|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-409 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 746.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 2 KRRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAG 81
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 82 MQAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVS 161
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 162 ACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLE 241
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 242 EYEHAKKRGARIYGELAGYGMSSDAHHITAP--DKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLA 319
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPapDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 320 FGDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGG 399
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 489910388 400 TNGSMAVRRV 409
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-407 |
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: 732.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVSA 162
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 163 CTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLEE 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 243 YEHAKKRGARIYGELAGYGMSSDAHHITAPDKDG--PRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLAF 320
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGegAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 321 GDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGGT 400
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 489910388 401 NGSMAVR 407
Cdd:TIGR03150 401 NASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-409 |
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: 664.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVSA 162
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 163 CTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLEE 242
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 243 YEHAKKRGARIYGELAGYGMSSDAHHITA--PDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLAF 320
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITApaPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 321 GDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGGT 400
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 489910388 401 NGSMAVRRV 409
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-406 |
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: 605.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVSA 162
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 163 CTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLEE 242
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 243 YEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGP--RRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLAF 320
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEgaARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 321 GDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGGT 400
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 489910388 401 NGSMAV 406
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-408 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 529.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 1 MKRRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKD--------FDVTQYMPAKEARQMDT 72
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 73 FIHYGLAAGMQAWRDCGL-EVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYG 151
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWdPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 152 MKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTR-NDDPTTASRPWDRDRDGFV 230
Cdd:PRK06333 162 FKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 231 LGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAP--DKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLG 308
Cdd:PRK06333 242 MGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGpeDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 309 DKNETDALKLAFGdHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECD-LDYCANEARPMKI 387
Cdd:PRK06333 322 DLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDM 400
|
410 420
....*....|....*....|.
gi 489910388 388 EIGLSNSFGFGGTNGSMAVRR 408
Cdd:PRK06333 401 DYALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-409 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 518.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVSA 162
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 163 CTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLEE 242
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 243 YEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRGILNALRNGGinADEVSYVNAHGTSTPLGDKNETDALKLAFGD 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKELFGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 323 HASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGGTNG 402
Cdd:PRK08439 320 KEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNG 399
|
....*..
gi 489910388 403 SMAVRRV 409
Cdd:PRK08439 400 VVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-409 |
2.17e-175 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 495.68 E-value: 2.17e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 2 KRRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAG 81
Cdd:PRK08722 3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 82 MQAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVS 161
Cdd:PRK08722 83 IQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAIST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 162 ACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVLVLE 241
Cdd:PRK08722 163 ACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 242 EYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRGIL--NALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLA 319
Cdd:PRK08722 243 EYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAmeAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 320 FGDHASKLV-VNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMK-IEIGLSNSFGF 397
Cdd:PRK08722 323 LGEAGSKQVlVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSFGF 402
|
410
....*....|..
gi 489910388 398 GGTNGSMAVRRV 409
Cdd:PRK08722 403 GGTNGSLIFKKM 414
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
12-409 |
2.87e-159 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 454.92 E-value: 2.87e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 12 IVSPVGNDIASAWDNIVNGRSGISRISRFD----------------PTPLTTHIAGEVK--DFDVTQYMPAKEArqmDTF 73
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPkflpdcipeqkalenlVAAMPCQIAAEVDqsEFDPSDFAPTKRE---SRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 74 IHYGLAAGMQAWRDCGL-EVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGM 152
Cdd:PTZ00050 78 THFAMAAAREALADAKLdILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 153 KGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTR-NDDPTTASRPWDRDRDGFVL 231
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 232 GEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDG--PRRGILNALRNGG-INADEVSYVNAHGTSTPLG 308
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGrgARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 309 DKNETDALKLAFGDH-ASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANE-ARPMK 386
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKtAHPLQ 397
|
410 420
....*....|....*....|....
gi 489910388 387 -IEIGLSNSFGFGGTNGSMAVRRV 409
Cdd:PTZ00050 398 sIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-404 |
2.48e-142 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 412.65 E-value: 2.48e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFD-PTP-------------LTTHIAGEV------KDFDVTQYM 62
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDlKMKsedeetqlytldqLPSRVAALVprgtgpGDFDEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 63 pakEARQMDTFIHYGLAAGMQAWRDCGLEVTETNA-ERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINL 141
Cdd:PLN02836 86 ---NSRSSSRFIGYALCAADEALSDARWLPSEDEAkERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 142 ISGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTR-NDDPTTASR 220
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 221 PWDRDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGpRRGIL---NALRNGGINADEVSY 297
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDG-RGAVLamtRALQQSGLHPNQVDY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 298 VNAHGTSTPLGDKNETDALKLAFGDHAS--KLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDL 375
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD 401
|
410 420 430
....*....|....*....|....*....|
gi 489910388 376 DYCANEARP-MKIEIGLSNSFGFGGTNGSM 404
Cdd:PLN02836 402 GFVPLTASKaMLIRAALSNSFGFGGTNASL 431
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-404 |
3.00e-124 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 370.08 E-value: 3.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 2 KRRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAG 81
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 82 MQAWRDCGLE---VTETNAERIGVIVGSGIGGLpRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYA 158
Cdd:PLN02787 208 KKALADGGITedvMKELDKTKCGVLIGSAMGGM-KVFNDAIEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 159 VVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGAGVL 238
Cdd:PLN02787 287 ISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 239 VLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGprRGIL----NALRNGGINADEVSYVNAHGTSTPLGDKNETD 314
Cdd:PLN02787 367 LLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEG--AGVIlcieKALAQSGVSKEDVNYINAHATSTKAGDLKEYQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 315 ALKLAFGDHaSKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLD-YCANEARPMKIEIGLSN 393
Cdd:PLN02787 445 ALMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSN 523
|
410
....*....|.
gi 489910388 394 SFGFGGTNGSM 404
Cdd:PLN02787 524 SFGFGGHNSSI 534
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3-409 |
2.83e-105 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 317.00 E-value: 2.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKdFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIG-VIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVS 161
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGlIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 162 ACTTGLHCIGDAARLIEYGDADVMLAGGAES---TVSPLgiggFAAMRALSTR-NDDPTTASRPWDRDRDGFVLGEGAGV 237
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEEldwEMSCL----FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 238 LVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRGILNALrnGGINADeVSYVNAHGTSTPLGDKNETDALK 317
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPSGEGAVRCMQMAL--ATVDTP-IDYINTHGTSTPVGDVKELGAIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 318 LAFGDHASKlvVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPE-CDLDYCANEARPMKIEIGLSNSFG 396
Cdd:PRK07967 314 EVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFG 391
|
410
....*....|...
gi 489910388 397 FGGTNGSMAVRRV 409
Cdd:PRK07967 392 FGGTNATLVFRRY 404
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
98-408 |
9.90e-99 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 297.80 E-value: 9.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 98 ERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLI 177
Cdd:PRK14691 26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 178 EYGDADVMLAGGAESTVSPLGIGGFAAMRALSTR-NDDPTTASRPWDRDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGE 256
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 257 LAGYGMSSDAHHIT--APDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLAFGDhASKLVVNSTKS 334
Cdd:PRK14691 186 IVGYGTSADAYHMTsgAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489910388 335 MTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECD-LDYCANEARPMKIEIGLSNSFGFGGTNGSMAVRR 408
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-408 |
1.24e-93 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 287.40 E-value: 1.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 5 VVITGLGIVSPVGNDIASAWDNIVNGRSGISR-----ISRFDptpLTTHIAGEVK-DFDvtQYMPAKEARQMDTFIHYGL 78
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEFD---LPVRIGGHLLeEFD--HQLTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 79 AAGMQAWRDCGleVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYA 158
Cdd:PRK07910 89 VLGRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 159 VVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRA-LSTRNDDPTTASRPWDRDRDGFVLGEGAGV 237
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 238 LVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRG--ILNALRNGGINADEVSYVNAHGTSTPLGDKNETDA 315
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGhaMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 316 LKLAFGDHasKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSF 395
Cdd:PRK07910 327 INNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSF 404
|
410
....*....|...
gi 489910388 396 GFGGTNGSMAVRR 408
Cdd:PRK07910 405 GFGGHNVALAFGR 417
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
3-407 |
1.21e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 281.88 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTP-LTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAG 81
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDgLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 82 MQAWRDCGL--EVTETNAERIGVIVGSGIGGLPrIEETQTEMLAKGPRRISPffvpASLINLIS----GQLSIAYGMKGP 155
Cdd:PRK09116 82 ELALEDAGLlgDPILTDGRMGIAYGSSTGSTDP-IGAFGTMLLEGSMSGITA----TTYVRMMPhttaVNVGLFFGLKGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 156 SYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAEStVSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGA 235
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 236 GVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDA 315
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 316 LKLAFGDHASklvVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPEC-DLDYCANEARPMKIEIGLSNS 394
Cdd:PRK09116 316 TAAVFGARMP---ISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMSNN 392
|
410
....*....|...
gi 489910388 395 FGFGGTNGSMAVR 407
Cdd:PRK09116 393 FAFGGINTSLIFK 405
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-404 |
1.06e-89 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 277.67 E-value: 1.06e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 5 VVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVkDFdvtqympAKEARQMDTFIHYGLA--AGM 82
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DF-------LPESPFGASALSEALArlAAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETN--------------------AERIGVIVGSGIGGLPRieetqtemlAKGPRRISPFFvPASLINLI 142
Cdd:PRK06501 85 EALAQAGIGKGDFPgplflaappvelewparfalAAAVGDNDAPSYDRLLR---------AARGGRFDALH-ERFQFGSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 143 SGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTTASRPW 222
Cdd:PRK06501 155 ADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 223 DRDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDG-PRRG-ILNALRNGGINADEVSYVNA 300
Cdd:PRK06501 235 SKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGsPAIGaIRAALADAGLTPEQIDYINA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 301 HGTSTPLGDKNETDALKLAFGDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCAN 380
Cdd:PRK06501 315 HGTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPN 394
|
410 420
....*....|....*....|....
gi 489910388 381 EARPMKIEIGLSNSFGFGGTNGSM 404
Cdd:PRK06501 395 VARDARVTAVLSNSFGFGGQNASL 418
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
4-408 |
2.71e-79 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 250.33 E-value: 2.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 4 RVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPL--------TTHIAGEVKDFDVTQYMPAKEARQMDTFIH 75
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPddagaglaSAFIGAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 76 YGLAAGMQAWRDC----------GLEVTETNAErigvivgsgIGGLPRIEETQTEMlakgPRRISPFFVPASLINLISGQ 145
Cdd:PRK07103 83 AALAAAREAWRDAalgpvdpdriGLVVGGSNLQ---------QREQALVHETYRDR----PAFLRPSYGLSFMDTDLVGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 146 LSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRN--DDPTTASRPWD 223
Cdd:PRK07103 150 CSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 224 RDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDGPRRGILNALRNGGINADEVSYVNAHGT 303
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 304 STPLGDKNETDALklaFGDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQ-DPECdlDYCANEA 382
Cdd:PRK07103 310 GSPLGDETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTA 384
|
410 420
....*....|....*....|....*.
gi 489910388 383 RPMKIEIGLSNSFGFGGTNGSMAVRR 408
Cdd:PRK07103 385 ESARIRYALSLSFGFGGINTALVLER 410
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
4-408 |
6.69e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 248.43 E-value: 6.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 4 RVVITGLGIVSPVGNDIASaWDNIVNGRSGISRISRFD---PTPLTThIAGEVKDF-DVTQymPAKEARQMDTfihyGLA 79
Cdd:PRK05952 3 KVVVTGIGLVSALGDLEQS-WQRLLQGKSGIKLHQPFPelpPLPLGL-IGNQPSSLeDLTK--TVVTAALKDA----GLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 80 AGMQawrDCGLEVTETnaerigvivgsgigglpRIEETQTEMLAK----GPRRISPFFVPASLINLISGQLSIA----YG 151
Cdd:PRK05952 75 PPLT---DCGVVIGSS-----------------RGCQGQWEKLARqmyqGDDSPDEELDLENWLDTLPHQAAIAaarqIG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 152 MKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTrnddptTASRPWDRDRDGFVL 231
Cdd:PRK05952 135 TQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 232 GEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHHITAPDKDG--PRRGILNALRNGGINADEVSYVNAHGTSTPLGD 309
Cdd:PRK05952 209 GEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGksAIAAIQQCLARSGLTPEDIDYIHAHGTATRLND 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 310 KNETDALKLAFGdhaSKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIfnQDPECDLDYcANEARPMKIEI 389
Cdd:PRK05952 289 QREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGL--QEPEFDLNF-VRQAQQSPLQN 362
|
410
....*....|....*....
gi 489910388 390 GLSNSFGFGGTNGSMAVRR 408
Cdd:PRK05952 363 VLCLSFGFGGQNAAIALGK 381
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
3-406 |
1.47e-78 |
|
"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: 248.12 E-value: 1.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIA---SAWDNIVNGRSGISRISRFdPTPLTTHIAGEVKDFDVTQYMpAKEARQMDTFIHYGLA 79
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDeveEFWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWD-AKRTGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 80 AGMQAWRDCGLEV-TETNAERIGVIVGSGIGGLprieETQTEMLAKGPRRISPFFVPA--SLINLISGQLSIAY-GMKGP 155
Cdd:cd00828 79 ATEEALADAGITDpYEVHPSEVGVVVGSGMGGL----RFLRRGGKLDARAVNPYVSPKwmLSPNTVAGWVNILLlSSHGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 156 SYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTvSPLGIGGFAAMRALSTRNDDPTTASRPWDRDRDGFVLGEGA 235
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 236 GVLVLEEYEHAKKRGARIYGELAGYGMSSD-AHHITAPDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETD 314
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDgAGRSVPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 315 ALKLAFGDHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEI--GLS 392
Cdd:cd00828 314 AIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVraALV 393
|
410
....*....|....
gi 489910388 393 NSFGFGGTNGSMAV 406
Cdd:cd00828 394 NAFGFGGSNAALVL 407
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-406 |
1.92e-78 |
|
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: 247.66 E-value: 1.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRISRFDPTPLTTHIAGEVKDFDVTQYMPAKEARQMDTFIHYGLAAGM 82
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 83 QAWRDCGLEVTETNAERIGVIVGSGIGGLpriEETQTEM---LAKGPRRISPFFVPASLINLISGQLSIAYGMKGPSYAV 159
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGF---EFGQRELqklWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 160 VSACTTGLHCIGDAARLIEYGdADVMLAGGAESTVSPLGIGGFAAMRALSTrNDDPTTASRPWDRDRDGFVLGEGAGVLV 239
Cdd:cd00832 158 VAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 240 LEEYEHAKKRGARIYGELAGYGMSSDAHHiTAPDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLA 319
Cdd:cd00832 236 LEDAAAARERGARVYGEIAGYAATFDPPP-GSGRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 320 FGDHAskLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEARPMKIEIGLSNSFGFGG 399
Cdd:cd00832 315 FGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGG 392
|
....*..
gi 489910388 400 TNGSMAV 406
Cdd:cd00832 393 FNSALVV 399
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-404 |
8.31e-68 |
|
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: 220.89 E-value: 8.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 4 RVVITGLGIVSPVGNDIASAWDNIVNGRSGISRI--SRFD----------PTPLTTHIAGEVKD---FDVTQY-MPAKEA 67
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpeDRWDadgyypdpgkPGKTYTRRGGFLDDvdaFDAAFFgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 68 RQMD------------TFIHYGLAAGMQAWRDCGLEVTETNAERIgvivgsgigglprieetqtEMLAKGPRRISPFFVP 135
Cdd:cd00833 82 EAMDpqqrlllevaweALEDAGYSPESLAGSRTGVFVGASSSDYL-------------------ELLARDPDEIDAYAAT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 136 ASLINLISGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALStrnddP 215
Cdd:cd00833 143 GTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----P 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 216 TTASRPWDRDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAH--HITAPDKDGPRRGILNALRNGGINAD 293
Cdd:cd00833 218 DGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQAALIRRAYARAGVDPS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 294 EVSYVNAHGTSTPLGDKNETDALKLAFGDHASK---LVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQD 370
Cdd:cd00833 298 DIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPN 377
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489910388 371 PECDLD----YCANEARPMKIEIGLS----NSFGFGGTNGSM 404
Cdd:cd00833 378 PKIDFEesplRVPTEARPWPAPAGPRragvSSFGFGGTNAHV 419
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
146-403 |
1.72e-63 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 208.54 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 146 LSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAEStVSPLGIGGFAAMRALSTrnddptTASRPWDRD 225
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP------QPCRPFSAN 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 226 RDGFVLGEGAGVLVLEeyehaKKRGARIYgeLAGYGMSSDAHHITAPDKDG--PRRGILNALRNGGINADEVSYVNAHGT 303
Cdd:PRK09185 216 RDGINIGEAAAFFLLE-----REDDAAVA--LLGVGESSDAHHMSAPHPEGlgAILAMQQALADAGLAPADIGYINLHGT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 304 STPLGDKNETDALKLAFGDHaskLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPECDLDYCANEAR 383
Cdd:PRK09185 289 ATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQ 365
|
250 260
....*....|....*....|
gi 489910388 384 PMKIEIGLSNSFGFGGTNGS 403
Cdd:PRK09185 366 ALAIRYVLSNSFAFGGNNCS 385
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-246 |
4.33e-58 |
|
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: 190.15 E-value: 4.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWDNIVNGRSGISRI--SRFDPT---PLTTHIAGEVK----------DFDVTQY-MPAKE 66
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDklyDPPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 67 ARQMDTFIHYGLAAGMQAWRDCGLEVTETNAERIGVIVGSGIGGLpriEETQTEMLAKGPRRISPFFVPASlINLISGQL 146
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 147 SIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTrnDDPTTASRPWDrdr 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
|
250 260
....*....|....*....|
gi 489910388 227 DGFVLGEGAGVLVLEEYEHA 246
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
75-406 |
7.05e-54 |
|
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: 182.07 E-value: 7.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 75 HYGLAAGMQAWRDCGLEVTETNAERIGVIVGSGIGGLPRIEETQTEMLAKGPRRISPFFVPASlinliSGQLSIAYGMKG 154
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLGIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 155 PSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALStrnddPTTASRPWDRDRDGFVLGEG 234
Cdd:cd00825 88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 235 AGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHH--ITAPDKDGPRRGILNALRNGGINADEVSYVNAHGTSTPLGDKNE 312
Cdd:cd00825 163 AGALVVEELEHALARGAHIYAEIVGTAATIDGAGmgAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 313 TDALKLAFGDHasKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQDPecDLDYCANEARPMKIEIGLS 392
Cdd:cd00825 243 LKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALL 318
|
330
....*....|....
gi 489910388 393 NSFGFGGTNGSMAV 406
Cdd:cd00825 319 NGFGLGGTNATLVL 332
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
18-401 |
3.77e-52 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 187.77 E-value: 3.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 18 NDIASAWDNIVNGRSGISRISR--------FDPTPLT-----THIAG---EVKDFDVTQY-MPAKEARQMD--------- 71
Cdd:COG3321 19 DDPEEFWRNLRAGRDAITEVPAdrwdadayYDPDPDApgktyVRWGGfldDVDEFDALFFgISPREAEAMDpqqrlllev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 72 ---TFIHYGLAAGMQAWRDCGLEVTETNAErigvivgsgigglprieetQTEMLAKGPRRISPFFVPASLINLISGQLSI 148
Cdd:COG3321 99 aweALEDAGYDPESLAGSRTGVFVGASSND-------------------YALLLLADPEAIDAYALTGNAKSVLAGRISY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 149 AYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALStrnddPTTASRPWDRDRDG 228
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 229 FVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAHH--ITAPDKDGPRRGILNALRNGGINADEVSYVNAHGTSTP 306
Cdd:COG3321 235 YVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 307 LGDKNETDALKLAFGDHASK---LVVNSTKSMTGHLLGAAG--G-IEAVfttLAVHNQISPPTINiFNQ-DPECDLD--- 376
Cdd:COG3321 315 LGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGvaGlIKAV---LALRHGVLPPTLH-FETpNPHIDFEnsp 390
|
410 420 430
....*....|....*....|....*....|.
gi 489910388 377 -YCANEARPMKIE-----IGLSnSFGFGGTN 401
Cdd:COG3321 391 fYVNTELRPWPAGggprrAGVS-SFGFGGTN 420
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
254-366 |
4.33e-40 |
|
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: 138.86 E-value: 4.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 254 YGELAGYGMSSDAHHITAPDKDGP--RRGILNALRNGGINADEVSYVNAHGTSTPLGDKNETDALKLAFGDHASK--LVV 329
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEgqARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 489910388 330 NSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINI 366
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
135-401 |
9.77e-37 |
|
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: 142.84 E-value: 9.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 135 PASLINLISGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDd 214
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 215 pttaSRPWDRDRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSDAH--HITAPDKDGPRRGILNALRNGGINA 292
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAKALKRAYDDAGFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 293 DEVSYVNAHGTSTPLGDKNETDALKLAFG---DHASKLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTINIFNQ 369
Cdd:TIGR02813 333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489910388 370 DPECDLD----YCANEARP-MKIEIGLS-----NSFGFGGTN 401
Cdd:TIGR02813 413 NPKLDIEnspfYLNTETRPwMQREDGTPrragiSSFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
143-406 |
1.76e-32 |
|
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: 122.94 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 143 SGQLSIAYGMK-GPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAEStvsplgiggfaamralstrnddpttasrp 221
Cdd:cd00327 47 AGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE----------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 222 wdrdrdgFVLGEGAGVLVLEEYEHAKKRGARIYGELAGYGMSSD-AHHITAPDKDGPRRGILNALRNGGINADEVSYVNA 300
Cdd:cd00327 98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 301 HGTSTPLGDKNETDALKLAFGDHAskLVVNSTKSMTGHLLGAAGGIEAVFTTLAVHNQISPPTinifNQDPECdldycan 380
Cdd:cd00327 171 HGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----PREPRT------- 237
|
250 260
....*....|....*....|....*.
gi 489910388 381 earpmkieiGLSNSFGFGGTNGSMAV 406
Cdd:cd00327 238 ---------VLLLGFGLGGTNAAVVL 254
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
156-401 |
4.25e-22 |
|
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: 95.47 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 156 SYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALStrnddPTTASRPWDRDRDGFVLGEGA 235
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 236 GVLVLEEYEHAKKRGARIYGELAGYGMSSDAHH--ITAPdkdgprrgilnalrNGginadevsyvnahgtstplgdknet 313
Cdd:smart00825 165 GVVVLKRLSDALRDGDPILAVIRGSAVNQDGRSngITAP--------------SG------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 314 dalklafgdhASKLVVNSTKSMTGHLLGAAgGIEAVF-TTLAVHNQISPPTINIFNQDPECDLD----YCANEARPMKIE 388
Cdd:smart00825 206 ----------PAQLLIGSVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPP 274
|
250
....*....|....*...
gi 489910388 389 -----IGLsNSFGFGGTN 401
Cdd:smart00825 275 grprrAGV-SSFGFGGTN 291
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
3-343 |
1.51e-13 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 71.52 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 3 RRVVITGLGIVSPVGNDIASAWdNIVNGRSGISRI--SRFDPTPLttHIAGEVkDFDvtQYMPAK-EARQMDTFIHYGL- 78
Cdd:PRK06519 6 NDVVITGIGLVSSLGEGLDAHW-NALSAGRPQPNVdtETFAPYPV--HPLPEI-DWS--QQIPKRgDQRQMETWQRLGTy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 79 AAGMqAWRDCGLE------------VTETNAERIGV------IVGSGIGGLPRI--EETQTEMlakgprRISPFFvpASL 138
Cdd:PRK06519 80 AAGL-ALDDAGIKgneellstmdmiVAAGGGERDIAvdtailNEARKRNDRGVLlnERLMTEL------RPTLFL--AQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 139 INLISGQLSIAYGMKGPSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALSTRNDDPTta 218
Cdd:PRK06519 151 SNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 219 srpWDR---DRDGFVLGEGAGVLVLEEYEHAKKRGARIYGELAgyGMSSDahhiTAPDKDGPRRGILNAL--RNGGINAD 293
Cdd:PRK06519 229 ---WSRggeDGGGFILGSGGAFLVLESREHAEARGARPYARIS--GVESD----RARRAPGDLEASLERLlkPAGGLAAP 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489910388 294 EVSYVNAHGTStplgdknETDALKLAFGDHASKLVVNSTKSMTGHLLGAA 343
Cdd:PRK06519 300 TAVISGATGAH-------PATAEEKAALEAALAGPVRGIGTLFGHTMEAQ 342
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
155-235 |
5.28e-07 |
|
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: 51.22 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 155 PSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAES-TVSPLGIGGFAAMRALSTRNDDPTTASRPWDRdRDGFVLGE 233
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESmSRAPMLLPKARWGYRMNAKLVDPMINPGLTDP-YTGLSMGE 158
|
..
gi 489910388 234 GA 235
Cdd:COG0183 159 TA 160
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
1-298 |
8.12e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 50.40 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 1 MKRRVVITGLGIVSPVGND-------IASAWDNIVNGR---SGISRISRFDPTPLTTHIAGEVKDF--------DVTQYM 62
Cdd:PRK06147 1 MMRALAIVGSGMVTAVGLDapsscaaIRARLDNFQETRfidPPGGEWLIGAPVPLPPPWRGPERLAemaapaiaEALEGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 63 PAKEARQMDTFIhyGLAAGMQAWRDCGLEVTetnaerigvivgsgigGLPRIEEtqtemlakgprRISPFFVPASLInli 142
Cdd:PRK06147 81 PALDASEAPLLL--CVAEEERPGRPPDLEER----------------LLRELEA-----------RLGLRLEPGSAV--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 143 sgqlsIAYGMKGpsyavvsacttGLHCIGDAARLIEYGDADVMLAGGAESTVSPLGIGGFAAMRALstrnddpTTASRPw 222
Cdd:PRK06147 129 -----IARGRVS-----------GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRL-------LTSQNS- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 223 drdrDGFVLGEGAGVLVLEEYEHAKKRGARIYgelaGYGMSSDAHHITAPdKDGPRRG------ILNALRNGGINADEVS 296
Cdd:PRK06147 185 ----NGFIPGEAAAAVLLGRPAGGEAPGLPLL----GLGLGREPAPVGES-EDLPLRGdgltqaIRAALAEAGCGLEDMD 255
|
..
gi 489910388 297 YV 298
Cdd:PRK06147 256 YR 257
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
155-235 |
1.39e-05 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 46.70 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489910388 155 PSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAESTvSPLGIGGFAAMRAlsTRNDDPTTASRPWDRDRDGFVL--- 231
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESM-SRAPYLLPKARRG--GRLGLNTLDGMLDDGLTDPFTGlsm 152
|
....
gi 489910388 232 GEGA 235
Cdd:cd00751 153 GITA 156
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
155-192 |
3.09e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 42.45 E-value: 3.09e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489910388 155 PSYAVVSACTTGLHCIGDAARLIEYGDADVMLAGGAES 192
Cdd:PRK05790 80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQES 117
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
163-192 |
2.09e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 39.94 E-value: 2.09e-03
10 20 30
....*....|....*....|....*....|
gi 489910388 163 CTTGLHCIGDAARLIEYGDADVMLAGGAES 192
Cdd:PRK09050 90 CGSGMDAVGTAARAIKAGEAELMIAGGVES 119
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
145-192 |
3.10e-03 |
|
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: 39.21 E-value: 3.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489910388 145 QLSIAYGMKGPSYAVV--SACTTGLHCIGDAARLIEYGDADVMLAGGAES 192
Cdd:pfam00108 65 QAALKAGIPDSAPAVTinKVCGSGLKAVYLAAQSIASGDADVVLAGGVES 114
|
|
| |
