|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-406 |
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: 748.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVkDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTA 160
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 161 CATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLEA 240
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 241 YEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVF 320
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 321 GDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAFGGH 399
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPnEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 46195975 400 NAVLVFK 406
Cdd:TIGR03150 401 NASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-408 |
0e+00 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 708.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVkDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTA 160
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 161 CATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLEA 240
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 241 YEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVF 320
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 321 GDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAFGGH 399
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPnEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 46195975 400 NAVLVFKRV 408
Cdd:COG0304 401 NASLVFKRY 409
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-408 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 698.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAA 79
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVkDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 80 QLALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVT 159
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 160 ACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLE 239
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 240 AYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRV 319
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 320 FGDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAFGG 398
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPnEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 46195975 399 HNAVLVFKRV 408
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-405 |
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: 671.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVpDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTA 160
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 161 CATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLEA 240
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 241 YEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVF 320
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 321 GDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAFGGH 399
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPnEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 46195975 400 NAVLVF 405
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-407 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 558.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV---------DVDPGAYLDRKELRRLDRF 71
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVpdlaedaeaGFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 72 VQYALIAAQLALEDAGLKPEDL-DPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGF 150
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPDTLeDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 151 TGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTR-NEEPEKASRPFTLSRDGFVM 229
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 230 GEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGD 309
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 310 RAEVLAIKRVFGdHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELD-LDFVP-EPREAKVD 387
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVAnKARPMDMD 401
|
410 420
....*....|....*....|
gi 46195975 388 YALSNSFAFGGHNAVLVFKR 407
Cdd:PRK06333 402 YALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-408 |
5.88e-180 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 506.96 E-value: 5.88e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAA 79
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEItDFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 80 QLALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVT 159
Cdd:PRK08439 81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 160 ACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLE 239
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 240 AYEHAKKRGARIYAELVGFGRSADAHHITEPHPEgkGAALAMARALKDAGIAPeqVGYINAHGTSTPAGDRAEVLAIKRV 319
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 320 FGDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAFGG 398
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPnVARKAELNVVMSNSFGFGG 396
|
410
....*....|
gi 46195975 399 HNAVLVFKRV 408
Cdd:PRK08439 397 TNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-408 |
6.47e-178 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 502.30 E-value: 6.47e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 11 ALTPIGVGQEAFHKAQLAGKSGVRPITRFDA----------------SALPVRIAAEVD---VDPGAYLDRKelrRLDRF 71
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqseFDPSDFAPTK---RESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 72 VQYALIAAQLALEDAGLKP-EDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGF 150
Cdd:PTZ00050 78 THFAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 151 TGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTR-NEEPEKASRPFTLSRDGFVM 229
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 230 GEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAG-IAPEQVGYINAHGTSTPAG 308
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 309 DRAEVLAIKRVFGDH-AKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVPEPREA--- 384
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHplq 397
|
410 420
....*....|....*....|....
gi 46195975 385 KVDYALSNSFAFGGHNAVLVFKRV 408
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-408 |
1.06e-161 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 461.57 E-value: 1.06e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDA--------------SALPVRIAAEV--DVDPGAYLDRKEL 65
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVprGTGPGDFDEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 66 --RRLDRFVQYALIAAQLALEDAGLKP-EDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASA 142
Cdd:PLN02836 86 nsRSSSRFIGYALCAADEALSDARWLPsEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 143 HIAMRYGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTR-NEEPEKASRPFT 221
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 222 LSRDGFVMGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAH 301
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 302 GTSTPAGDRAEVLAIKRVFGDHA--KRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP 379
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEHAtsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420 430
....*....|....*....|....*....|.
gi 46195975 380 --EPREAKVDYALSNSFAFGGHNAVLVFKRV 408
Cdd:PLN02836 406 ltASKAMLIRAALSNSFGFGGTNASLLFTSP 436
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-408 |
8.00e-158 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 450.99 E-value: 8.00e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVkDFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTA 160
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 161 CATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLVLEA 240
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 241 YEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVF 320
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 321 GDH-AKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAK-VDYALSNSFAFG 397
Cdd:PRK08722 324 GEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPhTARKVEsMEYAICNSFGFG 403
|
410
....*....|.
gi 46195975 398 GHNAVLVFKRV 408
Cdd:PRK08722 404 GTNGSLIFKKM 414
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-405 |
7.02e-140 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 410.14 E-value: 7.02e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIkSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPE---DLDPERVGTLVGTGIGGMETWEAQSRVfLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTV 157
Cdd:PLN02787 209 KALADGGITEDvmkELDKTKCGVLIGSAMGGMKVFNDAIEA-LRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 158 VTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVLV 237
Cdd:PLN02787 288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 238 LEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIK 317
Cdd:PLN02787 368 LEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALM 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 318 RVFGDHAKrLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFV--PEPREAKVDYALSNSFA 395
Cdd:PLN02787 448 RCFGQNPE-LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLvgPKKERLDIKVALSNSFG 526
|
410
....*....|
gi 46195975 396 FGGHNAVLVF 405
Cdd:PLN02787 527 FGGHNSSILF 536
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-407 |
6.97e-122 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 359.81 E-value: 6.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 4 VVVTGLGALTPIGVGQEAFHKAQLAGKSGVRP-----ITRFDasaLPVRIAAEVDVDPGAYLDRKELRRLDRFVQYALIA 78
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEFD---LPVRIGGHLLEEFDHQLTRVELRRMSYLQRMSTVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 79 AQLALEDAGlKPEdLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVV 158
Cdd:PRK07910 91 GRRVWENAG-SPE-VDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 159 TACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRA-LSTRNEEPEKASRPFTLSRDGFVMGEGAGVLV 237
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 238 LEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIK 317
Cdd:PRK07910 249 IETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAIN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 318 RVFGDHakRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-EPREAKVDYALSNSFAF 396
Cdd:PRK07910 329 NALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAgEPRPGNYRYAINNSFGF 406
|
410
....*....|.
gi 46195975 397 GGHNAVLVFKR 407
Cdd:PRK07910 407 GGHNVALAFGR 417
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-407 |
8.60e-118 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 349.31 E-value: 8.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 4 VVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEVDvdpgaYLDRKELRRLDRFVQYALIAAQLAL 83
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVD-----FLPESPFGASALSEALARLAAEEAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 84 EDAGLKPEDLD--------------PERVGTLVGTGIGGMETWEAQSRVfleRGPNRISPFFIPMMIANMAsAHIAMRYG 149
Cdd:PRK06501 88 AQAGIGKGDFPgplflaappvelewPARFALAAAVGDNDAPSYDRLLRA---ARGGRFDALHERFQFGSIA-DRLADRFG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 150 FTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVM 229
Cdd:PRK06501 164 TRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 230 GEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGD 309
Cdd:PRK06501 244 AEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPEND 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 310 RAEVLAIKRVFGDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVPE-PREAKVDY 388
Cdd:PRK06501 324 KMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNvARDARVTA 403
|
410
....*....|....*....
gi 46195975 389 ALSNSFAFGGHNAVLVFKR 407
Cdd:PRK06501 404 VLSNSFGFGGQNASLVLTA 422
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-408 |
2.23e-112 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 335.10 E-value: 2.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEVDVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVKLDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETW-EAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVT 159
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQvEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 160 ACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIgAFAVMRALSTR-NEEPEKASRPFTLSRDGFVMGEGAGVLVL 238
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSC-LFDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 239 EAYEHAKKRGARIYAELVGFGRSADAHHITEphPEGKGAALAMARALKDAGiapEQVGYINAHGTSTPAGDRAEVLAIKR 318
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 319 VFGDhaKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPEL-DLDFVPEPRE-AKVDYALSNSFAF 396
Cdd:PRK07967 315 VFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDnAELTTVMSNSFGF 392
|
410
....*....|..
gi 46195975 397 GGHNAVLVFKRV 408
Cdd:PRK07967 393 GGTNATLVFRRY 404
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-406 |
4.64e-112 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 334.26 E-value: 4.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFD-ASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIA 78
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrYDGLNTRLAAPIdDFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 79 AQLALEDAGLKPED-LDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISP-FFIPMMiANMASAHIAMRYGFTGPSST 156
Cdd:PRK09116 81 SELALEDAGLLGDPiLTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITAtTYVRMM-PHTTAVNVGLFFGLKGRVIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 157 VVTACATGADALGSALRMIQLGEADLVLAGGTEAaITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGAGVL 236
Cdd:PRK09116 160 TSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 237 VLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEgkGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAI 316
Cdd:PRK09116 239 VLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAE--TMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQAT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 317 KRVFGDhakRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPEL-DLDF-VPEPREAKVDYALSNSF 394
Cdd:PRK09116 317 AAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYiMGEAREIDTEYVMSNNF 393
|
410
....*....|..
gi 46195975 395 AFGGHNAVLVFK 406
Cdd:PRK09116 394 AFGGINTSLIFK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
96-407 |
1.40e-103 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 310.51 E-value: 1.40e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 96 ERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTACATGADALGSALRMI 175
Cdd:PRK14691 26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 176 QLGEADLVLAGGTEAAITPMAIGAFAVMRALSTR-NEEPEKASRPFTLSRDGFVMGEGAGVLVLEAYEHAKKRGARIYAE 254
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 255 LVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVFGDhAKRLMVSSTKS 334
Cdd:PRK14691 186 IVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46195975 335 MIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELD-LDFV---PEPREakVDYALSNSFAFGGHNAVLVFKR 407
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIagnAQPHD--MTYALSNGFGFAGVNASILLKR 339
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-404 |
3.95e-100 |
|
"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: 303.59 E-value: 3.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVG---QEAFHKAQLAGKSGVRPITRFDaSALPVRIAAEVdvdPGAYLDRKELRR---LDRFVQYA 75
Cdd:cd00828 1 SRVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQI---PTGDIPGWDAKRtgiVDRTTLLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 76 LIAAQLALEDAGLK-PEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPffIPMMIANMASAHIAMRYGF-TGP 153
Cdd:cd00828 77 LVATEEALADAGITdPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSP--KWMLSPNTVAGWVNILLLSsHGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 154 SSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAaITPMAIGAFAVMRALSTRNEEPEKASRPFTLSRDGFVMGEGA 233
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 234 GVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPeGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEV 313
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 314 LAIKRVFGDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFV---PEPREAKVDYAL 390
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVvglSRDLNLKVRAAL 392
|
410
....*....|....
gi 46195975 391 SNSFAFGGHNAVLV 404
Cdd:cd00828 393 VNAFGFGGSNAALV 406
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-407 |
1.50e-88 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 274.22 E-value: 1.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVR--------IAAEVD-VDPGAYLDRKELRRLDRF 71
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAgaglasafIGAELDsLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 72 VQYALIAAQLALEDAGLKPEDldPERVGTLV-GTGIGGMETWEAQSRvFLERgPNRISPFFIpmmIANMASAH---IAMR 147
Cdd:PRK07103 81 AQAALAAAREAWRDAALGPVD--PDRIGLVVgGSNLQQREQALVHET-YRDR-PAFLRPSYG---LSFMDTDLvglCSEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 148 YGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRN--EEPEKASRPFTLSRD 225
Cdd:PRK07103 154 FGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 226 GFVMGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKgaALAMARALKDAGIAPEQVGYINAHGTST 305
Cdd:PRK07103 234 GFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 306 PAGDRAEVLAIkrvFGDHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDP-DPEldLDFV-PEPRE 383
Cdd:PRK07103 312 PLGDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDER--FRWVgSTAES 386
|
410 420
....*....|....*....|....
gi 46195975 384 AKVDYALSNSFAFGGHNAVLVFKR 407
Cdd:PRK07103 387 ARIRYALSLSFGFGGINTALVLER 410
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-404 |
3.34e-88 |
|
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: 272.70 E-value: 3.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPITRFDASALPVRIAAEV-DVDPGAYLDRKELRRLDRFVQYALIAAQ 80
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVpDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 81 LALEDAGLKPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFfipMMIA---NMASAHIAMRYGFTGPSSTV 157
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAY---QSFAwfyAVNTGQISIRHGMRGPSGVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 158 VTACATGADALGSALRMIQLGeADLVLAGGTEAAITPMAIGAFAVMRALSTrNEEPEKASRPFTLSRDGFVMGEGAGVLV 237
Cdd:cd00832 158 VAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 238 LEAYEHAKKRGARIYAELVGFGRSADAhhitEPHPeGKGAALAMA--RALKDAGIAPEQVGYINAHGTSTPAGDRAEVLA 315
Cdd:cd00832 236 LEDAAAARERGARVYGEIAGYAATFDP----PPGS-GRPPGLARAirLALADAGLTPEDVDVVFADAAGVPELDRAEAAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 316 IKRVFGDHakRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFV-PEPREAKVDYALSNSF 394
Cdd:cd00832 311 LAAVFGPR--GVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVtGRPRPAALRTALVLAR 388
|
410
....*....|
gi 46195975 395 AFGGHNAVLV 404
Cdd:cd00832 389 GRGGFNSALV 398
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
3-404 |
1.25e-87 |
|
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: 272.12 E-value: 1.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 3 RVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPIT--RFDASAL--PVRIAAEVDVDPGAYLDR-------------KEL 65
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYypDPGKPGKTYTRRGGFLDDvdafdaaffgispREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 66 RRLDRFVQYALIAAQLALEDAGLKPEDLDPERVGTLVGTGiggMETWEAQsrvfLERGPNRISPFFIPMMIANMASAHIA 145
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGAS---SSDYLEL----LARDPDEIDAYAATGTSRAFLANRIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 146 MRYGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALStrneePEKASRPFTLSRD 225
Cdd:cd00833 155 YFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFDADAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 226 GFVMGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAH--HITEPHPEGkgAALAMARALKDAGIAPEQVGYINAHGT 303
Cdd:cd00833 230 GYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEA--QAALIRRAYARAGVDPSDIDYVEAHGT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 304 STPAGDRAEVLAIKRVFG---DHAKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDF--- 377
Cdd:cd00833 308 GTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEEspl 387
|
410 420 430
....*....|....*....|....*....|...
gi 46195975 378 ------VPEPREAKVDYALSNSFAFGGHNAVLV 404
Cdd:cd00833 388 rvpteaRPWPAPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-407 |
2.39e-86 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 267.30 E-value: 2.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAqLAGKSGVRPITRF-DASALPVRIAAEVDVDpgayldrkelrrLDRFVQYALIAA 79
Cdd:PRK05952 1 MMKVVVTGIGLVSALGDLEQSWQRL-LQGKSGIKLHQPFpELPPLPLGLIGNQPSS------------LEDLTKTVVTAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 80 qlaLEDAGLKPEDLDperVGTLVGT--GIGGM-ETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSST 156
Cdd:PRK05952 68 ---LKDAGLTPPLTD---CGVVIGSsrGCQGQwEKLARQMYQGDDSPDEELDLENWLDTLPHQAAIAAARQIGTQGPVLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 157 VVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTrneepeKASRPFTLSRDGFVMGEGAGVL 236
Cdd:PRK05952 142 PMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVLGEGGAIL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 237 VLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAI 316
Cdd:PRK05952 216 VLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 317 KRVFGdhaKRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEdpDPELDLDFVPEPREAKVDYALSNSFAF 396
Cdd:PRK05952 296 QALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNFVRQAQQSPLQNVLCLSFGF 370
|
410
....*....|.
gi 46195975 397 GGHNAVLVFKR 407
Cdd:PRK05952 371 GGQNAAIALGK 381
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-407 |
1.11e-85 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 265.94 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 1 MRRVVVTGLGALTPIGVGQEAFHKAQLAGK-SGVRPITRFDAsALPVRIAAEVDVDpgAYLDRKELRRLD----RFVQYA 75
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLV-DLPTWVGEVVGVE--LPALPAALAAFDcrnnRLALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 76 LIAAQLALEDAglkPEDLDPERVGTLVGTGIGGMETWEAQSRVFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSS 155
Cdd:PRK09185 78 LQQIEPAVEAA---IARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQQELGSLADFLRAYLGLSGPAY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 156 TVVTACATGADALGSALRMIQLGEADLVLAGGTEAaITPMAIGAFAVMRALSTRneepekASRPFTLSRDGFVMGEGAGV 235
Cdd:PRK09185 155 TISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQ------PCRPFSANRDGINIGEAAAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 236 LVLEayehakkRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLA 315
Cdd:PRK09185 228 FLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 316 IKRVFGDHakrLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPEL-DLDFVPEPREAKVDYALSNSF 394
Cdd:PRK09185 301 VAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALpPLYLVENAQALAIRYVLSNSF 377
|
410
....*....|...
gi 46195975 395 AFGGHNAVLVFKR 407
Cdd:PRK09185 378 AFGGNNCSLIFGR 390
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
70-404 |
1.70e-66 |
|
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: 214.81 E-value: 1.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 70 RFVQYALIAAQLALEDAGLKPEDLDPERVGTLVGTGIGGMEtweaqSRVFLERGPNRISPFFIPMMIANMASAHIAMRYG 149
Cdd:cd00825 10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPR-----FQVFGADAMRAVGPYVVTKAMFPGASGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 150 FTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALstrneEPEKASRPFTLSRDGFVM 229
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALS-----TPEKASRTFDAAADGFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 230 GEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGD 309
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 310 RAEVLAIKRVFGDHakRLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLdFVPEPREAKVDYA 389
Cdd:cd00825 240 VKELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLN-IVTETTPRELRTA 316
|
330
....*....|....*
gi 46195975 390 LSNSFAFGGHNAVLV 404
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-244 |
1.55e-65 |
|
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: 209.41 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAFHKAQLAGKSGVRPI--TRFDASAL---PVRIAAEVDVDPGAYLDR------------KE 64
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTKWGGLDDIfdfdplffgispRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 65 LRRLDRFVQYALIAAQLALEDAGLKPEDLDPERVGTLVGTGIGGmetWEAQSRVFLERGPNRISPFFIPMMiANMASAHI 144
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD---YAALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 145 AMRYGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTrnEEPEKASRPFtlsR 224
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF---A 231
|
250 260
....*....|....*....|
gi 46195975 225 DGFVMGEGAGVLVLEAYEHA 244
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
82-404 |
1.43e-58 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 206.65 E-value: 1.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 82 ALEDAGLKPEDLDPERVGTLVGTGIGGMETweaqsrvFLERGPNRISPFFIPMMIANMASAHIAMRYGFTGPSSTVVTAC 161
Cdd:COG3321 102 ALEDAGYDPESLAGSRTGVFVGASSNDYAL-------LLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTAC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 162 ATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALStrneePEKASRPFTLSRDGFVMGEGAGVLVLEAY 241
Cdd:COG3321 175 SSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 242 EHAKKRGARIYAELVGFGRSADAHH--ITEPHPEGKgaALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRV 319
Cdd:COG3321 250 SDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQ--AAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 320 FGDHAKR---LMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLD----FVPE-----PREAKVD 387
Cdd:COG3321 328 FGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTelrpwPAGGGPR 407
|
330
....*....|....*..
gi 46195975 388 YALSNSFAFGGHNAVLV 404
Cdd:COG3321 408 RAGVSSFGFGGTNAHVV 424
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
252-367 |
3.17e-52 |
|
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: 170.44 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 252 YAELVGFGRSADAHHITEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVFGDHAKR--LMV 329
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 46195975 330 SSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLE 367
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
51-406 |
4.39e-48 |
|
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: 176.35 E-value: 4.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 51 EVDVDPGAY-LDRKELRRLDRFVQYALIAAQLALEDAGLkPEDLDPERVGTLVGTGIGGMETWEAQSR--------VFLE 121
Cdd:TIGR02813 72 EVDFNPMEFgLPPNILELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVGGGQKQSSSLNARlqypvlkkVFKA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 122 RGPNR------ISPF---FI-------PMMIANMASAHIAMRYGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLA 185
Cdd:TIGR02813 151 SGVEDedsemlIKKFqdqYIhweensfPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMIT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 186 GGTEAAITPMAIGAFAVMRALSTrNEEpekaSRPFTLSRDGFVMGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAH 265
Cdd:TIGR02813 231 GGVCTDNSPFMYMSFSKTPAFTT-NED----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 266 --HITEPHPEGKgaALAMARALKDAGIAPEQVGYINAHGTSTPAGDRAEVLAIKRVFG---DHAKRLMVSSTKSMIGHLL 340
Cdd:TIGR02813 306 fkSIYAPRPEGQ--AKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTK 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46195975 341 GAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDFVP-------EPREAKVD----YALSNSFAFGGHNAVLVFK 406
Cdd:TIGR02813 384 STAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIENSPfylntetRPWMQREDgtprRAGISSFGFGGTNFHMVLE 460
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
70-404 |
4.83e-34 |
|
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: 127.18 E-value: 4.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 70 RFVQYALIAAQLALEDAGLKpedlDPERVGTLVGTGIGGMEtweaqsrvflergpnrispffipmmiANMASAHIAMRYG 149
Cdd:cd00327 6 TASELGFEAAEQAIADAGLS----KGPIVGVIVGTTGGSGE--------------------------FSGAAGQLAYHLG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 150 FT-GPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAaitpmaigafavmralstrneepekasrpftlsrdgFV 228
Cdd:cd00327 56 ISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FV 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 229 MGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHItEPHPEGKGAALAMARALKDAGIAPEQVGYINAHGTSTPAG 308
Cdd:cd00327 100 FGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 309 DRAEVLAIKRVFGDHAkrLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTinledpDPELDLdfvpepreakvdy 388
Cdd:cd00327 179 DAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------PREPRT------------- 237
|
330
....*....|....*.
gi 46195975 389 ALSNSFAFGGHNAVLV 404
Cdd:cd00327 238 VLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
82-404 |
3.15e-29 |
|
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: 115.12 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 82 ALEDAGLKPEDLDPERVGTLVGTGiggmetweaqsrvflergpnrispffipmmianmasahiamrygFTGPSSTVVTAC 161
Cdd:smart00825 62 ALEDAGIDPESLRGSRTGVFVGVS--------------------------------------------SSDYSVTVDTAC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 162 ATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALStrneePEKASRPFTLSRDGFVMGEGAGVLVLEAY 241
Cdd:smart00825 98 SSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLKRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 242 EHAKKRGARIYAELVGFGRSADAHH--ITEPHPEGkgaalamaralkdagiapeQvgyinahgtstpagdraevlaikrv 319
Cdd:smart00825 173 SDALRDGDPILAVIRGSAVNQDGRSngITAPSGPA-------------------Q------------------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 320 fgdhakrLMVSSTKSMIGHLLGAAGAVEAIATVQALYHGVIPPTINLEDPDPELDLDF---------VPEPREAKVDYAL 390
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEEsplrvptelTPWPPPGRPRRAG 281
|
330
....*....|....
gi 46195975 391 SNSFAFGGHNAVLV 404
Cdd:smart00825 282 VSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
2-257 |
7.76e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 78.46 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 2 RRVVVTGLGALTPIGVGQEAfHKAQLAGKsgvRPITRFDASAL---PVRIAAEVDVD---PgaylDRKELRRLDRFVQYA 75
Cdd:PRK06519 6 NDVVITGIGLVSSLGEGLDA-HWNALSAG---RPQPNVDTETFapyPVHPLPEIDWSqqiP----KRGDQRQMETWQRLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 76 LIAAQLALEDAGLKPedlDPERVGTL--------------VGTGIGGMETWEAQSRVFL-ERGPNRISPFFIPMMIANMA 140
Cdd:PRK06519 78 TYAAGLALDDAGIKG---NEELLSTMdmivaagggerdiaVDTAILNEARKRNDRGVLLnERLMTELRPTLFLAQLSNLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 141 SAHIAMRYGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTRNEEPEKASRPf 220
Cdd:PRK06519 155 AGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPVWSRGG- 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 46195975 221 tLSRDGFVMGEGAGVLVLEAYEHAKKRGARIYAELVG 257
Cdd:PRK06519 234 -EDGGGFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
66-301 |
2.39e-09 |
|
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: 58.43 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 66 RRLDR-FVQYALIAAQLALEDAGLKPEDLDPERVGTLVGtgiggmetweaqsrvflergpnrispFFIPMMIANMASAHI 144
Cdd:cd00829 10 RRSDRsPLELAAEAARAALDDAGLEPADIDAVVVGNAAG--------------------------GRFQSFPGALIAEYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 145 AMRYGftgPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEA--------------------------AITPMAIG 198
Cdd:cd00829 64 GLLGK---PATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKmsdvptgdeaggrasdlewegpeppgGLTPPALY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 199 A-------------------FAV-MRALSTRNE----------EPEKASR----PFTLSrDGFVMGEGAGVLVLeAYEHA 244
Cdd:cd00829 141 AlaarrymhrygttredlakVAVkNHRNAARNPyaqfrkpitvEDVLNSRmiadPLRLL-DCCPVSDGAAAVVL-ASEER 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 46195975 245 KKRGARIYAELVGFGRSADAHHITEPHPEGK--GAALAMARALKDAGIAPEQVGYINAH 301
Cdd:cd00829 219 ARELTDRPVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
148-298 |
3.75e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 51.56 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 148 YGFTGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAITPMAIGAFAVMRALSTrneepekASRPftlsrDGF 227
Cdd:PRK06147 120 LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-------SQNS-----NGF 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46195975 228 VMGEGAGVLVLEAYEHAKKRGARIYAelVGFGRSADAHHITEPHP-EGKGAALAMARALKDAGIAPEQVGYI 298
Cdd:PRK06147 188 IPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
153-233 |
4.48e-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: 48.52 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 153 PSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAAIT-PMAIGAFAVMRALSTRNEEPEKASRpFTLSRDGFVMGE 231
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLPKARWGYRMNAKLVDPMINPG-LTDPYTGLSMGE 158
|
..
gi 46195975 232 GA 233
Cdd:COG0183 159 TA 160
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
77-189 |
2.88e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 45.91 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 77 IAAQLALEDAGLKPEDLDPERVGTLVGTGIGgmetweaqsrvfleRGPNRispffipmmianmasaHIAMRYGF--TGPS 154
Cdd:PRK05790 32 IVIKAALERAGVPPEQVDEVIMGQVLQAGAG--------------QNPAR----------------QAALKAGLpvEVPA 81
|
90 100 110
....*....|....*....|....*....|....*
gi 46195975 155 STVVTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
82-233 |
6.45e-05 |
|
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: 44.91 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 82 ALEDAGLKPEDLDPERVGTLVGTGIGgmetweaqsrvflergpnrispffipMMIANMASahIAMRYGFTGPSSTVVTAC 161
Cdd:TIGR01930 32 LLERNPLDPELIDDVIFGNVLQAGEQ--------------------------QNIARQAA--LLAGLPESVPAYTVNRQC 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46195975 162 ATGADALGSALRMIQLGEADLVLAGGTEAA-----ITPMAIGAFAVMRALSTRNEEPEKASRPFTlsrdGFVMGEGA 233
Cdd:TIGR01930 84 ASGLQAVILAAQLIRAGEADVVVAGGVESMsrvpyGVPRSLRWGVKPGNAELEDARLKDLTDANT----GLPMGVTA 156
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
229-345 |
7.12e-05 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 44.70 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 229 MGEGAGVLVLEAYEHAKKRGARIYAELVGFGRSADAHHITEPHPegkgaALAMARALKDAGIAPEQVGY--INaHGTSTP 306
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAP-----ALAIPKALKHAGLEASQVDYyeIN-EAFSVV 323
|
90 100 110
....*....|....*....|....*....|....*....
gi 46195975 307 AgdraevLAIKRVFGDHAKRLMVSSTKSMIGHLLGAAGA 345
Cdd:PLN02644 324 A------LANQKLLGLDPEKVNVHGGAVSLGHPIGCSGA 356
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
153-189 |
7.86e-05 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 44.56 E-value: 7.86e-05
10 20 30
....*....|....*....|....*....|....*..
gi 46195975 153 PSSTVVTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVE 118
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
78-189 |
1.04e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 44.12 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 78 AAQLALEDAGLKPEDLDpervGTLVGTGIGGMetWEAQSRvflergpnrispffIPMMIANMAS-AHIamrygftgPSST 156
Cdd:PRK06064 29 AGLEALEDAGIDGKDID----AMYVGNMSAGL--FVSQEH--------------IAALIADYAGlAPI--------PATR 80
|
90 100 110
....*....|....*....|....*....|...
gi 46195975 157 VVTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:PRK06064 81 VEAACASGGAALRQAYLAVASGEADVVLAAGVE 113
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
77-189 |
1.17e-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: 43.45 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 77 IAAQLALEDAGLKPEDLDPERVGTLVGTGIGgmetweaqsrvflergpnrispffipMMIANMAsahiAMRYGF--TGPS 154
Cdd:pfam00108 29 EAIKAALERAGVDPEDVDEVIVGNVLQAGEG--------------------------QNPARQA----ALKAGIpdSAPA 78
|
90 100 110
....*....|....*....|....*....|....*
gi 46195975 155 STVVTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:pfam00108 79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVE 113
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
143-189 |
1.57e-04 |
|
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: 43.62 E-value: 1.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 46195975 143 HIAMRYGF--TGPSSTVVTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:cd00751 64 QAALLAGLpeSVPATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVE 112
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
71-191 |
2.26e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 43.21 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 71 FVQYALIAAQLALEDAGLKPEDLDPERVGTLVGTGIGGMetweaqsrvflergpnrispffipmmianMASAHIAMRYGF 150
Cdd:PRK06059 23 FVEYGVVAARAALADAGLDWRDVQLVVGADTIRNGYPGF-----------------------------VAGATFAQALGW 73
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 46195975 151 TG-PSSTVVTACATGADALGSALRMIQLGEADLVLAGGTEAA 191
Cdd:PRK06059 74 NGaPVSSSYAACASGSQALQSARAQILAGLCDVALVVGADTT 115
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
78-189 |
4.14e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 42.30 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 78 AAQLALEDAGLKPEDLDPERVGTLVGTGIGgmetweaqsrvfleRGPnrispffipmmiANMASAHIAMRYGFTgpSSTV 157
Cdd:PRK06366 33 AIKAVIDDAKLDPALVQEVIMGNVIQAGVG--------------QNP------------AGQAAYHAGLPFGVT--KYTV 84
|
90 100 110
....*....|....*....|....*....|..
gi 46195975 158 VTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:PRK06366 85 NVVCASGMLAVESAAREIMLGERDLVIAGGME 116
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
77-190 |
5.79e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 38.54 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 77 IAAQLALEDAGLKPEDLDPERVGTLVGTGIGGMetweaqsrvflergPNRIspffipmmianmasahiAMRYG---FTGP 153
Cdd:PRK08235 32 IAIKEALERANVSAEDVEEVIMGTVLQGGQGQI--------------PSRQ-----------------AARAAgipWEVQ 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 46195975 154 SSTVVTACATGADALGSALRMIQLGEADLVLAGGTEA 190
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMES 117
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
78-189 |
6.45e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 38.39 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195975 78 AAQLALEDAGLKPEDLDpervGTLVGTGIGGMetweaqsrvflergpnriSPFFIPMMIANMASAHIAMRygftgPSSTV 157
Cdd:PRK07516 29 VAREALAHAGIAAGDVD----GIFLGHFNAGF------------------SPQDFPASLVLQADPALRFK-----PATRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 46195975 158 VTACATGADALGSALRMIQLGEADLVLAGGTE 189
Cdd:PRK07516 82 ENACATGSAAVYAALDAIEAGRARIVLVVGAE 113
|
|
| |
