|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
2-406 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 859.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 2 TRRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRA 81
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 82 SELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK09116 81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATATIY 321
Cdd:PRK09116 241 EELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 322 GDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHEARKVDCEFLQSNNFAFGGINT 401
Cdd:PRK09116 321 GARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINT 400
|
....*
gi 15833595 402 SIIIK 406
Cdd:PRK09116 401 SLIFK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-408 |
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: 526.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIGDPIlTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:COG0304 80 REALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:COG0304 239 EELEHAKARGAKIYAEVVGYGASSDAYHITAPAPdgEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKVDCEFLQSNNFAF 396
Cdd:COG0304 319 VFGDhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 15833595 397 GGINTSIIIKRW 408
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-405 |
1.40e-158 |
|
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: 452.76 E-value: 1.40e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA-SGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIgDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:cd00834 80 EEALADAGLD-PEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:cd00834 239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDPdgEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEARKVDCEFLQSNNFAF 396
Cdd:cd00834 319 VFGEhakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 15833595 397 GGINTSIII 405
Cdd:cd00834 398 GGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-406 |
1.48e-116 |
|
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: 345.62 E-value: 1.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDA-SDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIGDPIlTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:TIGR03150 80 KEAVEDSGLDIEEE-DAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:TIGR03150 159 TACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQP--QRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:TIGR03150 239 EELEHAKARGAKIYAEIVGYGMSGDAYHITAPapEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKVDCEFLQSNNFAF 396
Cdd:TIGR03150 319 VFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|
gi 15833595 397 GGINTSIIIK 406
Cdd:TIGR03150 398 GGTNASLVFK 407
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-247 |
2.89e-32 |
|
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: 122.36 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPE--WQVYDGLH----------TLLGAPVDDFTLPEHYTRKRIR- 69
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKLYDppsriagkiyTKWGGLDDIFDFDPLFFGISPRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 70 --AMGRVSQMSTRASELALEQAGLIGDPILTSgETGIAYGSSTGSTGPVsefaTMLTEKHTNNITGTTYVQMMPHTTAVN 147
Cdd:pfam00109 81 aeRMDPQQRLLLEAAWEALEDAGITPDSLDGS-RTGVFIGSGIGDYAAL----LLLDEDGGPRRGSPFAVGTMPSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQHNDApkttpSPFDEN 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPC-----KAFDPF 230
|
250 260
....*....|....*....|.
gi 15833595 227 RDGLVIGEGAGTLILEELEHA 247
Cdd:pfam00109 231 ADGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
147-405 |
4.56e-13 |
|
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: 69.28 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 147 NTGLFFGLRGR----VIPTssACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSqhndapkttPS 221
Cdd:smart00825 77 RTGVFVGVSSSdysvTVDT--ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS---------PD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 222 ----PFDENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAH--ITQPQREtmqycmeqslkiaglsAQd 295
Cdd:smart00825 146 grckTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP----------------AQ- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 296 igyisahgtatdrgdmaeslatatiygdnVPLSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLNKPDPNc 371
Cdd:smart00825 209 -----------------------------LLIGSVKSNIGHLEAAAGV----AGLikvvLALKHGVIPPTLHFETPNPH- 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15833595 372 galdyIMHEARKVdcEFLQS---------------NNFAFGGINTSIII 405
Cdd:smart00825 255 -----IDLEESPL--RVPTEltpwpppgrprragvSSFGFGGTNAHVIL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
2-406 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 859.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 2 TRRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRA 81
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 82 SELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK09116 81 SELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATATIY 321
Cdd:PRK09116 241 EELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 322 GDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHEARKVDCEFLQSNNFAFGGINT 401
Cdd:PRK09116 321 GARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINT 400
|
....*
gi 15833595 402 SIIIK 406
Cdd:PRK09116 401 SLIFK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-408 |
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: 526.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIGDPIlTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:COG0304 80 REALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:COG0304 239 EELEHAKARGAKIYAEVVGYGASSDAYHITAPAPdgEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKVDCEFLQSNNFAF 396
Cdd:COG0304 319 VFGDhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 15833595 397 GGINTSIIIKRW 408
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-405 |
1.40e-158 |
|
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: 452.76 E-value: 1.40e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA-SGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIgDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:cd00834 80 EEALADAGLD-PEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:cd00834 239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPDPdgEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEARKVDCEFLQSNNFAF 396
Cdd:cd00834 319 VFGEhakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-LDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 15833595 397 GGINTSIII 405
Cdd:cd00834 398 GGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-406 |
1.48e-116 |
|
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: 345.62 E-value: 1.48e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDA-SDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIGDPIlTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPTS 162
Cdd:TIGR03150 80 KEAVEDSGLDIEEE-DAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 163 SACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:TIGR03150 159 TACATGTHAIGDAFRLIQRGDADVMIAGGAEAaITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCDAAHITQP--QRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:TIGR03150 239 EELEHAKARGAKIYAEIVGYGMSGDAYHITAPapEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKVDCEFLQSNNFAF 396
Cdd:TIGR03150 319 VFGDhayKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|
gi 15833595 397 GGINTSIIIK 406
Cdd:TIGR03150 398 GGTNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3-408 |
1.90e-113 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 337.92 E-value: 1.90e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDgLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSD-LAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLigDPILTSGE-TGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK07314 81 KQAVEDAGL--EITEENADrIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLI 240
Cdd:PRK07314 159 VTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 241 LEELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATA 318
Cdd:PRK07314 239 LEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPdgEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 319 TIYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKVDCEFLQSNNFA 395
Cdd:PRK07314 319 RVFGEhayKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEEC-DLDYVPNEARERKIDYALSNSFG 397
|
410
....*....|...
gi 15833595 396 FGGINTSIIIKRW 408
Cdd:PRK07314 398 FGGTNASLVFKRY 410
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-408 |
3.27e-95 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 291.52 E-value: 3.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 1 MTRRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEwQVYDGLHTLLGAPVDDFTL-------PEHY-TRKRIRAMG 72
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD-FPVGDLATKIGGQVPDLAEdaeagfdPDRYlDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 73 RVSQMSTRASELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNTGLFF 152
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 153 GLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEelcpseAAV-------FDTLFATSQH-NDAPKTTPSPFD 224
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTE------AAIdrvslagFAAARALSTRfNDAPEQASRPFD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 225 ENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAH 302
Cdd:PRK06333 235 RDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEdgEGARRAMLIALRQAGIPPEEVQHLNAH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 303 GTATDRGDMAESLATATIYGD--NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHE 380
Cdd:PRK06333 315 ATSTPVGDLGEVAAIKKVFGHvsGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANK 394
|
410 420
....*....|....*....|....*...
gi 15833595 381 ARKVDCEFLQSNNFAFGGINTSIIIKRW 408
Cdd:PRK06333 395 ARPMDMDYALSNGFGFGGVNASILFRRW 422
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-407 |
3.40e-89 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 275.84 E-value: 3.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDglHTL-LGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRA 81
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASD--FPVqIAGEITDFDPTEVMDPKEVKKADRFIQLGLKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 82 SELALEQAGLIGDPILtSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNIT----GTTYVQMMPHTTAVNtglfFGLRGR 157
Cdd:PRK08439 80 AREAMKDAGFLPEELD-AERFGVSSASGIGGLPNIEKNSIICFEKGPRKISpffiPSALVNMLGGFISIE----HGLKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 158 VIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGA 236
Cdd:PRK08439 155 NLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESaICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 237 GTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQYCMEQSLKIAGlsAQDIGYISAHGTATDRGDMAESLA 316
Cdd:PRK08439 235 GALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNETAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 317 TATIYGDNV---PLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEARKVDCEFLQSNN 393
Cdd:PRK08439 313 LKELFGSKEkvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECD-LDYIPNVARKAELNVVMSNS 391
|
410
....*....|....
gi 15833595 394 FAFGGINTSIIIKR 407
Cdd:PRK08439 392 FGFGGTNGVVIFKK 405
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
6-407 |
1.62e-85 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 266.56 E-value: 1.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 6 VITGMGgVTAfGENWqdvsARLLAYENAVRKMPE--------WQVYDGLHTLL-------GAPVD--DFTLPEHYTRKRi 68
Cdd:PTZ00050 1 VVTPLG-VGA-ESTW----EALIAGKSGIRKLTEfpkflpdcIPEQKALENLVaampcqiAAEVDqsEFDPSDFAPTKR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 69 raMGRVSQMSTRASELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTAVNT 148
Cdd:PTZ00050 74 --ESRATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 149 GLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFA-TSQHNDAPKTTPSPFDEN 226
Cdd:PTZ00050 152 AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEAsITPVSFAGFSRMRAlCTKYNDDPQRASRPFDKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 227 RDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRE--TMQYCMEQSLK-IAGLSAQDIGYISAHG 303
Cdd:PTZ00050 232 RAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDgrGARRCMENALKdGANININDVDYVNAHA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 304 TATDRGDMAESLATATIYGDN----VPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMH 379
Cdd:PTZ00050 312 TSTPIGDKIELKAIKKVFGDSgapkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEC-DLNLVQG 390
|
410 420 430
....*....|....*....|....*....|
gi 15833595 380 EAR--KVDCEFLQSNNFAFGGINTSIIIKR 407
Cdd:PTZ00050 391 KTAhpLQSIDAVLSTSFGFGGVNTALLFTK 420
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3-408 |
1.66e-83 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 261.14 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEW-------QVYdglhtllGAPvdDFTLPEHYTRKRIRAMGRVS 75
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFaemgmrsQVW-------GNV--KLDPTGLIDRKVMRFMGDAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 76 QMSTRASELALEQAGLIGDPIlTSGETGIAYGSSTGSTGPVSEFA-TMLTEKHTNNITGTTYVQMMPHTTAVNTGLFFGL 154
Cdd:PRK07967 73 AYAYLAMEQAIADAGLSEEQV-SNPRTGLIAGSGGGSTRNQVEAAdAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 155 RGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFA-TSQHNDAPKTTPSPFDENRDGLVIG 233
Cdd:PRK07967 152 KGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGAlSTKYNDTPEKASRAYDANRDGFVIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 234 EGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQYCMEQSLkiAGLSAqDIGYISAHGTATDRGDMAE 313
Cdd:PRK07967 232 GGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMAL--ATVDT-PIDYINTHGTSTPVGDVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 314 SLATATIYGDNVP-LSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHEARKVDCEFLQSN 392
Cdd:PRK07967 309 LGAIREVFGDKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSN 388
|
410
....*....|....*.
gi 15833595 393 NFAFGGINTSIIIKRW 408
Cdd:PRK07967 389 SFGFGGTNATLVFRRY 404
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-409 |
7.18e-79 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 250.09 E-value: 7.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 2 TRRVVITGMGGVTAFGENWQDVSARLLAYENAVR-------KMPEWQVYDGLHTL------LGAPVDDFTLPEHYTRK-- 66
Cdd:PLN02836 5 TRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRaltqddlKMKSEDEETQLYTLdqlpsrVAALVPRGTGPGDFDEElw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 67 -RIRAMGRVSQMSTRASELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPHTTA 145
Cdd:PLN02836 85 lNSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 146 VNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFA-TSQHNDAPKTTPSPF 223
Cdd:PLN02836 165 GHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESsIDALSIAGFSRSRAlSTKFNSCPTEASRPF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 224 DENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQ--YCMEQSLKIAGLSAQDIGYISA 301
Cdd:PLN02836 245 DCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGavLAMTRALQQSGLHPNQVDYVNA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 302 HGTATDRGDMAESLATATIYGD-----NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDY 376
Cdd:PLN02836 325 HATSTPLGDAVEARAIKTVFSEhatsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFV 404
|
410 420 430
....*....|....*....|....*....|...
gi 15833595 377 IMHEARKVDCEFLQSNNFAFGGINTSIIIKRWP 409
Cdd:PLN02836 405 PLTASKAMLIRAALSNSFGFGGTNASLLFTSPP 437
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-407 |
6.48e-77 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 244.53 E-value: 6.48e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDgLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTN-FSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGL-IGDPilTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITG----TTYVQMMphttAVNTGLFFGLRGR 157
Cdd:PRK08722 83 IQALDDSGLeVTEE--NAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPffvpSTIVNMI----AGNLSIMRGLRGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 158 VIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELC-PSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGA 236
Cdd:PRK08722 157 NIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKAStPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 237 GTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETM--QYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAE- 313
Cdd:PRK08722 237 GMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSggALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEi 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 314 ---SLATATIYGDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEARKVD-CEFL 389
Cdd:PRK08722 317 kgiKRALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLD-IDLVPHTARKVEsMEYA 395
|
410
....*....|....*...
gi 15833595 390 QSNNFAFGGINTSIIIKR 407
Cdd:PRK08722 396 ICNSFGFGGTNGSLIFKK 413
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-409 |
7.09e-74 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 236.84 E-value: 7.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 5 VVITGMGGVTAFG----ENWqdvsARLLAYENAVRKMPEWQVyDGLHTLLGAPVDdfTLPEhytrKRIRAMGRVSQMSTR 80
Cdd:PRK06501 13 VAVTGMGVVTSLGqgkaDNW----AALTAGESGIHTITRFPT-EGLRTRIAGTVD--FLPE----SPFGASALSEALARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 81 ASELALEQAGLI-GD----------PILTSGETGIAYGSSTGSTGPVSeFATMLTEKHTNnitgttyvqmmPHTTAVNTG 149
Cdd:PRK06501 82 AAEEALAQAGIGkGDfpgplflaapPVELEWPARFALAAAVGDNDAPS-YDRLLRAARGG-----------RFDALHERF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 150 LF----------FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAV-FDTLFATSQHNDAPKT 218
Cdd:PRK06501 150 QFgsiadrladrFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIrFSLLSALSTQNDPPEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 219 TPSPFDENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQ--PQRETMQYCMEQSLKIAGLSAQDI 296
Cdd:PRK06501 230 ASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRssPDGSPAIGAIRAALADAGLTPEQI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 297 GYISAHGTATDRGDMAESLATATIYGD---NVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgA 373
Cdd:PRK06501 310 DYINAHGTSTPENDKMEYLGLSAVFGErlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAI-P 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 15833595 374 LDYIMHEARKVDCEFLQSNNFAFGGINTSIIIKRWP 409
Cdd:PRK06501 389 LDVVPNVARDARVTAVLSNSFGFGGQNASLVLTAEP 424
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-408 |
2.72e-69 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 224.61 E-value: 2.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 5 VVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQV--YDGLHTLLGAPVDDFTlpEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVeeFDLPVRIGGHLLEEFD--HQLTRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGligDPILTSGETGIAYGSSTGSTGPVSEFATMLTEKHTNNITGTTyVQM-MPHTTAVNTGLFFGLRGRVIPT 161
Cdd:PRK07910 92 RRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLA-VQMyMPNGPAAAVGLERHAKAGVITP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE---ELCPseAAVFDTLFAT-SQHNDAPKTTPSPFDENRDGLVIGEGAG 237
Cdd:PRK07910 168 VSACASGSEAIAQAWRQIVLGEADIAICGGVEtriEAVP--IAGFAQMRIVmSTNNDDPAGACRPFDKDRDGFVFGEGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 238 TLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQ--YCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESL 315
Cdd:PRK07910 246 LMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERagHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 316 ATATIYGDNVP-LSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEARKVDCEFLQSNNF 394
Cdd:PRK07910 326 AINNALGGHRPaVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEID-LDVVAGEPRPGNYRYAINNSF 404
|
410
....*....|....
gi 15833595 395 AFGGINTSIIIKRW 408
Cdd:PRK07910 405 GFGGHNVALAFGRY 418
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-404 |
6.63e-63 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 211.38 E-value: 6.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVYDgLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQ-FPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLIGDPI--LTSGETGIAYGSSTGSTGPVSEFATMLTekhtnnitgTTYVQMMPH-----TTAVNTGLF---F 152
Cdd:PLN02787 208 KKALADGGITEDVMkeLDKTKCGVLIGSAMGGMKVFNDAIEALR---------ISYRKMNPFcvpfaTTNMGSAMLamdL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 153 GLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLV 231
Cdd:PLN02787 279 GWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAaIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 232 IGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRE--TMQYCMEQSLKIAGLSAQDIGYISAHGTATDRG 309
Cdd:PLN02787 359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEgaGVILCIEKALAQSGVSKEDVNYINAHATSTKAG 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 310 DMAESLATATIYGDNVPL--SSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHEARKVDCE 387
Cdd:PLN02787 439 DLKEYQALMRCFGQNPELrvNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIK 518
|
410
....*....|....*..
gi 15833595 388 FLQSNNFAFGGINTSII 404
Cdd:PLN02787 519 VALSNSFGFGGHNSSIL 535
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
4-407 |
4.52e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 199.51 E-value: 4.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 4 RVVITGMGGVTAFG---ENWQdvsaRLLAYENAVRkmpewqvydglhtlLGAPVDDF-TLPEHYTRKRIRAMGRVSQMST 79
Cdd:PRK05952 3 KVVVTGIGLVSALGdleQSWQ----RLLQGKSGIK--------------LHQPFPELpPLPLGLIGNQPSSLEDLTKTVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 80 RAselALEQAGLigDPILTsgETGIAYGSSTGSTGpvsEFATMLTEKHTNNITGTT------YVQMMPHTTAVNTGLFFG 153
Cdd:PRK05952 65 TA---ALKDAGL--TPPLT--DCGVVIGSSRGCQG---QWEKLARQMYQGDDSPDEeldlenWLDTLPHQAAIAAARQIG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 154 LRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEE-LCPSEAAVFDTLFATSqhndapKTTPSPFDENRDGLVI 232
Cdd:PRK05952 135 TQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALA------KTGAYPFDRQREGLVL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 233 GEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQ--RETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGD 310
Cdd:PRK05952 209 GEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEpdGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLND 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 311 MAESLATATIYGDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDpncGALDYIMhEARKVDCEFLQ 390
Cdd:PRK05952 289 QREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE---FDLNFVR-QAQQSPLQNVL 364
|
410
....*....|....*..
gi 15833595 391 SNNFAFGGINTSIIIKR 407
Cdd:PRK05952 365 CLSFGFGGQNAAIALGK 381
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-405 |
1.77e-57 |
|
"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: 193.42 E-value: 1.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSA---RLLAYENAVRKMPewQVYDGLHTLLGAPVDDFTLPEhYTRKRIRAMGRVSQMST 79
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVEEfweALREGRSGIAPVA--RLKSRFDRGVAGQIPTGDIPG-WDAKRTGIVDRTTLLAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 80 RASELALEQAGLIGDPILTSGETGIAYGSSTGSTGPVsEFATMLTEKHTNNITGTTyvqMMPHTTAVNT---GLFFGLRG 156
Cdd:cd00828 78 VATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFL-RRGGKLDARAVNPYVSPK---WMLSPNTVAGwvnILLLSSHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 157 RVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSQHNDAPKTTPSPFDENRDGLVIGEGA 236
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 237 GTLILEELEHAKARGATIYGEIVGFATNCDAAHITQP-QRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESL 315
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPaGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 316 ATATIY---GDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCgALDYIMHEARKV--DCEFLQ 390
Cdd:cd00828 314 AIAEVAgalGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV-EHLSVVGLSRDLnlKVRAAL 392
|
410
....*....|....*
gi 15833595 391 SNNFAFGGINTSIII 405
Cdd:cd00828 393 VNAFGFGGSNAALVL 407
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
154-408 |
1.28e-53 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 181.47 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 154 LRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEA-AVFDTLFATSQH-NDAPKTTPSPFDENRDGLV 231
Cdd:PRK14691 80 FKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSlAGFAAARALSTHfNSTPEKASRPFDTARDGFV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 232 IGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQR--ETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRG 309
Cdd:PRK14691 160 MGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEdgDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 310 DMAESLATATIYGDN--VPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALDYIMHEARKVDCE 387
Cdd:PRK14691 240 DLGEINAIKHLFGESnaLAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMT 319
|
250 260
....*....|....*....|.
gi 15833595 388 FLQSNNFAFGGINTSIIIKRW 408
Cdd:PRK14691 320 YALSNGFGFAGVNASILLKRW 340
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
5-407 |
1.75e-53 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 182.73 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 5 VVITGMGGVTAFGENWQDVSARLLAyenavRKMPEWQVYDG----LHTLLG--APVDDFTLPEHYTRKRIRamgrvsqmS 78
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRA-----GRASGMRPCDFwlvdLPTWVGevVGVELPALPAALAAFDCR--------N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 79 TRASELALEQaglIGDPILT------SGETGIAYGSSTGSTGpvsefATMLTEKHTNNITGTT-----YVQMMPHTTAVN 147
Cdd:PRK09185 71 NRLALLALQQ---IEPAVEAaiarygADRIGVVLGTSTSGIL-----EGELAYRRRDPAHGALpadyhYAQQELGSLADF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFDTLFATSqhndapKTTPSPFDENR 227
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLS------PQPCRPFSANR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 228 DGLVIGEGAGTLILEelehaKARGATI----YGEivgfatNCDAAHIT--QPQRETMQYCMEQSLKIAGLSAQDIGYISA 301
Cdd:PRK09185 217 DGINIGEAAAFFLLE-----REDDAAVallgVGE------SSDAHHMSapHPEGLGAILAMQQALADAGLAPADIGYINL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 302 HGTATDRGDMAESLATATIYGDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGAlDYIMHEA 381
Cdd:PRK09185 286 HGTATPLNDAMESRAVAAVFGDGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPP-LYLVENA 364
|
410 420
....*....|....*....|....*.
gi 15833595 382 RKVDCEFLQSNNFAFGGINTSIIIKR 407
Cdd:PRK09185 365 QALAIRYVLSNSFAFGGNNCSLIFGR 390
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
4-407 |
2.85e-46 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 164.05 E-value: 2.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 4 RVVITGMGGVTAFGENWQDVSARLLAYENAVRKM-------PEWQVYDGLHTLLGAPVDDFTLPEHYTRKRIRamgRVSQ 76
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMrrpgrqvPDDAGAGLASAFIGAELDSLALPERLDAKLLR---RASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 77 mSTRASELAL----EQAGLigDPILTSGeTGIAYGSStgstgpvsefatmltekhtnNITGTTYVQMMPH---------- 142
Cdd:PRK07103 80 -SAQAALAAAreawRDAAL--GPVDPDR-IGLVVGGS--------------------NLQQREQALVHETyrdrpaflrp 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 143 ---TTAVNTGLF------FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGA-EELCPSEAAVFDTLFA--TS 210
Cdd:PRK07103 136 sygLSFMDTDLVglcseqFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlMDLSYWECQALRSLGAmgSD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 211 QHNDAPKTTPSPFDENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITQPQRETMQYCMEQSLKIAG 290
Cdd:PRK07103 216 RFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 291 LSAQDIGYISAHGTATDRGDMAESLATATIYGDNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKP-DP 369
Cdd:PRK07103 296 LGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDE 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15833595 370 NC-----GALDYIMHEArkvdceflQSNNFAFGGINTSIIIKR 407
Cdd:PRK07103 376 RFrwvgsTAESARIRYA--------LSLSFGFGGINTALVLER 410
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
65-405 |
1.88e-39 |
|
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: 143.93 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 65 RKRIRAMG-RVSQMSTRASELALEQAGLigDPILTSGETGIAYgssTGSTGPVSEFATMLTEKHTNNITGTTYVQMMPhT 143
Cdd:cd00825 1 RAVITGLGsYVSILGFEAAERAIADAGL--SREYQKNPIVGVV---VGTGGGSPRFQVFGADAMRAVGPYVVTKAMFP-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 144 TAVNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCpseaAVFDTLFATSQHNDAPKTTPSPF 223
Cdd:cd00825 75 ASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA----APMDCEFDAMGALSTPEKASRTF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 224 DENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAH--ITQPQRETMQYCMEQSLKIAGLSAQDIGYISA 301
Cdd:cd00825 151 DAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGmgAFAPSAEGLARAAKEALAVAGLTVWDIDYLVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 302 HGTATDRGDMAESLATATIYGDN-VPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPncgALDYIMHE 380
Cdd:cd00825 231 HGTGTPIGDVKELKLLRSEFGDKsPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE---AGLNIVTE 307
|
330 340
....*....|....*....|....*
gi 15833595 381 ARKVDCEFLQSNNFAFGGINTSIII 405
Cdd:cd00825 308 TTPRELRTALLNGFGLGGTNATLVL 332
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
85-405 |
3.06e-39 |
|
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: 145.39 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 85 ALEQAGLIGDPILTSgETGIAYGSSTGSTGPVSEFATMLTEKHTnnITGTTyvqmmphtTAVNTGL---FFGLRGRVIPT 161
Cdd:cd00833 98 ALEDAGYSPESLAGS-RTGVFVGASSSDYLELLARDPDEIDAYA--ATGTS--------RAFLANRisyFFDLRGPSLTV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 162 SSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFdtlfATSQHNDAPKTTPSPFDENRDGLVIGEGAGTLIL 241
Cdd:cd00833 167 DTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVG----FSKAGMLSPDGRCRPFDADADGYVRGEGVGVVVL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 242 EELEHAKARGATIYGEIVGFATNCD--AAHITQPQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATAT 319
Cdd:cd00833 243 KRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 320 IYG------DNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGALD---YIMHEARKVDCEFLQ 390
Cdd:cd00833 323 VFGgsrsadQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsplRVPTEARPWPAPAGP 402
|
330
....*....|....*....
gi 15833595 391 S----NNFAFGGINTSIII 405
Cdd:cd00833 403 RragvSSFGFGGTNAHVIL 421
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-247 |
2.89e-32 |
|
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: 122.36 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPE--WQVYDGLH----------TLLGAPVDDFTLPEHYTRKRIR- 69
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKLYDppsriagkiyTKWGGLDDIFDFDPLFFGISPRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 70 --AMGRVSQMSTRASELALEQAGLIGDPILTSgETGIAYGSSTGSTGPVsefaTMLTEKHTNNITGTTYVQMMPHTTAVN 147
Cdd:pfam00109 81 aeRMDPQQRLLLEAAWEALEDAGITPDSLDGS-RTGVFIGSGIGDYAAL----LLLDEDGGPRRGSPFAVGTMPSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 148 TGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSQHNDApkttpSPFDEN 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGPC-----KAFDPF 230
|
250 260
....*....|....*....|.
gi 15833595 227 RDGLVIGEGAGTLILEELEHA 247
Cdd:pfam00109 231 ADGFVRGEGVGAVVLKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-382 |
8.18e-31 |
|
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: 121.70 E-value: 8.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGENWQDVSARLLAYENAVRKMPEWQVyDGLHTLLGAPVDDFTLPEHYTRKRIRAMGRVSQMSTRAS 82
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDP-SGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 83 ELALEQAGLigDPILTSG-ETGIAYGSSTGSTgpvsEFatmlTEKHTNNI--TGTTYV---QMMPHTTAVNTG---LFFG 153
Cdd:cd00832 80 DWALADAGV--DPAALPPyDMGVVTASAAGGF----EF----GQRELQKLwsKGPRHVsayQSFAWFYAVNTGqisIRHG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 154 LRGrviPTSSACT---SGSQAIGYAWEAIRHGyQTVMVAGGAEE-LCP--SEAAVFDTLFATSqhnDAPKTTPSPFDENR 227
Cdd:cd00832 150 MRG---PSGVVVAeqaGGLDALAQARRLVRRG-TPLVVSGGVDSaLCPwgWVAQLSSGRLSTS---DDPARAYLPFDAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 228 DGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAHITqPQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATD 307
Cdd:cd00832 223 AGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGS-GRPPGLARAIRLALADAGLTPEDVDVVFADAAGVP 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833595 308 RGDMAESLATATIYG-DNVPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLNKPDPNCGaLDYIMHEAR 382
Cdd:cd00832 302 ELDRAEAAALAAVFGpRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG-LDLVTGRPR 376
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
255-365 |
1.15e-28 |
|
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: 108.42 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 255 YGEIVGFATNCDAAHITQ--PQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATDRGDMAESLATATIYGDN-----VPL 327
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLtaPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGarkqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15833595 328 SSLKSYFGHTLGACGALEAWMSLQMMREGWFAPTLNLN 365
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
151-370 |
7.73e-26 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 110.35 E-value: 7.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 151 FFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELCPSEAAVFdtlfatsqHNDAPKTTPS----PFDEN 226
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFIL--------FSKGGMLSPDgrcrAFDAD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 227 RDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAH--ITQPQRETMQYCMEQSLKIAGLSAQDIGYISAHGT 304
Cdd:COG3321 232 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGT 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833595 305 ATDRGDMAESLATATIYGDN------VPLSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLNKPDPN 370
Cdd:COG3321 312 GTPLGDPIEAAALTAAFGQGrpadqpCAIGSVKSNIGHLEAAAGV----AGLikavLALRHGVLPPTLHFETPNPH 383
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
131-361 |
9.30e-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: 93.66 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 131 ITGTTY-VQMMPHTTAVNTGLFFGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGAEELcpseaavfdtlfat 209
Cdd:cd00327 33 IVGTTGgSGEFSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 210 sqhndapkttpspfdenrdglVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCD-AAHITQPQRETMQYCMEQSLKI 288
Cdd:cd00327 99 ---------------------VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGLARAARKALEG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833595 289 AGLSAQDIGYISAHGTATDRGDMAESLATATIYGDN-VPLSSLKSYFGHTLGACGALEAWMSLQMMREGWFAPT 361
Cdd:cd00327 158 AGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRsPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT 231
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
152-408 |
1.53e-19 |
|
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: 91.22 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 152 FGLRGRVIPTSSACTSGSQAIGYAWEAIRHGYQTVMVAGGaeeLCPSEAAvfdTLFATSQHNDAPKT--TPSPFDENRDG 229
Cdd:TIGR02813 193 FDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGG---VCTDNSP---FMYMSFSKTPAFTTneDIQPFDIDSKG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 230 LVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDA--AHITQPQRETMQYCMEQSLKIAGLSAQDIGYISAHGTATD 307
Cdd:TIGR02813 267 MMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 308 RGDMAESLATATIYG-DN-----VPLSSLKSYFGH---TLGACGALEAWMSLQmmrEGWFAPTLNLNKPDPNCGALD--- 375
Cdd:TIGR02813 347 AGDVAEFGGLVSVFSqDNdqkqhIALGSVKSQIGHtksTAGTAGMIKAVLALH---HKVLPPTINVDQPNPKLDIENspf 423
|
250 260 270
....*....|....*....|....*....|....*....
gi 15833595 376 YIMHEAR----KVDCEFLQS--NNFAFGGINTSIIIKRW 408
Cdd:TIGR02813 424 YLNTETRpwmqREDGTPRRAgiSSFGFGGTNFHMVLEEY 462
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
147-405 |
4.56e-13 |
|
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: 69.28 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 147 NTGLFFGLRGR----VIPTssACTSGSQAIGYAWEAIRHGYQTVMVAGGAE-ELCPSEAAVFDTLFATSqhndapkttPS 221
Cdd:smart00825 77 RTGVFVGVSSSdysvTVDT--ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS---------PD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 222 ----PFDENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNCDAAH--ITQPQREtmqycmeqslkiaglsAQd 295
Cdd:smart00825 146 grckTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGP----------------AQ- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 296 igyisahgtatdrgdmaeslatatiygdnVPLSSLKSYFGHTLGACGAleawMSL----QMMREGWFAPTLNLNKPDPNc 371
Cdd:smart00825 209 -----------------------------LLIGSVKSNIGHLEAAAGV----AGLikvvLALKHGVIPPTLHFETPNPH- 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15833595 372 galdyIMHEARKVdcEFLQS---------------NNFAFGGINTSIII 405
Cdd:smart00825 255 -----IDLEESPL--RVPTEltpwpppgrprragvSSFGFGGTNAHVIL 296
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
3-340 |
1.43e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 46.87 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 3 RRVVITGMGGVTAFGE----NWQDVSARLLAYENAVRKMPEWQVydglHTLlgAPVD-DFTLPEhytRKRIRAMGRVSQM 77
Cdd:PRK06519 6 NDVVITGIGLVSSLGEgldaHWNALSAGRPQPNVDTETFAPYPV----HPL--PEIDwSQQIPK---RGDQRQMETWQRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 78 STRASELALEQAGLIGDPILTS----------GE------TGIAYGSSTGSTGPVsefatMLTEKHTNNITGTTYVQMMP 141
Cdd:PRK06519 77 GTYAAGLALDDAGIKGNEELLStmdmivaaggGErdiavdTAILNEARKRNDRGV-----LLNERLMTELRPTLFLAQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 142 HTTAVNTGLFFGLrgrvipTSSACT------SGSQAIGYAWEAIRHGYQTVMVAGGAEElcpseAAVFDTLFATS--QHN 213
Cdd:PRK06519 152 NLLAGNISIVHKV------TGSSRTfmgeesAGVSAIEIAFARIASGQSDHALVGGAYN-----AERPDMLLLYElgGLL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833595 214 DAPKTTP--SPFDENRDGLVIGEGAGTLILEELEHAKARGATIYGEIVGFATNcdaahitQPQRE--TMQYCMEQSLKIA 289
Cdd:PRK06519 221 LKGGWAPvwSRGGEDGGGFILGSGGAFLVLESREHAEARGARPYARISGVESD-------RARRApgDLEASLERLLKPA 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15833595 290 GLSAQDIGYISAhgtATDRGDMAESLATATIYGDNVPLSSLKSYFGHTLGA 340
Cdd:PRK06519 294 GGLAAPTAVISG---ATGAHPATAEEKAALEAALAGPVRGIGTLFGHTMEA 341
|
|
| |
