|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
35-470 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 787.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 35 RPSAGRRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRLPGGAD--AGRTLEQLPSRVAAPVPRGKGDAEFD 112
Cdd:PLN02836 1 PPLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMKSEDEetQLYTLDQLPSRVAALVPRGTGPGDFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 113 EEAWTKdNKSISGFIAYALCAADEALRDANWLPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKIL 192
Cdd:PLN02836 81 EELWLN-SRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 193 INMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSLPQA 272
Cdd:PLN02836 160 INMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNSCPTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 273 ASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQI 352
Cdd:PLN02836 240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 353 DYLNAHATSTPLGDAVEANAIKSVFGDHATSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLF 432
Cdd:PLN02836 320 DYVNAHATSTPLGDAVEARAIKTVFSEHATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIF 399
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002238816 433 EGAFMPLSSPKKMPIRAAISNSFGFGGTNTSLLFSCPP 470
Cdd:PLN02836 400 DDGFVPLTASKAMLIRAALSNSFGFGGTNASLLFTSPP 437
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
40-466 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 557.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVPrgkgdaEFDEEAWT-- 117
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDT------------SDLAVKIAGEVK------DFNPDDYMsr 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 KDNKSISGFIAYALCAADEALRDANWLPsEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMAS 197
Cdd:PRK07314 64 KEARRMDRFIQYGIAAAKQAVEDAGLEI-TEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 198 GHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyNSLPQAASRPF 277
Cdd:PRK07314 143 GHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR-NDDPERASRPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 278 DCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNA 357
Cdd:PRK07314 222 DKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 358 HATSTPLGDAVEANAIKSVFGDHATSggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFM 437
Cdd:PRK07314 302 HGTSTPAGDKAETQAIKRVFGEHAYK--VAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYV 379
|
410 420
....*....|....*....|....*....
gi 1002238816 438 PLsSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:PRK07314 380 PN-EARERKIDYALSNSFGFGGTNASLVF 407
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
40-466 |
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: 550.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVPrgkgdaEFDEEAWT-- 117
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDA------------SDLPVKIAGEVK------DFDPEDYIdk 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 KDNKSISGFIAYALCAADEALRDANWlPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMAS 197
Cdd:TIGR03150 63 KEARRMDRFIQYALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 198 GHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTkYNSLPQAASRPF 277
Cdd:TIGR03150 142 GQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALST-RNDDPEKASRPF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 278 DCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNA 357
Cdd:TIGR03150 221 DKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 358 HATSTPLGDAVEANAIKSVFGDHATSggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFM 437
Cdd:TIGR03150 301 HGTSTPLGDKAETKAIKKVFGDHAYK--LAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYV 378
|
410 420
....*....|....*....|....*....
gi 1002238816 438 PLsSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:TIGR03150 379 PN-EAREAKIDYALSNSFGFGGTNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
40-467 |
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: 549.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVPrgkgdaEFDEEAW--T 117
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA------------SGLPVRIAGEVK------DFDPEEYldR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 KDNKSISGFIAYALCAADEALRDANWLPsEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMAS 197
Cdd:COG0304 63 KELRRMDRFTQYALAAAREALADAGLDL-DEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 198 GHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyNSLPQAASRPF 277
Cdd:COG0304 142 GHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTR-NDDPEKASRPF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 278 DCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNA 357
Cdd:COG0304 221 DKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 358 HATSTPLGDAVEANAIKSVFGDHATSggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFM 437
Cdd:COG0304 301 HGTSTPLGDAAETKAIKRVFGDHAYK--VPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYV 378
|
410 420 430
....*....|....*....|....*....|
gi 1002238816 438 PlSSPKKMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:COG0304 379 P-NEAREAKIDYALSNSFGFGGHNASLVFK 407
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
40-466 |
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: 543.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVPRGKGDAEFDEeawtKD 119
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA------------SGFPSRIAGEVPDFDPEDYLDR----KE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 120 NKSISGFIAYALCAADEALRDANWLPsEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMASGH 199
Cdd:cd00834 65 LRRMDRFAQFALAAAEEALADAGLDP-EELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 200 VSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSlPQAASRPFDC 279
Cdd:cd00834 144 VAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDD-PEKASRPFDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 280 GRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHA 359
Cdd:cd00834 223 DRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 360 TSTPLGDAVEANAIKSVFGDHATsgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFMPl 439
Cdd:cd00834 303 TSTPLNDAAESKAIKRVFGEHAK--KVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVP- 379
|
410 420
....*....|....*....|....*..
gi 1002238816 440 SSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:cd00834 380 NEAREAPIRYALSNSFGFGGHNASLVF 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
49-467 |
1.00e-179 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 509.23 E-value: 1.00e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 49 AVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRLPGGADAGRTLEQL----PSRVAAPVPRgkgdAEFDEEAWTKDNKSiS 124
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLvaamPCQIAAEVDQ----SEFDPSDFAPTKRE-S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 125 GFIAYALCAADEALRDANWLPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMASGHVSMRY 204
Cdd:PTZ00050 76 RATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 205 GFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSLPQAASRPFDCGRDGF 284
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDPQRASRPFDKDRAGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 285 VIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSG-LQADQIDYLNAHATSTP 363
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 364 LGDAVEANAIKSVFGDHATSgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFMPLSSPK 443
Cdd:PTZ00050 316 IGDKIELKAIKKVFGDSGAP-KLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAH 394
|
410 420
....*....|....*....|....*
gi 1002238816 444 -KMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:PTZ00050 395 pLQSIDAVLSTSFGFGGVNTALLFT 419
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
40-467 |
3.80e-179 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 508.00 E-value: 3.80e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVPRGKGDAE--FDEEAWT 117
Cdd:PRK06333 4 KRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPV------------GDLATKIGGQVPDLAEDAEagFDPDRYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 --KDNKSISGFIAYALCAADEALRDANWLPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINM 195
Cdd:PRK06333 72 dpKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 196 ASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSLPQAASR 275
Cdd:PRK06333 152 AAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNDAPEQASR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 276 PFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYL 355
Cdd:PRK06333 232 PFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 356 NAHATSTPLGDAVEANAIKSVFGdhaTSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGA 435
Cdd:PRK06333 312 NAHATSTPVGDLGEVAAIKKVFG---HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGL 388
|
410 420 430
....*....|....*....|....*....|..
gi 1002238816 436 FMPLSSPKKMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:PRK06333 389 DVVANKARPMDMDYALSNGFGFGGVNASILFR 420
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
40-467 |
5.92e-123 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 364.44 E-value: 5.92e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLrlpggadagrtlEQLPSRVAAPVprgkgdAEFDEEAWT-- 117
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDA------------SDFPVQIAGEI------TDFDPTEVMdp 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 KDNKSISGFIAYALCAADEALRDANWLPSEdEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMAS 197
Cdd:PRK08439 64 KEVKKADRFIQLGLKAAREAMKDAGFLPEE-LDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 198 GHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyNSLPQAASRPF 277
Cdd:PRK08439 143 GFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTR-NDDPKKASRPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 278 DCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDgrGATLAMKRALDQSGlqADQIDYLNA 357
Cdd:PRK08439 222 DKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAG--NPKIDYINA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 358 HATSTPLGDAVEANAIKSVFGDHATSGglALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFM 437
Cdd:PRK08439 298 HGTSTPYNDKNETAALKELFGSKEKVP--PVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYI 375
|
410 420 430
....*....|....*....|....*....|
gi 1002238816 438 PlSSPKKMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:PRK08439 376 P-NVARKAELNVVMSNSFGFGGTNGVVIFK 404
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
40-466 |
3.04e-116 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 347.38 E-value: 3.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRLpggadagrtleqLPSRVAAPVPrgkgDAEFDEEAWTKD 119
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTN------------FSTRFAGLVK----DFNCEEYMSKKD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 120 NKSISGFIAYALCAADEALRDANwLPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMASGH 199
Cdd:PRK08722 68 ARKMDLFIQYGIAAGIQALDDSG-LEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 200 VSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyNSLPQAASRPFDC 279
Cdd:PRK08722 147 LSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTR-NDEPQKASRPWDK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 280 GRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHA 359
Cdd:PRK08722 226 DRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 360 TSTPLGDAVEANAIKSVFGDhATSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFMPL 439
Cdd:PRK08722 306 TSTPAGDVAEIKGIKRALGE-AGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPH 384
|
410 420
....*....|....*....|....*..
gi 1002238816 440 SSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:PRK08722 385 TARKVESMEYAICNSFGFGGTNGSLIF 411
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
149-466 |
9.34e-105 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 315.51 E-value: 9.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 149 EKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDAT 228
Cdd:PRK14691 23 EKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 229 RMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSLPQAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKI 308
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 309 YAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHATSTPLGDAVEANAIKSVFGDhatSGGLAL 388
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE---SNALAI 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002238816 389 SSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFMPLSSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILL 337
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
40-467 |
3.87e-98 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 305.36 E-value: 3.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRlpggadagrtleQLPSRVAAPVprgkgdAEFDEEAWT-- 117
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCS------------QFPTRIAGEI------KSFSTDGWVap 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 118 KDNKSISGFIAYALCAADEALRDANWlpSEDEKKE----RTGVSIGGGIGSISDILDASQMiLENRLRRLSPYFIPKILI 193
Cdd:PLN02787 191 KLSKRMDKFMLYLLTAGKKALADGGI--TEDVMKEldktKCGVLIGSAMGGMKVFNDAIEA-LRISYRKMNPFCVPFATT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 194 NMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyNSLPQAA 273
Cdd:PLN02787 268 NMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQR-NDDPTKA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 274 SRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQID 353
Cdd:PLN02787 347 SRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVN 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 354 YLNAHATSTPLGDAVEANAIKSVFGDHAtsgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFE 433
Cdd:PLN02787 427 YINAHATSTKAGDLKEYQALMRCFGQNP---ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD 503
|
410 420 430
....*....|....*....|....*....|....
gi 1002238816 434 GAFMPLSSPKKMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:PLN02787 504 TKVLVGPKKERLDIKVALSNSFGFGGHNSSILFA 537
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
40-467 |
3.68e-91 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 282.72 E-value: 3.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRalaaedlRLPGGADAGrtleqLPSRVAapvprgkGDAEFDEEAWTkD 119
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT-------FSPEFAEMG-----MRSQVW-------GNVKLDPTGLI-D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 120 NKS---ISGFIAYALCAADEALRDANwLPSEDEKKERTGVSIGGGIGSISDILDASQMILENR-LRRLSPYFIPKILINM 195
Cdd:PRK07967 62 RKVmrfMGDASAYAYLAMEQAIADAG-LSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRgPKRVGPYAVTKAMAST 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 196 ASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAgFSRLRALSTKYNSLPQAASR 275
Cdd:PRK07967 141 VSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKYNDTPEKASR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 276 PFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQndGRGATLAMKRALdqSGLQADqIDYL 355
Cdd:PRK07967 220 AYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMAL--ATVDTP-IDYI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 356 NAHATSTPLGDAVEANAIKSVFGDHATsgglALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGa 435
Cdd:PRK07967 295 NTHGTSTPVGDVKELGAIREVFGDKSP----AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAG- 369
|
410 420 430
....*....|....*....|....*....|....
gi 1002238816 436 fMPL--SSPKKMPIRAAISNSFGFGGTNTSLLFS 467
Cdd:PRK07967 370 -MPIvtETTDNAELTTVMSNSFGFGGTNATLVFR 402
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
42-469 |
3.34e-88 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 275.46 E-value: 3.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 42 VVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAaedlrlpggaDAGRTLEQLPSRVAapvprGKGDAEFDEEAWTKDNK 121
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLD----------DPFVEEFDLPVRIG-----GHLLEEFDHQLTRVELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 122 SISGFIAYALCAADEALRDANwlpSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINMASGHVS 201
Cdd:PRK07910 79 RMSYLQRMSTVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 202 MRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSLPQAASRPFDCGR 281
Cdd:PRK07910 156 LERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRPFDKDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 282 DGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHATS 361
Cdd:PRK07910 236 DGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 362 TPLGDAVEANAIKSVFGDHATsgglALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGAFMPlSS 441
Cdd:PRK07910 316 TSVGDVAEGKAINNALGGHRP----AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVA-GE 390
|
410 420
....*....|....*....|....*...
gi 1002238816 442 PKKMPIRAAISNSFGFGGTNTSLLFSCP 469
Cdd:PRK07910 391 PRPGNYRYAINNSFGFGGHNVALAFGRY 418
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
40-466 |
7.78e-86 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 269.16 E-value: 7.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRgvgpTWD----RLVAGGCAVRALAAEDlRLPGgadagrtleqLPSRVAAPVPrgkgDAEFDEEA 115
Cdd:PRK09116 2 RRVVVTGMGGVTALGE----DWQtiaaRLKAGRNAVRRMPEWD-RYDG----------LNTRLAAPID----DFELPAHY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 116 WTKDNKSISGFIAYALCAADEALRDANWLPSEDEKKERTGVSIGGGIGSISDILDASQMILENRLRRLSPYFIPKILINM 195
Cdd:PRK09116 63 TRKKIRSMGRVSLMATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 196 ASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsIDALSIAGFSRLRALSTKyNSLPQAASR 275
Cdd:PRK09116 143 TAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTR-NDAPELTPR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 276 PFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGatLAMKRALDQSGLQADQIDYL 355
Cdd:PRK09116 221 PFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 356 NAHATSTPLGDAVEANAIKSVFGDHatsggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLFEGA 435
Cdd:PRK09116 299 NAHGTATDRGDIAESQATAAVFGAR-----MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGAL 373
|
410 420 430
....*....|....*....|....*....|.
gi 1002238816 436 FMPLSSPKKMPIRAAISNSFGFGGTNTSLLF 466
Cdd:PRK09116 374 DYIMGEAREIDTEYVMSNNFAFGGINTSLIF 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
42-470 |
6.93e-84 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 264.57 E-value: 6.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 42 VVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAaedlRLPggadagrtLEQLPSRVAapvprgkGDAEF-DEEAWTKDN 120
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTIT----RFP--------TEGLRTRIA-------GTVDFlPESPFGASA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 121 KSIsgfiAYALCAADEALRDANWL-------------PSEDEKKERtgvSIGGGIGSISDILDASQMILENRLRRLSPYF 187
Cdd:PRK06501 74 LSE----ALARLAAEEALAQAGIGkgdfpgplflaapPVELEWPAR---FALAAAVGDNDAPSYDRLLRAARGGRFDALH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 188 iPKILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKyN 267
Cdd:PRK06501 147 -ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQ-N 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 268 SLPQAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGL 347
Cdd:PRK06501 225 DPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 348 QADQIDYLNAHATSTPLGDAVEANAIKSVFGDHATSggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEK 427
Cdd:PRK06501 305 TPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLAS--IPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDN 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1002238816 428 PDTLFEGAFMPLSSpKKMPIRAAISNSFGFGGTNTSLLFSCPP 470
Cdd:PRK06501 383 PDPAIPLDVVPNVA-RDARVTAVLSNSFGFGGQNASLVLTAEP 424
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
41-464 |
3.03e-75 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 240.72 E-value: 3.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 41 RVVVTGLGAVTPLGrGVGPTWDRLVAGGCAVRalaaedLRLPggadagrtLEQLPsrvaaPVPRG-KGDAEFDEEAWTKD 119
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIK------LHQP--------FPELP-----PLPLGlIGNQPSSLEDLTKT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 120 nksisgfiayalcAADEALRDANWLPSEDEkkerTGVS------------IGGGIGSISDILDASQMILENRLRRLSpyf 187
Cdd:PRK05952 63 -------------VVTAALKDAGLTPPLTD----CGVVigssrgcqgqweKLARQMYQGDDSPDEELDLENWLDTLP--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 188 ipkiliNMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALStkyn 267
Cdd:PRK05952 123 ------HQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA---- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 268 slpQAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGL 347
Cdd:PRK05952 193 ---KTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 348 QADQIDYLNAHATSTPLGDAVEANAIKSVFGDhatsgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEK 427
Cdd:PRK05952 270 TPEDIDYIHAHGTATRLNDQREANLIQALFPH-----RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE 344
|
410 420 430
....*....|....*....|....*....|....*..
gi 1002238816 428 PDtlFEGAFmpLSSPKKMPIRAAISNSFGFGGTNTSL 464
Cdd:PRK05952 345 PE--FDLNF--VRQAQQSPLQNVLCLSFGFGGQNAAI 377
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
40-465 |
3.13e-74 |
|
"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: 239.26 E-value: 3.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPT---WDRLVAGGCAVRALAAEDLRLPGGadagrtleqlpsrVAAPVPRGkgdaefDEEAW 116
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRFDRG-------------VAGQIPTG------DIPGW 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 117 T-KDNKSISGFIAYALCAADEALRDANWLPSEDEKKERTGVSIGGGIGSisdiLDASQMILENRLRRLSPYFIPK--ILI 193
Cdd:cd00828 62 DaKRTGIVDRTTLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGG----LRFLRRGGKLDARAVNPYVSPKwmLSP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 194 NMASGHVSMRYGF-QGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIaGFSRLRALSTKYNsLPQA 272
Cdd:cd00828 138 NTVAGWVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALSTAEE-EPEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 273 ASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNdGRGATLAMKRALDQSGLQADQI 352
Cdd:cd00828 216 MSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 353 DYLNAHATSTPLGDAVEANAIKSVFGDHATSggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLF 432
Cdd:cd00828 295 DVISAHGTSTPANDVAESRAIAEVAGALGAP--LPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV 372
|
410 420 430
....*....|....*....|....*....|....
gi 1002238816 433 EGAFMPLSS-PKKMPIRAAISNSFGFGGTNTSLL 465
Cdd:cd00828 373 EHLSVVGLSrDLNLKVRAALVNAFGFGGSNAALV 406
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
41-465 |
2.85e-72 |
|
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: 234.37 E-value: 2.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 41 RVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRLPGGADAGRTLEQLPSRVAAPVprgKGDAEFDEEAWtkdn 120
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTRRGGFL---DDVDAFDAAFF---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 121 kSISGFIA--------YALCAADEALRDANWLPsEDEKKERTGVsigggigsisdILDAS----QMILENRLRRLSPYFI 188
Cdd:cd00833 75 -GISPREAeamdpqqrLLLEVAWEALEDAGYSP-ESLAGSRTGV-----------FVGASssdyLELLARDPDEIDAYAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 189 PKILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALStkyns 268
Cdd:cd00833 142 TGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 269 lPQAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMS--GDAHHITQPqnDGRGATLAMKRALDQSG 346
Cdd:cd00833 217 -PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAP--SGEAQAALIRRAYARAG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 347 LQADQIDYLNAHATSTPLGDAVEANAIKSVFG-DHATSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNL 425
Cdd:cd00833 294 VDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGgSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHF 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002238816 426 EKPDTLFEGAFMPLSSPKK--------MPIRAAIsNSFGFGGTNTSLL 465
Cdd:cd00833 374 ETPNPKIDFEESPLRVPTEarpwpapaGPRRAGV-SSFGFGGTNAHVI 420
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
42-470 |
9.46e-71 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 229.34 E-value: 9.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 42 VVVTGLGAVTPLGRGVGPTWDRLVAG---GCAVRALAAEDLRLPGGADAGRTLEQLPSRVAApvprgkgdaeFDeeawTK 118
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGrasGMRPCDFWLVDLPTWVGEVVGVELPALPAALAA----------FD----CR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 119 DNKsisgfiaYALCAA---DEALRDAnwlpSEDEKKERTGVsigggigsisdILDASQM-ILENR--LRRLSP------- 185
Cdd:PRK09185 70 NNR-------LALLALqqiEPAVEAA----IARYGADRIGV-----------VLGTSTSgILEGElaYRRRDPahgalpa 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 186 -YFIPKILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsIDALSIAGFSRLRALST 264
Cdd:PRK09185 128 dYHYAQQELGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 265 kynslpqAASRPFDCGRDGFVIGEGCGVMVLEaldhaKERGAKIYaeVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQ 344
Cdd:PRK09185 207 -------QPCRPFSANRDGINIGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGLGAILAMQQALAD 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 345 SGLQADQIDYLNAHATSTPLGDAVEANAIKSVFGDhatsgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLN 424
Cdd:PRK09185 273 AGLAPADIGYINLHGTATPLNDAMESRAVAAVFGD-----GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWN 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1002238816 425 LEKPDTlfegAFMP---LSSPKKMPIRAAISNSFGFGGTNTSLLFSCPP 470
Cdd:PRK09185 348 TGQPDP----ALPPlylVENAQALAIRYVLSNSFAFGGNNCSLIFGRAD 392
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
41-465 |
1.04e-63 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 211.81 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 41 RVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAEDLRLPGGADAGRTLE---------QLPSRVAAPVPRGkgdAEF 111
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAGAGLASAfigaeldslALPERLDAKLLRR---ASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 112 DEEAwtkdnksisgfiayALCAADEALRDANwLPSEDekKERTGVSIGGGIGSISDILDASQMiLENRLRRLSPYFIPKI 191
Cdd:PRK07103 80 SAQA--------------ALAAAREAWRDAA-LGPVD--PDRIGLVVGGSNLQQREQALVHET-YRDRPAFLRPSYGLSF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 192 LINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALST-KYNSLP 270
Cdd:PRK07103 142 MDTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSdRFADEP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 271 QAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGAtlAMKRALDQSGLQAD 350
Cdd:PRK07103 222 EAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 351 QIDYLNAHATSTPLGDAVEANAIKSVFGDHATsgglaLSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDT 430
Cdd:PRK07103 300 DIDYVNPHGTGSPLGDETELAALFASGLAHAW-----INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPID 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002238816 431 L---FEGAfmplsSPKKMPIRAAISNSFGFGGTNTSLL 465
Cdd:PRK07103 375 ErfrWVGS-----TAESARIRYALSLSFGFGGINTALV 407
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
129-465 |
9.94e-54 |
|
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: 183.22 E-value: 9.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 129 YALCAADEALRDANwLPSEDEKKERTGVSIGGGIGSisdilDASQMILENRLRRLSPYFIPKILINMASGHVSMRYGFQG 208
Cdd:cd00825 14 LGFEAAERAIADAG-LSREYQKNPIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 209 PNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALStkynslPQAASRPFDCGRDGFVIGE 288
Cdd:cd00825 88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST------PEKASRTFDAAADGFVFGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 289 GCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHATSTPLGDAV 368
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 369 EANAIKSVFGDHAtsggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDtlfEGAFMPLSSPKKMPIR 448
Cdd:cd00825 242 ELKLLRSEFGDKS----PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELD---EAGLNIVTETTPRELR 314
|
330
....*....|....*..
gi 1002238816 449 AAISNSFGFGGTNTSLL 465
Cdd:cd00825 315 TALLNGFGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
40-301 |
4.91e-51 |
|
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: 173.59 E-value: 4.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRalaaedlRLPGGADAGRTLEQLPSRVAAPVPRGKG----DAEFDEEA 115
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGIS-------EIPADRWDPDKLYDPPSRIAGKIYTKWGglddIFDFDPLF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 116 WT---KDNKSISGFIAYALCAADEALRDANWLPsEDEKKERTGVSIGGGIGSISDILDASqmiLENRLRRLSPYFIPKIl 192
Cdd:pfam00109 74 FGispREAERMDPQQRLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGIGDYAALLLLD---EDGGPRRGSPFAVGTM- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 193 INMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYnslPQA 272
Cdd:pfam00109 149 PSVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDG---PCK 225
|
250 260
....*....|....*....|....*....
gi 1002238816 273 ASRPFDcgrDGFVIGEGCGVMVLEALDHA 301
Cdd:pfam00109 226 AFDPFA---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
134-461 |
1.55e-49 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 182.38 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 134 ADEALRDANwLPSEDEKKERTGVsigggigsisdILDAS----QMILENRLRRLSPYFIPKILINMASGHVSMRYGFQGP 209
Cdd:COG3321 99 AWEALEDAG-YDPESLAGSRTGV-----------FVGASsndyALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 210 NHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALStkynslPQAASRPFDCGRDGFVIGEG 289
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS------PDGRCRAFDADADGYVRGEG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 290 CGVMVLEALDHAKERGAKIYAEVRGYGMS--GDAHHITQPqnDGRGATLAMKRALDQSGLQADQIDYLNAHATSTPLGDA 367
Cdd:COG3321 241 VGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRSNGLTAP--NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 368 VEANAIKSVFGDHATSGG-LALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDTLF---EGAF------M 437
Cdd:COG3321 319 IEAAALTAAFGQGRPADQpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIdfeNSPFyvntelR 398
|
330 340
....*....|....*....|....
gi 1002238816 438 PLSSPKKmPIRAAISnSFGFGGTN 461
Cdd:COG3321 399 PWPAGGG-PRRAGVS-SFGFGGTN 420
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
309-426 |
4.10e-49 |
|
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: 163.89 E-value: 4.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 309 YAEVRGYGMSGDAHHITQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHATSTPLGDAVEANAIKSVFGDHATSGGLAL 388
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1002238816 389 SSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLE 426
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
40-465 |
7.09e-46 |
|
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: 164.07 E-value: 7.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 40 RRVVVTGLGAVTPLGRGVGPTWDRLVAGGCAVRALAAED-----LRLPGGADAGRTLEQLPSRVAAPVPRgkgdaefdee 114
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDpsgypARLAGEVPDFDAAEHLPGRLLPQTDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 115 awtkdnksisgFIAYALCAADEALRDANWLPSEDEKKERtGVSIGGGIGSisdiLDASQMILENRL----RRLSPYFIPK 190
Cdd:cd00832 71 -----------MTRLALAAADWALADAGVDPAALPPYDM-GVVTASAAGG----FEFGQRELQKLWskgpRHVSAYQSFA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 191 ILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGdADVMVAGGTESSIDALSIAGFSRLRALSTKYNslP 270
Cdd:cd00832 135 WFYAVNTGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDD--P 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 271 QAASRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAhhitqPQNDGRGATL--AMKRALDQSGLQ 348
Cdd:cd00832 212 ARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRPPGLarAIRLALADAGLT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 349 ADQIDYLNAHATSTPLGDAVEANAIKSVFGdhatSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKP 428
Cdd:cd00832 287 PEDVDVVFADAAGVPELDRAEAAALAAVFG----PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDV 362
|
410 420 430
....*....|....*....|....*....|....*..
gi 1002238816 429 DTLFeGAFMPLSSPKKMPIRAAISNSFGFGGTNTSLL 465
Cdd:cd00832 363 PPAY-GLDLVTGRPRPAALRTALVLARGRGGFNSALV 398
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
189-461 |
1.08e-39 |
|
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: 153.24 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 189 PKILINMASGHVSMRYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNS 268
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 269 lpqaasRPFDCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGDAH--HITQPQNDGRGAtlAMKRALDQSG 346
Cdd:TIGR02813 258 ------QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAK--ALKRAYDDAG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 347 LQADQIDYLNAHATSTPLGDAVEANAIKSVFG-DHATSGGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNL 425
Cdd:TIGR02813 330 FAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINV 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002238816 426 EKPDTLF--EGAFMPLSSPKK--------MPIRAAISnSFGFGGTN 461
Cdd:TIGR02813 410 DQPNPKLdiENSPFYLNTETRpwmqredgTPRRAGIS-SFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
196-465 |
1.26e-30 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 119.09 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 196 ASGHVSMRYGFQ-GPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsidalsiagfsrlralstkynslpqaas 274
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 275 rpfdcgrdgFVIGEGCGVMVLEALDHAKERGAKIYAEVRGYGMSGD-AHHITQPQndGRGATLAMKRALDQSGLQADQID 353
Cdd:cd00327 98 ---------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVS--GEGLARAARKALEGAGLTPSDID 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 354 YLNAHATSTPLGDAVEANAIKSVFGDHatsgGLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTlnlekpdtlfe 433
Cdd:cd00327 167 YVEAHGTGTPIGDAVELALGLDPDGVR----SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------- 231
|
250 260 270
....*....|....*....|....*....|..
gi 1002238816 434 gafmplsspkKMPIRAAISNSFGFGGTNTSLL 465
Cdd:cd00327 232 ----------PREPRTVLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
215-465 |
1.12e-29 |
|
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: 117.43 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 215 TACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALStkynslPQAASRPFDCGRDGFVIGEGCGVMV 294
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 295 LEALDHAKERGAKIYAEVRGYGMSgdahhitqpqNDGRGATLAMKRALDQsglqadqidylnahatstplgdaveanaik 374
Cdd:smart00825 169 LKRLSDALRDGDPILAVIRGSAVN----------QDGRSNGITAPSGPAQ------------------------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 375 svfgdhatsggLALSSTKGAIGHLLGAAGSVEAIFTVLAIHHGIAPPTLNLEKPDT---LFEGAF------MPLSSPKKm 445
Cdd:smart00825 209 -----------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPhidLEESPLrvptelTPWPPPGR- 276
|
250 260
....*....|....*....|
gi 1002238816 446 PIRAAIsNSFGFGGTNTSLL 465
Cdd:smart00825 277 PRRAGV-SSFGFGGTNAHVI 295
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
220-354 |
6.74e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 51.17 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 220 GAHSIGDATRMIQFGDADVMVAGGTESSIDALSIAGFSRLRALSTKYNSlpqaasrpfdcgrDGFVIGEGCGVMVLEALD 299
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-------------NGFIPGEAAAAVLLGRPA 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002238816 300 HAKERGAKIYaevrGYGMSGDAHHITQPQN---DGRGATLAMKRALDQSGLQADQIDY 354
Cdd:PRK06147 203 GGEAPGLPLL----GLGLGREPAPVGESEDlplRGDGLTQAIRAALAEAGCGLEDMDY 256
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
212-246 |
3.23e-05 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 45.83 E-value: 3.23e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1002238816 212 AAVT---ACATGAHSIGDATRMIQFGDADVMVAGGTES 246
Cdd:COG0183 80 PAVTvnrVCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
216-246 |
1.95e-04 |
|
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: 43.62 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|.
gi 1002238816 216 ACATGAHSIGDATRMIQFGDADVMVAGGTES 246
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVES 113
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
217-246 |
4.89e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 42.45 E-value: 4.89e-04
10 20 30
....*....|....*....|....*....|
gi 1002238816 217 CATGAHSIGDATRMIQFGDADVMVAGGTES 246
Cdd:PRK05790 88 CGSGLKAVALAAQAIRAGDADIVVAGGQES 117
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
289-404 |
9.44e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 41.25 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 289 GCGVMVLEALDHAKERGAKIYAEVRGYGMSGdahhiTQPQNDGRGATLAMKRALDQSGLQADQIDY--LNAHATSTPLgd 366
Cdd:PRK06445 254 GASYVLLMSKKAVKKYGLKPMAKIRSFGFAG-----VPPAIMGKGPVPASKKALEKAGLSVKDIDLweINEAFAVVVL-- 326
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1002238816 367 aveaNAIKSVfgdhatsgGLALS--STKG---AIGHLLGAAGS 404
Cdd:PRK06445 327 ----YAIKEL--------GLDPEtvNIKGgaiAIGHPLGATGA 357
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
278-312 |
2.81e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 39.94 E-value: 2.81e-03
10 20 30
....*....|....*....|....*....|....*
gi 1002238816 278 DCGRDGFVIGEGCGVMVLEALDHAKERGAKIYAEV 312
Cdd:PRK06519 233 GEDGGGFILGSGGAFLVLESREHAEARGARPYARI 267
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
216-247 |
3.52e-03 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 39.52 E-value: 3.52e-03
10 20 30
....*....|....*....|....*....|..
gi 1002238816 216 ACATGAHSIGDATRMIQFGDADVMVAGGTESS 247
Cdd:TIGR01930 82 QCASGLQAVILAAQLIRAGEADVVVAGGVESM 113
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
216-246 |
4.83e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 38.82 E-value: 4.83e-03
10 20 30
....*....|....*....|....*....|.
gi 1002238816 216 ACATGAHSIGDATRMIQFGDADVMVAGGTES 246
Cdd:pfam00108 84 VCGSGLKAVYLAAQSIASGDADVVLAGGVES 114
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
286-404 |
7.57e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 38.54 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002238816 286 IGEGCGVMVLEALDHAKERGAKIYAEVRGYGmsgDAHHitQPQNDGRGATLAMKRALDQSGLQADQIDYLNAHatstplg 365
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYA---DAAQ--APELFTTAPALAIPKALKHAGLEASQVDYYEIN------- 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002238816 366 davEANAIKSVfgdhATSGGLALSSTK-----GA--IGHLLGAAGS 404
Cdd:PLN02644 318 ---EAFSVVAL----ANQKLLGLDPEKvnvhgGAvsLGHPIGCSGA 356
|
|
| |
