|
Name |
Accession |
Description |
Interval |
E-value |
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-410 |
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: 620.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:COG0304 2 RVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSAC 162
Cdd:COG0304 82 ALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTAC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 163 AIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILESL 242
Cdd:COG0304 162 ASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 243 SHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFG 322
Cdd:COG0304 242 EHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 323 KQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGGHN 402
Cdd:COG0304 322 DHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHN 401
|
....*...
gi 1261283549 403 AAIVLKKY 410
Cdd:COG0304 402 ASLVFKRY 409
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-408 |
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: 609.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:TIGR03150 2 RVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSAC 162
Cdd:TIGR03150 82 AVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTAC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 163 AIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILESL 242
Cdd:TIGR03150 162 ATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 243 SHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFG 322
Cdd:TIGR03150 242 EHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 323 KQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGGHN 402
Cdd:TIGR03150 322 DHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGTN 401
|
....*.
gi 1261283549 403 AAIVLK 408
Cdd:TIGR03150 402 ASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-411 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 587.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAA 80
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 81 EQAWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVS 160
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 161 ACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILE 240
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 241 SLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKEL 320
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 321 FGKQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGG 400
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|.
gi 1261283549 401 HNAAIVLKKYE 411
Cdd:PRK07314 401 TNASLVFKRYE 411
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-407 |
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: 567.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:cd00834 2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSAC 162
Cdd:cd00834 82 ALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTAC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 163 AIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILESL 242
Cdd:cd00834 162 ASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 243 SHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFG 322
Cdd:cd00834 242 EHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 323 KQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGGHN 402
Cdd:cd00834 322 EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGHN 401
|
....*
gi 1261283549 403 AAIVL 407
Cdd:cd00834 402 ASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-411 |
2.00e-173 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 491.05 E-value: 2.00e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRD--------FDADEILGKKEARRLDRF 72
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 73 SQFAIAAAEQAWADSKLDLNHI-DRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNA 151
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPDTLeDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 152 MGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTR-NDAPTQASRPFDEDRDGFVM 230
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 231 SEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGD 310
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 311 ISETKAIKELFGkQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCD-LDYVPGIARQVKIN 389
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401
|
410 420
....*....|....*....|..
gi 1261283549 390 TGVSNSFGFGGHNAAIVLKKYE 411
Cdd:PRK06333 402 YALSNGFGFGGVNASILFRRWE 423
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-410 |
5.44e-149 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 428.38 E-value: 5.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAA 80
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 81 EQAWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVS 160
Cdd:PRK08439 81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 161 ACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILE 240
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 241 SLSHALRRGAKIYAEVIGYGASSDAHHMvaTHPEGKGAYLAMKAALKNANIPleEIDVISAHATSTKVGDISETKAIKEL 320
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHI--TSPAPEGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 321 FGKQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGG 400
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396
|
410
....*....|
gi 1261283549 401 HNAAIVLKKY 410
Cdd:PRK08439 397 TNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-410 |
2.78e-148 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 427.19 E-value: 2.78e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 11 VVSPIGNNIRTFWNNLIKGESGISSIDTFDIT---------DHKAKIAGIVRDFDAdEILGKKE-------ARRLDRFSQ 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFlpdcipeqkALENLVAAMPCQIAA-EVDQSEFdpsdfapTKRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 75 FAIAAAEQAWADSKLD-LNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMG 153
Cdd:PTZ00050 80 FAMAAAREALADAKLDiLSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 154 PSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTR-NDAPTQASRPFDEDRDGFVMSE 232
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVMGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 233 GAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKN-ANIPLEEIDVISAHATSTKVGDI 311
Cdd:PTZ00050 240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 312 SETKAIKELFG-KQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINT 390
Cdd:PTZ00050 320 IELKAIKKVFGdSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQSI 399
|
410 420
....*....|....*....|..
gi 1261283549 391 GV--SNSFGFGGHNAAIVLKKY 410
Cdd:PTZ00050 400 DAvlSTSFGFGGVNTALLFTKY 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-409 |
7.20e-133 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 387.82 E-value: 7.20e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:PRK08722 5 RVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSAC 162
Cdd:PRK08722 85 ALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTAC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 163 AIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILILESL 242
Cdd:PRK08722 165 TTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEEY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 243 SHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFG 322
Cdd:PRK08722 245 EHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 323 KQ-AYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVK-INTGVSNSFGFGG 400
Cdd:PRK08722 325 EAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSFGFGG 404
|
....*....
gi 1261283549 401 HNAAIVLKK 409
Cdd:PRK08722 405 TNGSLIFKK 413
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-407 |
2.28e-122 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 361.80 E-value: 2.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSI--------DTFDITDHKA------KIAGIV------RDFDADEILg 62
Cdd:PLN02836 7 RVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqddlkmkSEDEETQLYTldqlpsRVAALVprgtgpGDFDEELWL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 63 kkEARRLDRFSQFAIAAAEQAWADSK-LDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAA 141
Cdd:PLN02836 86 --NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 142 AAQISIKWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTR-NDAPTQASRP 220
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 221 FDEDRDGFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVIS 300
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 301 AHATSTKVGDISETKAIKELFGKQAYQ--IPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDY 378
Cdd:PLN02836 324 AHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGF 403
|
410 420 430
....*....|....*....|....*....|
gi 1261283549 379 VPGIA-RQVKINTGVSNSFGFGGHNAAIVL 407
Cdd:PLN02836 404 VPLTAsKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-410 |
3.48e-113 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 341.96 E-value: 3.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:PLN02787 130 RVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGKK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLD---LNHIDRERLGVYVGSGIGGIETLIENIDALRQKgPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPV 159
Cdd:PLN02787 210 ALADGGITedvMKELDKTKCGVLIGSAMGGMKVFNDAIEALRIS-YRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSIS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 160 SACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGAGILIL 239
Cdd:PLN02787 289 TACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLLL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 240 ESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKE 319
Cdd:PLN02787 369 EELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 320 LFGkQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQ-VKINTGVSNSFGF 398
Cdd:PLN02787 449 CFG-QNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKErLDIKVALSNSFGF 527
|
410
....*....|..
gi 1261283549 399 GGHNAAIVLKKY 410
Cdd:PLN02787 528 GGHNSSILFAPY 539
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-410 |
1.51e-105 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 318.21 E-value: 1.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 4 VVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDIT--DHKAKIAG-IVRDFDADeiLGKKEARRLDRFSQFAIAAA 80
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEefDLPVRIGGhLLEEFDHQ--LTRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 81 EQAWADSKLDlnHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVS 160
Cdd:PRK07910 92 RRVWENAGSP--EVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 161 ACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATA-LSTRNDAPTQASRPFDEDRDGFVMSEGAGILIL 239
Cdd:PRK07910 170 ACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 240 ESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKE 319
Cdd:PRK07910 250 ETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 320 LFGKQayQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFG 399
Cdd:PRK07910 330 ALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFG 407
|
410
....*....|.
gi 1261283549 400 GHNAAIVLKKY 410
Cdd:PRK07910 408 GHNVALAFGRY 418
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-411 |
1.19e-101 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 307.75 E-value: 1.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVrDFDADEILGKKEARRLDRFSQFAIAAA 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNV-KLDPTGLIDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 81 EQAWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQ-KGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPV 159
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 160 SACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVAsFGNATALSTR-NDAPTQASRPFDEDRDGFVMSEGAGILI 238
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 239 LESLSHALRRGAKIYAEVIGYGASSDAHHMVAthPEGKGAYLAMKAALKNANIPleeIDVISAHATSTKVGDISETKAIK 318
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVDTP---IDYINTHGTSTPVGDVKELGAIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 319 ELFGKQAyqIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDP-LCDLDYVPGIARQVKINTGVSNSFG 397
Cdd:PRK07967 314 EVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPqAAGMPIVTETTDNAELTTVMSNSFG 391
|
410
....*....|....
gi 1261283549 398 FGGHNAAIVLKKYE 411
Cdd:PRK07967 392 FGGTNATLVFRRYK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
91-410 |
1.07e-96 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 292.79 E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 91 LNHID----RERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSACAIGN 166
Cdd:PRK14691 16 LTHADntekQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 167 TAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTR-NDAPTQASRPFDEDRDGFVMSEGAGILILESLSHA 245
Cdd:PRK14691 96 QAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 246 LRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFGkQA 325
Cdd:PRK14691 176 LARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFG-ES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 326 YQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCD-LDYVPGIARQVKINTGVSNSFGFGGHNAA 404
Cdd:PRK14691 255 NALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNAS 334
|
....*.
gi 1261283549 405 IVLKKY 410
Cdd:PRK14691 335 ILLKRW 340
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-408 |
2.75e-89 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 276.10 E-value: 2.75e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDH-KAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAA 79
Cdd:PRK09116 1 MRRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGlNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 80 AEQAWADSKLdLNH--IDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMS 157
Cdd:PRK09116 81 SELALEDAGL-LGDpiLTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPHTTAVNVGLFFGLKGRVIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 158 PVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEaaitDLS---VASFGNATALSTRNDAPTQASRPFDEDRDGFVMSEGA 234
Cdd:PRK09116 160 TSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAE----ELCpteAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 235 GILILESLSHALRRGAKIYAEVIGYGASSDAHHMvaTHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISET 314
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHV--TQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 315 KAIKELFGKqayQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLC-DLDYVPGIARQVKINTGVS 393
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMS 390
|
410
....*....|....*
gi 1261283549 394 NSFGFGGHNAAIVLK 408
Cdd:PRK09116 391 NNFAFGGINTSLIFK 405
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-407 |
2.91e-87 |
|
"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: 270.85 E-value: 2.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 2 ERVVITGMGVVSPIGNNIR---TFWNNLIKGESGISSIDTFDItDHKAKIAGIVRDFDADEilgkKEARR---LDRFSQF 75
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDeveEFWEALREGRSGIAPVARLKS-RFDRGVAGQIPTGDIPG----WDAKRtgiVDRTTLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 76 AIAAAEQAWADSKL-DLNHIDRERLGVYVGSGIGGIETLIENIDALRqkgpRRVSPTLVPGMI--SNAAAAQISIKWN-A 151
Cdd:cd00828 76 ALVATEEALADAGItDPYEVHPSEVGVVVGSGMGGLRFLRRGGKLDA----RAVNPYVSPKWMlsPNTVAGWVNILLLsS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 152 MGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAaITDLSVASFGNATALSTRNDAPTQASRPFDEDRDGFVMS 231
Cdd:cd00828 152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 232 EGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPeGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDI 311
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 312 SETKAIKELFGKQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIAR--QVKIN 389
Cdd:cd00828 310 AESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVR 389
|
410
....*....|....*...
gi 1261283549 390 TGVSNSFGFGGHNAAIVL 407
Cdd:cd00828 390 AALVNAFGFGGSNAALVL 407
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-410 |
8.48e-87 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 270.35 E-value: 8.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 4 VVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVrDFDADEILGKKEarRLDRFSQFAIAAAEQA 83
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DFLPESPFGASA--LSEALARLAAEEALAQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 84 WADSKLD-------------LNHIDRERLGVYVG-SGIGGIETLIEnidALRQKGPRRVSPTLVPGMISNAAAaqisikw 149
Cdd:PRK06501 90 AGIGKGDfpgplflaappveLEWPARFALAAAVGdNDAPSYDRLLR---AARGGRFDALHERFQFGSIADRLA------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 150 NAMGPSMSPVS---ACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAPTQASRPFDEDRD 226
Cdd:PRK06501 160 DRFGTRGLPISlstACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 227 GFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATST 306
Cdd:PRK06501 240 GFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 307 KVGDISETKAIKELFGKQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQV 386
Cdd:PRK06501 320 PENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDA 399
|
410 420
....*....|....*....|....
gi 1261283549 387 KINTGVSNSFGFGGHNAAIVLKKY 410
Cdd:PRK06501 400 RVTAVLSNSFGFGGQNASLVLTAE 423
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-409 |
8.53e-78 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 245.73 E-value: 8.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTfWNNLIKGESGISSIDTFdiTDHKAKIAGIVRDFDADeilgkkearrldrFSQFAIAAA 80
Cdd:PRK05952 1 MMKVVVTGIGLVSALGDLEQS-WQRLLQGKSGIKLHQPF--PELPPLPLGLIGNQPSS-------------LEDLTKTVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 81 EQAWADSKLDLNHIDrerLGVYVGS--GIGGI-ETLIENIDALRQKGPRRVSP----TLVPGMISNAAAAQISIKwnamG 153
Cdd:PRK05952 65 TAALKDAGLTPPLTD---CGVVIGSsrGCQGQwEKLARQMYQGDDSPDEELDLenwlDTLPHQAAIAAARQIGTQ----G 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 154 PSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALstrndAPTQASrPFDEDRDGFVMSEG 233
Cdd:PRK05952 138 PVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGAL-----AKTGAY-PFDRQREGLVLGEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 234 AGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISE 313
Cdd:PRK05952 212 GAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQRE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 314 TKAIKELFGkqaYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDplCDLDYVPGiARQVKINTGVS 393
Cdd:PRK05952 292 ANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFVRQ-AQQSPLQNVLC 365
|
410
....*....|....*.
gi 1261283549 394 NSFGFGGHNAAIVLKK 409
Cdd:PRK05952 366 LSFGFGGQNAAIALGK 381
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-407 |
7.85e-74 |
|
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: 235.72 E-value: 7.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 3 RVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIVRDFDADEILGKKEARRLDRFSQFAIAAAEQ 82
Cdd:cd00832 2 RAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAADW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 83 AWADSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGMISNAAAAQISIKWNAMGPSMSPVSAC 162
Cdd:cd00832 82 ALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAEQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 163 AIGNTAIGEAFRLIRSGeVDAVFAGGTEAAITDLSVASFGNATALSTRNDaPTQASRPFDEDRDGFVMSEGAGILILESL 242
Cdd:cd00832 162 AGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDD-PARAYLPFDAAAAGYVPGEGGAILVLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 243 SHALRRGAKIYAEVIGYGASSDAhhmvATHPeGKGAYL--AMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKEL 320
Cdd:cd00832 240 AAARERGARVYGEIAGYAATFDP----PPGS-GRPPGLarAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 321 FGkqAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLDYVPGIARQVKINTGVSNSFGFGG 400
Cdd:cd00832 315 FG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGG 392
|
....*..
gi 1261283549 401 HNAAIVL 407
Cdd:cd00832 393 FNSALVV 399
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
2-407 |
2.42e-63 |
|
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: 209.34 E-value: 2.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 2 ERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDT--FDITDHKA----------KIAGIVRDFDADEI----LGKKE 65
Cdd:cd00833 1 EPIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEdrWDADGYYPdpgkpgktytRRGGFLDDVDAFDAaffgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 66 ARRLDR------------FsqfaiaaaeqawADSKLDLNHIDRERLGVYVGSGigGIETLienidALRQKGPRRVSPTLV 133
Cdd:cd00833 81 AEAMDPqqrlllevaweaL------------EDAGYSPESLAGSRTGVFVGAS--SSDYL-----ELLARDPDEIDAYAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 134 PGMISNAAAAQISIKWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALStrnda 213
Cdd:cd00833 142 TGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 214 PTQASRPFDEDRDGFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPL 293
Cdd:cd00833 217 PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 294 EEIDVISAHATSTKVGDISETKAIKELFGKQAYQ---IPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENP 370
Cdd:cd00833 297 SDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETP 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1261283549 371 DPLCDLD----YVPGIARQVKINTGVS----NSFGFGGHNAAIVL 407
Cdd:cd00833 377 NPKIDFEesplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVIL 421
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-409 |
2.90e-62 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 206.04 E-value: 2.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSI------DTFDITDHKAK--IAGIVRDFDADEILGKKEARRLDRF 72
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMrrpgrqVPDDAGAGLASafIGAELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 73 SQFAIAAAEQAWADSKLDlnHIDRERLGVYVGsgiGGIETLIENIDALR--QKGPRRVSPTL-VPGMISNAAAAqISIKW 149
Cdd:PRK07103 81 AQAALAAAREAWRDAALG--PVDPDRIGLVVG---GSNLQQREQALVHEtyRDRPAFLRPSYgLSFMDTDLVGL-CSEQF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 150 NAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGteaAITDLS---VASFGNATALSTRNDA--PTQASRPFDED 224
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVG---ALMDLSyweCQALRSLGAMGSDRFAdePEAACRPFDQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 225 RDGFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAylAMKAALKNANIPLEEIDVISAHAT 304
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPEDIDYVNPHGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 305 STKVGDISETKAikeLFGKQAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENP-DPlcDLDYVPGIA 383
Cdd:PRK07103 310 GSPLGDETELAA---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDE--RFRWVGSTA 384
|
410 420
....*....|....*....|....*.
gi 1261283549 384 RQVKINTGVSNSFGFGGHNAAIVLKK 409
Cdd:PRK07103 385 ESARIRYALSLSFGFGGINTALVLER 410
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-245 |
1.31e-56 |
|
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: 186.30 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 2 ERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDT--FDITDH-----------KAKIAGIVRDFDADEILGK---KE 65
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPAdrWDPDKLydppsriagkiYTKWGGLDDIFDFDPLFFGispRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 66 ARRLDRFSQFAIAAAEQAWADSKLDLNHIDRERLGVYVGSGIGGIETLIEnidALRQKGPRRVSPTLVPGMiSNAAAAQI 145
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLL---LDEDGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 146 SIKWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTrnDAPTQASRPFDedr 225
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
|
250 260
....*....|....*....|
gi 1261283549 226 DGFVMSEGAGILILESLSHA 245
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
86-407 |
9.79e-56 |
|
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: 186.69 E-value: 9.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 86 DSKLDLNHIDRERLGVYVGSGIGGIETLIENIDALRQKGPRRVSPTLVPGmisnaAAAQISIKWNAMGPSMSPVSACAIG 165
Cdd:cd00825 25 DAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHGPAYDVSAACAGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 166 NTAIGEAFRLIRSGEVDAVFAGGTEA-AITDLSVASFGnatalsTRNDAPTQASRPFDEDRDGFVMSEGAGILILESLSH 244
Cdd:cd00825 100 LHALSLAADAVQNGKQDIVLAGGSEElAAPMDCEFDAM------GALSTPEKASRTFDAAADGFVFGDGAGALVVEELEH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 245 ALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFGKQ 324
Cdd:cd00825 174 ALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 325 ayQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPlcDLDYVPGIARQVKINTGVSNSFGFGGHNAA 404
Cdd:cd00825 254 --SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALLNGFGLGGTNAT 329
|
...
gi 1261283549 405 IVL 407
Cdd:cd00825 330 LVL 332
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-407 |
9.17e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 167.33 E-value: 9.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGISSIDTFDITDHKAKIAGIV-----------RDFD------ADEILGK 63
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRASGMRPCDFWLVDLPTWVGEVVgvelpalpaalAAFDcrnnrlALLALQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 64 KEARRLDRFSQFAiaaaeqawadskldlnhidRERLGVYVG---SGIGgietliENIDALRQKgpRRVSPTL-----VPG 135
Cdd:PRK09185 81 IEPAVEAAIARYG-------------------ADRIGVVLGtstSGIL------EGELAYRRR--DPAHGALpadyhYAQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 136 MISNAAAAQISIKWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAaITDLSVASFGNATALSTrndapt 215
Cdd:PRK09185 134 QELGSLADFLRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 216 QASRPFDEDRDGFVMSEGAGILILEslshalrRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEE 295
Cdd:PRK09185 207 QPCRPFSANRDGINIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPAD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 296 IDVISAHATSTKVGDISETKAIKELFGKqayQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCD 375
Cdd:PRK09185 280 IGYINLHGTATPLNDAMESRAVAAVFGD---GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALP 356
|
410 420 430
....*....|....*....|....*....|..
gi 1261283549 376 LDYVPGIARQVKINTGVSNSFGFGGHNAAIVL 407
Cdd:PRK09185 357 PLYLVENAQALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1-407 |
3.74e-47 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 173.52 E-value: 3.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 1 MERVVITGMGVVSPIGNNIRTFWNNLIKGESGIS-------SIDTFDITDHKA------KIAGIVRD---FDADEI-LGK 63
Cdd:COG3321 3 DEPIAIIGMACRFPGADDPEEFWRNLRAGRDAITevpadrwDADAYYDPDPDApgktyvRWGGFLDDvdeFDALFFgISP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 64 KEARRLD---RFSqfaiaaaeqawadskLD-----LNH--IDRERL-----GVYVGSGIGGIETLIenidalrQKGPRRV 128
Cdd:COG3321 83 REAEAMDpqqRLL---------------LEvaweaLEDagYDPESLagsrtGVFVGASSNDYALLL-------LADPEAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 129 SPTLVPGMISNAAAAQISIKWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALS 208
Cdd:COG3321 141 DAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 209 trndaPTQASRPFDEDRDGFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKN 288
Cdd:COG3321 221 -----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALAD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 289 ANIPLEEIDVISAHATSTKVGDISETKAIKELFGKQAYQ---IPITANKSMIGH------------MlgaaggaeaialA 353
Cdd:COG3321 296 AGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHleaaagvaglikA------------V 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261283549 354 MSLKEGIIPPTINLENPDPLCDLDYVPgiarqVKINT--------------GVSnSFGFGGHNAAIVL 407
Cdd:COG3321 364 LALRHGVLPPTLHFETPNPHIDFENSP-----FYVNTelrpwpagggprraGVS-SFGFGGTNAHVVL 425
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-368 |
1.62e-33 |
|
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: 121.52 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 253 YAEVIGYGASSDAHHMVATHPEGKGAYLAMKAALKNANIPLEEIDVISAHATSTKVGDISETKAIKELFGKQAYQ--IPI 330
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1261283549 331 TANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLE 368
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
95-410 |
3.47e-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: 126.66 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 95 DRERLGVYVGsgIGGIETLIENIDAlRQKGP--RRV----------SPTLV---------------PGMISNAAAAQISI 147
Cdd:TIGR02813 115 DRDKIGITLG--VGGGQKQSSSLNA-RLQYPvlKKVfkasgvededSEMLIkkfqdqyihweensfPGSLGNVISGRIAN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 148 KWNAMGPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTRNDAptqasRPFDEDRDG 227
Cdd:TIGR02813 192 RFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDI-----QPFDIDSKG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 228 FVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAH--HMVATHPEGKGAylAMKAALKNANIPLEEIDVISAHATS 305
Cdd:TIGR02813 267 MMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAK--ALKRAYDDAGFAPHTCGLIEAHGTG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 306 TKVGDISETKAIKELFGK---QAYQIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTINLENPDPLCDLD----Y 378
Cdd:TIGR02813 345 TAAGDVAEFGGLVSVFSQdndQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIEnspfY 424
|
330 340 350
....*....|....*....|....*....|....*....
gi 1261283549 379 V-----PGIARQ--VKINTGVSnSFGFGGHNAAIVLKKY 410
Cdd:TIGR02813 425 LntetrPWMQREdgTPRRAGIS-SFGFGGTNFHMVLEEY 462
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
140-407 |
7.37e-28 |
|
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: 110.61 E-value: 7.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 140 AAAAQISIKWNAM-GPSMSPVSACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAaitdlsvasfgnatalstrndaptqas 218
Cdd:cd00327 45 GAAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE--------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 219 rpfdedrdgFVMSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVaTHPEGKGAYLAMKAALKNANIPLEEIDV 298
Cdd:cd00327 98 ---------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 299 ISAHATSTKVGDISETKAIKELFGKQAyqIPITANKSMIGHMLGAAGGAEAIALAMSLKEGIIPPTinlenPDPLcdldy 378
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----PREP----- 235
|
250 260
....*....|....*....|....*....
gi 1261283549 379 vpgiarqvkiNTGVSNSFGFGGHNAAIVL 407
Cdd:cd00327 236 ----------RTVLLLGFGLGGTNAAVVL 254
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
161-407 |
8.01e-23 |
|
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: 97.40 E-value: 8.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 161 ACAIGNTAIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALStrndaPTQASRPFDEDRDGFVMSEGAGILILE 240
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 241 SLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEGKGaylamkaalknanipleeidvisahatstkvgdisetkaikel 320
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPA------------------------------------------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 321 fgkqayQIPITANKSMIGH------------MlgaaggaeaialAMSLKEGIIPPTINLENPDPLCDLDyvpgiARQVKI 388
Cdd:smart00825 208 ------QLLIGSVKSNIGHleaaagvaglikV------------VLALKHGVIPPTLHFETPNPHIDLE-----ESPLRV 264
|
250 260 270
....*....|....*....|....*....|...
gi 1261283549 389 NT--------------GVsNSFGFGGHNAAIVL 407
Cdd:smart00825 265 PTeltpwpppgrprraGV-SSFGFGGTNAHVIL 296
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
130-256 |
7.09e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 54.19 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 130 PTLVPGMISNAAAAQISIKWNA-------MGPSMSPVSACAIgntaigeAFRLIRSGEVDAVFAGGTEAAITD--LSVAS 200
Cdd:PRK06519 143 PTLFLAQLSNLLAGNISIVHKVtgssrtfMGEESAGVSAIEI-------AFARIASGQSDHALVGGAYNAERPdmLLLYE 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261283549 201 FGNataLSTRND-APTQASRPfdEDRDGFVMSEGAGILILESLSHALRRGAKIYAEV 256
Cdd:PRK06519 216 LGG---LLLKGGwAPVWSRGG--EDGGGFILGSGGAFLVLESREHAEARGARPYARI 267
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
230-302 |
3.76e-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: 42.47 E-value: 3.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261283549 230 MSEGAGILILESLSHALRRGAKIYAEVIGYGAssdahhmVATHPE--GKGAYLAMKAALKNANIPLEEIDVISAH 302
Cdd:cd00751 244 INDGAAAVLLMSEEKAKELGLKPLARIVGYAV-------AGVDPAimGIGPVPAIPKALKRAGLTLDDIDLIEIN 311
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
219-297 |
5.38e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 38.92 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 219 RP-FDEDrDGFV-------MSEGAGILILESLSHALRRGAKIYAEVIGYGASSDAHHMVATHPEgkgayLAMKAALKNAN 290
Cdd:PLN02644 232 RPsFKED-GGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPA-----LAIPKALKHAG 305
|
....*..
gi 1261283549 291 IPLEEID 297
Cdd:PLN02644 306 LEASQVD 312
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
168-297 |
6.35e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 38.46 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 168 AIGEAFRLIRSGEVDAVFAGGTEAAITDLSVASFGNATALSTrndaptqASRPfdedrDGFVMSEGAGILILESLSHALR 247
Cdd:PRK06147 139 ALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-------SQNS-----NGFIPGEAAAAVLLGRPAGGEA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1261283549 248 RGAKIYAevIGYGASSDAHHMVATHP-EGKGAYLAMKAALKNANIPLEEID 297
Cdd:PRK06147 207 PGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMD 255
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
224-299 |
8.13e-03 |
|
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: 38.12 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261283549 224 DRDGFV-------MSEGAGILILESLSHALRRGAKIYAEVIGYGAssdahhmVATHPE--GKGAYLAMKAALKNANIPLE 294
Cdd:COG0183 235 KKDGTVtagnasgINDGAAALLLMSEEAAKELGLKPLARIVAYAV-------AGVDPEimGIGPVPATRKALARAGLTLD 307
|
....*
gi 1261283549 295 EIDVI 299
Cdd:COG0183 308 DIDLI 312
|
|
| |
