|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
5-410 |
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: 644.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALsTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 1308460336 404 NATVVIK 410
Cdd:TIGR03150 401 NASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
5-412 |
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: 630.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 1308460336 404 NATVVIKKY 412
Cdd:COG0304 401 NASLVFKRY 409
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
4-413 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 616.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 4 RRRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYAT 83
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 84 DEAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVT 163
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 164 ACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALsTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 243 ELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNA 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 323 FGPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|.
gi 1308460336 403 HNATVVIKKYQ 413
Cdd:PRK07314 401 TNASLVFKRYE 411
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
5-409 |
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: 587.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 1308460336 404 NATVVI 409
Cdd:cd00834 401 NASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-247 |
2.23e-52 |
|
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: 175.52 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPI--THYDASN---DEVKLAAELKNIR-----------LEDKLEGKE 68
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKlydPPSRIAGKIYTKWgglddifdfdpLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 69 IRRTDRFTQLALYATDEAVKDASLNFEDIDIKRTGVYYTSGIGGLEtinDQKQRAMEKGYHRMSPFFIPSsIINLAAGNI 148
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYA---ALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 149 AIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRgDDVSKAsipFDVNRG 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP-DGPCKA---FDPFAD 232
|
250
....*....|....*....
gi 1308460336 229 GFVMGEGAGTLIIEELEHA 247
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
163-409 |
4.91e-16 |
|
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: 78.14 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 163 TACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRgDDVSKAsipFDVNRGGFVMGEGAGTLIIE 242
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSP-DGRCKT---FDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 243 ELEHAKKRNAKIYAEVIGYAATCDathitgpdpeGNGAkdsmlfaledGLVNPNevdyinahgtstplndkvetlairna 322
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQD----------GRSN----------GITAPS-------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 323 fgPHAyELNVSSTKSMTGHLLGASGaVEAII-TTLAVKDDFVPPTINTTDLDPECDLNYTlgkgvAKKVN---------- 391
Cdd:smart00825 205 --GPA-QLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEES-----PLRVPteltpwpppg 275
|
250 260
....*....|....*....|.
gi 1308460336 392 ---YALSNSLGFGGHNATVVI 409
Cdd:smart00825 276 rprRAGVSSFGFGGTNAHVIL 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
5-410 |
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: 644.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALsTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 1308460336 404 NATVVIK 410
Cdd:TIGR03150 401 NASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
5-412 |
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: 630.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 1308460336 404 NATVVIKKY 412
Cdd:COG0304 401 NASLVFKRY 409
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
4-413 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 616.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 4 RRRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYAT 83
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 84 DEAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVT 163
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 164 ACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALsTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 243 ELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNA 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 323 FGPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|.
gi 1308460336 403 HNATVVIKKYQ 413
Cdd:PRK07314 401 TNASLVFKRYE 411
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
5-409 |
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: 587.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALsTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 1308460336 404 NATVVI 409
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
3-414 |
6.53e-162 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 462.16 E-value: 6.53e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 3 NRRRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIrLEDKLEG---------KEIRRTD 73
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDL-AEDAEAGfdpdryldpKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 74 RFTQLALYATDEAVKDASLNFEDI-DIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKY 152
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPDTLeDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 153 GIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRG--DDVSKASIPFDVNRGGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfnDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 231 VMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPL 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 311 NDKVETLAIRNAFGpHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECD-LNYTLGKGVAKK 389
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....*
gi 1308460336 390 VNYALSNSLGFGGHNATVVIKKYQE 414
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
5-412 |
1.66e-155 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 444.95 E-value: 1.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALY-RGDDVSKASIPFDVNRGGFVMGEGAGTLIIEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 244 LEHAKKRNAKIYAEVIGYAATCDATHITGPDPEgnGAKDSMLFALEdgLVNPNEVDYINAHGTSTPLNDKVETLAIRNAF 323
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALE--MAGNPKIDYINAHGTSTPYNDKNETAALKELF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 324 GPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFGGH 403
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397
|
....*....
gi 1308460336 404 NATVVIKKY 412
Cdd:PRK08439 398 NGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
14-412 |
4.03e-150 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 431.81 E-value: 4.03e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 14 ALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDE----------------VKLAAELKNiRLEDKLEGKEIRRTDRFTQ 77
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDcipeqkalenlvaampCQIAAEVDQ-SEFDPSDFAPTKRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 78 LALYATDEAVKDASLNF-EDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKG 156
Cdd:PTZ00050 80 FAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 157 PAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRG--DDVSKASIPFDVNRGGFVMGE 234
Cdd:PTZ00050 160 PSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKynDDPQRASRPFDKDRAGFVMGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 235 GAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALED-GLVNPNEVDYINAHGTSTPLNDK 313
Cdd:PTZ00050 240 GAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIGDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 314 VETLAIRNAFGPH-AYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVA--KKV 390
Cdd:PTZ00050 320 IELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHplQSI 399
|
410 420
....*....|....*....|..
gi 1308460336 391 NYALSNSLGFGGHNATVVIKKY 412
Cdd:PTZ00050 400 DAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
5-408 |
5.83e-129 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 378.75 E-value: 5.83e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHydasnDEVKLAAELKNIRL---------------EDKLEGK-- 67
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQ-----DDLKMKSEDEETQLytldqlpsrvaalvpRGTGPGDfd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 68 -----EIRRTDRFTQLALYATDEAVKDASLN-FEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSII 141
Cdd:PLN02836 81 eelwlNSRSSSRFIGYALCAADEALSDARWLpSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 142 NLAAGNIAIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRG--DDVSKA 219
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfnSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 220 SIPFDVNRGGFVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVD 299
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 300 YINAHGTSTPLNDKVETLAIRNAFGPHAYE--LNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECD 377
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400
|
410 420 430
....*....|....*....|....*....|..
gi 1308460336 378 LNYT-LGKGVAKKVNYALSNSLGFGGHNATVV 408
Cdd:PLN02836 401 DGFVpLTASKAMLIRAALSNSFGFGGTNASLL 432
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-411 |
5.09e-124 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 365.48 E-value: 5.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 3 NRRRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYA 82
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 83 TDEAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHV 162
Cdd:PRK08722 82 GIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 163 TACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTLII 241
Cdd:PRK08722 162 TACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALsTRNDEPQKASRPWDKDRDGFVLGDGAGMMVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 242 EELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRN 321
Cdd:PRK08722 242 EEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 322 AFGPH-AYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTlgKGVAKKVN---YALSNS 397
Cdd:PRK08722 322 ALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLV--PHTARKVEsmeYAICNS 399
|
410
....*....|....
gi 1308460336 398 LGFGGHNATVVIKK 411
Cdd:PRK08722 400 FGFGGTNGSLIFKK 413
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
4-413 |
2.32e-111 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 337.34 E-value: 2.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 4 RRRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYAT 83
Cdd:PLN02787 128 QRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 84 DEAVKDASLNFE---DIDIKRTGVYYTSGIGGLETINDQKQrAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAIS 160
Cdd:PLN02787 208 KKALADGGITEDvmkELDKTKCGVLIGSAMGGMKVFNDAIE-ALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 161 HVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNRGGFVMGEGAGTL 239
Cdd:PLN02787 287 ISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALsQRNDDPTKASRPWDMNRDGFVMGEGAGVL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 240 IIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAI 319
Cdd:PLN02787 367 LLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQAL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 320 RNAFGPHAyELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAK-KVNYALSNSL 398
Cdd:PLN02787 447 MRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALSNSF 525
|
410
....*....|....*
gi 1308460336 399 GFGGHNATVVIKKYQ 413
Cdd:PLN02787 526 GFGGHNSSILFAPYK 540
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
5-410 |
3.71e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 280.72 E-value: 3.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASND-EVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYAT 83
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRYDGlNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 84 DEAVKDASLnFEDIDIK--RTGVYYTSGIGGLETIND----QKQRAMEK----GYHRMSPffipssiiNLAAGNIAIKYG 153
Cdd:PRK09116 82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGAfgtmLLEGSMSGitatTYVRMMP--------HTTAVNVGLFFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 154 IKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPigifGFAVMQALY----RGDDVSKASIPFDVNRGG 229
Cdd:PRK09116 153 LKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPT----EAAVFDTLFatstRNDAPELTPRPFDANRDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 230 FVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAkdSMLFALEDGLVNPNEVDYINAHGTSTP 309
Cdd:PRK09116 229 LVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGTATD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 310 LNDKVETLAIRNAFGPHayeLNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPEC-DLNYTLGKGVAK 388
Cdd:PRK09116 307 RGDIAESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREI 383
|
410 420
....*....|....*....|..
gi 1308460336 389 KVNYALSNSLGFGGHNATVVIK 410
Cdd:PRK09116 384 DTEYVMSNNFAFGGINTSLIFK 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
100-412 |
2.86e-88 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 271.60 E-value: 2.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 100 KRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTACASSTNALGEAFRAI 179
Cdd:PRK14691 26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 180 RDGYLDLAITGGSEGCVIPIGIFGFAVMQAL--YRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEELEHAKKRNAKIYAE 257
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALstHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 258 VIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAFGpHAYELNVSSTKS 337
Cdd:PRK14691 186 IVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFG-ESNALAITSTKS 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1308460336 338 MTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECD-LNYTLGKGVAKKVNYALSNSLGFGGHNATVVIKKY 412
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
7-412 |
1.10e-87 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 272.37 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 7 VVITGLGALTPVGNTVAETWEGIKNGKNGIAPIThyDASNDEVKLAAELKNIRLED---KLEGKEIRRTDRFTQLALYAT 83
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLD--DPFVEEFDLPVRIGGHLLEEfdhQLTRVELRRMSYLQRMSTVLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 84 DEAVKDASLnfEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVT 163
Cdd:PRK07910 92 RRVWENAGS--PEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 164 ACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALY--RGDDVSKASIPFDVNRGGFVMGEGAGTLII 241
Cdd:PRK07910 170 ACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMstNNDDPAGACRPFDKDRDGFVFGEGGALMVI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 242 EELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRN 321
Cdd:PRK07910 250 ETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 322 AFGPHAYElnVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFG 401
Cdd:PRK07910 330 ALGGHRPA--VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFG 407
|
410
....*....|.
gi 1308460336 402 GHNATVVIKKY 412
Cdd:PRK07910 408 GHNVALAFGRY 418
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
5-413 |
2.09e-84 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 263.46 E-value: 2.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKnIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAME-KGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVT 163
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGpRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 164 ACASSTNALGEAFRAIRDGYLDLAITGGSE------GCVipigifgFAVMQALY--RGDDVSKASIPFDVNRGGFVMGEG 235
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldwemSCL-------FDAMGALStkYNDTPEKASRAYDANRDGFVIAGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 236 AGTLIIEELEHAKKRNAKIYAEVIGYAATCDathitGPD---PEGNGAKDSMLFALEDglVNpNEVDYINAHGTSTPLND 312
Cdd:PRK07967 234 GGVVVVEELEHALARGAKIYAEIVGYGATSD-----GYDmvaPSGEGAVRCMQMALAT--VD-TPIDYINTHGTSTPVGD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 313 KVETLAIRNAFG---PHayelnVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPE-CDLNYTLGKGVAK 388
Cdd:PRK07967 306 VKELGAIREVFGdksPA-----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNA 380
|
410 420
....*....|....*....|....*
gi 1308460336 389 KVNYALSNSLGFGGHNATVVIKKYQ 413
Cdd:PRK07967 381 ELTTVMSNSFGFGGTNATLVFRRYK 405
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
7-412 |
4.41e-83 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 260.72 E-value: 4.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 7 VVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELknirleDKLEGKEIRRTDRFTQLALYATDEA 86
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLPESPFGASALSEALARLAAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 87 VKDASLNFEDID--------------IKRTGVYYTSGIGGlETINDQKQRAMEKG----YHRMSPFfipSSIinlaAGNI 148
Cdd:PRK06501 87 LAQAGIGKGDFPgplflaappvelewPARFALAAAVGDND-APSYDRLLRAARGGrfdaLHERFQF---GSI----ADRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 149 AIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL-YRGDDVSKASIPFDVNR 227
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALsTQNDPPEKASKPFSKDR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 228 GGFVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTS 307
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 308 TPLNDKVETLAIRNAFGPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVA 387
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARD 398
|
410 420
....*....|....*....|....*
gi 1308460336 388 KKVNYALSNSLGFGGHNATVVIKKY 412
Cdd:PRK06501 399 ARVTAVLSNSFGFGGQNASLVLTAE 423
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
5-409 |
1.81e-81 |
|
"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: 256.21 E-value: 1.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAET---WEGIKNGKNGIAPITHYDASNDeVKLAAELKnirlEDKLEGKEIRRT---DRFTQL 78
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRFD-RGVAGQIP----TGDIPGWDAKRTgivDRTTLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 79 ALYATDEAVKDASLNFED-IDIKRTGVYYTSGIGGLetinDQKQRAMEKGYHRMSPFFIP--SSIINLAAGNIAIKYGIK 155
Cdd:cd00828 76 ALVATEEALADAGITDPYeVHPSEVGVVVGSGMGGL----RFLRRGGKLDARAVNPYVSPkwMLSPNTVAGWVNILLLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 156 -GPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGcVIPIGIFGFAVMQALYRGDDV-SKASIPFDVNRGGFVMG 233
Cdd:cd00828 152 hGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEpEEMSRPFDETRDGFVEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 234 EGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPeGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDK 313
Cdd:cd00828 231 EGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 314 VETLAIRNAFGPHAYELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKG--VAKKVN 391
Cdd:cd00828 310 AESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSrdLNLKVR 389
|
410
....*....|....*...
gi 1308460336 392 YALSNSLGFGGHNATVVI 409
Cdd:cd00828 390 AALVNAFGFGGSNAALVL 407
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
5-409 |
1.21e-76 |
|
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: 243.42 E-value: 1.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQLALYATD 84
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTA 164
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGyLDLAITGGSEGCVIPIGIFGFAVMQALYRGDDVSKASIPFDVNRGGFVMGEGAGTLIIEEL 244
Cdd:cd00832 161 QAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 245 EHAKKRNAKIYAEVIGYAATCDathitgPDP---EGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRN 321
Cdd:cd00832 240 AAARERGARVYGEIAGYAATFD------PPPgsgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 322 AFGPHAyeLNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALSNSLGFG 401
Cdd:cd00832 314 VFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRG 391
|
....*...
gi 1308460336 402 GHNATVVI 409
Cdd:cd00832 392 GFNSALVV 399
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
7-409 |
3.60e-72 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 231.65 E-value: 3.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 7 VVITGLGALTPVGNTVAETWEGIKNGKN-GIAPITHYDASNDEVKLA-AELKNIRLEDKLEGKEIRrTDRFTQLALYATD 84
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRAsGMRPCDFWLVDLPTWVGEvVGVELPALPAALAAFDCR-NNRLALLALQQIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 85 EAVKDASLNFEDidiKRTGVYY---TSGIGGLE---TINDQKQRAMEKGYHR--MSPFfipssiiNLAAGnIAIKYGIKG 156
Cdd:PRK09185 83 PAVEAAIARYGA---DRIGVVLgtsTSGILEGElayRRRDPAHGALPADYHYaqQELG-------SLADF-LRAYLGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 157 PAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEG-CVIPIgiFGFAVMQALYRGddvskASIPFDVNRGGFVMGEG 235
Cdd:PRK09185 152 PAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSlCRLTL--NGFNSLESLSPQ-----PCRPFSANRDGINIGEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 236 AGTLIIEelehakkRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVE 315
Cdd:PRK09185 225 AAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAME 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 316 TLAIRNAFGPHayeLNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGKGVAKKVNYALS 395
Cdd:PRK09185 298 SRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLS 374
|
410
....*....|....
gi 1308460336 396 NSLGFGGHNATVVI 409
Cdd:PRK09185 375 NSFAFGGNNCSLIF 388
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
6-411 |
3.08e-70 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 226.09 E-value: 3.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 6 RVVITGLGALTPVGNtVAETWEGIKNGKNGIAPithydasndeVKLAAELKNIRLedKLEGKEIRRTDRFTQLALyatDE 85
Cdd:PRK05952 3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKL----------HQPFPELPPLPL--GLIGNQPSSLEDLTKTVV---TA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 86 AVKDASLnfeDIDIKRTGVYytsgIG---GLETINDQKQRAMEKGYHRMSPFFIPSSIINL----AAGNIAIKYGIKGPA 158
Cdd:PRK05952 67 ALKDAGL---TPPLTDCGVV----IGssrGCQGQWEKLARQMYQGDDSPDEELDLENWLDTlphqAAIAAARQIGTQGPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 159 ISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRgddvsKASIPFDVNRGGFVMGEGAGT 238
Cdd:PRK05952 140 LAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK-----TGAYPFDRQREGLVLGEGGAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 239 LIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLA 318
Cdd:PRK05952 215 LVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 319 IRNAFGPhayELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTdlDPECDLNYtLGKGVAKKVNYALSNSL 398
Cdd:PRK05952 295 IQALFPH---RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQ--EPEFDLNF-VRQAQQSPLQNVLCLSF 368
|
410
....*....|...
gi 1308460336 399 GFGGHNATVVIKK 411
Cdd:PRK05952 369 GFGGQNAAIALGK 381
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
6-411 |
1.77e-69 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 225.30 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 6 RVVITGLGALTPVGNTVAETWEGIKNGKNGI--------APITHYDASNDEVKLAAELKNIRLEDKLEGKEIRRTDRFTQ 77
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 78 LALYATDEAVKDASLnfEDIDIKRTGVYytsgIGGlETINDQKQRAMEKGYHRMSPFFIPSSIINL----AAGNIAIKYG 153
Cdd:PRK07103 83 AALAAAREAWRDAAL--GPVDPDRIGLV----VGG-SNLQQREQALVHETYRDRPAFLRPSYGLSFmdtdLVGLCSEQFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 154 IKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQAL---YRGDDVSKASIPFDVNRGGF 230
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgsdRFADEPEAACRPFDQDRDGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 231 VMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHitGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPL 310
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 311 NDKVETLAIRNAFGPHAYelnVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTD-LDPECdlNYTLGKGVAKK 389
Cdd:PRK07103 314 GDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEpIDERF--RWVGSTAESAR 388
|
410 420
....*....|....*....|..
gi 1308460336 390 VNYALSNSLGFGGHNATVVIKK 411
Cdd:PRK07103 389 IRYALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
6-409 |
1.14e-61 |
|
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: 205.10 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 6 RVVITGLGALTPVGNTVAETWEGIKNGKNGIAPIT--------HYDASNDE----VKLAAELKNIRLED----KLEGKEI 69
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedrwdadgYYPDPGKPgktyTRRGGFLDDVDAFDaaffGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 70 RRTDRFTQLALYATDEAVKDASLNFEDIDIKRTGVYYtsGIGGLETINDQKQRAMEkgyhrMSPFFIPSSIINLAAGNIA 149
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFV--GASSSDYLELLARDPDE-----IDAYAATGTSRAFLANRIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 150 IKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALyRGDDVSKasiPFDVNRGG 229
Cdd:cd00833 155 YFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGML-SPDGRCR---PFDADADG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 230 FVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCD--ATHITGPDPEGngAKDSMLFALEDGLVNPNEVDYINAHGTS 307
Cdd:cd00833 231 YVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgrTKGITAPSGEA--QAALIRRAYARAGVDPSDIDYVEAHGTG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 308 TPLNDKVETLAIRNAFGPHAYE---LNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLNYTLGK 384
Cdd:cd00833 309 TPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLR 388
|
410 420 430
....*....|....*....|....*....|...
gi 1308460336 385 GVAK--------KVNYALSNSLGFGGHNATVVI 409
Cdd:cd00833 389 VPTEarpwpapaGPRRAGVSSFGFGGTNAHVIL 421
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
74-409 |
1.81e-59 |
|
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: 196.70 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 74 RFTQLALYATDEAVKDASLNFEDIDIKRTGVYYTSGIGGLETINDQKQRAMEKGYHRMSPFFIPSsiinlAAGNIAIKYG 153
Cdd:cd00825 10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 154 IKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIfgfaVMQALYRGDDVSKASIPFDVNRGGFVMG 233
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDC----EFDAMGALSTPEKASRTFDAAADGFVFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 234 EGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDK 313
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 314 VETLAIRNAFGPHAyeLNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTINTTDLDPECDLnyTLGKGVAKKVNYA 393
Cdd:cd00825 241 KELKLLRSEFGDKS--PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLN--IVTETTPRELRTA 316
|
330
....*....|....*.
gi 1308460336 394 LSNSLGFGGHNATVVI 409
Cdd:cd00825 317 LLNGFGLGGTNATLVL 332
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
5-247 |
2.23e-52 |
|
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: 175.52 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 5 RRVVITGLGALTPVGNTVAETWEGIKNGKNGIAPI--THYDASN---DEVKLAAELKNIR-----------LEDKLEGKE 68
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKlydPPSRIAGKIYTKWgglddifdfdpLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 69 IRRTDRFTQLALYATDEAVKDASLNFEDIDIKRTGVYYTSGIGGLEtinDQKQRAMEKGYHRMSPFFIPSsIINLAAGNI 148
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYA---ALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 149 AIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRgDDVSKAsipFDVNRG 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP-DGPCKA---FDPFAD 232
|
250
....*....|....*....
gi 1308460336 229 GFVMGEGAGTLIIEELEHA 247
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
255-368 |
4.36e-43 |
|
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: 146.94 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 255 YAEVIGYAATCDATHITGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAFGPHAYE--LNV 332
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1308460336 333 SSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTIN 368
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
7-416 |
7.13e-38 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 146.17 E-value: 7.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 7 VVITGLGALTPVGNTVAETWEGIKNGKNGIAPIT--------HYDASNDE-----VKLAAELKNIRLEDKLE----GKEI 69
Cdd:COG3321 6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPadrwdadaYYDPDPDApgktyVRWGGFLDDVDEFDALFfgisPREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 70 RRTD---RftqLALYATDEAVKDASLNFEDIDIKRTGVYytSGIGGletiNDQKQRAMEkGYHRMSPFFIPSSIINLAAG 146
Cdd:COG3321 86 EAMDpqqR---LLLEVAWEALEDAGYDPESLAGSRTGVF--VGASS----NDYALLLLA-DPEAIDAYALTGNAKSVLAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 147 NIAIKYGIKGPAIShV-TACASSTNALGEAFRAIRDGYLDLAITGGSegCVI--PIGIFGFAVMQALYRgDDVSKAsipF 223
Cdd:COG3321 156 RISYKLDLRGPSVT-VdTACSSSLVAVHLACQSLRSGECDLALAGGV--NLMltPESFILFSKGGMLSP-DGRCRA---F 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 224 DVNRGGFVMGEGAGTLIIEELEHAKKRNAKIYAeVI------------GYAAtcdathitgpdPEGNGAKDSMLFALEDG 291
Cdd:COG3321 229 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYA-VIrgsavnqdgrsnGLTA-----------PNGPAQAAVIRRALADA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 292 LVNPNEVDYINAHGTSTPLNDKVETLAIRNAFGPHAYE---LNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPTIN 368
Cdd:COG3321 297 GVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLH 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1308460336 369 TTDLDPECDLN----YTLGKGVAKKVN----YALSNSLGFGGHNATVVIKKYQEEE 416
Cdd:COG3321 377 FETPNPHIDFEnspfYVNTELRPWPAGggprRAGVSSFGFGGTNAHVVLEEAPAAA 432
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
74-409 |
1.91e-33 |
|
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: 125.63 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 74 RFTQLALYATDEAVKDASLNFEdidiKRTGVYYTSGIGGletindqkqramekgyHRMSPffipssiinlAAGNIAIKYG 153
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKG----PIVGVIVGTTGGS----------------GEFSG----------AAGQLAYHLG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 154 IK-GPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIpigifgfavmqalyrgddvskasipfdvnrggfvm 232
Cdd:cd00327 56 ISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEEFVF----------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 233 GEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDATHItGPDPEGNGAKDSMLFALEDGLVNPNEVDYINAHGTSTPLND 312
Cdd:cd00327 101 GDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 313 KVETLAIRNAFGPHayELNVSSTKSMTGHLLGASGAVEAIITTLAVKDDFVPPtintTDLDPECdlnytlgkgvakkvny 392
Cdd:cd00327 180 AVELALGLDPDGVR--SPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP----TPREPRT---------------- 237
|
330
....*....|....*..
gi 1308460336 393 ALSNSLGFGGHNATVVI 409
Cdd:cd00327 238 VLLLGFGLGGTNAAVVL 254
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
72-415 |
6.56e-26 |
|
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: 110.87 E-value: 6.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 72 TDRFTQLALYATDEAVKDASLNfEDIDIKRTGVyyTSGIGG----LETINDQKQ-----------------RAM-----E 125
Cdd:TIGR02813 90 TDISQLLSLVVAKEVLNDAGLP-DGYDRDKIGI--TLGVGGgqkqSSSLNARLQypvlkkvfkasgvededSEMlikkfQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 126 KGYHRMSPFFIPSSIINLAAGNIAIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFA 205
Cdd:TIGR02813 167 DQYIHWEENSFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 206 VMQALYRGDDVSkasiPFDVNRGGFVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAATCDA--THITGPDPEGNgAKdS 283
Cdd:TIGR02813 247 KTPAFTTNEDIQ----PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQ-AK-A 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 284 MLFALEDGLVNPNEVDYINAHGTSTPLNDKVETLAIRNAFGPHAYELN---VSSTKSMTGHLLGASGAVEAIITTLAVKD 360
Cdd:TIGR02813 321 LKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQhiaLGSVKSQIGHTKSTAGTAGMIKAVLALHH 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1308460336 361 DFVPPTINTTDLDPECD-------LNYTLGKGVAKKVNY---ALSNSLGFGGHNATVVIKKYQEE 415
Cdd:TIGR02813 401 KVLPPTINVDQPNPKLDienspfyLNTETRPWMQREDGTprrAGISSFGFGGTNFHMVLEEYSPK 465
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
163-409 |
4.91e-16 |
|
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: 78.14 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 163 TACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRgDDVSKAsipFDVNRGGFVMGEGAGTLIIE 242
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSP-DGRCKT---FDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 243 ELEHAKKRNAKIYAEVIGYAATCDathitgpdpeGNGAkdsmlfaledGLVNPNevdyinahgtstplndkvetlairna 322
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQD----------GRSN----------GITAPS-------------------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 323 fgPHAyELNVSSTKSMTGHLLGASGaVEAII-TTLAVKDDFVPPTINTTDLDPECDLNYTlgkgvAKKVN---------- 391
Cdd:smart00825 205 --GPA-QLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEES-----PLRVPteltpwpppg 275
|
250 260
....*....|....*....|.
gi 1308460336 392 ---YALSNSLGFGGHNATVVI 409
Cdd:smart00825 276 rprRAGVSSFGFGGTNAHVIL 296
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
142-263 |
1.41e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 59.58 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 142 NLAAGNIAIKYGIKGPAISHVTACASSTNALGEAFRAIRDGYLDLAITGGSEGCVIPIGIFGFAVMQALYRGddvskasi 221
Cdd:PRK06519 152 NLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKG-------- 223
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1308460336 222 PF-------DVNRGGFVMGEGAGTLIIEELEHAKKRNAKIYAEVIGYAA 263
Cdd:PRK06519 224 GWapvwsrgGEDGGGFILGSGGAFLVLESREHAEARGARPYARISGVES 272
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
165-261 |
7.56e-04 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 41.48 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 165 CASSTNALGEAFRAIRDGYLDLAITGGSEgcvipigifgfavmqalyrgddvskasipfDVNRGGFVMGEGagtliieel 244
Cdd:PRK09050 90 CGSGMDAVGTAARAIKAGEAELMIAGGVE------------------------------SMSRAPFVMGKA--------- 130
|
90
....*....|....*..
gi 1308460336 245 EHAKKRNAKIYAEVIGY 261
Cdd:PRK09050 131 DSAFSRQAEIFDTTIGW 147
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
70-193 |
9.51e-03 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 38.01 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308460336 70 RRTDR-FTQLALYATDEAVKDASLNFEDIDikrtGVYYTSGIGGLETINdqkqramekgyhrmspffipssiinlAAGNI 148
Cdd:cd00829 10 RRSDRsPLELAAEAARAALDDAGLEPADID----AVVVGNAAGGRFQSF--------------------------PGALI 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1308460336 149 AIKYGIKGPAISHV-TACASSTNALGEAFRAIRDGYLDLAITGGSE 193
Cdd:cd00829 60 AEYLGLLGKPATRVeAAGASGSAAVRAAAAAIASGLADVVLVVGAE 105
|
|
| |
