|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-408 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 753.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 22776887 402 NVALVFK 408
Cdd:TIGR03150 401 NASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 741.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 2 NKRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAA 81
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 82 KMAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVT 161
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 162 ACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILE 240
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 241 SLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAV 320
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 321 FGDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGG 400
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 22776887 401 HNVALVFKKF 410
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-410 |
0e+00 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 722.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 22776887 402 NVALVFKKF 410
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-407 |
0e+00 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 667.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 22776887 402 NVALVF 407
Cdd:cd00834 401 NASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-245 |
2.10e-65 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 209.41 E-value: 2.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFV--TKVDKDLF---PAKVAAEVK----------NFDPTLY-MDKKD 66
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 67 ARKMDPFTQYAVAAAKMAVEDANLTINEANAERVGVWIGSGIGGmktWEDQHTKFMEKGAKRVSPFFVPMMiPDMAAGQV 146
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD---YAALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 147 SIQLGAKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALSTNeDPQKASRPFDknrN 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GPCKAFDPFA---D 232
|
250
....*....|....*....
gi 22776887 227 GFVMGEGAGILILESLESA 245
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
5-406 |
1.82e-27 |
|
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: 110.50 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSGIDfvtkvdkdlfpakvaaevkNFDPTLY-MDKKDARKMDP----FTQYAVA 79
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAAFFgISPREAEAMDPqqrlLLEVAWE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 80 AakmaVEDANLTINEANAERVGVWIGsgiggmktwedqhtkfmekgakrvspffvpMMIPDMAagqVSIQlgakginscs 159
Cdd:smart00825 62 A----LEDAGIDPESLRGSRTGVFVG------------------------------VSSSDYS---VTVD---------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 160 vTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedPQKASRPFDKNRNGFVMGEGAGILIL 239
Cdd:smart00825 95 -TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVGVVVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 240 ESLESALQRDATIYGEIVGyGAT---GDAYHITAPaeNGEGatramQialkdanlepsdvqyvnahgtstdlndkyetqa 316
Cdd:smart00825 170 KRLSDALRDGDPILAVIRG-SAVnqdGRSNGITAP--SGPA-----Q--------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 317 ikavfgdhasdLAISSTKSMTGHLLGAAgGIEAVI-SIKAIQDSIIPPTINYETPDPDCDLD----YVPNEARKQTVD-- 389
Cdd:smart00825 209 -----------LLIGSVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgr 276
|
410 420
....*....|....*....|
gi 22776887 390 ---AVVsNSLGFGGHNVALV 406
Cdd:smart00825 277 prrAGV-SSFGFGGTNAHVI 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
3-408 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 753.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTrNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 22776887 402 NVALVFK 408
Cdd:TIGR03150 401 NASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
2-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 741.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 2 NKRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAA 81
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 82 KMAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVT 161
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 162 ACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILE 240
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTrNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 241 SLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAV 320
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 321 FGDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGG 400
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 22776887 401 HNVALVFKKF 410
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
3-410 |
0e+00 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 722.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 22776887 402 NVALVFKKF 410
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
3-407 |
0e+00 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 667.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTrNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 22776887 402 NVALVF 407
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-411 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 562.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 1 MNKRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKN--------FDPTLYMDKKDARKMDP 72
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 73 FTQYAVAAAKMAVEDANLTI-NEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLG 151
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 152 AKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST--NEDPQKASRPFDKNRNGFV 229
Cdd:PRK06333 162 FKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTrfNDAPEQASRPFDRDRDGFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 230 MGEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLN 309
Cdd:PRK06333 242 MGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 310 DKYETQAIKAVFGdHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCD-LDYVPNEARKQTV 388
Cdd:PRK06333 322 DLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDM 400
|
410 420
....*....|....*....|...
gi 22776887 389 DAVVSNSLGFGGHNVALVFKKFV 411
Cdd:PRK06333 401 DYALSNGFGFGGVNASILFRRWE 423
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
12-410 |
0e+00 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 515.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 12 ALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDL----------------FPAKVAAEVKN--FDPTLYMDKKdarKMDPF 73
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLpdcipeqkalenlvaaMPCQIAAEVDQseFDPSDFAPTK---RESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 74 TQYAVAAAKMAVEDANLTI-NEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGA 152
Cdd:PTZ00050 78 THFAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 153 KGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST--NEDPQKASRPFDKNRNGFVM 230
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTkyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 231 GEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKD-ANLEPSDVQYVNAHGTSTDLN 309
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDgANININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 310 DKYETQAIKAVFGDH-ASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEAR--KQ 386
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQ 397
|
410 420
....*....|....*....|....
gi 22776887 387 TVDAVVSNSLGFGGHNVALVFKKF 410
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
3-410 |
1.26e-179 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 506.19 E-value: 1.26e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTrNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAEngEGATRAMQIALKDANLEPSDvqYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPKID--YINAHGTSTPYNDKNETAALKELF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397
|
....*....
gi 22776887 402 NVALVFKKF 410
Cdd:PRK08439 398 NGVVIFKKV 406
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
3-410 |
2.47e-152 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 437.13 E-value: 2.47e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILILES 241
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 242 LESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHAS-DLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARK-QTVDAVVSNSLGFG 399
Cdd:PRK08722 324 GEAGSkQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKvESMEYAICNSFGFG 403
|
410
....*....|.
gi 22776887 400 GHNVALVFKKF 410
Cdd:PRK08722 404 GTNGSLIFKKM 414
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
3-407 |
5.18e-150 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 432.29 E-value: 5.18e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDL--------------FPAKVAAEV------KNFDPTLYM 62
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMksedeetqlytldqLPSRVAALVprgtgpGDFDEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 63 DkkdARKMDPFTQYAVAAAKMAVEDAN-LTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDM 141
Cdd:PLN02836 86 N---SRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 142 AAGQVSIQLGAKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST--NEDPQKASR 219
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTkfNSCPTEASR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 220 PFDKNRNGFVMGEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYV 299
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 300 NAHGTSTDLNDKYETQAIKAVFGDHASD--LAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLD 377
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATSggLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402
|
410 420 430
....*....|....*....|....*....|.
gi 22776887 378 YVP-NEARKQTVDAVVSNSLGFGGHNVALVF 407
Cdd:PLN02836 403 FVPlTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-411 |
8.04e-116 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 348.51 E-value: 8.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLT---INEANAERVGVWIGSGIGGMKTWEDQhTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCS 159
Cdd:PLN02787 209 KALADGGITedvMKELDKTKCGVLIGSAMGGMKVFNDA-IEALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 160 VTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFDKNRNGFVMGEGAGILI 238
Cdd:PLN02787 288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQrNDDPTKASRPWDMNRDGFVMGEGAGVLL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 239 LESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIK 318
Cdd:PLN02787 368 LEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALM 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 319 AVFGDHaSDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLD-YVPNEARKQTVDAVVSNSLG 397
Cdd:PLN02787 448 RCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSNSFG 526
|
410
....*....|....
gi 22776887 398 FGGHNVALVFKKFV 411
Cdd:PLN02787 527 FGGHNSSILFAPYK 540
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
5-410 |
1.97e-108 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 325.53 E-value: 1.97e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSGI-----DFVTKVDkdlFPAKVAAEVK-NFDPtlYMDKKDARKMDPFTQYAV 78
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFD---LPVRIGGHLLeEFDH--QLTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 79 AAAKMAVEDANLTinEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSC 158
Cdd:PRK07910 89 VLGRRVWENAGSP--EVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 159 SVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKA-LST-NEDPQKASRPFDKNRNGFVMGEGAGI 236
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTnNDDPAGACRPFDKDRDGFVFGEGGAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 237 LILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQA 316
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 317 IKAVFGDHASdlAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSL 396
Cdd:PRK07910 327 INNALGGHRP--AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSF 404
|
410
....*....|....
gi 22776887 397 GFGGHNVALVFKKF 410
Cdd:PRK07910 405 GFGGHNVALAFGRY 418
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
3-408 |
4.62e-108 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 324.25 E-value: 4.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIdfVTKVDKDLFP---AKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVA 79
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAV--RRMPEWDRYDglnTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 80 AAKMAVEDANLTINEANAE-RVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSP-FFVPMMiPDMAAGQVSIQLGAKGINS 157
Cdd:PRK09116 80 ASELALEDAGLLGDPILTDgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITAtTYVRMM-PHTTAVNVGLFFGLKGRVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 158 CSVTACASGANSIGDAFKAIQRGDADIMISGG------TEAPISDMAFAgfSSSKalstNEDPQKASRPFDKNRNGFVMG 231
Cdd:PRK09116 159 PTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGaeelcpTEAAVFDTLFA--TSTR----NDAPELTPRPFDANRDGLVIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 232 EGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPaeNGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDK 311
Cdd:PRK09116 233 EGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 312 YETQAIKAVFGDHasdLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDC-DLDYVPNEARKQTVDA 390
Cdd:PRK09116 311 AESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEY 387
|
410
....*....|....*...
gi 22776887 391 VVSNSLGFGGHNVALVFK 408
Cdd:PRK09116 388 VMSNNFAFGGINTSLIFK 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
3-410 |
1.84e-107 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 322.39 E-value: 1.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKnFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTW-EDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVT 161
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQvEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 162 ACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAgFSSSKALST--NEDPQKASRPFDKNRNGFVMGEGAGILIL 239
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTkyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 240 ESLESALQRDATIYGEIVGYGATGDAYHITAPAenGEGATRAMQIALKDANlepSDVQYVNAHGTSTDLNDKYETQAIKA 319
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 320 VFGDHASdlAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPD-CDLDYVPNEARKQTVDAVVSNSLGF 398
Cdd:PRK07967 315 VFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFGF 392
|
410
....*....|..
gi 22776887 399 GGHNVALVFKKF 410
Cdd:PRK07967 393 GGTNATLVFRRY 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
5-407 |
1.18e-104 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 316.19 E-value: 1.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVknfdptlymdkkDARKMDPFT------QYAV 78
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------------DFLPESPFGasalseALAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 79 AAAKMAVEDANLTINEANA--------------ERVGVWIGSGIGGMKTWEDqhtkFME-KGAKRVSPFFVPMMIPDMAA 143
Cdd:PRK06501 81 LAAEEALAQAGIGKGDFPGplflaappvelewpARFALAAAVGDNDAPSYDR----LLRaARGGRFDALHERFQFGSIAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 144 gQVSIQLGAKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST-NEDPQKASRPFD 222
Cdd:PRK06501 157 -RLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTqNDPPEKASKPFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 223 KNRNGFVMGEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAH 302
Cdd:PRK06501 236 KDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 303 GTSTDLNDKYETQAIKAVFGDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNE 382
Cdd:PRK06501 316 GTSTPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNV 395
|
410 420
....*....|....*....|....*
gi 22776887 383 ARKQTVDAVVSNSLGFGGHNVALVF 407
Cdd:PRK06501 396 ARDARVTAVLSNSFGFGGQNASLVL 420
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
93-411 |
8.70e-102 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 305.88 E-value: 8.70e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 93 NEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTACASGANSIGD 172
Cdd:PRK14691 21 NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 173 AFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALST--NEDPQKASRPFDKNRNGFVMGEGAGILILESLESALQRDA 250
Cdd:PRK14691 101 AVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSThfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 251 TIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVFGDhASDLAI 330
Cdd:PRK14691 181 KPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 331 SSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCD-LDYVPNEARKQTVDAVVSNSLGFGGHNVALVFKK 409
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
..
gi 22776887 410 FV 411
Cdd:PRK14691 340 WV 341
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-406 |
1.50e-92 |
|
"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: 284.33 E-value: 1.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 4 RVVITGLGALSPVGNN---VDEMWESVTTGKSGIDFVTkVDKDLFPAKVAAEVKNFDPtlymDKKDARK---MDPFTQYA 77
Cdd:cd00828 2 RVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVA-RLKSRFDRGVAGQIPTGDI----PGWDAKRtgiVDRTTLLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 78 VAAAKMAVEDANLTI-NEANAERVGVWIGSGIGGMKTWEDqhtkFMEKGAKRVSPFFVPMMI--PDMAAGQVSI-QLGAK 153
Cdd:cd00828 77 LVATEEALADAGITDpYEVHPSEVGVVVGSGMGGLRFLRR----GGKLDARAVNPYVSPKWMlsPNTVAGWVNIlLLSSH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 154 GINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFaGFSSSKALSTNED-PQKASRPFDKNRNGFVMGE 232
Cdd:cd00828 153 GPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALSTAEEePEEMSRPFDETRDGFVEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 233 GAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAeNGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKY 312
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 313 ETQAIKAVFGDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARK--QTVDA 390
Cdd:cd00828 311 ESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlnLKVRA 390
|
410
....*....|....*.
gi 22776887 391 VVSNSLGFGGHNVALV 406
Cdd:cd00828 391 ALVNAFGFGGSNAALV 406
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
4-409 |
1.00e-91 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 281.56 E-value: 1.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 4 RVVITGLGALSPVGNnVDEMWESVTTGKSGIDFVTKvdkdlFPakvaaevkNFDPT-LYMDKKDARKMDPFTQYAVAAAk 82
Cdd:PRK05952 3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQP-----FP--------ELPPLpLGLIGNQPSSLEDLTKTVVTAA- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 maVEDANLTINEANAervGVWIGSGIGGMKTWEDQHTKfMEKGAKRVSPFFVPM----MIPDMAAGQVSIQLGAKGINSC 158
Cdd:PRK05952 68 --LKDAGLTPPLTDC---GVVIGSSRGCQGQWEKLARQ-MYQGDDSPDEELDLEnwldTLPHQAAIAAARQIGTQGPVLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 159 SVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedpQKASRPFDKNRNGFVMGEGAGILI 238
Cdd:PRK05952 142 PMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAYPFDRQREGLVLGEGGAILV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 239 LESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIK 318
Cdd:PRK05952 217 LESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 319 AVFGdhaSDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETpdPDCDLDYVpNEARKQTVDAVVSNSLGF 398
Cdd:PRK05952 297 ALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFV-RQAQQSPLQNVLCLSFGF 370
|
410
....*....|.
gi 22776887 399 GGHNVALVFKK 409
Cdd:PRK05952 371 GGQNAAIALGK 381
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
3-406 |
3.03e-81 |
|
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: 254.98 E-value: 3.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFPAKVAAEVKNFDPTLYMDKKDARKMDPFTQYAVAAAK 82
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 83 MAVEDANLTINEANAERVGVWIGSGIGGMKTWEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGAKGINSCSVTA 162
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 163 CASGANSIGDAFKAIQRGdADIMISGGTEAPISDMAFAGFSSSKALSTNEDPQKASRPFDKNRNGFVMGEGAGILILESL 242
Cdd:cd00832 161 QAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLSTSDDPARAYLPFDAAAAGYVPGEGGAILVLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 243 ESALQRDATIYGEIVGYGATGDAyhitAPAE-NGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVF 321
Cdd:cd00832 240 AAARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 322 GDHAsdLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYVPNEARKQTVDAVVSNSLGFGGH 401
Cdd:cd00832 316 GPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGF 393
|
....*
gi 22776887 402 NVALV 406
Cdd:cd00832 394 NSALV 398
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
5-407 |
4.26e-75 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 238.97 E-value: 4.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSG----IDFVTkVDKDLFPAKVAAevkNFDPTL--YMDKKDARKmdpfTQYAV 78
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRASgmrpCDFWL-VDLPTWVGEVVG---VELPALpaALAAFDCRN----NRLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 79 AAAKM---AVEDAnltINEANAERVGVWIG---SGIG----GMKTWEDQHTKF--------MEKGAkrVSPFfvpmmipd 140
Cdd:PRK09185 76 LALQQiepAVEAA---IARYGADRIGVVLGtstSGILegelAYRRRDPAHGALpadyhyaqQELGS--LADF-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 141 maagqVSIQLGAKGiNSCSV-TACASGANSIGDAFKAIQRGDADIMISGGTEApISDMAFAGFSSSKALSTnedpqKASR 219
Cdd:PRK09185 143 -----LRAYLGLSG-PAYTIsTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP-----QPCR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 220 PFDKNRNGFVMGEGAGILILESLESALQRdatiygeIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYV 299
Cdd:PRK09185 211 PFSANRDGINIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 300 NAHGTSTDLNDKYETQAIKAVFGDHasdLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLDYV 379
Cdd:PRK09185 284 NLHGTATPLNDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYL 360
|
410 420
....*....|....*....|....*...
gi 22776887 380 PNEARKQTVDAVVSNSLGFGGHNVALVF 407
Cdd:PRK09185 361 VENAQALAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
4-406 |
3.27e-71 |
|
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: 229.75 E-value: 3.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 4 RVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLFP------------AKVAAEVKN---FDPTLY-MDKKDA 67
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPEDRWDADGyypdpgkpgktyTRRGGFLDDvdaFDAAFFgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 68 RKMDPftQYAVA--AAKMAVEDANLTINEANAERVGVWIGSGiggmktwEDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQ 145
Cdd:cd00833 82 EAMDP--QQRLLleVAWEALEDAGYSPESLAGSRTGVFVGAS-------SSDYLELLARDPDEIDAYAATGTSRAFLANR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 146 VSIQLGAKGiNSCSV-TACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedPQKASRPFDKN 224
Cdd:cd00833 153 ISYFFDLRG-PSLTVdTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS----PDGRCRPFDAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 225 RNGFVMGEGAGILILESLESALQRDATIYGEIVGYGATGDAY--HITAPaeNGEGATRAMQIALKDANLEPSDVQYVNAH 302
Cdd:cd00833 228 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 303 GTSTDLNDKYETQAIKAVFGDHASD---LAISSTKSMTGHLLGAAgGIEAVI-SIKAIQDSIIPPTINYETPDPDCDLD- 377
Cdd:cd00833 306 GTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAA-GLAGLIkVVLALEHGVIPPNLHFETPNPKIDFEe 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 22776887 378 ---YVPNEAR-----KQTVDAVVsNSLGFGGHNVALV 406
Cdd:cd00833 385 splRVPTEARpwpapAGPRRAGV-SSFGFGGTNAHVI 420
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
3-409 |
1.92e-70 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 227.61 E-value: 1.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTKVDKDLF--------PAKVAAEVKNFDPTLYMDKKDARKMDPFT 74
Cdd:PRK07103 2 DEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPddagaglaSAFIGAELDSLALPERLDAKLLRRASLSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 75 QYAVAAAKMAVEDANLtiNEANAERVGVWIGsgigGMKTWEDQHTKFMEKGAKRvsPFFVP------MMIPDmAAGQVSI 148
Cdd:PRK07103 82 QAALAAAREAWRDAAL--GPVDPDRIGLVVG----GSNLQQREQALVHETYRDR--PAFLRpsyglsFMDTD-LVGLCSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 149 QLGAKGInSCSV-TACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALSTN---EDPQKASRPFDKN 224
Cdd:PRK07103 153 QFGIRGE-GFTVgGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDrfaDEPEAACRPFDQD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 225 RNGFVMGEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPaeNGEGATRAMQIALKDANLEPSDVQYVNAHGT 304
Cdd:PRK07103 232 RDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 305 STDLNDKYEtqaIKAVFGDHASDLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETP-DPDCdlDYVPNEA 383
Cdd:PRK07103 310 GSPLGDETE---LAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTA 384
|
410 420
....*....|....*....|....*.
gi 22776887 384 RKQTVDAVVSNSLGFGGHNVALVFKK 409
Cdd:PRK07103 385 ESARIRYALSLSFGFGGINTALVLER 410
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
3-245 |
2.10e-65 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 209.41 E-value: 2.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 3 KRVVITGLGALSPVGNNVDEMWESVTTGKSGIDFV--TKVDKDLF---PAKVAAEVK----------NFDPTLY-MDKKD 66
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 67 ARKMDPFTQYAVAAAKMAVEDANLTINEANAERVGVWIGSGIGGmktWEDQHTKFMEKGAKRVSPFFVPMMiPDMAAGQV 146
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD---YAALLLLDEDGGPRRGSPFAVGTM-PSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 147 SIQLGAKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALSTNeDPQKASRPFDknrN 226
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD-GPCKAFDPFA---D 232
|
250
....*....|....*....
gi 22776887 227 GFVMGEGAGILILESLESA 245
Cdd:pfam00109 233 GFVRGEGVGAVVLKRLSDA 251
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
73-406 |
4.15e-60 |
|
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: 198.24 E-value: 4.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 73 FTQYAVAAAKMAVEDANLTINEANAERVGVWIGSGIGGmktweDQHTKFMEKGAKRVSPFFVPMMIPDMAAGQVSIQLGA 152
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGS-----PRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 153 KGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedPQKASRPFDKNRNGFVMGE 232
Cdd:cd00825 86 HGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST----PEKASRTFDAAADGFVFGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 233 GAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKY 312
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 313 ETQAIKAVFGDHAsdLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYETPDPDCDLdyVPNEARKQTVDAVV 392
Cdd:cd00825 242 ELKLLRSEFGDKS--PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLN--IVTETTPRELRTAL 317
|
330
....*....|....
gi 22776887 393 SNSLGFGGHNVALV 406
Cdd:cd00825 318 LNGFGLGGTNATLV 331
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
5-406 |
7.77e-57 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 201.64 E-value: 7.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSGIDFVTK----VDKDLFPAKVAA------------EVKNFDPTLY-MDKKDA 67
Cdd:COG3321 6 IAIIGMACRFPGADDPEEFWRNLRAGRDAITEVPAdrwdADAYYDPDPDAPgktyvrwggfldDVDEFDALFFgISPREA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 68 RKMDPftQYAVA--AAKMAVEDANLTINEANAERVGVWIGSGIGGmktwedqHTKFMEKGAKRVSPFFVPMMIPDMAAGQ 145
Cdd:COG3321 86 EAMDP--QQRLLleVAWEALEDAGYDPESLAGSRTGVFVGASSND-------YALLLLADPEAIDAYALTGNAKSVLAGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 146 VSIQLGAKGInSCSV-TACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedPQKASRPFDKN 224
Cdd:COG3321 157 ISYKLDLRGP-SVTVdTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS----PDGRCRAFDAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 225 RNGFVMGEGAGILILESLESALQRDATIYGEIVGY-----GAT-GdayhITAPaeNGEGATRAMQIALKDANLEPSDVQY 298
Cdd:COG3321 232 ADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSavnqdGRSnG----LTAP--NGPAQAAVIRRALADAGVDPATVDY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 299 VNAHGTSTDLNDKYETQAIKAVFGDHASD---LAISSTKSMTGHLLGAAG--GIeavisIK---AIQDSIIPPTINYETP 370
Cdd:COG3321 306 VEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGvaGL-----IKavlALRHGVLPPTLHFETP 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22776887 371 DPDCDLD----YVPNEARKQTVD-----AVVSnSLGFGGHNVALV 406
Cdd:COG3321 381 NPHIDFEnspfYVNTELRPWPAGggprrAGVS-SFGFGGTNAHVV 424
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-368 |
1.96e-49 |
|
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: 163.12 E-value: 1.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 253 YGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPSDVQYVNAHGTSTDLNDKYETQAIKAVFGDHASD--LAI 330
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 22776887 331 SSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTINYE 368
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
135-410 |
7.57e-34 |
|
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: 134.36 E-value: 7.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 135 PMMIPDMAAGQVSIQLGAKGINSCSVTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALSTNEDP 214
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNEDI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 215 QkasrPFDKNRNGFVMGEGAGILILESLESALQRDATIYGEIVGYGATGDAYHITAPAENGEGATRAMQIALKDANLEPS 294
Cdd:TIGR02813 258 Q----PFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAPH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 295 DVQYVNAHGTSTDLNDKYETQAIKAVFG---DHASDLAISSTKSMTGH---LLGAAGGIEAVIsikAIQDSIIPPTINYE 368
Cdd:TIGR02813 334 TCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHtksTAGTAGMIKAVL---ALHHKVLPPTINVD 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 22776887 369 TPDPDCDLD----YVPNEARK--QTVD-----AVVSnSLGFGGHNVALVFKKF 410
Cdd:TIGR02813 411 QPNPKLDIEnspfYLNTETRPwmQREDgtprrAGIS-SFGFGGTNFHMVLEEY 462
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
142-406 |
4.22e-32 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 122.17 E-value: 4.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 142 AAGQVSIQLGAKGINSCSV-TACASGANSIGDAFKAIQRGDADIMISGGTEApisdmafagfssskalstnedpqkasrp 220
Cdd:cd00327 46 AAGQLAYHLGISGGPAYSVnQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 221 fdknrngFVMGEGAGILILESLESALQRDATIYGEIVGYGATGD-AYHITAPaeNGEGATRAMQIALKDANLEPSDVQYV 299
Cdd:cd00327 98 -------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAV--SGEGLARAARKALEGAGLTPSDIDYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 300 NAHGTSTDLNDKYETQAIKAVFGDHAsdLAISSTKSMTGHLLGAAGGIEAVISIKAIQDSIIPPTinyetpdpdcdldyv 379
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*..
gi 22776887 380 PNEARKqtvdaVVSNSLGFGGHNVALV 406
Cdd:cd00327 232 PREPRT-----VLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
5-406 |
1.82e-27 |
|
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: 110.50 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 5 VVITGLGALSPVGNNVDEMWESVTTGKSGIDfvtkvdkdlfpakvaaevkNFDPTLY-MDKKDARKMDP----FTQYAVA 79
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAAFFgISPREAEAMDPqqrlLLEVAWE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 80 AakmaVEDANLTINEANAERVGVWIGsgiggmktwedqhtkfmekgakrvspffvpMMIPDMAagqVSIQlgakginscs 159
Cdd:smart00825 62 A----LEDAGIDPESLRGSRTGVFVG------------------------------VSSSDYS---VTVD---------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 160 vTACASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALStnedPQKASRPFDKNRNGFVMGEGAGILIL 239
Cdd:smart00825 95 -TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS----PDGRCKTFDASADGYVRGEGVGVVVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 240 ESLESALQRDATIYGEIVGyGAT---GDAYHITAPaeNGEGatramQialkdanlepsdvqyvnahgtstdlndkyetqa 316
Cdd:smart00825 170 KRLSDALRDGDPILAVIRG-SAVnqdGRSNGITAP--SGPA-----Q--------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 317 ikavfgdhasdLAISSTKSMTGHLLGAAgGIEAVI-SIKAIQDSIIPPTINYETPDPDCDLD----YVPNEARKQTVD-- 389
Cdd:smart00825 209 -----------LLIGSVKSNIGHLEAAA-GVAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPgr 276
|
410 420
....*....|....*....|
gi 22776887 390 ---AVVsNSLGFGGHNVALV 406
Cdd:smart00825 277 prrAGV-SSFGFGGTNAHVI 295
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
162-234 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22776887 162 ACASGANSIGDAFKAIQRGDADIMISGGTE----APIsdMAFAGFSSSKALSTNEDPQKASRpFDKNRNGFVMGEGA 234
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVEsmsrAPM--LLPKARWGYRMNAKLVDPMINPG-LTDPYTGLSMGETA 160
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
164-309 |
3.93e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 45.40 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22776887 164 ASGANSIGDAFKAIQRGDADIMISGGTEAPISDMAFAGFSSSKALSTNEdpqkasrpfdkNRNGFVMGEGAGILILESLE 243
Cdd:PRK06147 134 VSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLTSQ-----------NSNGFIPGEAAAAVLLGRPA 202
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22776887 244 SALQRDATIYGeiVGYGATgdayhiTAPAEN-------GEGATRAMQIALKDANLEPSDVQYVnahgtSTDLN 309
Cdd:PRK06147 203 GGEAPGLPLLG--LGLGRE------PAPVGEsedlplrGDGLTQAIRAALAEAGCGLEDMDYR-----IADLN 262
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
162-234 |
7.67e-03 |
|
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: 38.23 E-value: 7.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22776887 162 ACASGANSIGDAFKAIQRGDADIMISGGTE----API-SDMAFAGFSSSKALSTNEDPQKASRPFdknrNGFVMGEGA 234
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVEsmsrAPYlLPKARRGGRLGLNTLDGMLDDGLTDPF----TGLSMGITA 156
|
|
| |
