|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
5-417 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 701.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDA-----SDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGIDkVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPN 164
Cdd:TIGR03150 76 LAAAKEAVEDSGLD-IEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 165 IPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDGAG 244
Cdd:TIGR03150 155 HAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 245 VVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPyAP---GQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQ 321
Cdd:TIGR03150 235 VLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAP-APegeGAARAMRAALKDAGI--NPEDVDYINAHGTSTPLGDKA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 322 ESQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKIDYVL 401
Cdd:TIGR03150 312 ETKAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYAL 391
|
410
....*....|....*.
gi 754252887 402 NNSFGFGGTNGSVIFK 417
Cdd:TIGR03150 392 SNSFGFGGTNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
4-419 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 684.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 4 NRRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYY 83
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDT-----SDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 84 GIAAANEALKDAGIDkVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGP 163
Cdd:PRK07314 76 GIAAAKQAVEDAGLE-ITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 164 NIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDGA 243
Cdd:PRK07314 155 NHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 244 GVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQ--ERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQ 321
Cdd:PRK07314 235 GILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEgaARAMKLALKDAGI--NPEDIDYINAHGTSTPAGDKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 322 ESQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKIDYVL 401
Cdd:PRK07314 313 ETQAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYAL 392
|
410
....*....|....*...
gi 754252887 402 NNSFGFGGTNGSVIFKKI 419
Cdd:PRK07314 393 SNSFGFGGTNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
5-419 |
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: 646.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDA-----SGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGIDkVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPN 164
Cdd:COG0304 76 LAAAREALADAGLD-LDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 165 IPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDGAG 244
Cdd:COG0304 155 YTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 245 VVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPyAP---GQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQ 321
Cdd:COG0304 235 VLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAP-APdgeGAARAMRAALKDAGL--SPEDIDYINAHGTSTPLGDAA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 322 ESQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKIDYVL 401
Cdd:COG0304 312 ETKAIKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYAL 391
|
410
....*....|....*...
gi 754252887 402 NNSFGFGGTNGSVIFKKI 419
Cdd:COG0304 392 SNSFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
5-416 |
0e+00 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 597.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDA-----SGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGIDKvSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPN 164
Cdd:cd00834 76 LAAAEEALADAGLDP-EELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 165 IPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDGAG 244
Cdd:cd00834 155 YTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 245 VVVLEEYERAKARGAKIYAEVVGFGMSADGYHMT--MPYAPGQERCIQNALADAGLEnnPDAIDYVNAHGTSTPLGDVQE 322
Cdd:cd00834 235 VLVLESLEHAKARGAKIYAEILGYGASSDAYHITapDPDGEGAARAMRAALADAGLS--PEDIDYINAHGTSTPLNDAAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 323 SQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKIDYVLN 402
Cdd:cd00834 313 SKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALS 392
|
410
....*....|....
gi 754252887 403 NSFGFGGTNGSVIF 416
Cdd:cd00834 393 NSFGFGGHNASLVF 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-419 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 513.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 3 SNRRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCY 82
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDT-----TNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 83 YGIAAANEALKDAGIdKVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRG 162
Cdd:PRK08722 77 YGIAAGIQALDDSGL-EVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDG 242
Cdd:PRK08722 156 PNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 243 AGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPY--APGQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDV 320
Cdd:PRK08722 236 AGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSedGSGGALAMEAAMRDAGV--TGEQIGYVNAHGTSTPAGDV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 321 QESQVVEKVIGQY-RKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMK-ID 398
Cdd:PRK08722 314 AEIKGIKRALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsME 393
|
410 420
....*....|....*....|.
gi 754252887 399 YVLNNSFGFGGTNGSVIFKKI 419
Cdd:PRK08722 394 YAICNSFGFGGTNGSLIFKKM 414
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
5-419 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 511.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDA-----SDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGIDkVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPN 164
Cdd:PRK08439 77 LKAAREAMKDAGFL-PEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 165 IPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDGAG 244
Cdd:PRK08439 156 LSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 245 VVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQERCIQNALADAGlenNPDaIDYVNAHGTSTPLGDVQESQ 324
Cdd:PRK08439 236 ALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAG---NPK-IDYINAHGTSTPYNDKNETA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 325 VVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKIDYVLNNS 404
Cdd:PRK08439 312 ALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNS 391
|
410
....*....|....*
gi 754252887 405 FGFGGTNGSVIFKKI 419
Cdd:PRK08439 392 FGFGGTNGVVIFKKV 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
3-418 |
2.51e-179 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 506.46 E-value: 2.51e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 3 SNRRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKN--------FDVDALVGKKDA 74
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPV-----GDLATKIGGQVPDlaedaeagFDPDRYLDPKDQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 75 KRVDPFCYYGIAAANEALKDAGIDKVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGII 154
Cdd:PRK06333 77 RKMDRFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 155 SINHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTR-NDDPQGASRPWDKD 233
Cdd:PRK06333 157 SIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 234 RDGFVLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQ--ERCIQNALADAGLEnnPDAIDYVNAH 311
Cdd:PRK06333 237 RDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEgaRRAMLIALRQAGIP--PEEVQHLNAH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 312 GTSTPLGDVQESQVVEKVIGQYRKdLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCN-LDYAAN 390
Cdd:PRK06333 315 ATSTPVGDLGEVAAIKKVFGHVSG-LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVAN 393
|
410 420
....*....|....*....|....*...
gi 754252887 391 AAKKMKIDYVLNNSFGFGGTNGSVIFKK 418
Cdd:PRK06333 394 KARPMDMDYALSNGFGFGGVNASILFRR 421
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
14-419 |
1.94e-158 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 453.38 E-value: 1.94e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 14 MVTPLGNDVPTTWANILAGKSGVETITGFDTPAPD-----------ISEFKVRFAARIKNFDVDALVGKKDaKRVDPFCY 82
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDcipeqkalenlVAAMPCQIAAEVDQSEFDPSDFAPT-KRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 83 YGIAAANEALKDAGIDKVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRG 162
Cdd:PTZ00050 80 FAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTR-NDDPQGASRPWDKDRDGFVLGD 241
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVMGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 242 GAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQ--ERCIQNALADAGLENNPDaIDYVNAHGTSTPLGD 319
Cdd:PTZ00050 240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRgaRRCMENALKDGANININD-VDYVNAHATSTPIGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 320 VQESQVVEKVIGQY-RKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMK-- 396
Cdd:PTZ00050 319 KIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLqs 398
|
410 420
....*....|....*....|...
gi 754252887 397 IDYVLNNSFGFGGTNGSVIFKKI 419
Cdd:PTZ00050 399 IDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-416 |
2.20e-144 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 418.04 E-value: 2.20e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 3 SNRRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTPAPD---------ISEFKVRFAARI------KNFDVDA 67
Cdd:PLN02836 4 PTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMKSedeetqlytLDQLPSRVAALVprgtgpGDFDEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 68 LVgkkDAKRVDPFCYYGIAAANEALKDAGIDKVSEEDSYKFGVCVSSGIGGI-ETLETTKAVIDTKGpSKISPFCIPSSI 146
Cdd:PLN02836 84 WL---NSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSItDILEAAQLICEKRL-RRLSPFFVPRIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 147 VNMLSGIISINHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTR-NDDPQG 225
Cdd:PLN02836 160 INMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 226 ASRPWDKDRDGFVLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQER--CIQNALADAGLenNPD 303
Cdd:PLN02836 240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAvlAMTRALQQSGL--HPN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 304 AIDYVNAHGTSTPLGDVQESQVVEKVIGQY--RKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHN--- 378
Cdd:PLN02836 318 QVDYVNAHATSTPLGDAVEARAIKTVFSEHatSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERpdp 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 754252887 379 -LDDG-CNLdyaaNAAKKMKIDYVLNNSFGFGGTNGSVIF 416
Cdd:PLN02836 398 iFDDGfVPL----TASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
5-416 |
6.82e-130 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 384.72 E-value: 6.82e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDC-----SQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGI--DKVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKgPSKISPFCIPSSIVNMLSGIISINHGLRG 162
Cdd:PLN02787 204 LTAGKKALADGGIteDVMKELDKTKCGVLIGSAMGGMKVFNDAIEALRIS-YRKMNPFCVPFATTNMGSAMLAMDLGWMG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKDRDGFVLGDG 242
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 243 AGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQE--RCIQNALADAGLenNPDAIDYVNAHGTSTPLGDV 320
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGviLCIEKALAQSGV--SKEDVNYINAHATSTKAGDL 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 321 QESQVVEKVIGQyRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAK-KMKIDY 399
Cdd:PLN02787 441 KEYQALMRCFGQ-NPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKeRLDIKV 519
|
410
....*....|....*..
gi 754252887 400 VLNNSFGFGGTNGSVIF 416
Cdd:PLN02787 520 ALSNSFGFGGHNSSILF 536
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
5-417 |
4.41e-108 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 324.25 E-value: 4.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdISEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDR----YDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAG-IDKVSEEDSyKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPfcipSSIVNMLSGIISIN----HG 159
Cdd:PRK09116 78 TRASELALEDAGlLGDPILTDG-RMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMPHTTAVNvglfFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 160 LRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEK--ASNAIGmggFAAARALSTRNDDPQGASRPWDKDRDGF 237
Cdd:PRK09116 153 LKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEElcPTEAAV---FDTLFATSTRNDAPELTPRPFDANRDGL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 238 VLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQERCIQNALADAGLEnnPDAIDYVNAHGTSTPL 317
Cdd:PRK09116 230 VIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLA--PEDIGYVNAHGTATDR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 318 GDVQESQVVEKVIGqyrKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGC-NLDYAANAAKKMK 396
Cdd:PRK09116 308 GDIAESQATAAVFG---ARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREID 384
|
410 420
....*....|....*....|.
gi 754252887 397 IDYVLNNSFGFGGTNGSVIFK 417
Cdd:PRK09116 385 TEYVMSNNFAFGGINTSLIFK 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
5-418 |
7.62e-100 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 303.52 E-value: 7.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETitgfdtpAPDISE--FKVRFAARIKnFDVDALVGKKDAKRVDPFCY 82
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITF-------SPEFAEmgMRSQVWGNVK-LDPTGLIDRKVMRFMGDASA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 83 YGIAAANEALKDAGI--DKVSEEDSykfGVCVSSGIGGIET-LETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHG 159
Cdd:PRK07967 74 YAYLAMEQAIADAGLseEQVSNPRT---GLIAGSGGGSTRNqVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 160 LRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGgFAAARALSTR-NDDPQGASRPWDKDRDGFV 238
Cdd:PRK07967 151 IKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 239 LGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQERCIQNALADAgleNNPdaIDYVNAHGTSTPLG 318
Cdd:PRK07967 230 IAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMALATV---DTP--IDYINTHGTSTPVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 319 DVQESQVVEKVIGQyrKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDD---GCNLdyAANAAKKM 395
Cdd:PRK07967 305 DVKELGAIREVFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPqaaGMPI--VTETTDNA 380
|
410 420
....*....|....*....|...
gi 754252887 396 KIDYVLNNSFGFGGTNGSVIFKK 418
Cdd:PRK07967 381 ELTTVMSNSFGFGGTNATLVFRR 403
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
7-418 |
1.07e-95 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 293.17 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 7 VVVTGLGMVTPLGNDVPTTWANILAGKSGVET-----ITGFDTPapdisefkVRFAARIKNfDVDALVGKKDAKRVDPFC 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEFDLP--------VRIGGHLLE-EFDHQLTRVELRRMSYLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 82 YYGIAAANEALKDAGIDKVseeDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLR 161
Cdd:PRK07910 85 RMSTVLGRRVWENAGSPEV---DTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 162 GPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARA-LSTRNDDPQGASRPWDKDRDGFVLG 240
Cdd:PRK07910 162 AGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 241 DGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQE--RCIQNALADAGLEnnPDAIDYVNAHGTSTPLG 318
Cdd:PRK07910 242 EGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERagHAMTRAIELAGLT--PGDIDHVNAHATGTSVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 319 DVQESQVVEKVIGQYRKdlVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKMKID 398
Cdd:PRK07910 320 DVAEGKAINNALGGHRP--AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYR 397
|
410 420
....*....|....*....|
gi 754252887 399 YVLNNSFGFGGTNGSVIFKK 418
Cdd:PRK07910 398 YAINNSFGFGGHNVALAFGR 417
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
103-418 |
1.28e-93 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 285.08 E-value: 1.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 103 EDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPNIPIVTACTTGTHNIGMAA 182
Cdd:PRK14691 23 EKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 183 RLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTR-NDDPQGASRPWDKDRDGFVLGDGAGVVVLEEYERAKARGAKI 261
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 262 YAEVVGFGMSADGYHMT--MPYAPGQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQESQVVEKVIGQyRKDLVM 339
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTsgAEDGDGAYRAMKIALRQAGI--TPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 340 SSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCN-LDYAANAAKKMKIDYVLNNSFGFGGTNGSVIFKK 418
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
7-416 |
1.07e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 283.06 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 7 VVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVdpfcyyGIA 86
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPT-----EGLRTRIAGTVDFLPESPFGASALSEAL------ARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 87 AANEALKDAGIDK-------------VSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGi 153
Cdd:PRK06501 82 AAEEALAQAGIGKgdfpgplflaappVELEWPARFALAAAVGDNDAPSYDRLLRAARGGRFDALHERFQFGSIADRLAD- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 154 isiNHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDDPQGASRPWDKD 233
Cdd:PRK06501 161 ---RFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 234 RDGFVLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTM--PYAPGQERCIQNALADAGLenNPDAIDYVNAH 311
Cdd:PRK06501 238 RDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRssPDGSPAIGAIRAALADAGL--TPEQIDYINAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 312 GTSTPLGDVQESQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANA 391
Cdd:PRK06501 316 GTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNV 395
|
410 420
....*....|....*....|....*
gi 754252887 392 AKKMKIDYVLNNSFGFGGTNGSVIF 416
Cdd:PRK06501 396 ARDARVTAVLSNSFGFGGQNASLVL 420
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-414 |
9.37e-83 |
|
"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: 259.29 E-value: 9.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTT---WANILAGKSGvetitgFDTPAPDISEFKVRFAARIKNFDVDAlvgkKDAKR---VD 78
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSG------IAPVARLKSRFDRGVAGQIPTGDIPG----WDAKRtgiVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 79 PFCYYGIAAANEALKDAGIDKVSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSivNMLSGIISINH 158
Cdd:cd00828 71 RTTLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLSP--NTVAGWVNILL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 159 GL-RGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAiGMGGFAAARALSTRNDDPQGASRPWDKDRDGF 237
Cdd:cd00828 149 LSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEE-GLSGFANMGALSTAEEEPEEMSRPFDETRDGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 238 VLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMT-MPYAPGQERCIQNALADAGLenNPDAIDYVNAHGTSTP 316
Cdd:cd00828 228 VEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSvPAGGKGIARAIRTALAKAGL--SLDDLDVISAHGTSTP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 317 LGDVQESQVVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDY--AANAAKK 394
Cdd:cd00828 306 ANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSvvGLSRDLN 385
|
410 420
....*....|....*....|
gi 754252887 395 MKIDYVLNNSFGFGGTNGSV 414
Cdd:cd00828 386 LKVRAALVNAFGFGGSNAAL 405
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
6-414 |
1.29e-72 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 232.63 E-value: 1.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 6 RVVVTGLGMVTPLGnDVPTTWANILAGKSGVEtitgFDTPAPDISEFKVrfaariknfdvdALVGKKDAkrvdPFCYYGI 85
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIK----LHQPFPELPPLPL------------GLIGNQPS----SLEDLTK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 86 AAANEALKDAGIDkVSEEDSykfGVCVSS--GIGGI-ETLETTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRG 162
Cdd:PRK05952 62 TVVTAALKDAGLT-PPLTDC---GVVIGSsrGCQGQwEKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAARQIGTQG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALStrnddPQGASrPWDKDRDGFVLGDG 242
Cdd:PRK05952 138 PVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAY-PFDRQREGLVLGEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 243 AGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQE--RCIQNALADAGLEnnPDAIDYVNAHGTSTPLGDV 320
Cdd:PRK05952 212 GAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSaiAAIQQCLARSGLT--PEDIDYIHAHGTATRLNDQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 321 QESQVVEKVIGQyrkDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLdyaANAAKKMKIDYV 400
Cdd:PRK05952 290 REANLIQALFPH---RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNF---VRQAQQSPLQNV 363
|
410
....*....|....
gi 754252887 401 LNNSFGFGGTNGSV 414
Cdd:PRK05952 364 LCLSFGFGGQNAAI 377
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
6-415 |
2.45e-72 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 232.83 E-value: 2.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 6 RVVVTGLGMVTPLGNDVPTTWANILAGKSGVETIT-------GFDTPAPDISEFKVRFAARIKNFD-VDAL---VGKKDA 74
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedrwdadGYYPDPGKPGKTYTRRGGFLDDVDaFDAAffgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 75 KRVDPFCYYGIAAANEALKDAGIDKVSEEDSyKFGVCVssGIGGIETLETTkavidTKGPSKISPFCIPSSIVNMLSGII 154
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGS-RTGVFV--GASSSDYLELL-----ARDPDEIDAYAATGTSRAFLANRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 155 SINHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALStrnddPQGASRPWDKDR 234
Cdd:cd00833 154 SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFDADA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 235 DGFVLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGY--HMTMPYAPGQERCIQNALADAGLenNPDAIDYVNAHG 312
Cdd:cd00833 229 DGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQAALIRRAYARAGV--DPSDIDYVEAHG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 313 TSTPLGDVQESQVVEKVIGQYRKD---LVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAA 389
Cdd:cd00833 307 TGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESP 386
|
410 420 430
....*....|....*....|....*....|....
gi 754252887 390 NAAKKMKIDYVLN--------NSFGFGGTNGSVI 415
Cdd:cd00833 387 LRVPTEARPWPAPagprragvSSFGFGGTNAHVI 420
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
5-415 |
1.19e-68 |
|
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: 222.62 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITGFDTpapdiSEFKVRFAARIKNFDVDALVGKKDAKRVDPFCYYG 84
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDP-----SGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 IAAANEALKDAGIDKvSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFcipSSI-----VNmlSGIISINHG 159
Cdd:cd00832 76 LAAADWALADAGVDP-AALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAY---QSFawfyaVN--TGQISIRHG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 160 LRGPNIPIVTACTTGTHNIGMAARLIASGdADAMLAGGSEKASNAIGMGGFAAARALSTrNDDPQGASRPWDKDRDGFVL 239
Cdd:cd00832 150 MRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 240 GDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGyhmtmPYAPGQE----RCIQNALADAGLenNPDAIDYVNAHGTST 315
Cdd:cd00832 228 GEGGAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRPpglaRAIRLALADAGL--TPEDVDVVFADAAGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 316 PLGDVQESQVVEKVIGQYRkdLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAKKM 395
Cdd:cd00832 301 PELDRAEAAALAAVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPA 378
|
410 420
....*....|....*....|
gi 754252887 396 KIDYVLNNSFGFGGTNGSVI 415
Cdd:cd00832 379 ALRTALVLARGRGGFNSALV 398
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
6-418 |
2.46e-66 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 217.21 E-value: 2.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 6 RVVVTGLGMVTPLGNDVPTTWANILAGKSGVETITgfDTPAPDISEFKVRFAARIKNFDVDALVgkkDAKRVDPFCYYG- 84
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMR--RPGRQVPDDAGAGLASAFIGAELDSLA---LPERLDAKLLRRa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 -------IAAANEALKDAGIDkvsEEDSYKFGVCVS-SGIGGIETLETTKAVIDTkgPSKISPFCIPSSIVNMLSGIISI 156
Cdd:PRK07103 78 slsaqaaLAAAREAWRDAALG---PVDPDRIGLVVGgSNLQQREQALVHETYRDR--PAFLRPSYGLSFMDTDLVGLCSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 157 NHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRN--DDPQGASRPWDKDR 234
Cdd:PRK07103 153 QFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 235 DGFVLGDGAGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHMTMPYAPGQERCIQNALADAGLEnnPDAIDYVNAHGTS 314
Cdd:PRK07103 233 DGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGLG--PEDIDYVNPHGTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 315 TPLGDVQEsqvVEKVIGQYRKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINL-HNLDDGCNldYAANAAK 393
Cdd:PRK07103 311 SPLGDETE---LAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLdEPIDERFR--WVGSTAE 385
|
410 420
....*....|....*....|....*
gi 754252887 394 KMKIDYVLNNSFGFGGTNGSVIFKK 418
Cdd:PRK07103 386 SARIRYALSLSFGFGGINTALVLER 410
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-254 |
1.31e-61 |
|
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: 199.78 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGvetITGFDTPAPDISEF---KVRFAARIKN--------FDVDAL---VG 70
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDG---ISEIPADRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLffgIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 71 KKDAKRVDPFCYYGIAAANEALKDAGIDKVSEEDSyKFGVCVSSGIGGIETLETtkaVIDTKGPSKISPFCIPSSIvNML 150
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGS-RTGVFIGSGIGDYAALLL---LDEDGGPRRGSPFAVGTMP-SVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 151 SGIISINHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTrnDDPQGASRPW 230
Cdd:pfam00109 153 AGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF 230
|
250 260
....*....|....*....|....
gi 754252887 231 DkdrDGFVLGDGAGVVVLEEYERA 254
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
159-416 |
3.98e-61 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 202.76 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 159 GLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASnaiGM--GGFAAARALSTrnddpqGASRPWDKDRDG 236
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLC---RLtlNGFNSLESLSP------QPCRPFSANRDG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 237 FVLGDGAGVVVLEeyerakaRGAKIYAEVVGFGMSADGYHMTMPYaP---GQERCIQNALADAGLEnnPDAIDYVNAHGT 313
Cdd:PRK09185 219 INIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPH-PeglGAILAMQQALADAGLA--PADIGYINLHGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 314 STPLGDVQESQVVEKVIGQYrkdLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANAAK 393
Cdd:PRK09185 289 ATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQ 365
|
250 260
....*....|....*....|...
gi 754252887 394 KMKIDYVLNNSFGFGGTNGSVIF 416
Cdd:PRK09185 366 ALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
83-415 |
5.97e-55 |
|
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: 185.15 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 83 YGIAAANEALKDAGIDKvSEEDSYKFGVCVSSGIGGIETLETTKAVIDTKGPSKISPFCIPSSivnmlSGIISINHGLRG 162
Cdd:cd00825 14 LGFEAAERAIADAGLSR-EYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLGIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALStrnddPQGASRPWDKDRDGFVLGDG 242
Cdd:cd00825 88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 243 AGVVVLEEYERAKARGAKIYAEVVGFGMSADGYHM--TMPYAPGQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDV 320
Cdd:cd00825 163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGMgaFAPSAEGLARAAKEALAVAGL--TVWDIDYLVAHGTGTPIGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 321 QESQVVEKVIGQYRkdLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDgcNLDYAANAAKKMKIDYV 400
Cdd:cd00825 241 KELKLLRSEFGDKS--PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*
gi 754252887 401 LNNSFGFGGTNGSVI 415
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
88-415 |
3.53e-52 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 188.16 E-value: 3.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 88 ANEALKDAGIDKVSEEDSyKFGVCVssGIGGietleTTKAVIDTKGPSKISPFCIPSSIVNMLSGIISINHGLRGPNIPI 167
Cdd:COG3321 99 AWEALEDAGYDPESLAGS-RTGVFV--GASS-----NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 168 VTACTTG---THnigMAARLIASGDADAMLAGGSeKASNAIGMG-GFAAARALStrnddPQGASRPWDKDRDGFVLGDGA 243
Cdd:COG3321 171 DTACSSSlvaVH---LACQSLRSGECDLALAGGV-NLMLTPESFiLFSKGGMLS-----PDGRCRAFDADADGYVRGEGV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 244 GVVVLEEYERAKARGAKIYAEVVGFGMSADGYH--MTMPYAPGQERCIQNALADAGLEnnPDAIDYVNAHGTSTPLGDVQ 321
Cdd:COG3321 242 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGVD--PATVDYVEAHGTGTPLGDPI 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 322 ESQVVEKVIGQYRKD---LVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDgcNLDYAANAAkkmkid 398
Cdd:COG3321 320 EAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNP--HIDFENSPF------ 391
|
330 340 350
....*....|....*....|....*....|...
gi 754252887 399 YVLN----------------NSFGFGGTNGSVI 415
Cdd:COG3321 392 YVNTelrpwpagggprragvSSFGFGGTNAHVV 424
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
262-377 |
4.54e-43 |
|
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: 146.94 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 262 YAEVVGFGMSADGYHMTM--PYAPGQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQESQVVEKVIGQYRKD--L 337
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLtaPNGEGQARAIRRALADAGV--DPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 754252887 338 VMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLH 377
Cdd:pfam02801 79 AIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
83-415 |
6.51e-33 |
|
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: 124.48 E-value: 6.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 83 YGIAAANEALKDAGIDKvseedSYKFGVCVSSGIGGIEtlettkavidtkgpskispFCIPSSIVNMLSGIISinhglrG 162
Cdd:cd00327 10 LGFEAAEQAIADAGLSK-----GPIVGVIVGTTGGSGE-------------------FSGAAGQLAYHLGISG------G 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 163 PNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKasnaigmggfaaaralstrnddpqgasrpwdkdrdgFVLGDG 242
Cdd:cd00327 60 PAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 243 AGVVVLEEYERAKARGAKIYAEVVGFGMSADG-YHMTMPYAPGQERCIQNALADAGLenNPDAIDYVNAHGTSTPLGDVQ 321
Cdd:cd00327 104 AAAAVVESEEHALRRGAHPQAEIVSTAATFDGaSMVPAVSGEGLARAARKALEGAGL--TPSDIDYVEAHGTGTPIGDAV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 322 ESQVVEKVIGQyrKDLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTinlhnlDDGCNLdyaanaakkmkidyVL 401
Cdd:cd00327 182 ELALGLDPDGV--RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------PREPRT--------------VL 239
|
330
....*....|....
gi 754252887 402 NNSFGFGGTNGSVI 415
Cdd:cd00327 240 LLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
169-415 |
2.06e-21 |
|
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: 93.55 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 169 TACTTGTHNIGMAARLIASGDADAMLAGGSekasNAI---GMG-GFAAARALStrnddPQGASRPWDKDRDGFVLGDGAG 244
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGV----NLIlspDTFvGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 245 VVVLEEYERAKARGAKIYAEVVGFGMSADGYH--MTMPYAPGQerciqnaladaglennpdaidyvnahgtstplgdvqe 322
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAPSGPAQ------------------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 323 sqvvekvigqyrkdLVMSSTKSMTGHLLGAAGAIESIFSVLAIRDQVAPPTINLHNLDDGCNLDYAANaakkmkidYVLN 402
Cdd:smart00825 209 --------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPL--------RVPT 266
|
250 260
....*....|....*....|....*....
gi 754252887 403 ----------------NSFGFGGTNGSVI 415
Cdd:smart00825 267 eltpwpppgrprragvSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-267 |
5.09e-14 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 73.06 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 1 MKSNRRVVVTGLGMVTPLGNDVPTTWaNILAGKSGvetitgfdTPAPDISEFK---VRFAARIknfDVDALVGKK-DAKR 76
Cdd:PRK06519 2 RMQPNDVVITGIGLVSSLGEGLDAHW-NALSAGRP--------QPNVDTETFApypVHPLPEI---DWSQQIPKRgDQRQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 77 VDPFCYYGIAAANEALKDAGIdKVSEEDSYKFGVCVSSGIG------------GIETLETTKAVIDTKGPSKISPFCIPS 144
Cdd:PRK06519 70 METWQRLGTYAAGLALDDAGI-KGNEELLSTMDMIVAAGGGerdiavdtailnEARKRNDRGVLLNERLMTELRPTLFLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 145 SIVNMLSGIISINHGLRGPNIPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASN-----AIGMGGFAAaralstr 219
Cdd:PRK06519 149 QLSNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERpdmllLYELGGLLL------- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 754252887 220 nddpQGASRP-WDK---DRDGFVLGDGAGVVVLEEYERAKARGAKIYAEVVG 267
Cdd:PRK06519 222 ----KGGWAPvWSRggeDGGGFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
87-311 |
6.95e-06 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 47.64 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 87 AANEALKDAGIDKVSEEdsykfGVCVSSGIGGIETLettkavidtkgpskispfcipssivnMLSGIISINHGLRGpnIP 166
Cdd:cd00829 23 AARAALDDAGLEPADID-----AVVVGNAAGGRFQS--------------------------FPGALIAEYLGLLG--KP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 167 IV---TACTTGTHNIGMAARLIASGDADAMLAGGSEKAS--------------------------NAIGMGGFAA----- 212
Cdd:cd00829 70 ATrveAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSdvptgdeaggrasdlewegpeppgglTPPALYALAArrymh 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 213 ---------------ARALSTRNDDPQG----------ASRP-WD--KDRDGFVLGDGAGVVVLEEYERAKARGAKiYAE 264
Cdd:cd00829 150 rygttredlakvavkNHRNAARNPYAQFrkpitvedvlNSRMiADplRLLDCCPVSDGAAAVVLASEERARELTDR-PVW 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 754252887 265 VVGFGMSADGYHMT----MPYAPGQERCIQNALADAGLEnnPDAIDYVNAH 311
Cdd:cd00829 229 ILGVGAASDTPSLSerddFLSLDAARLAARRAYKMAGIT--PDDIDVAELY 277
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
170-243 |
2.51e-05 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 46.21 E-value: 2.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754252887 170 ACTTGTHNIGMAARLIASGDADAMLAGGSEKASNA-IGMGGFAAARALSTRNDDPQGASRPWDkDRDGFVLGDGA 243
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRApMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGETA 160
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
84-239 |
5.68e-05 |
|
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: 45.16 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 84 GIAAANEALKDAGIDKvSEEDSYKFGVCVSSGIGGIetlettkavidtkgpskispfciPSSIVNMLSGIisinhglrGP 163
Cdd:cd00751 26 GAAVIKALLERAGLDP-EEVDDVIMGNVLQAGEGQN-----------------------PARQAALLAGL--------PE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754252887 164 NIPIVT---ACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAiGMGGFAAARAlsTRNDDPQGASRPWDKDRDGFVL 239
Cdd:cd00751 74 SVPATTvnrVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRA-PYLLPKARRG--GRLGLNTLDGMLDDGLTDPFTG 149
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
87-215 |
8.03e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 44.63 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 87 AANEALKDAGIDKvSEEDSYKFGVC---VSSGIGGIetlettkavidtkgpskisPFCIPssivnmlsgiisinhgLRGP 163
Cdd:PRK06157 34 AFLEALADAGIEP-KDIDAAWFGTHydeIGSGKSGT-------------------PLSRA----------------LRLP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 754252887 164 NIPIV---TACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAiGMGGFAAARA 215
Cdd:PRK06157 78 NIPVTrveNFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDT-GYGGLPVANP 131
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
169-274 |
8.44e-05 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 40.58 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 169 TACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIgmggfaaaralstrndDPQgasrpwdkDRDGFVL-GDGAGVVV 247
Cdd:pfam08545 5 AACSGFVYALSTAAALIRSGRAKNVLVIGAETLSKIL----------------DWT--------DRSTAVLfGDGAGAVV 60
|
90 100
....*....|....*....|....*..
gi 754252887 248 LeeyERAKARGAKIyaevVGFGMSADG 274
Cdd:pfam08545 61 L---EATDEPGARI----LDSVLGSDG 80
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
5-299 |
3.62e-04 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 42.31 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 5 RRVVVTGLGMVTPLGNDVPTTWANILAGKSGVETitgfdtpapdisefkVRFAARIKNfdvDALVGkkdAKRVDPFCYYG 84
Cdd:PRK06147 3 RALAIVGSGMVTAVGLDAPSSCAAIRARLDNFQE---------------TRFIDPPGG---EWLIG---APVPLPPPWRG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 85 ----IAAANEALKDAgIDKVSEED--SYKFGVCVSSgiggietlettkavidtkgPSKISPFC-IPSSIVNMLSGII--S 155
Cdd:PRK06147 62 perlAEMAAPAIAEA-LEGLPALDasEAPLLLCVAE-------------------EERPGRPPdLEERLLRELEARLglR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 156 INHGLRgpniPIVTACTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTrnddpqgASRPwdkdrD 235
Cdd:PRK06147 122 LEPGSA----VIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-------SQNS-----N 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754252887 236 GFVLGDGAGVVVLEEYERAKARGAKIYAevVGFGMSADGYHMTMPyAPGQER----CIQNALADAGLE 299
Cdd:PRK06147 186 GFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGREPAPVGESED-LPLRGDgltqAIRAALAEAGCG 250
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
171-204 |
9.43e-04 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 41.09 E-value: 9.43e-04
10 20 30
....*....|....*....|....*....|....
gi 754252887 171 CTTGTHNIGMAARLIASGDADAMLAGGSEKASNA 204
Cdd:PRK09050 90 CGSGMDAVGTAARAIKAGEAELMIAGGVESMSRA 123
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
158-261 |
2.45e-03 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 39.89 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754252887 158 HG-LRGPNIPIVTA---CTTGTHNIGMAARLIASGDADAMLAGGSEKASNAIGMGGFAAARALSTRNDdpQGASRPWDKD 233
Cdd:PRK06816 107 HGeLGAPPIEVVSSagvCAAGMMALKYAYLSVKAGESRNAVATASELASRWFRASRFEAEEEKLAELE--ENPEIAFEKD 184
|
90 100
....*....|....*....|....*...
gi 754252887 234 RDGFVLGDGAGVVVLEEYERAKARGAKI 261
Cdd:PRK06816 185 FLRWMLSDGAGAVLLENKPRPDGLSLRI 212
|
|
| |
