|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
3-405 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 807.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSYEQYDGLNTKLAAPILDFELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGLIGNDVLTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFFGLKGRVIPTS 162
Cdd:PRK09116 82 ELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIPTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 163 SACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTLVLE 242
Cdd:PRK09116 162 SACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 243 EYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNATANALG 322
Cdd:PRK09116 242 ELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQATAAVFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 323 -KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYIAGQGRELDVKYLMSNNFAFGGINTS 401
Cdd:PRK09116 322 aRMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGALDYIMGEAREIDTEYVMSNNFAFGGINTS 401
|
....
gi 491603036 402 IIFK 405
Cdd:PRK09116 402 LIFK 405
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-406 |
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: 515.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSYEQyDGLNTKLAAPILDFELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGLIGNDVlTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFFGLKGRVIPTS 162
Cdd:COG0304 80 REALADAGLDLDEV-DPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 163 SACTSGSQAIGYAYEAIKHGYQTVMVAGGAE-ELCPTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTLVL 241
Cdd:COG0304 159 TACASGAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 242 EEYEHAVARGAKIYAEVIGFASNCDAAHVTQ--PQMETMQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNATAN 319
Cdd:COG0304 239 EELEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 320 ALG----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELDVKYLMSNNFAF 395
Cdd:COG0304 319 VFGdhayKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPEC-DLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|.
gi 491603036 396 GGINTSIIFKK 406
Cdd:COG0304 398 GGHNASLVFKR 408
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-404 |
9.58e-160 |
|
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: 455.46 E-value: 9.58e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSyEQYDGLNTKLAAPILDFELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITR-FDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGLIGNDvLTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFFGLKGRVIPTS 162
Cdd:cd00834 80 EEALADAGLDPEE-LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 163 SACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELC-PTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTLVL 241
Cdd:cd00834 159 TACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 242 EEYEHAVARGAKIYAEVIGFASNCDAAHVTQP--QMETMQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNATAN 319
Cdd:cd00834 239 ESLEHAKARGAKIYAEILGYGASSDAYHITAPdpDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 320 ALG----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELDVKYLMSNNFAF 395
Cdd:cd00834 319 VFGehakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPEC-DLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 491603036 396 GGINTSIIF 404
Cdd:cd00834 398 GGHNASLVF 406
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-406 |
7.53e-119 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 351.40 E-value: 7.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 2 NRRVVVTGMSGVTAFGNDWQSVEPKLRDCQNA----TQYMPSyeqydGLNTKLAAPILDFELPKHYKRKQVRGMGRVSKL 77
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGigpiTHFDTS-----DLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 78 ATVATENALSQAGLIGNDVLTNgQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATtYVQMM-PHTTAVNVGLFFGLKG 156
Cdd:PRK07314 76 GIAAAKQAVEDAGLEITEENAD-RIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPF-FVPMAiINMAAGHVSIRYGAKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 157 RVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEE-LCPTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEG 235
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAaITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 236 AGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQM--ETMQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAE 313
Cdd:PRK07314 234 AGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPdgEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 314 SNATANALG----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELDVKYLM 389
Cdd:PRK07314 314 TQAIKRVFGehayKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEEC-DLDYVPNEARERKIDYAL 392
|
410
....*....|....*..
gi 491603036 390 SNNFAFGGINTSIIFKK 406
Cdd:PRK07314 393 SNSFGFGGTNASLVFKR 409
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-406 |
6.57e-92 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 282.39 E-value: 6.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSYEQYDgLNTKLAAPILDFELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASD-FPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGLIGNDVLTNgQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAIT----ATTYVQMMPHTTAVNvglfFGLKGRV 158
Cdd:PRK08439 81 REAMKDAGFLPEELDAE-RFGVSSASGIGGLPNIEKNSIICFEKGPRKISpffiPSALVNMLGGFISIE----HGLKGPN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 159 IPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEE-LCPTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAG 237
Cdd:PRK08439 156 LSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESaICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 238 TLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQICMEMAMQNAGIPaeKIDYVSAHGTATDRGDIAESNAT 317
Cdd:PRK08439 236 ALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 318 ANALG---KVP-ISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELDVKYLMSNNF 393
Cdd:PRK08439 314 KELFGskeKVPpVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPEC-DLDYIPNVARKAELNVVMSNSF 392
|
410
....*....|...
gi 491603036 394 AFGGINTSIIFKK 406
Cdd:PRK08439 393 GFGGTNGVVIFKK 405
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-407 |
4.80e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 280.73 E-value: 4.80e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 1 MNRRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSyEQYDGLNTKLAAPILD--------FELPKHYKRKQVRGMG 72
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTD-FPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 73 RVSKLATVATENALSQAGLIGNDVLTNGQTGIAYGSSTGSTDAIgAFGVMLNEKTTKAITATTYVQMM-PHTTAVNVGLF 151
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAI-AEAVRTLDSRGPRRLSPFTIPSFlTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 152 FGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTES-AVFDTLFATSLK-NEYPKSTPRPYDSDRDG 229
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSlAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 230 LVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQM--ETMQICMEMAMQNAGIPAEKIDYVSAHGTATD 307
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEdgEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 308 RGDIAESNATANALG---KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYIAGQGRELD 384
Cdd:PRK06333 320 VGDLGEVAAIKKVFGhvsGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGLDVVANKARPMD 399
|
410 420
....*....|....*....|...
gi 491603036 385 VKYLMSNNFAFGGINTSIIFKKM 407
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRW 422
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3-407 |
5.39e-91 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 280.02 E-value: 5.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSYEQYdGLNTKLA-APILDFElpKHYKRKQVRGMGRVSKLATVA 81
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEM-GMRSQVWgNVKLDPT--GLIDRKVMRFMGDASAYAYLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 82 TENALSQAGLIGNDVlTNGQTGIAYGSSTGSTDAI-GAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFFGLKGRVIP 160
Cdd:PRK07967 79 MEQAIADAGLSEEQV-SNPRTGLIAGSGGGSTRNQvEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 161 TSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTESAVFDTLFATSLK-NEYPKSTPRPYDSDRDGLVIGEGAGTL 239
Cdd:PRK07967 158 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 240 VLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQICMEMAMQNAGIPaekIDYVSAHGTATDRGDIAESNATAN 319
Cdd:PRK07967 238 VVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATVDTP---IDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 320 ALG-KVP-ISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYIAGQGRELDVKYLMSNNFAFGG 397
Cdd:PRK07967 315 VFGdKSPaISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTDNAELTTVMSNSFGFGG 394
|
410
....*....|
gi 491603036 398 INTSIIFKKM 407
Cdd:PRK07967 395 TNATLVFRRY 404
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
73-407 |
5.49e-85 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 265.40 E-value: 5.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 73 RVSKLATVATENALSQAGLIGNDVLTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFF 152
Cdd:PTZ00050 76 RATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 153 GLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEE-LCPTESAVFDTLFATSLK-NEYPKSTPRPYDSDRDGL 230
Cdd:PTZ00050 156 KLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEAsITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 231 VIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQME--TMQICMEMAMQNAG-IPAEKIDYVSAHGTATD 307
Cdd:PTZ00050 236 VMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDgrGARRCMENALKDGAnININDVDYVNAHATSTP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 308 RGDIAESNATANALG-----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYI--AGQG 380
Cdd:PTZ00050 316 IGDKIELKAIKKVFGdsgapKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAEC-DLNLVqgKTAH 394
|
330 340
....*....|....*....|....*..
gi 491603036 381 RELDVKYLMSNNFAFGGINTSIIFKKM 407
Cdd:PTZ00050 395 PLQSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-407 |
1.03e-80 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 254.16 E-value: 1.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNdwqSVEPKLRDCQNATQYMPSYEQYDGLN--TKLAAPILDFELPKHYKRKQVRGMGRVSKLATV 80
Cdd:PRK08722 4 RRVVVTGMGMLSPVGN---TVESSWKALLAGQSGIVNIEHFDTTNfsTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 81 ATENALSQAGLIGNDVlTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLFFGLKGRVIP 160
Cdd:PRK08722 81 AGIQALDDSGLEVTEE-NAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 161 TSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELC-PTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTL 239
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKAStPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 240 VLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETM--QICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNAT 317
Cdd:PRK08722 240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSggALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 318 ANALG-----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELD-VKYLMSN 391
Cdd:PRK08722 320 KRALGeagskQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGL-DIDLVPHTARKVEsMEYAICN 398
|
410
....*....|....*.
gi 491603036 392 NFAFGGINTSIIFKKM 407
Cdd:PRK08722 399 SFGFGGTNGSLIFKKM 414
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-404 |
5.22e-75 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 240.08 E-value: 5.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFG----NDWQSV---EPKLRDCQNATQYMPSYEQ------YDGLNTKLAAPILDFELPKHYKRK--- 66
Cdd:PLN02836 6 RRVVVTGLGLVTPLGcgveTTWRRLiagECGVRALTQDDLKMKSEDEetqlytLDQLPSRVAALVPRGTGPGDFDEElwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 67 QVRGMGRVSKLATVATENALSQAGLIGNDVLTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAV 146
Cdd:PLN02836 86 NSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 147 NVGLFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTES-AVFDTLFATSLK-NEYPKSTPRPYD 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSiAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 225 SDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQ--ICMEMAMQNAGIPAEKIDYVSAH 302
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGavLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 303 GTATDRGDIAESNATANAL------GKVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYI 376
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFsehatsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420
....*....|....*....|....*...
gi 491603036 377 AGQGRELDVKYLMSNNFAFGGINTSIIF 404
Cdd:PLN02836 406 LTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-406 |
9.64e-69 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 223.07 E-value: 9.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 5 VVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYM--PSYEQYDgLNTKLAAPILDfELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLddPFVEEFD-LPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGliGNDVLTNgQTGIAYGSSTGSTDAIgAFGVMLNEKTTKAITATTYVQM-MPHTTAVNVGLFFGLKGRVIPT 161
Cdd:PRK07910 92 RRVWENAG--SPEVDTN-RLMVSIGTGLGSAEEL-VFAYDDMRARGLRAVSPLAVQMyMPNGPAAAVGLERHAKAGVITP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 162 SSACTSGSQAIGYAYEAIKHGYQTVMVAGGAE---ELCPTesAVFDTLFAT-SLKNEYPKSTPRPYDSDRDGLVIGEGAG 237
Cdd:PRK07910 168 VSACASGSEAIAQAWRQIVLGEADIAICGGVEtriEAVPI--AGFAQMRIVmSTNNDDPAGACRPFDKDRDGFVFGEGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 238 TLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQI--CMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESN 315
Cdd:PRK07910 246 LMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAghAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 316 ATANALG--KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAGQGRELDVKYLMSNNF 393
Cdd:PRK07910 326 AINNALGghRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEI-DLDVVAGEPRPGNYRYAINNSF 404
|
410
....*....|...
gi 491603036 394 AFGGINTSIIFKK 406
Cdd:PRK07910 405 GFGGHNVALAFGR 417
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-404 |
1.02e-67 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 223.70 E-value: 1.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSYEQYDgLNTKLAAPILDFELPKHYKRKQVRGMGRVSKLATVAT 82
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQ-FPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 83 ENALSQAGLIGN--DVLTNGQTGIAYGSSTGS----TDAIGAFGVmlnekttkaitatTYVQMMPHTT---AVNVG---- 149
Cdd:PLN02787 208 KKALADGGITEDvmKELDKTKCGVLIGSAMGGmkvfNDAIEALRI-------------SYRKMNPFCVpfaTTNMGsaml 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 150 -LFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEE-LCPTESAVFDTLFATSLKNEYPKSTPRPYDSDR 227
Cdd:PLN02787 275 aMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAaIIPIGLGGFVACRALSQRNDDPTKASRPWDMNR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 228 DGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQI--CMEMAMQNAGIPAEKIDYVSAHGTA 305
Cdd:PLN02787 355 DGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVilCIEKALAQSGVSKEDVNYINAHATS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 306 TDRGDIAESNATANALGKVP---ISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCgDLDYIAG-QGR 381
Cdd:PLN02787 435 TKAGDLKEYQALMRCFGQNPelrVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGV-DTKVLVGpKKE 513
|
410 420
....*....|....*....|...
gi 491603036 382 ELDVKYLMSNNFAFGGINTSIIF 404
Cdd:PLN02787 514 RLDIKVALSNSFGFGGHNSSILF 536
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-404 |
7.45e-62 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 205.25 E-value: 7.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 5 VVVTGMSGVTAFGN----DWQSVEPKLRDCQNATQYmPSyeqyDGLNTKLAAPIlDFeLPkhykrkqVRGMGRVS---KL 77
Cdd:PRK06501 13 VAVTGMGVVTSLGQgkadNWAALTAGESGIHTITRF-PT----EGLRTRIAGTV-DF-LP-------ESPFGASAlseAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 78 ATVATENALSQAGLIGNDVltNGQTGIA-------------YGSSTGSTDAIGafgvmlnekttkaitattYVQMM---- 140
Cdd:PRK06501 79 ARLAAEEALAQAGIGKGDF--PGPLFLAappvelewparfaLAAAVGDNDAPS------------------YDRLLraar 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 141 --PHTTAVNVGLF----------FGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTESAV-FDTLF 207
Cdd:PRK06501 139 ggRFDALHERFQFgsiadrladrFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIrFSLLS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 208 ATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQ--PQMETMQICMEMA 285
Cdd:PRK06501 219 ALSTQNDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRssPDGSPAIGAIRAA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 286 MQNAGIPAEKIDYVSAHGTATDRGDIAESNATANALG----KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTL 361
Cdd:PRK06501 299 LADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGerlaSIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTI 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 491603036 362 NLENLDEQCgDLDYIAGQGRELDVKYLMSNNFAFGGINTSIIF 404
Cdd:PRK06501 379 NYDNPDPAI-PLDVVPNVARDARVTAVLSNSFGFGGQNASLVL 420
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-402 |
7.07e-54 |
|
"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: 184.18 E-value: 7.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGNDWQSVEPKLRD-CQNATQYMPSYEQYDGLNTKLAAPILDFELP-KHYKRkqVRGMGRVSKLATV 80
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVEEFWEAlREGRSGIAPVARLKSRFDRGVAGQIPTGDIPgWDAKR--TGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 81 ATENALSQAGLIGNDVLTNGQTGIAYGSSTGSTDAIGAFGVMLNEKTTKAITATTYVQmmPHTTAVNVGLFFGLKGRVIP 160
Cdd:cd00828 79 ATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLS--PNTVAGWVNILLLSSHGPIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 161 T-SSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTESAVFDTLFATSLKNEYPKSTPRPYDSDRDGLVIGEGAGTL 239
Cdd:cd00828 157 TpVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 240 VLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMET-MQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNATA 318
Cdd:cd00828 237 VLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKgIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 319 NALGK----VPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYIAG-QGRELDVKYLMSNNF 393
Cdd:cd00828 317 EVAGAlgapLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLsRDLNLKVRAALVNAF 396
|
....*....
gi 491603036 394 AFGGINTSI 402
Cdd:cd00828 397 GFGGSNAAL 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
145-406 |
3.30e-53 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 180.31 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 145 AVNVGLFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTES-AVFDTLFATSLK-NEYPKSTPRP 222
Cdd:PRK14691 71 AGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSlAGFAAARALSTHfNSTPEKASRP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 223 YDSDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQ--PQMETMQICMEMAMQNAGIPAEKIDYVS 300
Cdd:PRK14691 151 FDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSgaEDGDGAYRAMKIALRQAGITPEQVQHLN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 301 AHGTATDRGDIAESNATANALGK---VPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLDYIA 377
Cdd:PRK14691 231 AHATSTPVGDLGEINAIKHLFGEsnaLAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIA 310
|
250 260
....*....|....*....|....*....
gi 491603036 378 GQGRELDVKYLMSNNFAFGGINTSIIFKK 406
Cdd:PRK14691 311 GNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
136-404 |
3.41e-50 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 173.87 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 136 YVQMMPHTTAVNVGLFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCPTESAVFDTLFATSlkney 215
Cdd:PRK09185 131 YAQQELGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLS----- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 216 pkSTP-RPYDSDRDGLVIGEGAGTLVLE-EYEHAVArgakiyaeVIGFASNCDAAHVT--QPQMETMQICMEMAMQNAGI 291
Cdd:PRK09185 206 --PQPcRPFSANRDGINIGEAAAFFLLErEDDAAVA--------LLGVGESSDAHHMSapHPEGLGAILAMQQALADAGL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 292 PAEKIDYVSAHGTATDRGDIAESNATANALG-KVPISSLKSYFGHTLGACGAIEA---WLGLEMmhtgWFNP-TLNLENL 366
Cdd:PRK09185 276 APADIGYINLHGTATPLNDAMESRAVAAVFGdGVPCSSTKGLTGHTLGAAGAVEAaicWLALRH----GLPPhGWNTGQP 351
|
250 260 270
....*....|....*....|....*....|....*...
gi 491603036 367 DEQCGDLDYIAgQGRELDVKYLMSNNFAFGGINTSIIF 404
Cdd:PRK09185 352 DPALPPLYLVE-NAQALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
4-402 |
8.70e-49 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 169.85 E-value: 8.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 4 RVVVTGMSGVTAFGN---DWQsvepKLRDCQNATQY------MPSYEQydGLNTKLAAPIldfelpkhykrkqvrgmgrv 74
Cdd:PRK05952 3 KVVVTGIGLVSALGDleqSWQ----RLLQGKSGIKLhqpfpeLPPLPL--GLIGNQPSSL-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 75 SKLATVATENALSQAGLigndVLTNGQTGIAYGSSTG---STDAIGAFGVMLNEKTTKAITATTYVQMMPHTTAVNVGLF 151
Cdd:PRK05952 57 EDLTKTVVTAALKDAGL----TPPLTDCGVVIGSSRGcqgQWEKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAARQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 152 FGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEE-LCPTESAVFDTLFATSLKNEYPkstprpYDSDRDGL 230
Cdd:PRK05952 133 IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYP------FDRQREGL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 231 VIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQME--TMQICMEMAMQNAGIPAEKIDYVSAHGTATDR 308
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDgkSAIAAIQQCLARSGLTPEDIDYIHAHGTATRL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 309 GDIAESNATANALG-KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDeqcGDLDYIAgQGRELDVKY 387
Cdd:PRK05952 287 NDQREANLIQALFPhRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE---FDLNFVR-QAQQSPLQN 362
|
410
....*....|....*
gi 491603036 388 LMSNNFAFGGINTSI 402
Cdd:PRK05952 363 VLCLSFGFGGQNAAI 377
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
65-403 |
4.80e-45 |
|
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: 158.57 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 65 RKQVRGMG-RVSKLATVATENALSQAGLiGNDVLTNGQTGIAYGSSTGStdaiGAFGVMLNEKTTKAITATTYVQMMPhT 143
Cdd:cd00825 1 RAVITGLGsYVSILGFEAAERAIADAGL-SREYQKNPIVGVVVGTGGGS----PRFQVFGADAMRAVGPYVVTKAMFP-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 144 TAVNVGLFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELCptesAVFDTLFATSLKNEYPKSTPRPY 223
Cdd:cd00825 75 ASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELA----APMDCEFDAMGALSTPEKASRTF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 224 DSDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQM--ETMQICMEMAMQNAGIPAEKIDYVSA 301
Cdd:cd00825 151 DAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPsaEGLARAAKEALAVAGLTVWDIDYLVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 302 HGTATDRGDIAESNATANALG--KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEqcgDLDYIAGQ 379
Cdd:cd00825 231 HGTGTPIGDVKELKLLRSEFGdkSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE---AGLNIVTE 307
|
330 340
....*....|....*....|....
gi 491603036 380 GRELDVKYLMSNNFAFGGINTSII 403
Cdd:cd00825 308 TTPRELRTALLNGFGLGGTNATLV 331
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
4-406 |
1.11e-44 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 159.81 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 4 RVVVTGMSGVTAFGNDWQSVEPKLRDCQNATQYMPSY------EQYDGLNTK-LAAPILDFELPKHYKRKQVRGMGRVSK 76
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPgrqvpdDAGAGLASAfIGAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 77 LATVATENALSQAGLigNDVLTNgQTGIAYGSSTgstdaigafgVMLNEKTTKAITATTYVQMMPHTTAVN------VGL 150
Cdd:PRK07103 83 AALAAAREAWRDAAL--GPVDPD-RIGLVVGGSN----------LQQREQALVHETYRDRPAFLRPSYGLSfmdtdlVGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 151 F---FGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGA-EELCPTESAVFDTLFA--TSLKNEYPKSTPRPYD 224
Cdd:PRK07103 150 CseqFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGAlMDLSYWECQALRSLGAmgSDRFADEPEAACRPFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 225 SDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQICMEMAMQNAGIPAEKIDYVSAHGT 304
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 305 ATDRGDIAESNATANA-LGKVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLEN-LDEQCgdlDYIAGQGRE 382
Cdd:PRK07103 310 GSPLGDETELAALFASgLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERF---RWVGSTAES 386
|
410 420
....*....|....*....|....
gi 491603036 383 LDVKYLMSNNFAFGGINTSIIFKK 406
Cdd:PRK07103 387 ARIRYALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
151-403 |
3.14e-38 |
|
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: 142.70 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 151 FFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAE-ELCPTESAVFDTLFATSlkneyPKSTPRPYDSDRDG 229
Cdd:cd00833 156 FFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFSKAGMLS-----PDGRCRPFDADADG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 230 LVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCD--AAHVTQPQMETMQICMEMAMQNAGIPAEKIDYVSAHGTATD 307
Cdd:cd00833 231 YVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 308 RGDIAESNATANALGK-------VPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGDLD---YIA 377
Cdd:cd00833 311 LGDPIEVEALAKVFGGsrsadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEsplRVP 390
|
250 260 270
....*....|....*....|....*....|
gi 491603036 378 GQGRELDVKYLMS----NNFAFGGINTSII 403
Cdd:cd00833 391 TEARPWPAPAGPRragvSSFGFGGTNAHVI 420
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-247 |
6.54e-29 |
|
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: 113.11 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMSGVTAFGND----WQSvepkLRDCQNATQYMPSY----EQYDGLNTKLAAPILDFELPKHYK---------- 64
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDpeefWEN----LLEGRDGISEIPADrwdpDKLYDPPSRIAGKIYTKWGGLDDIfdfdplffgi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 65 -RKQVRGMGRVSKLATVATENALSQAGLIGNDvLTNGQTGIAYGSSTGSTDAIgafgVMLNEKTTKAITATTYVQMMPHT 143
Cdd:pfam00109 77 sPREAERMDPQQRLLLEAAWEALEDAGITPDS-LDGSRTGVFIGSGIGDYAAL----LLLDEDGGPRRGSPFAVGTMPSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 144 TAVNVGLFFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAE-ELCPTESAVFDTLFATSlkneyPKSTPRP 222
Cdd:pfam00109 152 IAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLS-----PDGPCKA 226
|
250 260
....*....|....*....|....*
gi 491603036 223 YDSDRDGLVIGEGAGTLVLEEYEHA 247
Cdd:pfam00109 227 FDPFADGFVRGEGVGAVVLKRLSDA 251
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
255-364 |
2.17e-27 |
|
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: 104.96 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 255 YAEVIGFASNCDAAHVTQ--PQMETMQICMEMAMQNAGIPAEKIDYVSAHGTATDRGDIAESNATANALGK------VPI 326
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLtaPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSgarkqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 491603036 327 SSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLE 364
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-383 |
7.17e-26 |
|
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: 107.83 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 3 RRVVVTGMsGVTA---FGND--WQSVepkLRDCQN---ATQYMPSyeqydGLNTKLAAPILDFELPKHYKRKQVRGMGRV 74
Cdd:cd00832 1 RRAVVTGI-GVVApngLGVEeyWKAV---LDGRSGlgpITRFDPS-----GYPARLAGEVPDFDAAEHLPGRLLPQTDRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 75 SKLATVATENALSQAGLiGNDVLTNGQTGIAYGSSTGSTDaigaFGvmLNEKTTKAITATTYV---QMMPHTTAVNVG-- 149
Cdd:cd00832 72 TRLALAAADWALADAGV-DPAALPPYDMGVVTASAAGGFE----FG--QRELQKLWSKGPRHVsayQSFAWFYAVNTGqi 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 150 -LFFGLKGrviPTSSACT---SGSQAIGYAYEAIKHGyQTVMVAGGAEE-LCPTESA--VFDTLFATSlknEYPKSTPRP 222
Cdd:cd00832 145 sIRHGMRG---PSGVVVAeqaGGLDALAQARRLVRRG-TPLVVSGGVDSaLCPWGWVaqLSSGRLSTS---DDPARAYLP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 223 YDSDRDGLVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTqPQMETMQICMEMAMQNAGIPAEKIDYVSAH 302
Cdd:cd00832 218 FDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPGS-GRPPGLARAIRLALADAGLTPEDVDVVFAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 303 GTATDRGDIAESNATANALG--KVPISSLKSYFGHTLGACGAIEAWLGLEMMHTGWFNPTLNLENLDEQCGdLDYIAGQG 380
Cdd:cd00832 297 AAGVPELDRAEAAALAAVFGprGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG-LDLVTGRP 375
|
...
gi 491603036 381 REL 383
Cdd:cd00832 376 RPA 378
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
151-403 |
3.96e-24 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 104.95 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 151 FFGLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAE-ELCPTESAVFDTLFATSlkneyPKSTPRPYDSDRDG 229
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNlMLTPESFILFSKGGMLS-----PDGRCRAFDADADG 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 230 LVIGEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAH--VTQPQMETMQICMEMAMQNAGIPAEKIDYVSAHGTATD 307
Cdd:COG3321 235 YVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTP 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 308 RGDIAEsnatANALGKV-----------PISSLKSYFGHTLGACGA---IEAWLgleMMHTGWFNPTLNLENLDEQCgDL 373
Cdd:COG3321 315 LGDPIE----AAALTAAfgqgrpadqpcAIGSVKSNIGHLEAAAGVaglIKAVL---ALRHGVLPPTLHFETPNPHI-DF 386
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 491603036 374 D----YIAGQGRELD---------VkylmsNNFAFGGINTSII 403
Cdd:COG3321 387 EnspfYVNTELRPWPagggprragV-----SSFGFGGTNAHVV 424
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
153-353 |
4.12e-21 |
|
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: 91.74 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 153 GLKGRVIPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEELcptesavfdtlfatslkneypkstprpydsdrdglVI 232
Cdd:cd00327 56 ISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEF-----------------------------------VF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 233 GEGAGTLVLEEYEHAVARGAKIYAEVIGFASNCDAAHVTQPQMETMQI-CMEMAMQNAGIPAEKIDYVSAHGTATDRGDI 311
Cdd:cd00327 101 GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVSGEGLArAARKALEGAGLTPSDIDYVEAHGTGTPIGDA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491603036 312 AE--SNATANALGKVPISSLKSYFGHTLGACG-AIEAWLGLEMMH 353
Cdd:cd00327 181 VElaLGLDPDGVRSPAVSATLIMTGHPLGAAGlAILDELLLMLEH 225
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
164-403 |
7.34e-12 |
|
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: 65.43 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 164 ACTSGSQAIGYAYEAIKHGYQTVMVAGGAE-ELCPTESAVFDTLFATSlkneyPKSTPRPYDSDRDGLVIGEGAGTLVLE 242
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 243 EYEHAVARGAKIYAEVIGFASNCDAAhvtqpqmetmqicmemamqNAGIpaekidyvsahgtatdrgdiaesnaTA-NAL 321
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGR-------------------SNGI-------------------------TApSGP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 322 GKVPISSLKSYFGHTLGA---CGAIEAwlgLEMMHTGWFNPTLNLENLDEQCgDLD----YIAGQGREL---DVKYLMS- 390
Cdd:smart00825 207 AQLLIGSVKSNIGHLEAAagvAGLIKV---VLALKHGVIPPTLHFETPNPHI-DLEesplRVPTELTPWpppGRPRRAGv 282
|
250
....*....|...
gi 491603036 391 NNFAFGGINTSII 403
Cdd:smart00825 283 SSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
167-263 |
1.68e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 46.49 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 167 SGSQAIGYAYEAIKHGYQTVMVAGGAEElcpTESavFDTLFATSLKNEYPKSTPRPY----DSDRDGLVIGEGAGTLVLE 242
Cdd:PRK06519 177 AGVSAIEIAFARIASGQSDHALVGGAYN---AER--PDMLLLYELGGLLLKGGWAPVwsrgGEDGGGFILGSGGAFLVLE 251
|
90 100
....*....|....*....|.
gi 491603036 243 EYEHAVARGAKIYAEVIGFAS 263
Cdd:PRK06519 252 SREHAEARGARPYARISGVES 272
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
221-342 |
3.45e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 39.31 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491603036 221 RPYDSDRDGLV-------IGEGAGTLVLEEYEHAVARGAKIYAEVIGFAsncDAAHVTQPQMETMQICMEMAMQNAGIPA 293
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYA---DAAQAPELFTTAPALAIPKALKHAGLEA 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491603036 294 EKIDYVsahgtatdrgDIAESNAT---ANA--LG----KVPISSLKSYFGHTLGACGA 342
Cdd:PLN02644 309 SQVDYY----------EINEAFSVvalANQklLGldpeKVNVHGGAVSLGHPIGCSGA 356
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
164-193 |
4.30e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 39.00 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|
gi 491603036 164 ACTSGSQAIGYAYEAIKHGYQTVMVAGGAE 193
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVE 112
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
145-195 |
4.74e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 38.96 E-value: 4.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491603036 145 AVNVGLFFGLKGRV--IPTSSACTSGSQAIGYAYEAIKHGYQTVMVAGGAEEL 195
Cdd:PRK07661 68 ARNIGALAGLPYTVpaITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESM 120
|
|
| |
