEDvmKELDKTKCGVLIGSAMGGMKVFND-AIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWM 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 200 GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGE 278
Cdd:PLN02787 282 GPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:PLN02787 362 GAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLK 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 359 ENKAIKHLFKDHAyALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNyVPLKAQEWKTEKRf 438
Cdd:PLN02787 442 EYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLDIK- 518
|
410
....*....|....*....
gi 8923559 439 IGLTNSFGFGGTNATLCIA 457
Cdd:PLN02787 519 VALSNSFGFGGHNSSILFA 537
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
44-454 |
1.11e-90 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 281.62 E-value: 1.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSL---VGEEYkSIPCSVAAYVPRGSDEGqfneqnfVSKSDIKSMSSPTI 120
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLddpFVEEF-DLPVRIGGHLLEEFDHQ-------LTRVELRRMSYLQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAIGAAELAMKDSGwhpQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK07910 86 MSTVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 201 PNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARA-LST-NSDPKLACRPFHPKRDGFVMGE 278
Cdd:PRK07910 163 GVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTnNDDPAGACRPFDKDRDGFVFGE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:PRK07910 243 GGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 359 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVplkAQEWKTEKRF 438
Cdd:PRK07910 323 EGKAINNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV---AGEPRPGNYR 397
|
410
....*....|....*.
gi 8923559 439 IGLTNSFGFGGTNATL 454
Cdd:PRK07910 398 YAINNSFGFGGHNVAL 413
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
42-456 |
6.20e-88 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 274.17 E-value: 6.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVG-EEYKSIPCSVAAYVPrgsdegQFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEwDRYDGLNTRLAAPID------DFELPAHYTRKKIRSMGRVSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKG 200
Cdd:PRK09116 76 MATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 201 PNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALST-NSDPKLACRPFHPKRDGFVMGEG 279
Cdd:PRK09116 156 RVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 280 AAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTPLGDAAE 359
Cdd:PRK09116 235 AGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 360 NKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYvpLKAQEWKTEKRF 438
Cdd:PRK09116 313 SQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDY--IMGEAREIDTEY 387
|
410
....*....|....*...
gi 8923559 439 IgLTNSFGFGGTNATLCI 456
Cdd:PRK09116 388 V-MSNNFAFGGINTSLIF 404
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
43-458 |
3.99e-86 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 268.84 E-value: 3.99e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 43 RVVITGIGLVTPLGvGTHLVWDRLIGGESGIvSLVG--EEYKSIPCSVAAYVPrgsdegqfneqnfvskSDIKSMSSPTI 120
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI-KLHQpfPELPPLPLGLIGNQP----------------SSLEDLTKTVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAigaaelAMKDSGWHPqSEADqvaTGVAIGMG---------MIPLEVVSETALNFQTKGYNKVSpffvpkILVNMAAGQ 191
Cdd:PRK05952 65 TA------ALKDAGLTP-PLTD---CGVVIGSSrgcqgqwekLARQMYQGDDSPDEELDLENWLD------TLPHQAAIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdpKLACRPFHPKR 271
Cdd:PRK05952 129 AARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 272 DGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATS 351
Cdd:PRK05952 204 EGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 352 TPLGDAAENKAIKHLFkdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLdcSEPEFDLNYVpLKAQE 431
Cdd:PRK05952 284 TRLNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNFV-RQAQQ 357
|
410 420
....*....|....*....|....*..
gi 8923559 432 WKTEKrfiGLTNSFGFGGTNATLCIAG 458
Cdd:PRK05952 358 SPLQN---VLCLSFGFGGQNAAIALGK 381
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
42-454 |
4.82e-83 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 261.53 E-value: 4.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVslVGEEYKSI--PCSVAAYVprgsdegQFNEQNFVSKSDIKSMSSPT 119
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMgmRSQVWGNV-------KLDPTGLIDRKVMRFMGDAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 120 IMAIGAAELAMKDSGWhpqsEADQVA---TGVAIGMG-MIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIR 195
Cdd:PRK07967 73 AYAYLAMEQAIADAGL----SEEQVSnprTGLIAGSGgGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 196 YKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAgFSRARALST--NSDPKLACRPFHPKRDG 273
Cdd:PRK07967 149 FKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 274 FVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITApdPEGEGALRCMAAALkdAGVQpEEISYINAHATSTP 353
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 354 LGDAAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYVPLKAQEW 432
Cdd:PRK07967 303 VGDVKELGAIREVFGDK--SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNA 380
|
410 420
....*....|....*....|..
gi 8923559 433 KTEkrfIGLTNSFGFGGTNATL 454
Cdd:PRK07967 381 ELT---TVMSNSFGFGGTNATL 399
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
44-458 |
2.42e-80 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 255.33 E-value: 2.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 44 VVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVprgsdegqfneqNFVsksDIKSMSSPTI--- 120
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFL---PESPFGASALsea 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAIGAAELAMKDSG--------------------WHPQSEADQvATGVAIGMGMIPLEVVSETalnfqtkgyNKVSPFFv 180
Cdd:PRK06501 78 LARLAAEEALAQAGigkgdfpgplflaappveleWPARFALAA-AVGDNDAPSYDRLLRAARG---------GRFDALH- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 181 PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSD- 259
Cdd:PRK06501 147 ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDp 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 260 PKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQP 339
Cdd:PRK06501 227 PEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 340 EEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPE 419
Cdd:PRK06501 307 EQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPA 386
|
410 420 430
....*....|....*....|....*....|....*....
gi 8923559 420 FDLNYVPLKAQEWKTEKRfigLTNSFGFGGTNATLCIAG 458
Cdd:PRK06501 387 IPLDVVPNVARDARVTAV---LSNSFGFGGQNASLVLTA 422
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
42-454 |
3.75e-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: 3.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLV---WDRLIGGESGIVSLVGEEYKSiPCSVAAYVPRGSDEGQFneqnfVSKSDIksMSSP 118
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRF-DRGVAGQIPTGDIPGWD-----AKRTGI--VDRT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFqtkgYNKVSPFFVPK--ILVNMAAGQVSIRY 196
Cdd:cd00828 73 TLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPKwmLSPNTVAGWVNILL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 197 KLK-GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALSTNSD-PKLACRPFHPKRDGF 274
Cdd:cd00828 149 LSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEePEEMSRPFDETRDGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 275 VMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPeGEGALRCMAAALKDAGVQPEEISYINAHATSTPL 354
Cdd:cd00828 228 VEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 355 GDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKT 434
Cdd:cd00828 307 NDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNL 386
|
410 420
....*....|....*....|
gi 8923559 435 EKRfIGLTNSFGFGGTNATL 454
Cdd:cd00828 387 KVR-AALVNAFGFGGSNAAL 405
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
198-454 |
1.76e-73 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 236.28 E-value: 1.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 198 LKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDScISPLSLAGFSRARALStnsdpKLACRPFHPKRDGFVMG 277
Cdd:PRK09185 149 LSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS-----PQPCRPFSANRDGINIG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 278 EGAAVLVLE-EYEHAVQrrariyaeVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:PRK09185 223 EAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLND 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 357 AAENKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYvpLKAQEWKTEK 436
Cdd:PRK09185 295 AMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLY--LVENAQALAI 369
|
250
....*....|....*...
gi 8923559 437 RFIgLTNSFGFGGTNATL 454
Cdd:PRK09185 370 RYV-LSNSFAFGGNNCSL 386
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
129-452 |
9.29e-69 |
|
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: 224.74 E-value: 9.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 129 AMKDSGWHPQSEADQvATGVAIGMGmiplevvSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTA 208
Cdd:cd00833 98 ALEDAGYSPESLAGS-RTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 209 CTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGEGAAVLVLEEY 288
Cdd:cd00833 170 CSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----PDGRCRPFDADADGYVRGEGVGVVVLKRL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 289 EHAVQRRARIYAEVLGYGLS--GDAGHITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHL 366
Cdd:cd00833 246 SDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 367 F---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWK--TEKR 437
Cdd:cd00833 324 FggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEARPWPapAGPR 403
|
330
....*....|....*
gi 8923559 438 FIGLtNSFGFGGTNA 452
Cdd:cd00833 404 RAGV-SSFGFGGTNA 417
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
43-457 |
5.39e-59 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 199.10 E-value: 5.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 43 RVVITGIGLVTPLGVGTHLVWDRLIGGESGI--VSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTI 120
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvMRRPGRQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAIGAAELAMKDSGWHPqseADQVATGVAIGMGMIPLEvvsETALNFQTkgYNKVSPFFVPK-ILVNM---AAGQVSIRY 196
Cdd:PRK07103 83 AALAAAREAWRDAALGP---VDPDRIGLVVGGSNLQQR---EQALVHET--YRDRPAFLRPSyGLSFMdtdLVGLCSEQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 197 KLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTN---SDPKLACRPFHPKRDG 273
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrfaDEPEAACRPFDQDRDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 274 FVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEgaLRCMAAALKDAGVQPEEISYINAHATSTP 353
Cdd:PRK07103 235 FIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 354 LGDAAENKAIKHLFKDHAYalaVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDcsEP-EFDLNYVPLKAQEW 432
Cdd:PRK07103 313 LGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD--EPiDERFRWVGSTAESA 387
|
410 420
....*....|....*....|....*
gi 8923559 433 KTEkrfIGLTNSFGFGGTNATLCIA 457
Cdd:PRK07103 388 RIR---YALSLSFGFGGINTALVLE 409
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
42-291 |
5.45e-56 |
|
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: 186.30 E-value: 5.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGE-----EYKSIPCSVA--AYVPRG--SDEGQFNEQNF-VSKSD 111
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADrwdpdKLYDPPSRIAgkIYTKWGglDDIFDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 112 IKSMSSPTIMAIGAAELAMKDSGWHPQSEaDQVATGVAIGMGMiplEVVSETALNFQTKGYNKVSPFFVPKIlVNMAAGQ 191
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSL-DGSRTGVFIGSGI---GDYAALLLLDEDGGPRRGSPFAVGTM-PSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 192 VSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsDPklaCRPFHPKR 271
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GP---CKAFDPFA 231
|
250 260
....*....|....*....|
gi 8923559 272 DGFVMGEGAAVLVLEEYEHA 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 |
3.33e-55 |
|
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: 186.69 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 119 TIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPkilvnmAAGQVSIRYKL 198
Cdd:cd00825 12 SILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG------ASGQIATPLGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 199 KGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGE 278
Cdd:cd00825 86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 279 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAA 358
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 359 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTekrf 438
Cdd:cd00825 242 ELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRT---- 315
|
330
....*....|....*.
gi 8923559 439 iGLTNSFGFGGTNATL 454
Cdd:cd00825 316 -ALLNGFGLGGTNATL 330
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
42-425 |
8.74e-55 |
|
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: 187.57 E-value: 8.74e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 42 RRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPrGSDEGQFNEQNFVSKSDiksmsSPTIM 121
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVP-DFDAAEHLPGRLLPQTD-----RMTRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 122 AIGAAELAMKDSGWHPqSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPF--FVPKILVNmaAGQVSIRYKLK 199
Cdd:cd00832 75 ALAAADWALADAGVDP-AALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsFAWFYAVN--TGQISIRHGMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 200 GPNHAVSTACTTGAHAVGDSFRFIAHGdADVMVAGGTDSCISPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEG 279
Cdd:cd00832 152 GPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 280 AAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaghitaPDP---EGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 356
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELD 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923559 357 AAENKAIKHLFKdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYV 425
Cdd:cd00832 305 RAEAAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV 371
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
129-452 |
1.92e-53 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 193.17 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 129 AMKDSGWHPQSEADQvATGVAIGMGMiplevvsETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTA 208
Cdd:COG3321 102 ALEDAGYDPESLAGS-RTGVFVGASS-------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 209 CTTGAHAVgdsfrfiaH--------GDADVMVAGGTDSCISPLSLAGFSRARALStnsdPKLACRPFHPKRDGFVMGEGA 280
Cdd:COG3321 174 CSSSLVAV--------HlacqslrsGECDLALAGGVNLMLTPESFILFSKGGMLS----PDGRCRAFDADADGYVRGEGV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 281 AVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGH---ITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPLGDA 357
Cdd:COG3321 242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 358 AENKAIKHLFKDHAYA---LAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLK 428
Cdd:COG3321 319 IEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGV--AGLikAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTE 396
|
330 340
....*....|....*....|....*.
gi 8923559 429 AQEWKTEK--RFIGLtNSFGFGGTNA 452
Cdd:COG3321 397 LRPWPAGGgpRRAGV-SSFGFGGTNA 421
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
299-414 |
1.34e-46 |
|
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: 156.96 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 299 YAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAV 376
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 8923559 377 SSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLD 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 |
3.73e-35 |
|
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: 139.76 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 181 PKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDp 260
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 261 klaCRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDA--GHITAPDPEGEGalRCMAAALKDAGVQ 338
Cdd:TIGR02813 257 ---IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 339 PEEISYINAHATSTPLGDAAENKAIKHLF---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDC 415
Cdd:TIGR02813 332 PHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQ 411
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 8923559 416 SEPEFDLNYVPL----KAQEWKTEK----RFIGLTnSFGFGGTN 451
Cdd:TIGR02813 412 PNPKLDIENSPFylntETRPWMQREdgtpRRAGIS-SFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
188-456 |
2.93e-32 |
|
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: 123.32 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 188 AAGQVSIRYKLK-GPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCisplslagfsraralstnsdpklacrp 266
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF--------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 267 fhpkrdgfVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGHITAPDPEGEGALRCMAAALKDAGVQPEEISYIN 346
Cdd:cd00327 99 --------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 347 AHATSTPLGDAAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN-LDCsepefdlnyv 425
Cdd:cd00327 170 AHGTGTPIGDAVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTPRePRT---------- 237
|
250 260 270
....*....|....*....|....*....|.
gi 8923559 426 plkaqewktekrfiGLTNSFGFGGTNATLCI 456
Cdd:cd00327 238 --------------VLLLGFGLGGTNAAVVL 254
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
204-452 |
1.77e-27 |
|
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: 111.27 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 204 AVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSdpklACRPFHPKRDGFVMGEGAAVL 283
Cdd:smart00825 92 TVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDG----RCKTFDASADGYVRGEGVGVV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 284 VLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstplgdaaenk 361
Cdd:smart00825 168 VLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q----------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 362 aikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLKAQEWKTE 435
Cdd:smart00825 209 ------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274
|
250
....*....|....*....
gi 8923559 436 --KRFIGLtNSFGFGGTNA 452
Cdd:smart00825 275 grPRRAGV-SSFGFGGTNA 292
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
41-412 |
3.24e-11 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 64.59 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 41 HRRVVITGIGLVTPLGVGTHLVWDRLiggESGIVSLVGEEYKSIPCSVAAYVPRGSDegqfneQNFVSKSDIKSMSspTI 120
Cdd:PRK06519 5 PNDVVITGIGLVSSLGEGLDAHWNAL---SAGRPQPNVDTETFAPYPVHPLPEIDWS------QQIPKRGDQRQME--TW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 121 MAIG--AAELAMKDSGWHPQSEA----DQVatgVAIGMGMIPLEV----------VSETALNFQTKGYNKVSPFFVPKIL 184
Cdd:PRK06519 74 QRLGtyAAGLALDDAGIKGNEELlstmDMI---VAAGGGERDIAVdtailnearkRNDRGVLLNERLMTELRPTLFLAQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 185 VNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNsdpklac 264
Cdd:PRK06519 151 SNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKG------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 265 rPFHP-------KRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEvlgygLSGDAGHITAPDPegeGAL-RCMAAALKDAG 336
Cdd:PRK06519 224 -GWAPvwsrggeDGGGFILGSGGAFLVLESREHAEARGARPYAR-----ISGVESDRARRAP---GDLeASLERLLKPAG 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8923559 337 VQPEEISYINAHATSTPLgdAAENKAikhlFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN 412
Cdd:PRK06519 295 GLAAPTAVISGATGAHPA--TAEEKA----ALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD 364
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
196-345 |
2.02e-08 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 55.80 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 196 YKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPklacrpfhpkrDGFV 275
Cdd:PRK06147 120 LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFI 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923559 276 MGEGAAVLVLEEYEHAVQRRARIYAevLGYGL--SGDAGHITAPdPEGEGALRCMAAALKDAGVQPEEISYI 345
Cdd:PRK06147 189 PGEAAAAVLLGRPAGGEAPGLPLLG--LGLGRepAPVGESEDLP-LRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
205-296 |
1.30e-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: 43.90 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923559 205 VSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSC-----ISPLSLAGFSR-ARALSTNSDPKLACRpfhpkRDGFVMGE 278
Cdd:COG0183 84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsrapmLLPKARWGYRMnAKLVDPMINPGLTDP-----YTGLSMGE 158
|
90 100
....*....|....*....|....*...
gi 8923559 279 GAAVLVlEEY--------EHAV--QRRA 296
Cdd:COG0183 159 TAENVA-ERYgisreeqdAFALrsHQRA 185
|
|
| |
