|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
6-420 |
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: 577.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAAT-AAVDPGEVLPRPLARKLDRSAQFALIAAK 84
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEvKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGYtapagEDQPVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGVH 164
Cdd:COG0304 81 EALADAGL-----DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 165 TPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGAGV 244
Cdd:COG0304 156 TVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 245 VVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKA 324
Cdd:COG0304 236 LVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 325 LRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGsiAAINN 404
Cdd:COG0304 316 IKRVFGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKID--YALSN 393
|
410
....*....|....*.
gi 2784255941 405 SFGFGGHNVVLAFRSV 420
Cdd:COG0304 394 SFGFGGHNASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
6-417 |
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: 548.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAATA-AVDPGEVLPRPLARKLDRSAQFALIAAK 84
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVpDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGYTAPAgedqpVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGVH 164
Cdd:cd00834 81 EALADAGLDPEE-----LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 165 TPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGAGV 244
Cdd:cd00834 156 TVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 245 VVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKA 324
Cdd:cd00834 236 LVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 325 LRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGsiAAINN 404
Cdd:cd00834 316 IKRVFGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIR--YALSN 393
|
410
....*....|...
gi 2784255941 405 SFGFGGHNVVLAF 417
Cdd:cd00834 394 SFGFGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
6-418 |
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: 541.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEgeRF--AELPVRIAA-TAAVDPGEVLPRPLARKLDRSAQFALIA 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPIT--RFdaSDLPVKIAGeVKDFDPEDYIDKKEARRMDRFIQYALAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 83 AKEAWADAGYTAPagedqPVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAG 162
Cdd:TIGR03150 79 AKEAVEDSGLDIE-----EEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 163 VHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGA 242
Cdd:TIGR03150 154 NHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 243 GVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEI 322
Cdd:TIGR03150 234 GVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAET 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 323 KALRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGsiAAI 402
Cdd:TIGR03150 314 KAIKKVFGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKID--YAL 391
|
410
....*....|....*.
gi 2784255941 403 NNSFGFGGHNVVLAFR 418
Cdd:TIGR03150 392 SNSFGFGGTNASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
5-420 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 515.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 5 NRTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAATA-AVDPGEVLPRPLARKLDRSAQFALIAA 83
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVkDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 84 KEAWADAGYTaPAGEDqpvtPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGV 163
Cdd:PRK07314 81 KQAVEDAGLE-ITEEN----ADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 164 HTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGAG 243
Cdd:PRK07314 156 HSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 244 VVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIK 323
Cdd:PRK07314 236 ILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 324 ALRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGsiAAIN 403
Cdd:PRK07314 316 AIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKID--YALS 393
|
410
....*....|....*..
gi 2784255941 404 NSFGFGGHNVVLAFRSV 420
Cdd:PRK07314 394 NSFGFGGTNASLVFKRY 410
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
6-418 |
9.48e-154 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 441.36 E-value: 9.48e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIA---------ATAAVDPGEVLPRPLARKLDRSA 76
Cdd:PRK06333 4 KRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGgqvpdlaedAEAGFDPDRYLDPKDQRKMDRFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 77 QFALIAAKEAWADAGYTAPAGEDQpvtpERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLE 156
Cdd:PRK06333 84 LFAMAAAKEALAQAGWDPDTLEDR----ERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 157 VNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKN-NENPQQASRPYDKARDG 235
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 236 FVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTP 315
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 316 QGDIAEIKALRKVLGDDmDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEA-DIVRGEPREL 394
Cdd:PRK06333 320 VGDLGEVAAIKKVFGHV-SGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEGlDVVANKARPM 398
|
410 420
....*....|....*....|....
gi 2784255941 395 PAGsiAAINNSFGFGGHNVVLAFR 418
Cdd:PRK06333 399 DMD--YALSNGFGFGGVNASILFR 420
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
15-420 |
6.17e-142 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 411.39 E-value: 6.17e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 15 ATTPLGGDSASTWEGLLAGRSGVRPLEGERF----------------AELPVRIAATaaVDPGEVLPRPLA--RKLDRSA 76
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAE--VDQSEFDPSDFAptKRESRAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 77 QFALIAAKEAWADAGYTAPAGEDQpvtpERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLE 156
Cdd:PTZ00050 79 HFAMAAAREALADAKLDILSEKDQ----ERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 157 VNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMS-KNNENPQQASRPYDKARDG 235
Cdd:PTZ00050 155 HKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtKYNDDPQRASRPFDKDRAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 236 FVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQN-LLDSTDLKPSEVVHLNAHATST 314
Cdd:PTZ00050 235 FVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENaLKDGANININDVDYVNAHATST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 315 PQGDIAEIKALRKVLGDDMDH-IAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRE 393
Cdd:PTZ00050 315 PIGDKIELKAIKKVFGDSGAPkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAH 394
|
410 420
....*....|....*....|....*..
gi 2784255941 394 LPAGSIAAINNSFGFGGHNVVLAFRSV 420
Cdd:PTZ00050 395 PLQSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
8-417 |
8.40e-137 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 398.33 E-value: 8.40e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 8 VVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEgERFAE---LPVRIAATAAVDPGEVLPRPLARKLDRSAQFALIAAK 84
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLD-DPFVEefdLPVRIGGHLLEEFDHQLTRVELRRMSYLQRMSTVLGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGytAPAgedqpVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGVH 164
Cdd:PRK07910 93 RVWENAG--SPE-----VDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 165 TPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANM-MAMSKNNENPQQASRPYDKARDGFVLGEGAG 243
Cdd:PRK07910 166 TPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMrIVMSTNNDDPAGACRPFDKDRDGFVFGEGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 244 VVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIK 323
Cdd:PRK07910 246 LMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 324 ALRKVLGddMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRelPAGSIAAIN 403
Cdd:PRK07910 326 AINNALG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPR--PGNYRYAIN 401
|
410
....*....|....
gi 2784255941 404 NSFGFGGHNVVLAF 417
Cdd:PRK07910 402 NSFGFGGHNVALAF 415
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-420 |
1.48e-121 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 359.88 E-value: 1.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 2 SSTNRTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGE--------------RFAELPVRIAATA--AVDPGEVLP 65
Cdd:PLN02836 2 PLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDdlkmksedeetqlyTLDQLPSRVAALVprGTGPGDFDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 66 RPLA--RKLDRSAQFALIAAKEAWADAGYtAPAGEDQPvtpERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPM 143
Cdd:PLN02836 82 ELWLnsRSSSRFIGYALCAADEALSDARW-LPSEDEAK---ERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 144 LMPNSPSANVGLEVNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMS-KNNENP 222
Cdd:PLN02836 158 ILINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALStKFNSCP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 223 QQASRPYDKARDGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPS 302
Cdd:PLN02836 238 TEASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 303 EVVHLNAHATSTPQGDIAEIKALRKVLGDDM--DHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDD 380
Cdd:PLN02836 318 QVDYVNAHATSTPLGDAVEARAIKTVFSEHAtsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2784255941 381 EVEADIVR-GEPRELPAgsIAAINNSFGFGGHNVVLAFRSV 420
Cdd:PLN02836 398 IFDDGFVPlTASKAMLI--RAALSNSFGFGGTNASLLFTSP 436
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
6-420 |
1.04e-106 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 320.91 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAATAA-VDPGEVLPRPLARKLDRSAQFALIAAK 84
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITdFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGYTAPAgedqpVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGVH 164
Cdd:PRK08439 82 EAMKDAGFLPEE-----LDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 165 TPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGAGV 244
Cdd:PRK08439 157 SSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 245 VVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTG--RGVAAALQNlldstdLKPSEVVHLNAHATSTPQGDIAEI 322
Cdd:PRK08439 237 LVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGplRAMKAALEM------AGNPKIDYINAHGTSTPYNDKNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 323 KALRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRElpAGSIAAI 402
Cdd:PRK08439 311 AALKELFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARK--AELNVVM 388
|
410
....*....|....*...
gi 2784255941 403 NNSFGFGGHNVVLAFRSV 420
Cdd:PRK08439 389 SNSFGFGGTNGVVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
4-420 |
7.05e-104 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 314.25 E-value: 7.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 4 TNRTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAATAA-VDPGEVLPRPLARKLDRSAQFALIA 82
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKdFNCEEYMSKKDARKMDLFIQYGIAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 83 AKEAWADAGYTapagedqpVTPE---RLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNA 159
Cdd:PRK08722 82 GIQALDDSGLE--------VTEEnahRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 160 RAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLG 239
Cdd:PRK08722 154 RGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 240 EGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDI 319
Cdd:PRK08722 234 DGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 320 AEIKALRKVLGDD-MDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELpAGS 398
Cdd:PRK08722 314 AEIKGIKRALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKV-ESM 392
|
410 420
....*....|....*....|..
gi 2784255941 399 IAAINNSFGFGGHNVVLAFRSV 420
Cdd:PRK08722 393 EYAICNSFGFGGTNGSLIFKKM 414
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
6-418 |
4.81e-93 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 285.80 E-value: 4.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRplEGERFAELPVR--IAATAAVDPGEVLPRPLARKLDRSAQFALIAA 83
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGIT--FSPEFAEMGMRsqVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 84 KEAWADAGYTapagEDQpVTPERLGTVIASGIGGVTTLLDQYDVLKE-KGVRRVSPHTVPMLMPNSPSANVGLEVNARAG 162
Cdd:PRK07967 80 EQAIADAGLS----EEQ-VSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 163 VHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAaFANMMAMS-KNNENPQQASRPYDKARDGFVLGEG 241
Cdd:PRK07967 155 NYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALStKYNDTPEKASRAYDANRDGFVIAGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 242 AGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQpePTGRGVAAALQNLLDSTDlkpSEVVHLNAHATSTPQGDIAE 321
Cdd:PRK07967 234 GGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 322 IKALRKVLGDDMDHIavSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEA-DIVRgEPRElPAGSIA 400
Cdd:PRK07967 309 LGAIREVFGDKSPAI--SATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGmPIVT-ETTD-NAELTT 384
|
410
....*....|....*...
gi 2784255941 401 AINNSFGFGGHNVVLAFR 418
Cdd:PRK07967 385 VMSNSFGFGGTNATLVFR 402
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
6-417 |
1.63e-92 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 288.80 E-value: 1.63e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAA---TAAVDpGEVLPRpLARKLDRSAQFALIA 82
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGeikSFSTD-GWVAPK-LSKRMDKFMLYLLTA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 83 AKEAWADAGYTAPAGEDqpVTPERLGTVIASGIGGVTTLLDQYDVLKeKGVRRVSPHTVPMLMPNSPSANVGLEVNARAG 162
Cdd:PLN02787 207 GKKALADGGITEDVMKE--LDKTKCGVLIGSAMGGMKVFNDAIEALR-ISYRKMNPFCVPFATTNMGSAMLAMDLGWMGP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 163 VHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEGA 242
Cdd:PLN02787 284 NYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 243 GVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEI 322
Cdd:PLN02787 364 GVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 323 KALRKVLGDDMDhIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRElPAGSIAAI 402
Cdd:PLN02787 444 QALMRCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKE-RLDIKVAL 521
|
410
....*....|....*
gi 2784255941 403 NNSFGFGGHNVVLAF 417
Cdd:PLN02787 522 SNSFGFGGHNSSILF 536
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
6-418 |
7.27e-92 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 283.03 E-value: 7.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPL-EGERFAELPVRIAATAavdPGEVLPRPLARKLDRS----AQFAL 80
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMpEWDRYDGLNTRLAAPI---DDFELPAHYTRKKIRSmgrvSLMAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 81 IAAKEAWADAGYTapagEDQPVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNAR 160
Cdd:PRK09116 79 RASELALEDAGLL----GDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 161 AGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAaIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGE 240
Cdd:PRK09116 155 GRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 241 GAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVaaALQNLLDSTDLKPSEVVHLNAHATSTPQGDIA 320
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 321 EIKALRKVLGDDMdhiAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEV-EADIVRGEPRELPAGSI 399
Cdd:PRK09116 312 ESQATAAVFGARM---PISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388
|
410
....*....|....*....
gi 2784255941 400 AaiNNSFGFGGHNVVLAFR 418
Cdd:PRK09116 389 M--SNNFAFGGINTSLIFK 405
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
8-415 |
4.74e-82 |
|
"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: 257.75 E-value: 4.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 8 VVVTGIGATTPLG---GDSASTWEGLLAGRSGVRPLEGERfAELPVRIAATA--AVDPGEVLPRPlaRKLDRSAQFALIA 82
Cdd:cd00828 3 VVITGIGVVSPHGegcDEVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIptGDIPGWDAKRT--GIVDRTTLLALVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 83 AKEAWADAGYTAPagedQPVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTvpMLMPNSPSANVGLEVNARAG 162
Cdd:cd00828 80 TEEALADAGITDP----YEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKW--MLSPNTVAGWVNILLLSSHG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 163 -VHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAaIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGEG 241
Cdd:cd00828 154 pIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 242 AGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPePTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAE 321
Cdd:cd00828 233 AGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 322 IKALRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGSIAA 401
Cdd:cd00828 312 SRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVRAA 391
|
410
....*....|....
gi 2784255941 402 INNSFGFGGHNVVL 415
Cdd:cd00828 392 LVNAFGFGGSNAAL 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
99-418 |
1.49e-81 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 254.27 E-value: 1.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 99 DQPVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEVNARAGVHTPVSACASGAEAIG 178
Cdd:PRK14691 20 DNTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 179 YAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKN-NENPQQASRPYDKARDGFVLGEGAGVVVLESAEHAAGRG 257
Cdd:PRK14691 100 DAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 258 ARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKALRKVLGDDmDHIA 337
Cdd:PRK14691 180 AKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGES-NALA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 338 VSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEA-DIVRGEPRelPAGSIAAINNSFGFGGHNVVLA 416
Cdd:PRK14691 259 ITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGlNIIAGNAQ--PHDMTYALSNGFGFAGVNASIL 336
|
..
gi 2784255941 417 FR 418
Cdd:PRK14691 337 LK 338
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
8-419 |
2.42e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 249.97 E-value: 2.42e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 8 VVVTGIGATTPLGgDSASTWEGLLAGRSGVRPLEgeRFAELPvriaataavdpgevlPRPLARKLDRSAQFALI---AAK 84
Cdd:PRK05952 4 VVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQ--PFPELP---------------PLPLGLIGNQPSSLEDLtktVVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGYTAPAGEdqpvtperLGTVIASGIGgvttlldqYDVLKEKGVR-----RVSPHTVPML------MPNSPSANV 153
Cdd:PRK05952 66 AALKDAGLTPPLTD--------CGVVIGSSRG--------CQGQWEKLARqmyqgDDSPDEELDLenwldtLPHQAAIAA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 154 GLEVNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKnnenpqQASRPYDKAR 233
Cdd:PRK05952 130 ARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 234 DGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATS 313
Cdd:PRK05952 204 EGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 314 TPQGDIAEIKALRKVLGDDmdhIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDEldDEVEADIVRgEPRE 393
Cdd:PRK05952 284 TRLNDQREANLIQALFPHR---VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFVR-QAQQ 357
|
410 420
....*....|....*....|....*.
gi 2784255941 394 LPAGSIAAInnSFGFGGHNVVLAFRS 419
Cdd:PRK05952 358 SPLQNVLCL--SFGFGGQNAAIALGK 381
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
8-417 |
5.61e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 250.32 E-value: 5.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 8 VVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEgeRFA--ELPVRIAATaaVDpgeVLPRPLARKLDRSAQFALIAAKE 85
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTIT--RFPteGLRTRIAGT--VD---FLPESPFGASALSEALARLAAEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 86 AWADAGY-----------TAPagedqPVTPE---RLGTVIASGIGGVTTlldqYDVLKEKGVRRVSPHTVPMLMPNSPSA 151
Cdd:PRK06501 86 ALAQAGIgkgdfpgplflAAP-----PVELEwpaRFALAAAVGDNDAPS----YDRLLRAARGGRFDALHERFQFGSIAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 152 NVGLEVNARAgvhTPVS---ACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNENPQQASRP 228
Cdd:PRK06501 157 RLADRFGTRG---LPISlstACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 229 YDKARDGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLN 308
Cdd:PRK06501 234 FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYIN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 309 AHATSTPQGDIAEIKALRKVLGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVR 388
Cdd:PRK06501 314 AHGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVP 393
|
410 420
....*....|....*....|....*....
gi 2784255941 389 GEPRELPAGSIaaINNSFGFGGHNVVLAF 417
Cdd:PRK06501 394 NVARDARVTAV--LSNSFGFGGQNASLVL 420
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
7-419 |
1.19e-67 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 220.67 E-value: 1.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 7 TVVVTGIGATTPLGGDSASTWEGLLAGRSGV-------RPLEGERFAELPVRI--AATAAVDPGEVLPRPLARKLDRSAQ 77
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgRQVPDDAGAGLASAFigAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 78 FALIAAKEAWADAGYtapagedQPVTPERLGTVIAsgiGGVTTLLDQYDVLKEKGVRR--VSPHTVPMLMPnspSANVGL 155
Cdd:PRK07103 83 AALAAAREAWRDAAL-------GPVDPDRIGLVVG---GSNLQQREQALVHETYRDRPafLRPSYGLSFMD---TDLVGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 156 --EVNARAGV-HTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAM--SKNNENPQQASRPYD 230
Cdd:PRK07103 150 csEQFGIRGEgFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgsDRFADEPEAACRPFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 231 KARDGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHiaQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAH 310
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 311 ATSTPQGDIAEIKALRkvlGDDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEvEADIVRGE 390
Cdd:PRK07103 308 GTGSPLGDETELAALF---ASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDE-RFRWVGST 383
|
410 420
....*....|....*....|....*....
gi 2784255941 391 PRelPAGSIAAINNSFGFGGHNVVLAFRS 419
Cdd:PRK07103 384 AE--SARIRYALSLSFGFGGINTALVLER 410
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
7-417 |
1.71e-56 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 190.82 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 7 TVVVTGIGATTPLGGDSASTWEGLLAGR-SGVRPLEGERfAELPVRIAATAAVDPgEVLPRPLARKLDRSAQFALIAAkE 85
Cdd:PRK09185 3 PVYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWL-VDLPTWVGEVVGVEL-PALPAALAAFDCRNNRLALLAL-Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 86 AWADAGYTAPA--GedqpvtPERLGTVIA---SGIGGvttlldqydvlKEKGVRRVSPHT--------VPMLMPNSPSAN 152
Cdd:PRK09185 80 QIEPAVEAAIAryG------ADRIGVVLGtstSGILE-----------GELAYRRRDPAHgalpadyhYAQQELGSLADF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 153 VglevNARAGVHTPV----SACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHpLPVAAFANMMAMSKnnenpqQASRP 228
Cdd:PRK09185 143 L----RAYLGLSGPAytisTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCR-LTLNGFNSLESLSP------QPCRP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 229 YDKARDGFVLGEGAGVVVLESAEHAAGRgarvyceVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLN 308
Cdd:PRK09185 212 FSANRDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYIN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 309 AHATSTPQGDIAEIKALRKVLGddmDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVR 388
Cdd:PRK09185 285 LHGTATPLNDAMESRAVAAVFG---DGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLV 361
|
410 420
....*....|....*....|....*....
gi 2784255941 389 GEPRELPAGsiAAINNSFGFGGHNVVLAF 417
Cdd:PRK09185 362 ENAQALAIR--YVLSNSFAFGGNNCSLIF 388
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
6-415 |
6.99e-56 |
|
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: 189.49 E-value: 6.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGERFAELPVRIAA-TAAVDPGEVLPRPLARKLDRSAQFALIAAK 84
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGeVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 85 EAWADAGYTAPAgedqpVTPERLGTVIASGIGGVTTLLDQYDVLKEKGVRRVSPHtvpMLMPNSPSANVGlEVNARAGVH 164
Cdd:cd00832 81 WALADAGVDPAA-----LPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAY---QSFAWFYAVNTG-QISIRHGMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 165 TPVSAC----ASGAEAIGYAVEMIRTGrADVVVAGGTEAAIHPLPVAAFANMMAMSKNnENPQQASRPYDKARDGFVLGE 240
Cdd:cd00832 152 GPSGVVvaeqAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTS-DDPARAYLPFDAAAAGYVPGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 241 GAGVVVLESAEHAAGRGARVYCEVLGQGLSADShhiaqPEPTGR--GVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGD 318
Cdd:cd00832 230 GGAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRppGLARAIRLALADAGLTPEDVDVVFADAAGVPELD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 319 IAEIKALRKVLGDdmDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAGs 398
Cdd:cd00832 305 RAEAAALAAVFGP--RGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALR- 381
|
410
....*....|....*..
gi 2784255941 399 iAAINNSFGFGGHNVVL 415
Cdd:cd00832 382 -TALVLARGRGGFNSAL 397
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
6-253 |
3.88e-54 |
|
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: 180.14 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTWEGLLAGRSGVRPLEGER-----FAELPVRIAATAAVDPGEVLPRPL------------ 68
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADRwdpdkLYDPPSRIAGKIYTKWGGLDDIFDfdplffgispre 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 69 ARKLDRSAQFALIAAKEAWADAGYTAPAGEDqpvtpERLGTVIASGIGGvttlLDQYDVLKEKGV-RRVSPHTVPMlMPN 147
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDG-----SRTGVFIGSGIGD----YAALLLLDEDGGpRRGSPFAVGT-MPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 148 SPSANVGLEVNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNneNPQQASR 227
Cdd:pfam00109 151 VIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD--GPCKAFD 228
|
250 260
....*....|....*....|....*.
gi 2784255941 228 PYDkarDGFVLGEGAGVVVLESAEHA 253
Cdd:pfam00109 229 PFA---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
8-415 |
1.37e-49 |
|
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: 173.51 E-value: 1.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 8 VVVTGIGATTPlGGDSAST-WEGLLAGRSGVRPLEGERFAelpvriaATAAVDPGEVLPRPLARK---LDRSAQF----- 78
Cdd:cd00833 3 IAIVGMACRFP-GAADPDEfWENLLEGRDAISEIPEDRWD-------ADGYYPDPGKPGKTYTRRggfLDDVDAFdaaff 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 79 ----------------ALIAAKEAWADAGYTapageDQPVTPERLGTVIASGiggvttlLDQYDVLKEKGVRRVSPHTVP 142
Cdd:cd00833 75 gispreaeamdpqqrlLLEVAWEALEDAGYS-----PESLAGSRTGVFVGAS-------SSDYLELLARDPDEIDAYAAT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 143 MLMPNSPSANVGLEVNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSKNNenp 222
Cdd:cd00833 143 GTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDG--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 223 qqASRPYDKARDGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSAD--SHHIAQPEPTGRgvAAALQNLLDSTDLK 300
Cdd:cd00833 220 --RCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAPSGEAQ--AALIRRAYARAGVD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 301 PSEVVHLNAHATSTPQGDIAEIKALRKVLG---DDMDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDE 377
Cdd:cd00833 296 PSDIDYVEAHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFET 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2784255941 378 LDDEVEAD----IVRGEPRELPAGS---IAAInNSFGFGGHN--VVL 415
Cdd:cd00833 376 PNPKIDFEesplRVPTEARPWPAPAgprRAGV-SSFGFGGTNahVIL 421
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
78-416 |
5.12e-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: 158.95 E-value: 5.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 78 FALIAAKEAWADAGYTApagedQPVTPERLGTVIASGIGGvttllDQYDVLKEKGVRRVSPHTVPMLMPNSPSANVGLEV 157
Cdd:cd00825 14 LGFEAAERAIADAGLSR-----EYQKNPIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 158 NARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAaihplPVAAFANMMAMSKNNENPQQASRPYDKARDGFV 237
Cdd:cd00825 84 GIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEE-----LAAPMDCEFDAMGALSTPEKASRTFDAAADGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 238 LGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQG 317
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 318 DIAEIKALRKVLGDdmDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLDELDDEVEADIVRGEPRELPAG 397
Cdd:cd00825 239 DVKELKLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRELRTA 316
|
330
....*....|....*....
gi 2784255941 398 SIaainNSFGFGGHNVVLA 416
Cdd:cd00825 317 LL----NGFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
261-376 |
1.36e-35 |
|
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: 127.30 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 261 YCEVLGQGLSADSHHIAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKALRKVLGD--DMDHIAV 338
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSgaRKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2784255941 339 SATKSMTGHLLGGAGGIETVATVLALHHRIAPPTINLD 376
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
169-415 |
1.87e-31 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 127.30 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 169 ACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSknnenPQQASRPYDKARDGFVLGEGAGVVVLE 248
Cdd:COG3321 173 ACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 249 SAEHAAGRGARVYCEVLG---------QGLSAdshhiaqpePTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDI 319
Cdd:COG3321 248 RLSDALRDGDRIYAVIRGsavnqdgrsNGLTA---------PNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 320 AEIKALRKVLGDDMD---HIAVSATKSMTGHLLGGAGgietVA----TVLALHHRIAPPTINLDELDDEVEAD----IVR 388
Cdd:COG3321 319 IEAAALTAAFGQGRPadqPCAIGSVKSNIGHLEAAAG----VAglikAVLALRHGVLPPTLHFETPNPHIDFEnspfYVN 394
|
250 260 270
....*....|....*....|....*....|..
gi 2784255941 389 GEPRELPAGS---IAAInNSFGFGGHN--VVL 415
Cdd:COG3321 395 TELRPWPAGGgprRAGV-SSFGFGGTNahVVL 425
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
59-412 |
2.44e-31 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 127.04 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 59 DPGEV-LPRPLARKLDRSAQFALIAAKEAWADAGYtaPAGEDQpvtpERLGtvIASGIGGVTTLLD------QYDVLKEK 131
Cdd:TIGR02813 76 NPMEFgLPPNILELTDISQLLSLVVAKEVLNDAGL--PDGYDR----DKIG--ITLGVGGGQKQSSslnarlQYPVLKKV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 132 -GVRRVSPHTVPMLMPNSPSANVGLEVNARAGVHTPV-------------------SACASGAEAIGYAVEMIRTGRADV 191
Cdd:TIGR02813 148 fKASGVEDEDSEMLIKKFQDQYIHWEENSFPGSLGNVisgrianrfdlggmncvvdAACAGSLAAIRMALSELLEGRSEM 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 192 VVAGGTEAAIHPLPVAAFANMMAMSKNnenpqQASRPYDKARDGFVLGEGAGVVVLESAEHAAGRGARVYCEVLGQGLSA 271
Cdd:TIGR02813 228 MITGGVCTDNSPFMYMSFSKTPAFTTN-----EDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 272 DSH--HIAQPEPTGRgvAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKALRKVLGDDMD---HIAVSATKSMTG 346
Cdd:TIGR02813 303 DGKfkSIYAPRPEGQ--AKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDqkqHIALGSVKSQIG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 347 HLLGGAGGIETVATVLALHHRIAPPTINLDE-------------LDDEVEADIVR--GEPRElpagsiAAInNSFGFGGH 411
Cdd:TIGR02813 381 HTKSTAGTAGMIKAVLALHHKVLPPTINVDQpnpkldienspfyLNTETRPWMQRedGTPRR------AGI-SSFGFGGT 453
|
.
gi 2784255941 412 N 412
Cdd:TIGR02813 454 N 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
168-415 |
2.10e-23 |
|
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: 98.29 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 168 SACASGAEAIGYAVEMIRTGRADVVVAGGTEAaihplpvaafanmmamsknnenpqqasrpydkardgFVLGEGAGVVVL 247
Cdd:cd00327 66 QACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGAAAAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 248 ESAEHAAGRGARVYCEVLGQGLSADSHHiAQPEPTGRGVAAALQNLLDSTDLKPSEVVHLNAHATSTPQGDIAEIKALRK 327
Cdd:cd00327 110 ESEEHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 328 VLGDdmDHIAVSATKSMTGHLLGGAGGIETVATVLALHHRIAPPTinldelddeveadivrgeprelPAGSIAAINNSFG 407
Cdd:cd00327 189 PDGV--RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----------------------PREPRTVLLLGFG 244
|
....*...
gi 2784255941 408 FGGHNVVL 415
Cdd:cd00327 245 LGGTNAAV 252
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
169-415 |
1.28e-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: 94.32 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 169 ACASGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMSknnenPQQASRPYDKARDGFVLGEGAGVVVLE 248
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 249 SAEHAAGRGARVYCEVLGQGLSAD--SHHIAQPeptgrgvaaalqnlldstdlkpsevvhlNAHAtstpqgdiaeikalr 326
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDgrSNGITAP----------------------------SGPA--------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 327 kvlgddmdHIAVSATKSMTGHLLGGAGgietVA----TVLALHHRIAPPTINLDELDDEVEAD-----IVRgEPRELPAG 397
Cdd:smart00825 208 --------QLLIGSVKSNIGHLEAAAG----VAglikVVLALKHGVIPPTLHFETPNPHIDLEesplrVPT-ELTPWPPP 274
|
250 260
....*....|....*....|...
gi 2784255941 398 S---IAAInNSFGFGGHN--VVL 415
Cdd:smart00825 275 GrprRAGV-SSFGFGGTNahVIL 296
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-349 |
5.04e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 54.57 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 1 MSSTNRTVVVTGIGATTPLGGDSASTWEgLLAGRSGVRPLEGERFAELPVRiaataavdpgevlprPLArKLDRSAQfal 80
Cdd:PRK06519 1 MRMQPNDVVITGIGLVSSLGEGLDAHWN-ALSAGRPQPNVDTETFAPYPVH---------------PLP-EIDWSQQ--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 81 IAAK------EAWadagytapagedqpvtpERLGTVIA------SGIGGVTTLLDQYD--VLKEKGVRRVsphTVPMLMP 146
Cdd:PRK06519 61 IPKRgdqrqmETW-----------------QRLGTYAAglalddAGIKGNEELLSTMDmiVAAGGGERDI---AVDTAIL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 147 NS--PSANVGLEVNAR------------------AG----VH-------TPVSACASGAEAIGYAVEMIRTGRADVVVAG 195
Cdd:PRK06519 121 NEarKRNDRGVLLNERlmtelrptlflaqlsnllAGnisiVHkvtgssrTFMGEESAGVSAIEIAFARIASGQSDHALVG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 196 GTEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKarDGFVLGEGAGVVVLESAEHAAGRGARVYCEVlgQGLSADShh 275
Cdd:PRK06519 201 GAYNAERPDMLLLYELGGLLLKGGWAPVWSRGGEDG--GGFILGSGGAFLVLESREHAEARGARPYARI--SGVESDR-- 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784255941 276 iAQPEPTgrGVAAALQNLLDSTDLKPSEVVHLNAhATSTPQGDIAEIKALRKVLGddmdhIAVSATKSMTGHLL 349
Cdd:PRK06519 275 -ARRAPG--DLEASLERLLKPAGGLAAPTAVISG-ATGAHPATAEEKAALEAALA-----GPVRGIGTLFGHTM 339
|
|
| FabG2 |
COG4982 |
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and ... |
166-417 |
7.08e-07 |
|
3-oxoacyl-ACP reductase domain of yeast-type fatty acid synthase FAS1 [Lipid transport and metabolism];
Pssm-ID: 444006 [Multi-domain] Cd Length: 3088 Bit Score: 51.99 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 166 PVSACASGAEAIGYAVEMIRTGRADVVVAGG-----TEAAIHPLPVAAFANMMAMSKNNENPQQASRPYDKARDGFVLGE 240
Cdd:COG4982 2727 PVAACATAAVSVEEGVDKIRLGKADFVVAGGiddigVESITGFGDMNATADSEEMLAKGIDDRFFSRANDRRRGGFVEAQ 2806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 241 GAGVVVLESAEHAAGRGARVYCEVLGQGLSADSHHIAQPEPTGRGVAAA-------LQNLLDSTDLKPSEVVHLNAHATS 313
Cdd:COG4982 2807 GGGTILLARGDVAAKLGLPVLGVVAFAQSFADGAHTSIPAPGLGALAAArggkdskLARDLAKLGVTADDIAVVSKHDTS 2886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 314 TPQGDIAE-------IKALRKVLGDDMdhiAVSATKSMTGHLLGGA------GGIETVATVLalhhriAPPTINLDELDD 380
Cdd:COG4982 2887 TNANDPNEselherlAHAIGRTDGNPL---FVVSQKSLTGHAKGGAaafqliGLCQVLRSGV------IPPNRSLDCVDD 2957
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2784255941 381 EVEAD---IVRGEPRELPAG--SIAAINNSFGFGGHNVVLAF 417
Cdd:COG4982 2958 KLAGDdhlVWLREPLRLGAKgpLKAGLLTSLGFGHVSGLLAV 2999
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
6-289 |
3.35e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 48.86 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 6 RTVVVTGIGATTPLGGDSASTwegLLAGRSGVRPLEGERFAELP---VRIAATAAvdpgevLPRPLaRKLDRSAQFALIA 82
Cdd:PRK06147 3 RALAIVGSGMVTAVGLDAPSS---CAAIRARLDNFQETRFIDPPggeWLIGAPVP------LPPPW-RGPERLAEMAAPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 83 AKEAwadagyTAPAGEDQPVTPERLGTVIASGIGGVTTLLDQydvlkekgvrrvspHTVPMLMPN-SPSANVGLEVNARA 161
Cdd:PRK06147 73 IAEA------LEGLPALDASEAPLLLCVAEEERPGRPPDLEE--------------RLLRELEARlGLRLEPGSAVIARG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 162 GVhtpvsacaSGAEAIGYAVEMIRTGRADVVVAGGTEAAIHPLPVAAFANMMAMsKNNENPqqasrpydkarDGFVLGEG 241
Cdd:PRK06147 133 RV--------SGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRL-LTSQNS-----------NGFIPGEA 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2784255941 242 AGVVVLESAEHAAGRGARvyceVLGQGLSADSHHIAQPEP---TGRGVAAA 289
Cdd:PRK06147 193 AAAVLLGRPAGGEAPGLP----LLGLGLGREPAPVGESEDlplRGDGLTQA 239
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
145-198 |
5.70e-06 |
|
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: 48.24 E-value: 5.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 145 MPNSPSANVGLEVNARAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTE 198
Cdd:cd00751 53 LQAGEGQNPARQAALLAGLPESVPAttvnrvCGSGLQAVALAAQSIAAGEADVVVAGGVE 112
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
169-198 |
6.25e-06 |
|
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: 48.14 E-value: 6.25e-06
10 20 30
....*....|....*....|....*....|
gi 2784255941 169 ACASGAEAIGYAVEMIRTGRADVVVAGGTE 198
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVE 116
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
145-204 |
4.43e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 45.39 E-value: 4.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784255941 145 MPNSPSANVGLEVNARAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTEAAIH-PL 204
Cdd:PRK08170 58 MPSPDEANIARVVALRLGCGEKVPAwtvqrnCASGMQALDSAAANIALGRADLVLAGGVEAMSHaPL 124
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
160-198 |
5.04e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 45.14 E-value: 5.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2784255941 160 RAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTE 198
Cdd:PRK05790 72 KAGLPVEVPAltinkvCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
151-242 |
1.27e-04 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 43.76 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 151 ANVGLEVNARAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTEA-AIHPLPVAAFANMMAMSKNNENPQ 223
Cdd:TIGR01930 58 QNIARQAALLAGLPESVPAytvnrqCASGLQAVILAAQLIRAGEADVVVAGGVESmSRVPYGVPRSLRWGVKPGNAELED 137
|
90
....*....|....*....
gi 2784255941 224 QASRPYDKARDGFVLGEGA 242
Cdd:TIGR01930 138 ARLKDLTDANTGLPMGVTA 156
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
160-212 |
3.07e-04 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 42.29 E-value: 3.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784255941 160 RAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTE---AAIHPLPVAAFANM 212
Cdd:pfam00108 69 KAGIPDSAPAvtinkvCGSGLKAVYLAAQSIASGDADVVLAGGVEsmsHAPYALPTDARSGL 130
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
144-260 |
4.02e-04 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 42.20 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784255941 144 LMPNSPSANVGLEVNARAGVHTPVSACASGAEAIGYAVEMIRTGRADVVVAGGTEAAihplpvaafANMMAMSKNNENPQ 223
Cdd:PRK06816 98 LMPGHASMVHGELGAPPIEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASELA---------SRWFRASRFEAEEE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2784255941 224 QASRPYDKARDGF-------VLGEGAGVVVLESAEHAAGRGARV 260
Cdd:PRK06816 169 KLAELEENPEIAFekdflrwMLSDGAGAVLLENKPRPDGLSLRI 212
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
170-198 |
1.41e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 40.74 E-value: 1.41e-03
10 20
....*....|....*....|....*....
gi 2784255941 170 CASGAEAIGYAVEMIRTGRADVVVAGGTE 198
Cdd:PRK06205 88 CGSGLQAVITAAMQVQTGAADVVIAGGAE 116
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
152-199 |
1.96e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 40.12 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2784255941 152 NVGLEVNARAGVHTPVSA------CASGAEAIGYAVEMIRTGRADVVVAGGTEA 199
Cdd:PRK07661 66 NMARNIGALAGLPYTVPAitinryCSSGLQSIAYGAERIMLGHSEAVIAGGAES 119
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
170-213 |
2.51e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 39.70 E-value: 2.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2784255941 170 CASGAEAIGYAVEMIRTGRADVVVAGGTEA---AIHPLPVAAFANMM 213
Cdd:PRK08235 88 CASGLRAVTLADQIIRAGDASVIVAGGMESmsnAPYILPGARWGYRM 134
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
168-222 |
2.56e-03 |
|
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: 39.94 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2784255941 168 SACASGAEAIGYAVEMIRTGRADVVVAGGTEA-AIHPLPVAAFANMMAMSKNNENP 222
Cdd:cd00829 75 AAGASGSAAVRAAAAAIASGLADVVLVVGAEKmSDVPTGDEAGGRASDLEWEGPEP 130
|
|
| |
