|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
1-180 |
7.54e-106 |
|
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: 309.03 E-value: 7.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:TIGR03150 229 MGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:TIGR03150 309 DKAETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID 388
|
170 180
....*....|....*....|
gi 578806266 161 krfIGLTNSFGFGGTNATLC 180
Cdd:TIGR03150 389 ---YALSNSFGFGGTNASLV 405
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-181 |
6.55e-104 |
|
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: 304.08 E-value: 6.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:cd00834 309 DAAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR 388
|
170 180
....*....|....*....|.
gi 578806266 161 krfIGLTNSFGFGGTNATLCI 181
Cdd:cd00834 389 ---YALSNSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-181 |
3.46e-102 |
|
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: 299.70 E-value: 3.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:COG0304 309 DAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID 388
|
170 180
....*....|....*....|.
gi 578806266 161 krfIGLTNSFGFGGTNATLCI 181
Cdd:COG0304 389 ---YALSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-179 |
1.22e-100 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 295.93 E-value: 1.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:PRK07314 310 DKAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID 389
|
170
....*....|....*....
gi 578806266 161 krfIGLTNSFGFGGTNATL 179
Cdd:PRK07314 390 ---YALSNSFGFGGTNASL 405
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
24-139 |
2.62e-47 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 150.41 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 24 YAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAV 101
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806266 102 SSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLD 139
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
2-177 |
2.59e-15 |
|
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: 71.98 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstpl 79
Cdd:smart00825 161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q---------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 80 gdaaenkaikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLK 153
Cdd:smart00825 209 -------------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTE 267
|
170 180
....*....|....*....|....*.
gi 578806266 154 AQEWKTE--KRFIGLtNSFGFGGTNA 177
Cdd:smart00825 268 LTPWPPPgrPRRAGV-SSFGFGGTNA 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
1-180 |
7.54e-106 |
|
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: 309.03 E-value: 7.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:TIGR03150 229 MGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:TIGR03150 309 DKAETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID 388
|
170 180
....*....|....*....|
gi 578806266 161 krfIGLTNSFGFGGTNATLC 180
Cdd:TIGR03150 389 ---YALSNSFGFGGTNASLV 405
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
1-181 |
6.55e-104 |
|
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: 304.08 E-value: 6.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:cd00834 309 DAAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR 388
|
170 180
....*....|....*....|.
gi 578806266 161 krfIGLTNSFGFGGTNATLCI 181
Cdd:cd00834 389 ---YALSNSFGFGGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
1-181 |
3.46e-102 |
|
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: 299.70 E-value: 3.46e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:COG0304 309 DAAETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID 388
|
170 180
....*....|....*....|.
gi 578806266 161 krfIGLTNSFGFGGTNATLCI 181
Cdd:COG0304 389 ---YALSNSFGFGGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-179 |
1.22e-100 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 295.93 E-value: 1.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:PRK07314 310 DKAETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID 389
|
170
....*....|....*....
gi 578806266 161 krfIGLTNSFGFGGTNATL 179
Cdd:PRK07314 390 ---YALSNSFGFGGTNASL 405
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
1-179 |
8.59e-83 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 251.25 E-value: 8.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PLN02836 253 IGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPLG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAY--ALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQewK 158
Cdd:PLN02836 333 DAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVPLTAS--K 410
|
170 180
....*....|....*....|.
gi 578806266 159 TEKRFIGLTNSFGFGGTNATL 179
Cdd:PLN02836 411 AMLIRAALSNSFGFGGTNASL 431
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
1-179 |
1.42e-80 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 244.99 E-value: 1.42e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAG-VQPEEISYINAHATSTPL 79
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPI 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 80 GDAAENKAIKHLFKDH-AYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWK 158
Cdd:PTZ00050 317 GDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPL 396
|
170 180
....*....|....*....|.
gi 578806266 159 TEKRfIGLTNSFGFGGTNATL 179
Cdd:PTZ00050 397 QSID-AVLSTSFGFGGVNTAL 416
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-179 |
1.59e-80 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 245.29 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK06333 242 MGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKdHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQEWKT 159
Cdd:PRK06333 322 DLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDM 400
|
170 180
....*....|....*....|
gi 578806266 160 EkrfIGLTNSFGFGGTNATL 179
Cdd:PRK06333 401 D---YALSNGFGFGGVNASI 417
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-176 |
3.77e-66 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 207.66 E-value: 3.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGegALRCMAAALKDAGVqpEEISYINAHATSTPLG 80
Cdd:PRK08439 230 MGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEG--PLRAMKAALEMAGN--PKIDYINAHGTSTPYN 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:PRK08439 306 DKNETAALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELN 385
|
170
....*....|....*.
gi 578806266 161 krfIGLTNSFGFGGTN 176
Cdd:PRK08439 386 ---VVMSNSFGFGGTN 398
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-183 |
1.65e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 192.57 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFkdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLdcSEPEFDLNYVpLKAQEWKTE 160
Cdd:PRK05952 288 DQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNFV-RQAQQSPLQ 361
|
170 180
....*....|....*....|...
gi 578806266 161 KrfiGLTNSFGFGGTNATLCIAG 183
Cdd:PRK05952 362 N---VLCLSFGFGGQNAAIALGK 381
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-179 |
1.49e-59 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 190.98 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK08722 232 LGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAG 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKH-LFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQewKT 159
Cdd:PRK08722 312 DVAEIKGIKRaLGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTAR--KV 389
|
170 180
....*....|....*....|
gi 578806266 160 EKRFIGLTNSFGFGGTNATL 179
Cdd:PRK08722 390 ESMEYAICNSFGFGGTNGSL 409
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
2-179 |
2.50e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 179.27 E-value: 2.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLE-EYEHAVQrrariyaeVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK09185 222 GEAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYvpLKAQEWKTE 160
Cdd:PRK09185 294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLY--LVENAQALA 368
|
170
....*....|....*....
gi 578806266 161 KRFIgLTNSFGFGGTNATL 179
Cdd:PRK09185 369 IRYV-LSNSFAFGGNNCSL 386
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
1-183 |
1.55e-53 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 175.59 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK06501 243 MAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPEN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:PRK06501 323 DKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVT 402
|
170 180
....*....|....*....|...
gi 578806266 161 KRfigLTNSFGFGGTNATLCIAG 183
Cdd:PRK06501 403 AV---LSNSFGFGGQNASLVLTA 422
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
1-181 |
1.58e-53 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 173.38 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PRK14691 160 MGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFD-LNYVPLKAQewkT 159
Cdd:PRK14691 240 DLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQ---P 315
|
170 180
....*....|....*....|..
gi 578806266 160 EKRFIGLTNSFGFGGTNATLCI 181
Cdd:PRK14691 316 HDMTYALSNGFGFAGVNASILL 337
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
2-181 |
1.83e-51 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 169.78 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTPLGD 81
Cdd:PRK09116 232 GEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 82 AAENKAIKHLFKDHayaLAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYvpLKAQEWKTE 160
Cdd:PRK09116 310 IAESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDY--IMGEAREID 384
|
170 180
....*....|....*....|.
gi 578806266 161 KRFIgLTNSFGFGGTNATLCI 181
Cdd:PRK09116 385 TEYV-MSNNFAFGGINTSLIF 404
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
2-179 |
1.79e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 167.60 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 81
Cdd:PRK07910 241 GEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 82 AAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVplkAQEWKTEK 161
Cdd:PRK07910 321 VAEGKAINNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVV---AGEPRPGN 395
|
170
....*....|....*...
gi 578806266 162 RFIGLTNSFGFGGTNATL 179
Cdd:PRK07910 396 YRYAINNSFGFGGHNVAL 413
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-182 |
4.04e-50 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 169.39 E-value: 4.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:PLN02787 359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAyALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNyVPLKAQEWKTE 160
Cdd:PLN02787 439 DLKEYQALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTK-VLVGPKKERLD 516
|
170 180
....*....|....*....|..
gi 578806266 161 KRfIGLTNSFGFGGTNATLCIA 182
Cdd:PLN02787 517 IK-VALSNSFGFGGHNSSILFA 537
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-179 |
2.48e-48 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 161.76 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 4 GAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITApdPEGEGALRCMAAALkdAGVQpEEISYINAHATSTPLGDAA 83
Cdd:PRK07967 233 GGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 84 ENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEF-DLNYVPLKAQEWKTEkr 162
Cdd:PRK07967 308 ELGAIREVFGDK--SPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNAELT-- 383
|
170
....*....|....*..
gi 578806266 163 fIGLTNSFGFGGTNATL 179
Cdd:PRK07967 384 -TVMSNSFGFGGTNATL 399
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
24-139 |
2.62e-47 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 150.41 E-value: 2.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 24 YAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAY--ALAV 101
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806266 102 SSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLD 139
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
2-182 |
2.09e-41 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 143.63 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEgaLRCMAAALKDAGVQPEEISYINAHATSTPLGD 81
Cdd:PRK07103 238 GEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPLGD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 82 AAENKAIKHLFKDHAYalaVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDcsEP-EFDLNYVPLKAQEWKTE 160
Cdd:PRK07103 316 ETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLD--EPiDERFRWVGSTAESARIR 390
|
170 180
....*....|....*....|..
gi 578806266 161 krfIGLTNSFGFGGTNATLCIA 182
Cdd:PRK07103 391 ---YALSLSFGFGGINTALVLE 409
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
2-177 |
4.48e-41 |
|
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: 143.08 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLS--GDAGHITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTPL 79
Cdd:cd00833 234 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAPSGEAQAAL--IRRAYARAGVDPSDIDYVEAHGTGTPL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 80 GDAAENKAIKHLF---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLN----YVPL 152
Cdd:cd00833 312 GDPIEVEALAKVFggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPT 391
|
170 180
....*....|....*....|....*..
gi 578806266 153 KAQEWK--TEKRFIGLtNSFGFGGTNA 177
Cdd:cd00833 392 EARPWPapAGPRRAGV-SSFGFGGTNA 417
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
1-179 |
2.50e-36 |
|
"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: 130.25 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPeGEGALRCMAAALKDAGVQPEEISYINAHATSTPLG 80
Cdd:cd00828 229 EAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPAN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 81 DAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTE 160
Cdd:cd00828 308 DVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLK 387
|
170
....*....|....*....
gi 578806266 161 KRfIGLTNSFGFGGTNATL 179
Cdd:cd00828 388 VR-AALVNAFGFGGSNAAL 405
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
2-177 |
3.30e-35 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 130.38 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGH---ITAPDPEGEGALrcMAAALKDAGVQPEEISYINAHATSTP 78
Cdd:COG3321 238 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQD-GRsngLTAPNGPAQAAV--IRRALADAGVDPATVDYVEAHGTGTP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 79 LGDAAENKAIKHLFKDHAYA---LAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----Y 149
Cdd:COG3321 315 LGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGV--AGLikAVLALRHGVLPPTLHFETPNPHIDFEnspfY 392
|
170 180 190
....*....|....*....|....*....|
gi 578806266 150 VPLKAQEWKTEK--RFIGLtNSFGFGGTNA 177
Cdd:COG3321 393 VNTELRPWPAGGgpRRAGV-SSFGFGGTNA 421
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
2-179 |
1.43e-31 |
|
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: 116.20 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 81
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 82 AAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTek 161
Cdd:cd00825 240 VKELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRT-- 315
|
170
....*....|....*...
gi 578806266 162 rfiGLTNSFGFGGTNATL 179
Cdd:cd00825 316 ---ALLNGFGLGGTNATL 330
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
2-181 |
6.04e-24 |
|
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: 94.43 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGD 81
Cdd:cd00327 101 GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFD-GASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 82 AAENKAIKHLFKDHayALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN-LDCsepefdlnyvplkaqewkte 160
Cdd:cd00327 180 AVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTPRePRT-------------------- 237
|
170 180
....*....|....*....|.
gi 578806266 161 krfiGLTNSFGFGGTNATLCI 181
Cdd:cd00327 238 ----VLLLGFGLGGTNAAVVL 254
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
1-176 |
2.24e-23 |
|
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: 96.23 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDA--GHITAPDPEGEGalRCMAAALKDAGVQPEEISYINAHATSTP 78
Cdd:TIGR02813 269 IGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQA--KALKRAYDDAGFAPHTCGLIEAHGTGTA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 79 LGDAAENKAIKHLF---KDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPL--- 152
Cdd:TIGR02813 347 AGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPFyln 426
|
170 180
....*....|....*....|....*....
gi 578806266 153 -KAQEWKTEK----RFIGLTnSFGFGGTN 176
Cdd:TIGR02813 427 tETRPWMQREdgtpRRAGIS-SFGFGGTN 454
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-150 |
3.77e-21 |
|
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: 88.96 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDaghitaPDP---EGEGALRCMAAALKDAGVQPEEISYINAHATSTP 78
Cdd:cd00832 228 GEGGAILVLEDAAAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVP 301
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806266 79 LGDAAENKAIKHLFKdhAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYV 150
Cdd:cd00832 302 ELDRAEAAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLV 371
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
2-177 |
2.59e-15 |
|
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: 71.98 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 2 GEGAAVLVLEEYEHAVQRRARIYAEVLGYGL--SGDAGHITAPDPEGegalrcmaaalkdagvQpeeisyinahatstpl 79
Cdd:smart00825 161 GEGVGVVVLKRLSDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPA----------------Q---------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 80 gdaaenkaikhlfkdhayaLAVSSTKGATGHLLGAAGAveAAF--TTLACYYQKLPPTLNLDCSEPEFDLN----YVPLK 153
Cdd:smart00825 209 -------------------LLIGSVKSNIGHLEAAAGV--AGLikVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTE 267
|
170 180
....*....|....*....|....*.
gi 578806266 154 AQEWKTE--KRFIGLtNSFGFGGTNA 177
Cdd:smart00825 268 LTPWPPPgrPRRAGV-SSFGFGGTNA 292
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-137 |
1.95e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 43.79 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806266 1 MGEGAAVLVLEEYEHAVQRRARIYAEvlgygLSGDAGHITAPDPegeGAL-RCMAAALKDAGVQPEEISYINAHATSTPL 79
Cdd:PRK06519 241 LGSGGAFLVLESREHAEARGARPYAR-----ISGVESDRARRAP---GDLeASLERLLKPAGGLAAPTAVISGATGAHPA 312
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 578806266 80 gdAAENKAikhlFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLN 137
Cdd:PRK06519 313 --TAEEKA----ALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD 364
|
|
| |
