|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-408 |
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: 746.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLEE 241
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 242 YEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVF 321
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 322 GDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGGT 401
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 39983586 402 NATLLFK 408
Cdd:TIGR03150 401 NASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 705.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAA 80
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 81 HYAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVS 160
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 161 ACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLE 240
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 241 EYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSV 320
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 321 FGDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGG 400
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 39983586 401 TNATLLFKKV 410
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-410 |
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: 682.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLEE 241
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 242 YEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVF 321
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 322 GDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGGT 401
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 39983586 402 NATLLFKKV 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 ... |
2-407 |
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: 639.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLEE 241
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 242 YEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVF 321
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 322 GDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGGT 401
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 39983586 402 NATLLF 407
Cdd:cd00834 401 NASLVF 406
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-410 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 551.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAA 80
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 81 HYAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVS 160
Cdd:PRK08439 81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 161 ACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLE 240
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 241 EYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPegEGAARCMKMALNNAGVrpEEVDYINAHGTSTPFNDYYETLAVKSV 320
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGN--PKIDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 321 FGDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGG 400
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396
|
410
....*....|
gi 39983586 401 TNATLLFKKV 410
Cdd:PRK08439 397 TNGVVIFKKV 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-409 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 529.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVK--------GFDPEQYIDKKEVKKMDLF 72
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 73 IQYAMAAAHYAMEDSGLQI-TEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGA 151
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 152 KGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTR-NDDPTAASRPFEKNRDGFVL 230
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 231 AEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFND 310
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 311 YYETLAVKSVFGDyAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECD-LDYVPNAAREKSIT 389
Cdd:PRK06333 323 LGEVAAIKKVFGH-VSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401
|
410 420
....*....|....*....|
gi 39983586 390 YALSNNFGFGGTNATLLFKK 409
Cdd:PRK06333 402 YALSNGFGFGGVNASILFRR 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-410 |
4.90e-166 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 471.80 E-value: 4.90e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLEE 241
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 242 YEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVF 321
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 322 GDY-AKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAARE-KSITYALSNNFGFG 399
Cdd:PRK08722 324 GEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKvESMEYAICNSFGFG 403
|
410
....*....|.
gi 39983586 400 GTNATLLFKKV 410
Cdd:PRK08722 404 GTNGSLIFKKM 414
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
11-410 |
1.45e-161 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 460.70 E-value: 1.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 11 AVSPLGVGNAANWDALVSGTSGIGHITRFDA----------------SDLPVRIAGEVKG--FDPEQYidkKEVKKMDLF 72
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQseFDPSDF---APTKRESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 73 IQYAMAAAHYAMEDSGLQITEE-NAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGA 151
Cdd:PTZ00050 78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 152 KGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTR-NDDPTAASRPFEKNRDGFVL 230
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 231 AEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAG-VRPEEVDYINAHGTSTPFN 309
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 310 DYYETLAVKSVFGDY-AKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAR--EK 386
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQ 397
|
410 420
....*....|....*....|....
gi 39983586 387 SITYALSNNFGFGGTNATLLFKKV 410
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-407 |
5.86e-150 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 431.91 E-value: 5.86e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDA--------------SDLPVRIAGEV-KGFDPEQYIDKK-- 64
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVpRGTGPGDFDEELwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 65 EVKKMDLFIQYAMAAAHYAMEDSGLQITE-ENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPG 143
Cdd:PLN02836 86 NSRSSSRFIGYALCAADEALSDARWLPSEdEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 144 HISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTR-NDDPTAASRPFE 222
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 223 KNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAH 302
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 303 GTSTPFNDYYETLAVKSVFGDYA--KKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVP 380
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEHAtsGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420
....*....|....*....|....*...
gi 39983586 381 -NAAREKSITYALSNNFGFGGTNATLLF 407
Cdd:PLN02836 406 lTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-407 |
2.42e-121 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 358.56 E-value: 2.42e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 4 VVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVkgfdpeQYIDKKEVKKMDLFIQYAMAAAHYA 83
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLPESPFGASALSEALARLAAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 84 MEDSGLQITE--------------ENAERTGVLVGAGLGGLPTiekYHAAMLEGGHKKISPFFIPMLIINLAPgHISIKY 149
Cdd:PRK06501 87 LAQAGIGKGDfpgplflaappvelEWPARFALAAAVGDNDAPS---YDRLLRAARGGRFDALHERFQFGSIAD-RLADRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 150 GAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFV 229
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 230 LAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFN 309
Cdd:PRK06501 243 MAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPEN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 310 DYYETLAVKSVFGDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSIT 389
Cdd:PRK06501 323 DKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVT 402
|
410
....*....|....*...
gi 39983586 390 YALSNNFGFGGTNATLLF 407
Cdd:PRK06501 403 AVLSNSFGFGGQNASLVL 420
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-407 |
1.71e-116 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 350.43 E-value: 1.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGlqITEE--NAERTGVLVGAGLGGLPTIEKYHAAM--LEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLS 157
Cdd:PLN02787 209 KALADGG--ITEDvmKELDKTKCGVLIGSAMGGMKVFNDAIeaLRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 158 SVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIV 237
Cdd:PLN02787 287 ISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 238 VLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAV 317
Cdd:PLN02787 367 LLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQAL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 318 KSVFGDyAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREK-SITYALSNNF 396
Cdd:PLN02787 447 MRCFGQ-NPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALSNSF 525
|
410
....*....|.
gi 39983586 397 GFGGTNATLLF 407
Cdd:PLN02787 526 GFGGHNSSILF 536
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-410 |
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 39983586 1 MRRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKgFDPEQYIDKKEVKKMDLFIQYAMAAA 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 81 HYAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEG-GHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSV 159
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPrGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 160 SACATGTHSIGDAYHMIKRGDADAMIAGGTES---TVTPLgiggFAVMKALSTR-NDDPTAASRPFEKNRDGFVLAEGAG 235
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEEldwEMSCL----FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 236 IVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPApeGEGAARCMKMALnnAGVRpEEVDYINAHGTSTPFNDYYETL 315
Cdd:PRK07967 236 VVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVKELG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 316 AVKSVFGDyaKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPE-CDLDYVPNAAREKSITYALSN 394
Cdd:PRK07967 311 AIREVFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSN 388
|
410
....*....|....*.
gi 39983586 395 NFGFGGTNATLLFKKV 410
Cdd:PRK07967 389 SFGFGGTNATLVFRRY 404
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-409 |
3.71e-102 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 309.35 E-value: 3.71e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 4 VVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITR--FDASDLPVRIAGEVKGfDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDpfVEEFDLPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGlqITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:PRK07910 93 RVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKA-LSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLE 240
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 241 EYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSV 320
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 321 FGdyAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGG 400
Cdd:PRK07910 331 LG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408
|
....*....
gi 39983586 401 TNATLLFKK 409
Cdd:PRK07910 409 HNVALAFGR 417
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
94-409 |
1.75e-100 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 302.42 E-value: 1.75e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 94 ENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSACATGTHSIGDAY 173
Cdd:PRK14691 23 EKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 174 HMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTR-NDDPTAASRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAKI 252
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 253 YAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVFGDyAKKVMVSS 332
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITS 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39983586 333 TKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECD-LDYVPNAAREKSITYALSNNFGFGGTNATLLFKK 409
Cdd:PRK14691 262 TKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-408 |
8.25e-98 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 297.67 E-value: 8.25e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGvgnaANWD----ALVSGTSGIGHITRFD-ASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQY 75
Cdd:PRK09116 1 MRRVVVTGMGGVTALG----EDWQtiaaRLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 76 AMAAAHYAMEDSGL----QITeeNAERTGVLVGAGLGGLPTIEkyHAAMLEGGH-KKISP-FFIPMLIiNLAPGHISIKY 149
Cdd:PRK09116 77 ATRASELALEDAGLlgdpILT--DGRMGIAYGSSTGSTDPIGA--FGTMLLEGSmSGITAtTYVRMMP-HTTAVNVGLFF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 150 GAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTEStVTPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFV 229
Cdd:PRK09116 152 GLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 230 LAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPegEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFN 309
Cdd:PRK09116 231 IGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQA--ETMQIAMELALKDAGLAPEDIGYVNAHGTATDRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 310 DYYETLAVKSVFGDyakKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPEC-DLDYVPNAAREKSI 388
Cdd:PRK09116 309 DIAESQATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDT 385
|
410 420
....*....|....*....|
gi 39983586 389 TYALSNNFGFGGTNATLLFK 408
Cdd:PRK09116 386 EYVMSNNFAFGGINTSLIFK 405
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-405 |
9.29e-88 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 271.15 E-value: 9.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGvGNAANWDALVSGTSGIGHITRFdaSDLPVRiagevkgfdPEQYIDKKEVKKMDLfiqyAMAAA 80
Cdd:PRK05952 1 MMKVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPF--PELPPL---------PLGLIGNQPSSLEDL----TKTVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 81 HYAMEDSGL-----------------QITEENAERTGVLVGAGLGGLPTIEKYhaamLEgghkkispfFIPMLIINLAPG 143
Cdd:PRK05952 65 TAALKDAGLtppltdcgvvigssrgcQGQWEKLARQMYQGDDSPDEELDLENW----LD---------TLPHQAAIAAAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 144 HIsikyGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALStrnddPTAASrPFEK 223
Cdd:PRK05952 132 QI----GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KTGAY-PFDR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 224 NRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHG 303
Cdd:PRK05952 202 QREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 304 TSTPFNDYYETLAVKSVFGdyaKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEqdPECDLDYVPNaA 383
Cdd:PRK05952 282 TATRLNDQREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFVRQ-A 355
|
410 420
....*....|....*....|..
gi 39983586 384 REKSITYALSNNFGFGGTNATL 405
Cdd:PRK05952 356 QQSPLQNVLCLSFGFGGQNAAI 377
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-406 |
1.07e-83 |
|
"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: 261.60 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNA---ANWDALVSGTSGIGHITRFDaSDLPVRIAGEVKGFDPEQYiDKKEVKKMDLFIQYAMA 78
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDeveEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGW-DAKRTGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 79 AAHYAMEDSGLQI-TEENAERTGVLVGAGLGGlpTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKY-GAKGPNL 156
Cdd:cd00828 79 ATEEALADAGITDpYEVHPSEVGVVVGSGMGG--LRFLRRGGKLDARAVNPYVSPKWMLSPNTVAGWVNILLlSSHGPIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 157 SSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVtPLGIGGFAVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGI 236
Cdd:cd00828 157 TPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL-EEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 237 VVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPeGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLA 316
Cdd:cd00828 236 LVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 317 VKSVFGDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAR--EKSITYALSN 394
Cdd:cd00828 315 IAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAALVN 394
|
410
....*....|..
gi 39983586 395 NFGFGGTNATLL 406
Cdd:cd00828 395 AFGFGGSNAALV 406
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-406 |
1.75e-75 |
|
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: 239.95 E-value: 1.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVRIAGEVKGFDPEQYIDKKEVKKMDLFIQYAMAAAH 81
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 82 YAMEDSGLQITEENAERTGVLVGAGLGGLPTIEKYHAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSA 161
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATGTHSIGDAYHMIKRGdADAMIAGGTESTVTPLGIGGFAVMKALSTrNDDPTAASRPFEKNRDGFVLAEGAGIVVLEE 241
Cdd:cd00832 161 QAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILVLED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 242 YEAAKKRGAKIYAEIVGYGLTGDAyhltAPAP-EGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSV 320
Cdd:cd00832 239 AAAARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 321 FGDYAkkVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSITYALSNNFGFGG 400
Cdd:cd00832 315 FGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGG 392
|
....*.
gi 39983586 401 TNATLL 406
Cdd:cd00832 393 FNSALV 398
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
150-407 |
2.19e-72 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 232.04 E-value: 2.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 150 GAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTES-TVTPLGigGFAVMKALStrnDDPTaasRPFEKNRDGF 228
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSlCRLTLN--GFNSLESLS---PQPC---RPFSANRDGI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 229 VLAEGAGIVVLEeyeaakkRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPF 308
Cdd:PRK09185 220 NIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 309 NDYYETLAVKSVFGDYakkVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLDYVPNAAREKSI 388
Cdd:PRK09185 293 NDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAI 369
|
250
....*....|....*....
gi 39983586 389 TYALSNNFGFGGTNATLLF 407
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLIF 388
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-409 |
1.72e-69 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 224.91 E-value: 1.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 1 MRRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHITRFDASDLPVR--------IAGEVKGFDPEQYIDKKEVKKMDLF 72
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAgaglasafIGAELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 73 IQYAMAAAHYAMEDSGLQ----------ITEENAErtgvlvgaglgglptiEKYHAAMLE--GGHKK-ISPFFIPMLIIN 139
Cdd:PRK07103 81 AQAALAAAREAWRDAALGpvdpdriglvVGGSNLQ----------------QREQALVHEtyRDRPAfLRPSYGLSFMDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 140 LAPGHISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRN--DDPTAA 217
Cdd:PRK07103 145 DLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 218 SRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEgaARCMKMALNNAGVRPEEVD 297
Cdd:PRK07103 225 CRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDID 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 298 YINAHGTSTPFNDYYEtlaVKSVFGDYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQ-DPECdl 376
Cdd:PRK07103 303 YVNPHGTGSPLGDETE---LAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF-- 377
|
410 420 430
....*....|....*....|....*....|...
gi 39983586 377 DYVPNAAREKSITYALSNNFGFGGTNATLLFKK 409
Cdd:PRK07103 378 RWVGSTAESARIRYALSLSFGFGGINTALVLER 410
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
3-403 |
2.05e-59 |
|
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: 198.94 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 3 RVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHIT--RFDASDLP----------VRIAG---EVKGFDPEQY-IDKKEV 66
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYpdpgkpgktyTRRGGfldDVDAFDAAFFgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 67 KKMD----LFIQYAMAAAhyamEDSGLQITEENAERTGVLVGAGLGGlptiekyHAAMLEGGHKKISPFFIPMLIINLAP 142
Cdd:cd00833 82 EAMDpqqrLLLEVAWEAL----EDAGYSPESLAGSRTGVFVGASSSD-------YLELLARDPDEIDAYAATGTSRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 143 GHISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALStrnddPTAASRPFE 222
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 223 KNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAH 302
Cdd:cd00833 226 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAH 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 303 GTSTPFNDYYETLAVKSVFGDY---AKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQDPECDLD-- 377
Cdd:cd00833 306 GTGTPLGDPIEVEALAKVFGGSrsaDQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEes 385
|
410 420 430
....*....|....*....|....*....|..
gi 39983586 378 --YVPNAARE----KSITYALSNNFGFGGTNA 403
Cdd:cd00833 386 plRVPTEARPwpapAGPRRAGVSSFGFGGTNA 417
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
122-406 |
3.66e-57 |
|
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: 190.54 E-value: 3.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 122 EGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPlgiggF 201
Cdd:cd00825 56 ADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAP-----M 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 202 AVMKALSTRNDDPTAASRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARC 281
Cdd:cd00825 131 DCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 282 MKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVFGDyaKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVI 361
Cdd:cd00825 211 AKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFI 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 39983586 362 PPTINYQEQDPecDLDYVPNAAREKSITYALSNNFGFGGTNATLL 406
Cdd:cd00825 289 PPSIHIEELDE--AGLNIVTETTPRELRTALLNGFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-367 |
9.61e-52 |
|
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: 169.29 E-value: 9.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 253 YAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVFGDYAKK--VMV 330
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 39983586 331 SSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINY 367
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-245 |
2.62e-50 |
|
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: 170.12 E-value: 2.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 2 RRVVVTGVGAVSPLGVGNAANWDALVSGTSGIGHI--TRFDAS---DLPVRIAGEVKG----------FDPEQY-IDKKE 65
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDklyDPPSRIAGKIYTkwgglddifdFDPLFFgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 66 VKKMDLFIQYAMAAAHYAMEDSGLQITEENAERTGVLVGAGLGGLptiEKYHAAMLEGGHKKISPFFIPMlIINLAPGHI 145
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 146 SIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTrnDDPTAASRPFeknR 225
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF---A 231
|
250 260
....*....|....*....|
gi 39983586 226 DGFVLAEGAGIVVLEEYEAA 245
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
117-403 |
2.58e-42 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 159.27 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 117 HAAMLEGGHKKISPFFIPMLIINLAPGHISIKYGAKGPNLSSVSACATGTHSIgdayHM----IKRGDADAMIAGGTEST 192
Cdd:COG3321 129 YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAV----HLacqsLRSGECDLALAGGVNLM 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 193 VTPLGIGGFAVMKALStrnddPTAASRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGY---------GLTg 263
Cdd:COG3321 205 LTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSavnqdgrsnGLT- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 264 dayhltapAPEGEGAARCMKMALNNAGVRPEEVDYINAHGTSTPFNDYYETLAVKSVFGDYAKK---VMVSSTKSMTGHL 340
Cdd:COG3321 279 --------APNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHL 350
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39983586 341 LGAAG--GVeaVFTLMAMDKGVIPPTINYQEQDPECDLD----YVPNAARE----KSITYALSNNFGFGGTNA 403
Cdd:COG3321 351 EAAAGvaGL--IKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRPwpagGGPRRAGVSSFGFGGTNA 421
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
141-406 |
7.45e-35 |
|
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: 129.49 E-value: 7.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 141 APGHISIKYG-AKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTEStvtplgiggfavmkalstrnddptaasr 219
Cdd:cd00327 46 AAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 220 pfeknrdgFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGD-AYHLTAPApeGEGAARCMKMALNNAGVRPEEVDY 298
Cdd:cd00327 98 --------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVS--GEGLARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 299 INAHGTSTPFNDYYETLAVKSVFGDyaKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTinyqEQDPECdldy 378
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGV--RSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT----PREPRT---- 237
|
250 260
....*....|....*....|....*...
gi 39983586 379 vpnaareksityALSNNFGFGGTNATLL 406
Cdd:cd00327 238 ------------VLLLGFGLGGTNAAVV 253
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
134-402 |
4.53e-30 |
|
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: 123.19 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 134 PMLIINLAPGHISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDd 213
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 214 ptaaSRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGDAYHLTAPAPEGEGAARCMKMALNNAGVRP 293
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 294 EEVDYINAHGTSTPFNDYYETLAVKSVFG---DYAKKVMVSSTKSMTGHLLGAAGGVEAVFTLMAMDKGVIPPTINYQEQ 370
Cdd:TIGR02813 333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 39983586 371 DPECDLD----YV-----PNAAREKSITY-ALSNNFGFGGTN 402
Cdd:TIGR02813 413 NPKLDIEnspfYLntetrPWMQREDGTPRrAGISSFGFGGTN 454
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
172-403 |
4.75e-24 |
|
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: 100.87 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 172 AYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALStrnddPTAASRPFEKNRDGFVLAEGAGIVVLEEYEAAKKRGAK 251
Cdd:smart00825 107 ACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDP 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 252 IYAEIVGYGLT--GDAYHLTAPAPEGEgaarcmkmalnnagvrpeevdyinahgtstpfndyyetLAVKSVfgdyakkvm 329
Cdd:smart00825 182 ILAVIRGSAVNqdGRSNGITAPSGPAQ--------------------------------------LLIGSV--------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 330 vsstKSMTGHLLGAAGgVEAVF-TLMAMDKGVIPPTINYQEQDPECDLD----YVPNAARE----KSITYALSNNFGFGG 400
Cdd:smart00825 215 ----KSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPwpppGRPRRAGVSSFGFGG 289
|
...
gi 39983586 401 TNA 403
Cdd:smart00825 290 TNA 292
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
161-299 |
5.79e-06 |
|
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: 48.14 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 161 ACATGTHSIGDAYHMIKRGDADAMIAGGTES-TVTPLGIGGFAVMKALSTRNDDPTAA---------------------- 217
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESmSRAPMLLPKARWGYRMNAKLVDPMINpgltdpytglsmgetaenvaer 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 218 ---SR----------------------------PFE-KNRDGFVLAE--------------------------------- 232
Cdd:COG0183 167 ygiSReeqdafalrshqraaaaiaagrfddeivPVEvPDRKGEVVVDrdegprpdttleklaklkpafkkdgtvtagnas 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39983586 233 ----GAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGD--AYHLTAPAPegegAARcmkMALNNAGVRPEEVDYI 299
Cdd:COG0183 247 gindGAAALLLMSEEAAKELGLKPLARIVAYAVAGVdpEIMGIGPVP----ATR---KALARAGLTLDDIDLI 312
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
139-258 |
5.69e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 44.94 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 139 NLAPGHISIKYGAKGPNLSSVSACATGTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTRNDDPTAAS 218
Cdd:PRK06519 152 NLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGLLLKGGWAPVWSR 231
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 39983586 219 RPFEKnrDGFVLAEGAGIVVLEEYEAAKKRGAKIYAEIVG 258
Cdd:PRK06519 232 GGEDG--GGFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
165-299 |
6.57e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 44.63 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 165 GTHSIGDAYHMIKRGDADAMIAGGTESTVTPLGIGGFAVMKALSTrnddptaasrpfEKNRDGFVLAEGAGIVVLEEYEA 244
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT------------SQNSNGFIPGEAAAAVLLGRPAG 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 39983586 245 AKKRGAKIYAeiVGYGLTGDAYHLTAPAP-EGEGAARCMKMALNNAGVRPEEVDYI 299
Cdd:PRK06147 204 GEAPGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
161-192 |
1.92e-04 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 43.24 E-value: 1.92e-04
10 20 30
....*....|....*....|....*....|..
gi 39983586 161 ACATGTHSIGDAYHMIKRGDADAMIAGGTEST 192
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVESM 114
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
162-345 |
4.06e-04 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 42.39 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 162 CATgTHSIG----DAYHM--IKRGDAdAMIAGGTESTVTPLGIGG-----FAVM---KALSTRNDDPTAASRPFEKNRDG 227
Cdd:PLN02644 163 CAD-QYSISreeqDAYAIqsYERAIA-AQEAGAFAWEIVPVEVPGgrgrpSVIVdkdEGLGKFDPAKLRKLRPSFKEDGG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 228 FVLA-------EGAGIVVLEEYEAAKKRGAKIYAEIVGYgltGDAyhltAPAPE--GEGAARCMKMALNNAGVRPEEVdy 298
Cdd:PLN02644 241 SVTAgnassisDGAAALVLVSGEKALELGLQVIAKIRGY---ADA----AQAPElfTTAPALAIPKALKHAGLEASQV-- 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 39983586 299 inahgtstpfnDYYE--------TLAVKSVFGDYAKKVMVSSTKSMTGHLLGAAG 345
Cdd:PLN02644 312 -----------DYYEineafsvvALANQKLLGLDPEKVNVHGGAVSLGHPIGCSG 355
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
161-192 |
6.25e-04 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 41.83 E-value: 6.25e-04
10 20 30
....*....|....*....|....*....|..
gi 39983586 161 ACATGTHSIGDAYHMIKRGDADAMIAGGTEST 192
Cdd:TIGR01930 82 QCASGLQAVILAAQLIRAGEADVVVAGGVESM 113
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
219-299 |
2.02e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 40.14 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39983586 219 RP-FEKnrDGFVLA-------EGAGIVVLEEYEAAKKRGAKIYAEIVGYGLTGdayhlTAPAPEGEGAARCMKMALNNAG 290
Cdd:PRK05790 233 RPaFDK--DGTVTAgnasginDGAAAVVVMSEAKAKELGLTPLARIVSYAVAG-----VDPAIMGIGPVPAIRKALEKAG 305
|
....*....
gi 39983586 291 VRPEEVDYI 299
Cdd:PRK05790 306 WSLADLDLI 314
|
|
| |
