|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
4-409 |
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: 793.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTA 163
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 164 CATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVLEE 242
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 243 LEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVF 322
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 323 GDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGGH 402
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 56379182 403 NATLIFK 409
Cdd:TIGR03150 401 NASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3-411 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 785.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 3 KRRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAA 82
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 83 LMAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVT 162
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 163 ACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVLE 241
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 242 ELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEV 321
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 322 FGDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGG 401
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 56379182 402 HNATLIFKKY 411
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-411 |
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: 748.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTA 163
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 164 CATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVLEE 242
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 243 LEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVF 322
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 323 GDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGGH 402
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 56379182 403 NATLIFKKY 411
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4-408 |
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: 690.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTA 163
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 164 CATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVLEE 242
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 243 LEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVF 322
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 323 GDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGGH 402
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 56379182 403 NATLIF 408
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-412 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 588.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 1 MEKRRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKD--------FDPSLFIDRREARKMD 72
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 73 RFTQFAVAAALMAVKDANLDI-NESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIIL 151
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 152 GAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST--NPDPKTASRPFDKKRDGF 229
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 230 VMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEY 309
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 310 NDKYETAAIKEVFGdHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECD-LDYVPNEARKQD 388
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....
gi 56379182 389 VRAVLSNSFGFGGHNATLIFKKYV 412
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWE 423
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4-411 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 533.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTA 163
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 164 CATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVLEE 242
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 243 LEHALRRGAKIYAEIVGYGATADAYHITAPAPggEGGVRAMRQALHDAGLKpeEIDYINAHGTSTEYNDKYETAAIKEVF 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKELF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 323 GDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGGH 402
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397
|
....*....
gi 56379182 403 NATLIFKKY 411
Cdd:PRK08439 398 NGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-411 |
0e+00 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 531.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 13 AVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDD----------------FPAKVAAEVK--DFDPSLFidrREARKMDRF 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLpdcipeqkalenlvaaMPCQIAAEVDqsEFDPSDF---APTKRESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 75 TQFAVAAALMAVKDANLDI-NESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGA 153
Cdd:PTZ00050 78 THFAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 154 KGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST--NPDPKTASRPFDKKRDGFVM 231
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 232 GEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKP-EEIDYINAHGTSTEYN 310
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 311 DKYETAAIKEVFGDH-AYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEAR--KQ 387
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQ 397
|
410 420
....*....|....*....|....
gi 56379182 388 DVRAVLSNSFGFGGHNATLIFKKY 411
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4-408 |
5.17e-169 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 480.44 E-value: 5.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTrvnPDDF-----------------PAKVAAEV------KDFDPS 60
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALT---QDDLkmksedeetqlytldqlPSRVAALVprgtgpGDFDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 61 LFIdrrEARKMDRFTQFAVAAALMAVKDAN-LDINESNAERVGVWIGSGIGGM-ETFEQQFEIFQQRGyRRVSPFFVPMM 138
Cdd:PLN02836 83 LWL---NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSItDILEAAQLICEKRL-RRLSPFFVPRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 139 IPDMAAGQVSIILGAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST--NPDPK 216
Cdd:PLN02836 159 LINMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 217 TASRPFDKKRDGFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEE 296
Cdd:PLN02836 239 EASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 297 IDYINAHGTSTEYNDKYETAAIKEVFGDHAY--KLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPE 374
Cdd:PLN02836 319 VDYVNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398
|
410 420 430
....*....|....*....|....*....|....*
gi 56379182 375 CDLDYVPNEARKQD-VRAVLSNSFGFGGHNATLIF 408
Cdd:PLN02836 399 FDDGFVPLTASKAMlIRAALSNSFGFGGTNASLLF 433
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-410 |
2.79e-157 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 449.84 E-value: 2.79e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 1 MEKRRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVA 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 81 AALMAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCT 160
Cdd:PRK08722 81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 161 VTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVV 239
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 240 LEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIK 319
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 320 EVFGDH-AYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARK-QDVRAVLSNSF 397
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKvESMEYAICNSF 400
|
410
....*....|...
gi 56379182 398 GFGGHNATLIFKK 410
Cdd:PRK08722 401 GFGGTNGSLIFKK 413
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-412 |
1.16e-130 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 386.64 E-value: 1.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 1 MEKRRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVA 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 81 AALMAVKDANLD---INESNAERVGVWIGSGIGGMETFEQQFEIFQQrGYRRVSPFFVPMMIPDMAAGQVSIILGAKGIN 157
Cdd:PLN02787 206 AGKKALADGGITedvMKELDKTKCGVLIGSAMGGMKVFNDAIEALRI-SYRKMNPFCVPFATTNMGSAMLAMDLGWMGPN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 158 SCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGEGAG 236
Cdd:PLN02787 285 YSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGEGAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 237 IVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETA 316
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 317 AIKEVFGDHAyKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLD-YVPNEARKQDVRAVLSN 395
Cdd:PLN02787 445 ALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSN 523
|
410
....*....|....*..
gi 56379182 396 SFGFGGHNATLIFKKYV 412
Cdd:PLN02787 524 SFGFGGHNSSILFAPYK 540
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-411 |
1.51e-121 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 359.04 E-value: 1.51e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 6 VVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTR--VNPDDFPAKVAAEVK-DFDPSLfiDRREARKMDRFTQFAVAAA 82
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDpfVEEFDLPVRIGGHLLeEFDHQL--TRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 83 LMAVKDANLDinESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVT 162
Cdd:PRK07910 92 RRVWENAGSP--EVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 163 ACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCA-NTALST-NPDPKTASRPFDKKRDGFVMGEGAGIVVL 240
Cdd:PRK07910 170 ACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQmRIVMSTnNDDPAGACRPFDKDRDGFVFGEGGALMVI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 241 EELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKE 320
Cdd:PRK07910 250 ETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 321 VFGDHayKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFG 400
Cdd:PRK07910 330 ALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFG 407
|
410
....*....|.
gi 56379182 401 GHNATLIFKKY 411
Cdd:PRK07910 408 GHNVALAFGRY 418
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-411 |
4.66e-121 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 357.44 E-value: 4.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKdFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQ-RGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVT 162
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 163 ACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAgFCANTALST--NPDPKTASRPFDKKRDGFVMGEGAGIVVL 240
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 241 EELEHALRRGAKIYAEIVGYGATADAYHITAPApgGEGGVRAMRQALHDAGLKpeeIDYINAHGTSTEYNDKYETAAIKE 320
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMALATVDTP---IDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 321 VFGDHAykLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPE-CDLDYVPNEARKQDVRAVLSNSFGF 399
Cdd:PRK07967 315 VFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFGF 392
|
410
....*....|..
gi 56379182 400 GGHNATLIFKKY 411
Cdd:PRK07967 393 GGTNATLVFRRY 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
6-411 |
6.44e-115 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 342.38 E-value: 6.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 6 VVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVkDFdpsLFIDRREArkMDRFTQFAVAAALMA 85
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DF---LPESPFGA--SALSEALARLAAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 86 VKDANLDINESNA--------------ERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQvsiiL 151
Cdd:PRK06501 87 LAQAGIGKGDFPGplflaappvelewpARFALAAAVGDNDAPSYDRLLRAARGGRFDALHERFQFGSIADRLADR----F 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 152 GAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALSTNPD-PKTASRPFDKKRDGFV 230
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDpPEKASKPFSKDRDGFV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 231 MGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYN 310
Cdd:PRK06501 243 MAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPEN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 311 DKYETAAIKEVFGDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVR 390
Cdd:PRK06501 323 DKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVT 402
|
410 420
....*....|....*....|.
gi 56379182 391 AVLSNSFGFGGHNATLIFKKY 411
Cdd:PRK06501 403 AVLSNSFGFGGQNASLVLTAE 423
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4-409 |
6.85e-114 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 338.89 E-value: 6.85e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIdivtRVNP-----DDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFA 78
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAV----RRMPewdryDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 79 VAAALMAVKDANLDINESNAE-RVGVWIGSGIGGME---TFEQQFEIFQQRGYRRVSpfFVPMMiPDMAAGQVSIILGAK 154
Cdd:PRK09116 78 TRASELALEDAGLLGDPILTDgRMGIAYGSSTGSTDpigAFGTMLLEGSMSGITATT--YVRMM-PHTTAVNVGLFFGLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 155 GINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEApITKMSFAGFCANTALST-NPDPKTASRPFDKKRDGFVMGE 233
Cdd:PRK09116 155 GRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTrNDAPELTPRPFDANRDGLVIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 234 GAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPggEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKY 313
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQA--ETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 314 ETAAIKEVFGDhayKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPEC-DLDYVPNEARKQDVRAV 392
Cdd:PRK09116 312 ESQATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388
|
410
....*....|....*..
gi 56379182 393 LSNSFGFGGHNATLIFK 409
Cdd:PRK09116 389 MSNNFAFGGINTSLIFK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
94-412 |
5.31e-109 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 324.37 E-value: 5.31e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 94 NESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTACATGANSIGD 173
Cdd:PRK14691 21 NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 174 AFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALST--NPDPKTASRPFDKKRDGFVMGEGAGIVVLEELEHALRRGA 251
Cdd:PRK14691 101 AVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 252 KIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVFGDhAYKLAV 331
Cdd:PRK14691 181 KPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 332 SSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECD-LDYVPNEARKQDVRAVLSNSFGFGGHNATLIFKK 410
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
..
gi 56379182 411 YV 412
Cdd:PRK14691 340 WV 341
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
5-406 |
2.46e-106 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 318.92 E-value: 2.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 5 RVVVTGIGAVTPLGnDAETTWKNIIAGQSGIdivTRVNP-DDFPAKVAAEVKDFDPSLfidrrearkmDRFTQFAVAAAL 83
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI---KLHQPfPELPPLPLGLIGNQPSSL----------EDLTKTVVTAAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 mavKDANLDINESNAervGVWIGSGIGgmetFEQQFEIFQQRGYR-RVSPFFVPMM------IPDMAAGQVSIILGAKGI 156
Cdd:PRK05952 69 ---KDAGLTPPLTDC---GVVIGSSRG----CQGQWEKLARQMYQgDDSPDEELDLenwldtLPHQAAIAAARQIGTQGP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 157 NSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALStnpdpKTASRPFDKKRDGFVMGEGAG 236
Cdd:PRK05952 139 VLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQREGLVLGEGGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 237 IVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETA 316
Cdd:PRK05952 214 ILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREAN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 317 AIKEVFGdhaYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETpdPECDLDYVpNEARKQDVRAVLSNS 396
Cdd:PRK05952 294 LIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFV-RQAQQSPLQNVLCLS 367
|
410
....*....|
gi 56379182 397 FGFGGHNATL 406
Cdd:PRK05952 368 FGFGGQNAAI 377
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-406 |
1.99e-95 |
|
"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: 291.65 E-value: 1.99e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETT---WKNIIAGQSGIdIVTRVNPDDFPAKVAAEVKDFDpslfIDRREARK---MDRFTQF 77
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGI-APVARLKSRFDRGVAGQIPTGD----IPGWDAKRtgiVDRTTLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 78 AVAAALMAVKDANL-DINESNAERVGVWIGSGIGGMEtfEQQFEIFQQrgYRRVSPFFVPMMI--PDMAAGQVSIIL-GA 153
Cdd:cd00828 76 ALVATEEALADAGItDPYEVHPSEVGVVVGSGMGGLR--FLRRGGKLD--ARAVNPYVSPKWMlsPNTVAGWVNILLlSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 154 KGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFaGFCANTALSTNPD-PKTASRPFDKKRDGFVMG 232
Cdd:cd00828 152 HGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALSTAEEePEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 233 EGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGeGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDK 312
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVISAHGTSTPANDV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 313 YETAAIKEVFGDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARK--QDVR 390
Cdd:cd00828 310 AESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlnLKVR 389
|
410
....*....|....*.
gi 56379182 391 AVLSNSFGFGGHNATL 406
Cdd:cd00828 390 AALVNAFGFGGSNAAL 405
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4-407 |
3.36e-93 |
|
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: 285.79 E-value: 3.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSLFIDRREARKMDRFTQFAVAAAL 83
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGINSCTVTA 163
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 164 CATGANSIGDAFKVIQRGdADVMITGGTEAPITKMSFAGFCANTALSTNPDPKTASRPFDKKRDGFVMGEGAGIVVLEEL 243
Cdd:cd00832 161 QAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 244 EHALRRGAKIYAEIVGYGATADAyhitAPAPGGEGG-VRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVF 322
Cdd:cd00832 240 AAARERGARVYGEIAGYAATFDP----PPGSGRPPGlARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 323 GDHAykLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLSNSFGFGGH 402
Cdd:cd00832 316 GPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGF 393
|
....*
gi 56379182 403 NATLI 407
Cdd:cd00832 394 NSALV 398
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
6-408 |
1.57e-85 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 265.94 E-value: 1.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 6 VVVTGIGAVTPLGNDAETTWKNIIAGQSGidivtRVNPDDF-----PAKVAAEVKDFDPSLfidRREARKMD-RFTQFAV 79
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRAS-----GMRPCDFwlvdlPTWVGEVVGVELPAL---PAALAAFDcRNNRLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 80 AAALM---AVKDAnldINESNAERVGVWIGSGIGGMETFEQQFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILGAKGi 156
Cdd:PRK09185 76 LALQQiepAVEAA---IARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQQELGSLADFLRAYLGLSG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 157 NSCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEApITKMSFAGFCANTALStnpdpKTASRPFDKKRDGFVMGEGA 235
Cdd:PRK09185 152 PAYTIsTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS-----PQPCRPFSANRDGINIGEAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 236 GIVVLE-ELEHALRrgakiyaeIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYE 314
Cdd:PRK09185 226 AFFLLErEDDAAVA--------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAME 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 315 TAAIKEVFGDHaykLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLDYVPNEARKQDVRAVLS 394
Cdd:PRK09185 298 SRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLS 374
|
410
....*....|....
gi 56379182 395 NSFGFGGHNATLIF 408
Cdd:PRK09185 375 NSFAFGGNNCSLIF 388
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-410 |
5.71e-81 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 254.57 E-value: 5.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 5 RVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDF--------PAKVAAEVKDFDPSLFIDRREARKMDRFTQ 76
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPddagaglaSAFIGAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 77 FAVAAALMAVKDANLDinESNAERVGVWI-GSGIGGMETFeQQFEIFQQRgYRRVSP-FFVPMMIPDmAAGQVSIILGAK 154
Cdd:PRK07103 83 AALAAAREAWRDAALG--PVDPDRIGLVVgGSNLQQREQA-LVHETYRDR-PAFLRPsYGLSFMDTD-LVGLCSEQFGIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 155 GInSCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALSTNP---DPKTASRPFDKKRDGFV 230
Cdd:PRK07103 158 GE-GFTVgGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfadEPEAACRPFDQDRDGFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 231 MGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEggVRAMRQALHDAGLKPEEIDYINAHGTSTEYN 310
Cdd:PRK07103 237 YGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 311 DKYETAAIKEVFGDHAYklaVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETP-DPECdlDYVPNEARKQDV 389
Cdd:PRK07103 315 DETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESARI 389
|
410 420
....*....|....*....|.
gi 56379182 390 RAVLSNSFGFGGHNATLIFKK 410
Cdd:PRK07103 390 RYALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
5-407 |
3.04e-78 |
|
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: 247.86 E-value: 3.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 5 RVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVT--RVNPDDFPAKVAA-------------EVKDFDPSLF-IDRREA 68
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYPDPGKpgktytrrggfldDVDAFDAAFFgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 69 RKMDRftQFAVAaaLM----AVKDANLDINESNAERVGVWIGSgiggmetFEQQFEIFQQRGYRRVSPFFVPMMIPDMAA 144
Cdd:cd00833 82 EAMDP--QQRLL--LEvaweALEDAGYSPESLAGSRTGVFVGA-------SSSDYLELLARDPDEIDAYAATGTSRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 145 GQVSIILGAKGiNSCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALStnPDPKtaSRPFD 223
Cdd:cd00833 151 NRISYFFDLRG-PSLTVdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS--PDGR--CRPFD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 224 KKRDGFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAY--HITAPapGGEGGVRAMRQALHDAGLKPEEIDYIN 301
Cdd:cd00833 226 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 302 AHGTSTEYNDKYETAAIKEVFG---DHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLD 378
Cdd:cd00833 304 AHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFE 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 56379182 379 ----YVPNEAR----KQDVRAVLSNSFGFGGHNATLI 407
Cdd:cd00833 384 esplRVPTEARpwpaPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
73-407 |
1.71e-71 |
|
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: 227.90 E-value: 1.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 73 RFTQFAVAAALMAVKDANLDINESNAERVGVWIGSGIGGMEtfeqqFEIFQQRGYRRVSPFFVPMMIPDMAAGQVSIILG 152
Cdd:cd00825 10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPR-----FQVFGADAMRAVGPYVVTKAMFPGASGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 153 AKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSfagfCANTALSTNPDPKTASRPFDKKRDGFVMG 232
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMD----CEFDAMGALSTPEKASRTFDAAADGFVFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 233 EGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDK 312
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 313 YETAAIKEVFGDHayKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPecDLDYVPNEARKQDVRAV 392
Cdd:cd00825 241 KELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*
gi 56379182 393 LSNSFGFGGHNATLI 407
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-246 |
2.87e-65 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 209.03 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIV--TRVNPDDF---PAKVAAEVK----------DFDPSLF-IDRRE 67
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 68 ARKMDRFTQFAVAAALMAVKDANLDINESNAERVGVWIGSGIGGMETFEQQFEifqQRGYRRVSPFFVPMMiPDMAAGQV 147
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDE---DGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 148 SIILGAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALSTNpDPKTASRPFDkkrD 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GPCKAFDPFA---D 232
|
250
....*....|....*....
gi 56379182 228 GFVMGEGAGIVVLEELEHA 246
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
6-404 |
6.76e-62 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 216.28 E-value: 6.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 6 VVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVT--RVNPDDF--PAKVAA------------EVKDFDPSLF-IDRREA 68
Cdd:COG3321 6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPadRWDADAYydPDPDAPgktyvrwggfldDVDEFDALFFgISPREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 69 RKMD---RftqfavaaaLM------AVKDANLDINESNAERVGVWIGSGIggmetfeQQFEIFQQRGYRRVSPFFVPMMI 139
Cdd:COG3321 86 EAMDpqqR---------LLlevaweALEDAGYDPESLAGSRTGVFVGASS-------NDYALLLLADPEAIDAYALTGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 140 PDMAAGQVSIILGAKGInSCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALStnpdPKTA 218
Cdd:COG3321 150 KSVLAGRISYKLDLRGP-SVTVdTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS----PDGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 219 SRPFDKKRDGFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATAD-AYH-ITAPapGGEGGVRAMRQALHDAGLKPEE 296
Cdd:COG3321 225 CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP--NGPAQAAVIRRALADAGVDPAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 297 IDYINAHGTSTEYNDKYETAAIKEVFGDHAYK---LAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDP 373
Cdd:COG3321 303 VDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNP 382
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 56379182 374 ECDLD----YVPNEAR-----KQDVRAVLSnSFGFGGHNA 404
Cdd:COG3321 383 HIDFEnspfYVNTELRpwpagGGPRRAGVS-SFGFGGTNA 421
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
254-369 |
6.95e-53 |
|
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: 171.98 E-value: 6.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 254 YAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGLKPEEIDYINAHGTSTEYNDKYETAAIKEVFGDHAYK--LAV 331
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 56379182 332 SSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYE 369
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
143-407 |
4.72e-41 |
|
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: 146.05 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 143 AAGQVSIILGAKGINSCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEApitkmsfagfcantalstnpdpktasrp 221
Cdd:cd00327 46 AAGQLAYHLGISGGPAYSVnQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 222 fdkkrdgFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATAD-AYHItaPAPGGEGGVRAMRQALHDAGLKPEEIDYI 300
Cdd:cd00327 98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMV--PAVSGEGLARAARKALEGAGLTPSDIDYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 301 NAHGTSTEYNDKYETAAIKEVFGDHAykLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTinyetpdpecdldyv 380
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*..
gi 56379182 381 pnearKQDVRAVLSNSFGFGGHNATLI 407
Cdd:cd00327 232 -----PREPRTVLLLGFGLGGTNAAVV 253
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
136-411 |
7.45e-41 |
|
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: 155.16 E-value: 7.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 136 PMMIPDMAAGQVSIILGAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGGT---EAPITKMSFAgfcANTALSTN 212
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVctdNSPFMYMSFS---KTPAFTTN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 213 PDpktaSRPFDKKRDGFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGGEGGVRAMRQALHDAGL 292
Cdd:TIGR02813 255 ED----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 293 KPEEIDYINAHGTSTEYNDKYETAAIKEVFG---DHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYE 369
Cdd:TIGR02813 331 APHTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVD 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 56379182 370 TPDPECDLD----YVPNEAR----KQD---VRAVLSnSFGFGGHNATLIFKKY 411
Cdd:TIGR02813 411 QPNPKLDIEnspfYLNTETRpwmqREDgtpRRAGIS-SFGFGGTNFHMVLEEY 462
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
6-407 |
3.53e-34 |
|
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: 128.60 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 6 VVVTGIGAVTPLGNDAETTWKNIIAGQSGIDivtrvnpddfpakvaaevkDFDPSLF-IDRREARKMD---RFtqfavaa 81
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAAFFgISPREAEAMDpqqRL------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 82 ALM----AVKDANLDINESNAERVGVWIGSGIGGmetfeqqfeifqqrgYrrvspffvpmmipdmaagqvsiilgakgin 157
Cdd:smart00825 55 LLEvaweALEDAGIDPESLRGSRTGVFVGVSSSD---------------Y------------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 158 SCTV-TACATGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALStnPDPKtaSRPFDKKRDGFVMGEGAG 236
Cdd:smart00825 90 SVTVdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS--PDGR--CKTFDASADGYVRGEGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 237 IVVLEELEHALRRGAKIYAEIVGY-----GATADayhITAPAPGGeggvramrQalhdaglkpeeidyinahgtsteynd 311
Cdd:smart00825 166 VVVLKRLSDALRDGDPILAVIRGSavnqdGRSNG---ITAPSGPA--------Q-------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 312 kyetaaikevfgdhaykLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINYETPDPECDLD----YVPNEAR-- 385
Cdd:smart00825 209 -----------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTpw 271
|
410 420
....*....|....*....|....
gi 56379182 386 --KQDVRAVLSNSFGFGGHNATLI 407
Cdd:smart00825 272 ppPGRPRRAGVSSFGFGGTNAHVI 295
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
4-300 |
6.74e-09 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 56.95 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 4 RRVVVTGIGAVTPLGNDAETTWKNIIAGQSGIDIVTRVNPDDFPAKVAAEVKDFDPSlfidrREARKMDRFTQFAVAAAL 83
Cdd:PRK06147 3 RALAIVGSGMVTAVGLDAPSSCAAIRARLDNFQETRFIDPPGGEWLIGAPVPLPPPW-----RGPERLAEMAAPAIAEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 84 MAVKD-----ANLDINESNAERVGVWIGsgiggmETFEQQFEIFQQRGYRRVSPFFVpmmipdMAAGQVSiilgakgins 158
Cdd:PRK06147 78 EGLPAldaseAPLLLCVAEEERPGRPPD------LEERLLRELEARLGLRLEPGSAV------IARGRVS---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 159 ctvtacatGANSIGDAFKVIQRGDADVMITGGTEAPITKMSFAGFCANTALSTNPDPktasrpfdkkrDGFVMGEGAGIV 238
Cdd:PRK06147 136 --------GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQNS-----------NGFIPGEAAAAV 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56379182 239 VLEELEHALRRGAKIYAeiVGYGATADAYHITAPAPG-GEGGVRAMRQALHDAGLKPEEIDYI 300
Cdd:PRK06147 197 LLGRPAGGEAPGLPLLG--LGLGREPAPVGESEDLPLrGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-384 |
3.08e-07 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 52.26 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 1 MEKRRVVVTGIGAVTPLGNDAETTWkNIIAGQSGIDIV--TRVNPddFPAKVAAEVkDFDpsLFIDRR-EARKMDRFTQF 77
Cdd:PRK06519 3 MQPNDVVITGIGLVSSLGEGLDAHW-NALSAGRPQPNVdtETFAP--YPVHPLPEI-DWS--QQIPKRgDQRQMETWQRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 78 AVAAALMAVKDANLDINESNAERVGVWIGSGiGGMETFEQQFEIFQQRGYRRVSPFFV---------PMM----IPDMAA 144
Cdd:PRK06519 77 GTYAAGLALDDAGIKGNEELLSTMDMIVAAG-GGERDIAVDTAILNEARKRNDRGVLLnerlmtelrPTLflaqLSNLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 145 GQVSIILGAKGINSCTVTACATGANSIGDAFKVIQRGDADVMITGG---TEAPITKM--SFAGFCANTALStnpdPKTAS 219
Cdd:PRK06519 156 GNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGaynAERPDMLLlyELGGLLLKGGWA----PVWSR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 220 RPFDKkrDGFVMGEGAGIVVLEELEHALRRGAKIYAEIVGYgatadayhITAPAPGGEGGVRA-MRQALHDAGLKPEEID 298
Cdd:PRK06519 232 GGEDG--GGFILGSGGAFLVLESREHAEARGARPYARISGV--------ESDRARRAPGDLEAsLERLLKPAGGLAAPTA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 299 YIN----AHGTSTEyndkyETAAIkevfgDHAYKLAVSSTKSMTGHLLGATGAVEAIFSVLAIRDGIIPPTINyetPDPE 374
Cdd:PRK06519 302 VISgatgAHPATAE-----EKAAL-----EAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD---ASGE 368
|
410
....*....|
gi 56379182 375 CDLDYVPNEA 384
Cdd:PRK06519 369 KPMSGAAREA 378
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
212-360 |
1.30e-06 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 50.09 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 212 NPDPKTASRPFDKKRDGFV-------MGEGAGIVVLEELEHALRRGAKIYAEIVGYGATADA--YHITAPApggeggvRA 282
Cdd:PLN02644 224 DPAKLRKLRPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQApeLFTTAPA-------LA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 283 MRQALHDAGLKPEEIDYInahgtstEYNDKYETAAI--KEVFGDHAYKLAVSSTKSMTGHLLGATGA--VEAIFSVLAIR 358
Cdd:PLN02644 297 IPKALKHAGLEASQVDYY-------EINEAFSVVALanQKLLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSK 369
|
..
gi 56379182 359 DG 360
Cdd:PLN02644 370 NG 371
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
234-347 |
1.97e-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: 46.32 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 234 GAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHI--TAPAPggeggvrAMRQALHDAGLKPEEIDYInahgtstEYNd 311
Cdd:cd00751 247 GAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAImgIGPVP-------AIPKALKRAGLTLDDIDLI-------EIN- 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 56379182 312 kyE------TAAIKEVFGDHAyKL-----AVSstksmTGHLLGATGA 347
Cdd:cd00751 312 --EafaaqaLACLKELGLDPE-KVnvnggAIA-----LGHPLGASGA 350
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
234-300 |
2.36e-05 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 46.21 E-value: 2.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56379182 234 GAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHI--TAPAPggeggvrAMRQALHDAGLKPEEIDYI 300
Cdd:COG0183 251 GAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEImgIGPVP-------ATRKALARAGLTLDDIDLI 312
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
234-347 |
6.85e-05 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 44.71 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 234 GAGIVVLEELEHALRRGAKIYAEIVGYGATAdayhiTAPAPGGEGGVRAMRQALHDAGLKPEEIDY--IN-AHGTSTEYn 310
Cdd:PRK06445 254 GASYVLLMSKKAVKKYGLKPMAKIRSFGFAG-----VPPAIMGKGPVPASKKALEKAGLSVKDIDLweINeAFAVVVLY- 327
|
90 100 110
....*....|....*....|....*....|....*..
gi 56379182 311 dkyetaAIKEvFGDHAYKLAVSSTKSMTGHLLGATGA 347
Cdd:PRK06445 328 ------AIKE-LGLDPETVNIKGGAIAIGHPLGATGA 357
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
233-347 |
2.40e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 43.16 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 233 EGAGIVVLEELEHALRRGAKIYAEIVGYGATADAYHITAPAPGgeggvRAMRQALHDAGLKPEEIDYInahgtstEYNDK 312
Cdd:PRK08235 252 DGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPG-----YAINALLEKTGKTVEDIDLF-------EINEA 319
|
90 100 110
....*....|....*....|....*....|....*..
gi 56379182 313 YETAAI--KEVFGDHAYKLAVSSTKSMTGHLLGATGA 347
Cdd:PRK08235 320 FAAVALasTEIAGIDPEKVNVNGGAVALGHPIGASGA 356
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
220-300 |
3.54e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 42.45 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 220 RP-FDKkrDGFV-------MGEGAGIVVLEELEHALRRGAKIYAEIVGYGATAdayhiTAPAPGGEGGVRAMRQALHDAG 291
Cdd:PRK05790 233 RPaFDK--DGTVtagnasgINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAG-----VDPAIMGIGPVPAIRKALEKAG 305
|
....*....
gi 56379182 292 LKPEEIDYI 300
Cdd:PRK05790 306 WSLADLDLI 314
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
233-348 |
1.21e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 40.85 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 233 EGAGIVVLEElEHALRR-GAKIYAEIVGYGATAD--AYHITAPAPggeggvrAMRQALHDAGLKPEEIDyinahgtSTEY 309
Cdd:PRK07801 241 DGASAVLLAS-ERAVKRhGLTPRARIHHLSVRGDdpVFMLTAPIP-------ATRYALEKTGLSIDDID-------VVEI 305
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 56379182 310 NDKYET---AAIKEVFGDHAyKLAVSSTKSMTGHLLGATGAV 348
Cdd:PRK07801 306 NEAFAPvvlAWLKETGADPA-KVNPNGGAIALGHPLGATGAK 346
|
|
| PRK06840 |
PRK06840 |
3-oxoacyl-ACP synthase; |
279-372 |
5.40e-03 |
|
3-oxoacyl-ACP synthase;
Pssm-ID: 235872 Cd Length: 339 Bit Score: 38.45 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56379182 279 GVRAMRQALHDAGLKPEEIDYINAHGtsTEYNDKY-ETAAIK---EVFGDHAYKL---AVSSTkSMTG-----HLLGATG 346
Cdd:PRK06840 57 AIAAAKPALKQAGVDPAAIDVVIYIG--SEHKDYPvWSSAPKiqhEIGAKNAWAFdimAVCAS-FPIAlkvakDLLYSDP 133
|
90 100
....*....|....*....|....*.
gi 56379182 347 AVEAIFSVLAIRDGIIpptINYETPD 372
Cdd:PRK06840 134 SIENVLLVGGYRNSDL---VDYDNPR 156
|
|
| |
