|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-199 |
5.46e-113 |
|
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: 328.21 E-value: 5.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEA 80
Cdd:COG0304 201 DALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:COG0304 281 MRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVI 360
|
170 180 190
....*....|....*....|....*....|....*....
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:COG0304 361 PPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-199 |
1.82e-106 |
|
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: 311.39 E-value: 1.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEA 80
Cdd:cd00834 201 AALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:cd00834 281 MRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVL 360
|
170 180 190
....*....|....*....|....*....|....*....
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:cd00834 361 PPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGG 399
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-199 |
4.28e-100 |
|
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: 295.16 E-value: 4.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:TIGR03150 202 AMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:TIGR03150 282 RAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVP 361
|
170 180 190
....*....|....*....|....*....|....*...
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:TIGR03150 362 PTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-199 |
9.70e-94 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 278.98 E-value: 9.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:PRK07314 203 AARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAM 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:PRK07314 283 KLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIP 362
|
170 180 190
....*....|....*....|....*....|....*...
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK07314 363 PTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
52-167 |
6.37e-44 |
|
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: 142.32 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 52 YAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYD--VPV 129
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1145801129 130 SSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLH 167
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
17-180 |
7.56e-16 |
|
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: 73.90 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 17 SRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGfaSRCNAyhmtglrpdgvemaeairtaldearlDGSAVD 96
Cdd:smart00825 148 CKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRG--SAVNQ--------------------------DGRSNG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 97 YINAHGSGtkQndrhetaafkrslgdhaydVPVSSIKSMIGHSLGAIGsleVAA---SALAIEHNTVPPTANLHTPDPAC 173
Cdd:smart00825 200 ITAPSGPA--Q-------------------LLIGSVKSNIGHLEAAAG---VAGlikVVLALKHGVIPPTLHFETPNPHI 255
|
....*..
gi 1145801129 174 DLDYTPL 180
Cdd:smart00825 256 DLEESPL 262
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-199 |
5.46e-113 |
|
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: 328.21 E-value: 5.46e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEA 80
Cdd:COG0304 201 DALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:COG0304 281 MRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVI 360
|
170 180 190
....*....|....*....|....*....|....*....
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:COG0304 361 PPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-199 |
1.82e-106 |
|
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: 311.39 E-value: 1.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEA 80
Cdd:cd00834 201 AALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:cd00834 281 MRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVL 360
|
170 180 190
....*....|....*....|....*....|....*....
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:cd00834 361 PPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGG 399
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-199 |
4.28e-100 |
|
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: 295.16 E-value: 4.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:TIGR03150 202 AMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAM 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:TIGR03150 282 RAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVP 361
|
170 180 190
....*....|....*....|....*....|....*...
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:TIGR03150 362 PTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-199 |
9.70e-94 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 278.98 E-value: 9.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:PRK07314 203 AARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAM 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:PRK07314 283 KLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIP 362
|
170 180 190
....*....|....*....|....*....|....*...
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK07314 363 PTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
2-199 |
1.87e-74 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 229.62 E-value: 1.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVemAEAI 81
Cdd:PRK08439 203 AMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGP--LRAM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARldGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:PRK08439 281 KAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILP 358
|
170 180 190
....*....|....*....|....*....|....*...
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK08439 359 PTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
10-199 |
3.84e-72 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 224.19 E-value: 3.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 10 NDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTAL-DEA 88
Cdd:PTZ00050 218 NDDPQRASRPFDKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALkDGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 89 RLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDH-AYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLH 167
Cdd:PTZ00050 298 NININDVDYVNAHATSTPIGDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLE 377
|
170 180 190
....*....|....*....|....*....|....
gi 1145801129 168 TPDPACDLDYTPLTARS--QRTDTVLSVGRGFGG 199
Cdd:PTZ00050 378 NPDAECDLNLVQGKTAHplQSIDAVLSTSFGFGG 411
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
2-199 |
7.91e-68 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 213.32 E-value: 7.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPR-NDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEA 80
Cdd:PRK06333 214 AARALSTRfNDAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGdHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:PRK06333 294 MLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIA 372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 161 PPTANLHTPDPACD-LDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK06333 373 PPTLNLENPDPAAEgLDVVANKARPMDMDYALSNGFGFGG 412
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-199 |
1.67e-66 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 209.87 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 5 ATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTA 84
Cdd:PRK06501 219 ALSTQNDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 85 LDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTA 164
Cdd:PRK06501 299 LADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTI 378
|
170 180 190
....*....|....*....|....*....|....*
gi 1145801129 165 NLHTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK06501 379 NYDNPDPAIPLDVVPNVARDARVTAVLSNSFGFGG 413
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-199 |
3.13e-66 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 208.69 E-value: 3.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTglRPDGVEMAEA 80
Cdd:PRK09116 203 DTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVT--QPQAETMQIA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 81 IRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHaydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:PRK09116 281 MELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWF 357
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 161 PPTANLHTPDPAC-DLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK09116 358 APTLNLTQVDPACgALDYIMGEAREIDTEYVMSNNFAFGG 397
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-199 |
6.15e-56 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 182.51 E-value: 6.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:PRK08722 205 AAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAM 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDH-AYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:PRK08722 285 EAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIV 364
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTARS-QRTDTVLSVGRGFGG 199
Cdd:PRK08722 365 PPTINLDDPEEGLDIDLVPHTARKvESMEYAICNSFGFGG 404
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4-199 |
2.71e-55 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 181.14 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 4 KATSPR-NDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIR 82
Cdd:PLN02836 227 RALSTKfNSCPTEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 83 TALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYD--VPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTV 160
Cdd:PLN02836 307 RALQQSGLHPNQVDYVNAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIA 386
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 161 PPTANLHTPDPACDLDYTPLTA-RSQRTDTVLSVGRGFGG 199
Cdd:PLN02836 387 PPTLNLERPDPIFDDGFVPLTAsKAMLIRAALSNSFGFGG 426
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
19-199 |
2.75e-51 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 169.46 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 19 PFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEARLDGSAVDYI 98
Cdd:PRK05952 198 PFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 99 NAHGSGTKQNDRHETAAFKRSLGdhaYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTPDpaCDLDYT 178
Cdd:PRK05952 278 HAHGTATRLNDQREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFV 352
|
170 180
....*....|....*....|.
gi 1145801129 179 pLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK05952 353 -RQAQQSPLQNVLCLSFGFGG 372
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-199 |
3.98e-49 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 167.08 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAI 81
Cdd:PLN02787 332 ACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAyDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:PLN02787 412 EKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVH 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 162 PTANLHTPDPACDLDYTpLTARSQRTD--TVLSVGRGFGG 199
Cdd:PLN02787 491 PNINLENPESGVDTKVL-VGPKKERLDikVALSNSFGFGG 529
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-199 |
6.02e-48 |
|
"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: 161.45 E-value: 6.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 2 AIKATSPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMtGLRPDGVEMAEAI 81
Cdd:cd00828 202 NMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGR-SVPAGGKGIARAI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 82 RTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVP 161
Cdd:cd00828 281 RTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIP 360
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1145801129 162 PTANLHTPDPACDLDYTPLTARS--QRTDTVLSVGRGFGG 199
Cdd:cd00828 361 PTANLDDVDPDVEHLSVVGLSRDlnLKVRAALVNAFGFGG 400
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
7-199 |
8.01e-46 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 156.04 E-value: 8.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 7 SPRNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALD 86
Cdd:PRK07910 218 STNNDDPAGACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 87 EARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHayDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANL 166
Cdd:PRK07910 298 LAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNL 375
|
170 180 190
....*....|....*....|....*....|...
gi 1145801129 167 HTPDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK07910 376 ENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-199 |
1.47e-44 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 152.52 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 1 DAIKATSPR-NDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGlrPDGVEMAE 79
Cdd:PRK07967 201 DAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 80 AIRTALdeARLDGSaVDYINAHGSGTKQNDRHETAAFKRSLGDHAydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNT 159
Cdd:PRK07967 279 CMQMAL--ATVDTP-IDYINTHGTSTPVGDVKELGAIREVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGF 353
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1145801129 160 VPPTANLHTPDPACDlDYTPLTARSQRT--DTVLSVGRGFGG 199
Cdd:PRK07967 354 IAPSANIEELDPQAA-GMPIVTETTDNAelTTVMSNSFGFGG 394
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
52-167 |
6.37e-44 |
|
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: 142.32 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 52 YAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEARLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYD--VPV 129
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1145801129 130 SSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLH 167
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
9-199 |
2.15e-42 |
|
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: 146.74 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 9 RNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDgveMAEAIRTALDEA 88
Cdd:cd00832 207 TSDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGSGRPPG---LARAIRLALADA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 89 RLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHT 168
Cdd:cd00832 284 GLTPEDVDVVFADAAGVPELDRAEAAALAAVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTD 361
|
170 180 190
....*....|....*....|....*....|.
gi 1145801129 169 PDPACDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:cd00832 362 VPPAYGLDLVTGRPRPAALRTALVLARGRGG 392
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
10-200 |
8.21e-41 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 141.40 E-value: 8.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 10 NDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEAR 89
Cdd:PRK14691 141 NSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 90 LDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDhAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTP 169
Cdd:PRK14691 221 ITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENP 299
|
170 180 190
....*....|....*....|....*....|..
gi 1145801129 170 DPACD-LDYTPLTARSQRTDTVLSVGRGFGGL 200
Cdd:PRK14691 300 DPAAKgLNIIAGNAQPHDMTYALSNGFGFAGV 331
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
11-200 |
1.76e-40 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 141.71 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 11 DEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGlrPDGVEMAEAIRTALDEARL 90
Cdd:PRK07103 219 DEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPD--PSLEGEMRVIRAALRRAGL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 91 DGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYdvpVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTP- 169
Cdd:PRK07103 297 GPEDIDYVNPHGTGSPLGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPi 373
|
170 180 190
....*....|....*....|....*....|.
gi 1145801129 170 DPACDLDYTplTARSQRTDTVLSVGRGFGGL 200
Cdd:PRK07103 374 DERFRWVGS--TAESARIRYALSLSFGFGGI 402
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
17-199 |
2.57e-40 |
|
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: 141.54 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 17 SRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEARLDGSAVD 96
Cdd:cd00833 221 CRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDID 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 97 YINAHGSGTKQNDRHETAAFKRSLGDHAYD---VPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTPDPAC 173
Cdd:cd00833 301 YVEAHGTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKI 380
|
170 180 190
....*....|....*....|....*....|....
gi 1145801129 174 DLDYTPLTARSQ-----RTDTVLSVGR---GFGG 199
Cdd:cd00833 381 DFEESPLRVPTEarpwpAPAGPRRAGVssfGFGG 414
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
18-199 |
1.79e-37 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 133.43 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 18 RPFDASRNGFVLGEGSAVLVLEELESARRRgahvyaeIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEARLDGSAVDY 97
Cdd:PRK09185 210 RPFSANRDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGY 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 98 INAHGSGTKQNDRHETAAFKRSLGDHaydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTPDPACDLDY 177
Cdd:PRK09185 283 INLHGTATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLY 359
|
170 180
....*....|....*....|..
gi 1145801129 178 TPLTARSQRTDTVLSVGRGFGG 199
Cdd:PRK09185 360 LVENAQALAIRYVLSNSFAFGG 381
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
9-199 |
9.80e-34 |
|
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: 122.36 E-value: 9.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 9 RNDEPETASRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMTGLRPDGVEMAEAIRTALDEA 88
Cdd:cd00825 139 ALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 89 RLDGSAVDYINAHGSGTKQNDRHETAAFKRSLGDHAydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHT 168
Cdd:cd00825 219 GLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKS--PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEE 296
|
170 180 190
....*....|....*....|....*....|.
gi 1145801129 169 PDPacDLDYTPLTARSQRTDTVLSVGRGFGG 199
Cdd:cd00825 297 LDE--AGLNIVTETTPRELRTALLNGFGLGG 325
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
17-180 |
1.74e-29 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 114.58 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 17 SRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFAS----RCNAYhmtgLRPDGVEMAEAIRTALDEARLDG 92
Cdd:COG3321 225 CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVnqdgRSNGL----TAPNGPAQAAVIRRALADAGVDP 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 93 SAVDYINAHGSGTKQNDRHETAAFKRSLGDHAYD---VPVSSIKSMIGHslgaigsLEVAA-------SALAIEHNTVPP 162
Cdd:COG3321 301 ATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGH-------LEAAAgvaglikAVLALRHGVLPP 373
|
170
....*....|....*...
gi 1145801129 163 TANLHTPDPACDLDYTPL 180
Cdd:COG3321 374 TLHFETPNPHIDFENSPF 391
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
18-185 |
9.11e-24 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 98.15 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 18 RPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRCNAYHMT--GLRPDGveMAEAIRTALDEARLDGSAV 95
Cdd:TIGR02813 258 QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEG--QAKALKRAYDDAGFAPHTC 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 96 DYINAHGSGTKQNDRHETAAFKRSLG---DHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTPDPA 172
Cdd:TIGR02813 336 GLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPK 415
|
170
....*....|...
gi 1145801129 173 CDLDYTPLTARSQ 185
Cdd:TIGR02813 416 LDIENSPFYLNTE 428
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
27-199 |
6.37e-22 |
|
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: 89.43 E-value: 6.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 27 FVLGEGSAVLVLEELESARRRGAHVYAEIAGfasrcnaYHMTGLRPDGVEM------AEAIRTALDEARLDGSAVDYINA 100
Cdd:cd00327 98 FVFGDGAAAAVVESEEHALRRGAHPQAEIVS-------TAATFDGASMVPAvsgeglARAARKALEGAGLTPSDIDYVEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 101 HGSGTKQNDRHETAAFKRSLGDHAydVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTanlhtpdpacdldytpl 180
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------- 231
|
170
....*....|....*....
gi 1145801129 181 tarSQRTDTVLSVGRGFGG 199
Cdd:cd00327 232 ---PREPRTVLLLGFGLGG 247
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
17-180 |
7.56e-16 |
|
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: 73.90 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 17 SRPFDASRNGFVLGEGSAVLVLEELESARRRGAHVYAEIAGfaSRCNAyhmtglrpdgvemaeairtaldearlDGSAVD 96
Cdd:smart00825 148 CKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRG--SAVNQ--------------------------DGRSNG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 97 YINAHGSGtkQndrhetaafkrslgdhaydVPVSSIKSMIGHSLGAIGsleVAA---SALAIEHNTVPPTANLHTPDPAC 173
Cdd:smart00825 200 ITAPSGPA--Q-------------------LLIGSVKSNIGHLEAAAG---VAGlikVVLALKHGVIPPTLHFETPNPHI 255
|
....*..
gi 1145801129 174 DLDYTPL 180
Cdd:smart00825 256 DLEESPL 262
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
26-172 |
6.32e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 54.57 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145801129 26 GFVLGEGSAVLVLEELESARRRGAHVYAEIAGFASRcnayhmTGLRPDGvEMAEAIRTALDEArLDGSAVDYINAHGSGT 105
Cdd:PRK06519 238 GFILGSGGAFLVLESREHAEARGARPYARISGVESD------RARRAPG-DLEASLERLLKPA-GGLAAPTAVISGATGA 309
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1145801129 106 kqndrHETAAFKRSLGDHAYDVPVSSIKSMIGHSLGAIGSLEVAASALAIEHNTVPPTANLHTPDPA 172
Cdd:PRK06519 310 -----HPATAEEKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFDASGEKPM 371
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1-44 |
6.33e-06 |
|
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: 45.32 E-value: 6.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1145801129 1 DAIKATSPrnDEPETASRPFDasrNGFVLGEGSAVLVLEELESA 44
Cdd:pfam00109 213 SAAGMLSP--DGPCKAFDPFA---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
25-98 |
1.66e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 44.24 E-value: 1.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1145801129 25 NGFVLGEGSAVLVLEELESARRRGAHVYAeiAGFASRCNAYHMTG---LRPDGveMAEAIRTALDEARLDGSAVDYI 98
Cdd:PRK06147 185 NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGREPAPVGESEdlpLRGDG--LTQAIRAALAEAGCGLEDMDYR 257
|
|
| |
