|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
3-413 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 756.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 3 KRRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGVAA 82
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDY-MSRKEARRMDRFIQYGIAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 83 GVQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVT 162
Cdd:PRK07314 80 AKQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 163 TACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVLVL 242
Cdd:PRK07314 160 TACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 243 EEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKK 322
Cdd:PRK07314 240 EELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 323 VFGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGFG 402
Cdd:PRK07314 320 VFGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFG 399
|
410
....*....|.
gi 743523938 403 GTNGSLIFKRV 413
Cdd:PRK07314 400 GTNASLVFKRY 410
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
4-411 |
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 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGVAAG 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDY-IDKKEARRMDRFIQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTT 163
Cdd:TIGR03150 80 KEAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 164 ACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVLVLE 243
Cdd:TIGR03150 160 ACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 244 EYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKKV 323
Cdd:TIGR03150 240 ELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 324 FGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGFGG 403
Cdd:TIGR03150 320 FGDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
....*...
gi 743523938 404 TNGSLIFK 411
Cdd:TIGR03150 400 TNASLVFK 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
4-413 |
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: 692.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGVAAG 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEY-LDRKELRRMDRFTQYALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTT 163
Cdd:COG0304 80 REALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 164 ACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVLVLE 243
Cdd:COG0304 160 ACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 244 EYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKKV 323
Cdd:COG0304 240 ELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 324 FGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGFGG 403
Cdd:COG0304 320 FGDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGG 399
|
410
....*....|
gi 743523938 404 TNGSLIFKRV 413
Cdd:COG0304 400 HNASLVFKRY 409
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
1-413 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 650.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 1 MSKRRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGV 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEY-MSKKDARKMDLFIQYGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 81 AAGVQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIA 160
Cdd:PRK08722 80 AAGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 161 VTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVL 240
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 241 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGM 320
Cdd:PRK08722 240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 321 KKVFGEHASA-LMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVA-KAGSFEYALSNS 398
Cdd:PRK08722 320 KRALGEAGSKqVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTArKVESMEYAICNS 399
|
410
....*....|....*
gi 743523938 399 FGFGGTNGSLIFKRV 413
Cdd:PRK08722 400 FGFGGTNGSLIFKKM 414
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
4-410 |
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: 638.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGVAAG 83
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDY-LDRKELRRMDRFAQFALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTT 163
Cdd:cd00834 80 EEALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 164 ACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVLVLE 243
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 244 EYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKKV 323
Cdd:cd00834 240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 324 FGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGFGG 403
Cdd:cd00834 320 FGEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGG 399
|
....*..
gi 743523938 404 TNGSLIF 410
Cdd:cd00834 400 HNASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-412 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 546.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 1 MSKRRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKD--------FDPEEFgINRKEARKM 72
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRY-LDPKDQRKM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 73 DLFIQYGVAAGVQALEDSGL-IINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIM 151
Cdd:PRK06333 80 DRFILFAMAAAKEALAQAGWdPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 152 KGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTR-NDEPQKASRPWDKDRDG 230
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 231 FVLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTP 310
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 311 LGDVAELRGMKKVFGeHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECD-LDLVPHVAKAG 389
Cdd:PRK06333 320 VGDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPM 398
|
410 420
....*....|....*....|...
gi 743523938 390 SFEYALSNSFGFGGTNGSLIFKR 412
Cdd:PRK06333 399 DMDYALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4-413 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 513.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGVAAG 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEV-MDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTT 163
Cdd:PRK08439 81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 164 ACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGVLVLE 243
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 244 EYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSdgDGGARAMKNAIKDAGIAPeqIGYINAHGTSTPLGDVAELRGMKKV 323
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 324 FGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGFGG 403
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396
|
410
....*....|
gi 743523938 404 TNGSLIFKRV 413
Cdd:PRK08439 397 TNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-413 |
7.96e-164 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 466.86 E-value: 7.96e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 13 MLSPVGNTAESSWQALLNGQSGISLIDHFDASE----------------FATRFAGLVK--DFDPEEFGINRKEARkmdl 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLpdcipeqkalenlvaaMPCQIAAEVDqsEFDPSDFAPTKRESR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 75 FIQYGVAAGVQALEDSGLIINEE-NAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKG 153
Cdd:PTZ00050 77 ATHFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 154 MQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTR-NDEPQKASRPWDKDRDGFV 232
Cdd:PTZ00050 157 LKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 233 LGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAG-IAPEQIGYINAHGTSTPL 311
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 312 GDVAELRGMKKVFGEH-ASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVP-HVAKA- 388
Cdd:PTZ00050 317 GDKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQgKTAHPl 396
|
410 420
....*....|....*....|....*
gi 743523938 389 GSFEYALSNSFGFGGTNGSLIFKRV 413
Cdd:PTZ00050 397 QSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4-413 |
8.62e-152 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 436.92 E-value: 8.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLI-------DHFDA-------SEFATRFAGLV------KDFDPEEFG 63
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqddlkmKSEDEetqlytlDQLPSRVAALVprgtgpGDFDEELWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 64 INRKEARkmdlFIQYGVAAGVQALEDSG-LIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIIN 142
Cdd:PLN02836 86 NSRSSSR----FIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 143 MVSGHLSIMKGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTR-NDEPQKAS 221
Cdd:PLN02836 162 MAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 222 RPWDKDRDGFVLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGY 301
Cdd:PLN02836 242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 302 INAHGTSTPLGDVAELRGMKKVFGEHAS--ALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDL 379
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDD 401
|
410 420 430
....*....|....*....|....*....|....*
gi 743523938 380 DLVPHVA-KAGSFEYALSNSFGFGGTNGSLIFKRV 413
Cdd:PLN02836 402 GFVPLTAsKAMLIRAALSNSFGFGGTNASLLFTSP 436
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-410 |
4.25e-130 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 385.10 E-value: 4.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 1 MSKRRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFgINRKEARKMDLFIQYGV 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGW-VAPKLSKRMDKFMLYLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 81 AAGVQALEDSGL---IINEENAERVGVAIGSGIGGLGLIEQNHSSLiNGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGP 157
Cdd:PLN02787 205 TAGKKALADGGItedVMKELDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 158 NIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGA 237
Cdd:PLN02787 284 NYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 238 GVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAEL 317
Cdd:PLN02787 364 GVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 318 RGMKKVFGEHaSALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAG-SFEYALS 396
Cdd:PLN02787 444 QALMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERlDIKVALS 522
|
410
....*....|....
gi 743523938 397 NSFGFGGTNGSLIF 410
Cdd:PLN02787 523 NSFGFGGHNSSILF 536
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4-411 |
4.54e-113 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 336.96 E-value: 4.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFD-ASEFATRFAGLVKDFD-PEEFgiNRKEARKMDLFIQYGVA 81
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFElPAHY--TRKKIRSMGRVSLMATR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 82 AGVQALEDSGLIINEENAE-RVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPffvpSTIINMVSgH-----LSIMKGMQ 155
Cdd:PRK09116 80 ASELALEDAGLLGDPILTDgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMP-HttavnVGLFFGLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 156 GPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKAStPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGD 235
Cdd:PRK09116 155 GRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 236 GAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPpsDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVA 315
Cdd:PRK09116 234 GAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 316 ELRGMKKVFGEHasaLMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDEC-DLDLVPHVAKAGSFEYA 394
Cdd:PRK09116 312 ESQATAAVFGAR---MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYV 388
|
410
....*....|....*..
gi 743523938 395 LSNSFGFGGTNGSLIFK 411
Cdd:PRK09116 389 MSNNFAFGGINTSLIFK 405
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-412 |
2.16e-111 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 333.24 E-value: 2.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 6 VVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEF--ATRFAG-LVKDFDPEefgINRKEARKMDLFIQYGVAA 82
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFdlPVRIGGhLLEEFDHQ---LTRVELRRMSYLQRMSTVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 83 GVQALEDSGliINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVT 162
Cdd:PRK07910 91 GRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 163 TACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKA-LSTRNDEPQKASRPWDKDRDGFVLGDGAGVLV 241
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 242 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMK 321
Cdd:PRK07910 249 IETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAIN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 322 KVFGEHASAlmVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGF 401
Cdd:PRK07910 329 NALGGHRPA--VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGF 406
|
410
....*....|.
gi 743523938 402 GGTNGSLIFKR 412
Cdd:PRK07910 407 GGHNVALAFGR 417
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
127-412 |
5.43e-110 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 327.07 E-value: 5.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 127 GPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAA 206
Cdd:PRK14691 53 GPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 207 AKALSTR-NDEPQKASRPWDKDRDGFVLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAM 285
Cdd:PRK14691 133 ARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 286 KNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKKVFGEhASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVP 365
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 743523938 366 PTINLDNPDDECD-LDLVPHVAKAGSFEYALSNSFGFGGTNGSLIFKR 412
Cdd:PRK14691 292 ATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-413 |
1.26e-107 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 323.16 E-value: 1.26e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKdFDPEEFgINRKEARKMDLFIQYGVAAG 83
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGL-IDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVG-VAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVT 162
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGlIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 163 TACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGgFAAAKALSTR-NDEPQKASRPWDKDRDGFVLGDGAGVLV 241
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 242 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPpsDGDGGARAMKNAIKDAGiapEQIGYINAHGTSTPLGDVAELRGMK 321
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELGAIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 322 KVFGEHASAlmVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDE-CDLDLVPHVAKAGSFEYALSNSFG 400
Cdd:PRK07967 314 EVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFG 391
|
410
....*....|...
gi 743523938 401 FGGTNGSLIFKRV 413
Cdd:PRK07967 392 FGGTNATLVFRRY 404
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
6-412 |
2.65e-104 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 315.03 E-value: 2.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 6 VVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEFGinrkearKMDLFIQYGVAAGVQ 85
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFG-------ASALSEALARLAAEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 86 ALEDSGLI--------------INEENAERVGVAIGSGIGGlgliEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIM 151
Cdd:PRK06501 86 ALAQAGIGkgdfpgplflaappVELEWPARFALAAAVGDND----APSYDRLLRAARGGRFDALHERFQFGSIADRLADR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 152 KGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGF 231
Cdd:PRK06501 162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 232 VLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPL 311
Cdd:PRK06501 242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 312 GDVAELRGMKKVFGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSF 391
Cdd:PRK06501 322 NDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARV 401
|
410 420
....*....|....*....|.
gi 743523938 392 EYALSNSFGFGGTNGSLIFKR 412
Cdd:PRK06501 402 TAVLSNSFGFGGQNASLVLTA 422
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-408 |
5.74e-86 |
|
"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: 267.38 E-value: 5.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTA---ESSWQALLNGQSGISLIDHFDaSEFATRFAGLVKDFDPEEFGINRkeARKMDLFIQYGV 80
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCdevEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGWDAKR--TGIVDRTTLLAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 81 AAGVQALEDSGLIINEE-NAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPStiINMVSGHLSIM-KGMQGPN 158
Cdd:cd00828 78 VATEEALADAGITDPYEvHPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLS--PNTVAGWVNILlLSSHGPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 159 IAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEkASTPMGMGGFAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAG 238
Cdd:cd00828 156 KTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 239 VLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPpSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELR 318
Cdd:cd00828 235 VLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 319 GMKKVFGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKA--GSFEYALS 396
Cdd:cd00828 314 AIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDlnLKVRAALV 393
|
410
....*....|..
gi 743523938 397 NSFGFGGTNGSL 408
Cdd:cd00828 394 NAFGFGGSNAAL 405
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
5-409 |
4.71e-82 |
|
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: 257.87 E-value: 4.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 5 RVVVTGLGMLSPVGNTAESSWQALLNGQSGISLI--DHFDASEF----------ATRFAGLVKD---FDPEEFGINRKEA 69
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpeDRWDADGYypdpgkpgktYTRRGGFLDDvdaFDAAFFGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 70 RKMD----LFIQygVAAgvQALEDSGLIINEENAERVGVaigsgigGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVS 145
Cdd:cd00833 82 EAMDpqqrLLLE--VAW--EALEDAGYSPESLAGSRTGV-------FVGASSSDYLELLARDPDEIDAYAATGTSRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 146 GHLSIMKGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALStrndePQKASRPWD 225
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 226 KDRDGFVLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAY--HMTAPpsDGDGGARAMKNAIKDAGIAPEQIGYIN 303
Cdd:cd00833 226 ADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDIDYVE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 304 AHGTSTPLGDVAELRGMKKVFGEHASA---LMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLD 380
Cdd:cd00833 304 AHGTGTPLGDPIEVEALAKVFGGSRSAdqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFE 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 743523938 381 ----LVPHVAK----AGSFEYALSNSFGFGGTNGSLI 409
Cdd:cd00833 384 esplRVPTEARpwpaPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-412 |
6.49e-81 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 254.57 E-value: 6.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 5 RVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASE-------FATRFAG--LVKDFDPEefGINRKEARKMDLF 75
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVpddagagLASAFIGaeLDSLALPE--RLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 76 IQYGVAAGVQALEDSGLiiNEENAERVGVAIGSGIGGLGLIEQNHSSLINGgPRKLSPFFVPSTIINMVSGHLSIMKGMQ 155
Cdd:PRK07103 81 AQAALAAAREAWRDAAL--GPVDPDRIGLVVGGSNLQQREQALVHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQFGIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 156 GPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRN--DEPQKASRPWDKDRDGFVL 233
Cdd:PRK07103 158 GEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGFIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 234 GDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPpsDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGD 313
Cdd:PRK07103 238 GEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 314 VAELRGMkkvFGEHASALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDEcDLDLVPHVAKAGSFEY 393
Cdd:PRK07103 316 ETELAAL---FASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDE-RFRWVGSTAESARIRY 391
|
410
....*....|....*....
gi 743523938 394 ALSNSFGFGGTNGSLIFKR 412
Cdd:PRK07103 392 ALSLSFGFGGINTALVLER 410
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
5-408 |
3.38e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 249.20 E-value: 3.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 5 RVVVTGLGMLSPVGNtAESSWQALLNGQSGISLIDHFdaSEFATRFAGLVKDfDPEEFGINRKEARKmdlfiqygvaagv 84
Cdd:PRK05952 3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPF--PELPPLPLGLIGN-QPSSLEDLTKTVVT------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 85 QALEDSGLIINEENAervGVAIGSGIGGLGLIE----QNHSSLINGGPRKLSPFFVpSTIINMVSGHLSIMKGMQGPNIA 160
Cdd:PRK05952 66 AALKDAGLTPPLTDC---GVVIGSSRGCQGQWEklarQMYQGDDSPDEELDLENWL-DTLPHQAAIAAARQIGTQGPVLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 161 VTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALStrndepQKASRPWDKDRDGFVLGDGAGVL 240
Cdd:PRK05952 142 PMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA------KTGAYPFDRQREGLVLGEGGAIL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 241 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGM 320
Cdd:PRK05952 216 VLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 321 KKVFGehaSALMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPddECDLDLVPHvAKAGSFEYALSNSFG 400
Cdd:PRK05952 296 QALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP--EFDLNFVRQ-AQQSPLQNVLCLSFG 369
|
....*...
gi 743523938 401 FGGTNGSL 408
Cdd:PRK05952 370 FGGQNAAI 377
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
153-412 |
2.47e-73 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 234.35 E-value: 2.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 153 GMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTpMGMGGFAAAKALSTRndepqkASRPWDKDRDGFV 232
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCR-LTLNGFNSLESLSPQ------PCRPFSANRDGIN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 233 LGDGAGVLVLEeyehakaRGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLG 312
Cdd:PRK09185 221 IGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 313 DVAELRGMKKVFGEHasaLMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFE 392
Cdd:PRK09185 294 DAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIR 370
|
250 260
....*....|....*....|
gi 743523938 393 YALSNSFGFGGTNGSLIFKR 412
Cdd:PRK09185 371 YVLSNSFAFGGNNCSLIFGR 390
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4-409 |
3.80e-71 |
|
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: 229.17 E-value: 3.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLIDHFDASEFATRFAGLVKDFDPEEfGINRKEARKMDLFIQYGVAAG 83
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAE-HLPGRLLPQTDRMTRLALAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 84 VQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQGPNIAVTT 163
Cdd:cd00832 80 DWALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 164 ACTTGTHAIGMAGRMIAYGdADVMVAGGAEKASTPMGMGGFAAAKALSTrNDEPQKASRPWDKDRDGFVLGDGAGVLVLE 243
Cdd:cd00832 160 EQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILVLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 244 EYEHAKARGAKIYAELVGFGMSgdayhMTAPPSDG--DGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMK 321
Cdd:cd00832 238 DAAAARERGARVYGEIAGYAAT-----FDPPPGSGrpPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 322 KVFGEHAsaLMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLDLVPHVAKAGSFEYALSNSFGF 401
Cdd:cd00832 313 AVFGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGR 390
|
....*...
gi 743523938 402 GGTNGSLI 409
Cdd:cd00832 391 GGFNSALV 398
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-248 |
1.52e-68 |
|
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: 217.50 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 4 RRVVVTGLGMLSPVGNTAESSWQALLNGQSGISLI--DHFDASEF---ATRFAGLVK----------DFDPEEFGINRKE 68
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 69 ARKMDLFIQYGVAAGVQALEDSGLIINEENAERVGVAIGSGIGGLGLIEqnhSSLINGGPRKLSPFFVPsTIINMVSGHL 148
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALL---LLDEDGGPRRGSPFAVG-TMPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 149 SIMKGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTrnDEPQKASRPWDkdr 228
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
|
250 260
....*....|....*....|
gi 743523938 229 DGFVLGDGAGVLVLEEYEHA 248
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
19-405 |
3.45e-64 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 223.21 E-value: 3.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 19 NTAESSWQALLNGQSGISLI--DHFDASEFA-----------TRFAGLVKD---FDPEEFGINRKEARKMD----LFIQy 78
Cdd:COG3321 19 DDPEEFWRNLRAGRDAITEVpaDRWDADAYYdpdpdapgktyVRWGGFLDDvdeFDALFFGISPREAEAMDpqqrLLLE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 79 gVAAgvQALEDSGLIINEENAERVGV---AIGsgigglglieQNHSSLINGGPRKLSPFFVPSTIINMVSGHLSIMKGMQ 155
Cdd:COG3321 98 -VAW--EALEDAGYDPESLAGSRTGVfvgASS----------NDYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 156 GPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALStrndePQKASRPWDKDRDGFVLGD 235
Cdd:COG3321 165 GPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 236 GAGVLVLEEYEHAKARGAKIYAELVGFGMS--GDAYHMTAPpsDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGD 313
Cdd:COG3321 240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRSNGLTAP--NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 314 VAELRGMKKVFGEHASA---LMVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDECDLD---------L 381
Cdd:COG3321 318 PIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFEnspfyvnteL 397
|
410 420
....*....|....*....|....
gi 743523938 382 VPHVAKAGSFeYALSNSFGFGGTN 405
Cdd:COG3321 398 RPWPAGGGPR-RAGVSSFGFGGTN 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
78-409 |
4.82e-58 |
|
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: 192.85 E-value: 4.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 78 YGVAAGVQALEDSGLIINEENAERVGVAIGSGIGGLGLIEQNHSSLINGGPRKLSPFFVPStiinmVSGHLSIMKGMQGP 157
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 158 NIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMgmggfAAAKALSTRNDEPQKASRPWDKDRDGFVLGDGA 237
Cdd:cd00825 89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPM-----DCEFDAMGALSTPEKASRTFDAAADGFVFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 238 GVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAEL 317
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 318 RGMKKVFGEHASAlmVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNPDDecDLDLVPHVAKAGSFEYALSN 397
Cdd:cd00825 244 KLLRSEFGDKSPA--VSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALLN 319
|
330
....*....|..
gi 743523938 398 SFGFGGTNGSLI 409
Cdd:cd00825 320 GFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
256-371 |
2.90e-50 |
|
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: 165.43 E-value: 2.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 256 YAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPLGDVAELRGMKKVFGEHA--SALMV 333
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 743523938 334 SSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLD 371
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
137-411 |
8.46e-41 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 155.16 E-value: 8.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 137 PSTIINMVSGHLSIMKGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALSTRNDe 216
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 217 pqkaSRPWDKDRDGFVLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSDGDGGARAMKNAIKDAGIAP 296
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 297 EQIGYINAHGTSTPLGDVAELRGMKKVFGEHASALM---VSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTINLDNP 373
Cdd:TIGR02813 333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQhiaLGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 743523938 374 DDECDLDLVPHVAKA----------GSFEYALSNSFGFGGTNGSLIFK 411
Cdd:TIGR02813 413 NPKLDIENSPFYLNTetrpwmqredGTPRRAGISSFGFGGTNFHMVLE 460
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
152-409 |
2.56e-34 |
|
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: 127.95 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 152 KGMQGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKastpmgmggfaaakalstrndepqkasrpwdkdrdgF 231
Cdd:cd00327 55 GISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 232 VLGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTAPPSdGDGGARAMKNAIKDAGIAPEQIGYINAHGTSTPL 311
Cdd:cd00327 99 VFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVS-GEGLARAARKALEGAGLTPSDIDYVEAHGTGTPI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 312 GDVAELRGMKKVFGEHASAlmVSSTKSMTGHLLGAAGAIEAIITVLSLRDQMVPPTinldnpDDECDLdlvphvakagsf 391
Cdd:cd00327 178 GDAVELALGLDPDGVRSPA--VSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------PREPRT------------ 237
|
250
....*....|....*...
gi 743523938 392 eyALSNSFGFGGTNGSLI 409
Cdd:cd00327 238 --VLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
6-409 |
2.69e-29 |
|
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: 115.50 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 6 VVVTGLGMLSPVGNTAESSWQALLNGQSGISlidhfdasefatrfaglvkDFDPEEFGINRKEARKMD----LFIQygVA 81
Cdd:smart00825 1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD-------------------LFDAAFFGISPREAEAMDpqqrLLLE--VA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 82 agVQALEDSGLIINEENAERVGVaigsgigglglieqnhsslinggprklspfFVPSTiinmvsghlsimkgMQGPNIAV 161
Cdd:smart00825 60 --WEALEDAGIDPESLRGSRTGV------------------------------FVGVS--------------SSDYSVTV 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 162 TTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKALStrndePQKASRPWDKDRDGFVLGDGAGVLV 241
Cdd:smart00825 94 DTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVV 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 242 LEEYEHAKARGAKIYAELVGfgmsgdayhmTAPPSDGdggaramknaiKDAGI-APeqigyiNAhgtstplgdvaelrgm 320
Cdd:smart00825 169 LKRLSDALRDGDPILAVIRG----------SAVNQDG-----------RSNGItAP------SG---------------- 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 321 kkvfgehASALMVSSTKSMTGHLLGAAGaIEAII-TVLSLRDQMVPPTINLDNPDDECDLD---------LVPHVAkAGS 390
Cdd:smart00825 206 -------PAQLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplrvpteLTPWPP-PGR 276
|
410
....*....|....*....
gi 743523938 391 FEYALSNSFGFGGTNGSLI 409
Cdd:smart00825 277 PRRAGVSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-347 |
4.43e-12 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 67.29 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 1 MSKRRVVVTGLGMLSPVGNTAESSWQALlNGQSGISLIDhfdasefATRFA-----GLVK-DFDPEefgINRK-EARKMD 73
Cdd:PRK06519 3 MQPNDVVITGIGLVSSLGEGLDAHWNAL-SAGRPQPNVD-------TETFApypvhPLPEiDWSQQ---IPKRgDQRQME 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 74 LFIQYGV-AAGVqALEDSGLIINEE------------NAERvGVAIGSGIGGLGLIEQNHSSLINggpRKLSPFFVPSTI 140
Cdd:PRK06519 72 TWQRLGTyAAGL-ALDDAGIKGNEEllstmdmivaagGGER-DIAVDTAILNEARKRNDRGVLLN---ERLMTELRPTLF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 141 I----NMVSGHLSIMKGmqgpniaVTTACTT-------GTHAIGMAGRMIAYGDADVMVAGGAEKASTPMGMGGFAAAKA 209
Cdd:PRK06519 147 LaqlsNLLAGNISIVHK-------VTGSSRTfmgeesaGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 210 LSTRNDEPQKASRPWDKDrdGFVLGDGAGVLVLEEYEHAKARGAKIYAELVgfGMSGDayhmTAPPSDGDGGARaMKNAI 289
Cdd:PRK06519 220 LLKGGWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARIS--GVESD----RARRAPGDLEAS-LERLL 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 743523938 290 KDAGIAPEQIGYINahGTStplgDVAELRGMKKVFGEHASALMVSSTKSMTGHLLGAA 347
Cdd:PRK06519 291 KPAGGLAAPTAVIS--GAT----GAHPATAEEKAALEAALAGPVRGIGTLFGHTMEAQ 342
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
168-332 |
3.04e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 51.94 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 168 GTHAIGMAGRMIAYGDAD-VMVAGGAEKASTPMGMGGFAAAKALSTRNDEpqkasrpwdkdrdGFVLGDGAGVLVLEEYE 246
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPrVLVAGVDSLLTGPTLAHYEARDRLLTSQNSN-------------GFIPGEAAAAVLLGRPA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 247 HAKARGAKIYAelVGFGM-SGDAYHMTAPPSDGDGGARAMKNAIKDAGIAPEQIGYInahgtstplgdVAELRGMKKVFG 325
Cdd:PRK06147 203 GGEAPGLPLLG--LGLGRePAPVGESEDLPLRGDGLTQAIRAALAEAGCGLEDMDYR-----------IADLNGEQYRFK 269
|
....*..
gi 743523938 326 EHASALM 332
Cdd:PRK06147 270 EAALAEM 276
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
155-302 |
2.53e-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: 49.29 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 155 QGPNIA-----------------VTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKAST-PMGMGGFAAAKALSTRNDE 216
Cdd:COG0183 61 QGQNPArqaallaglpesvpavtVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLPKARWGYRMNAKLVD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 217 P-----------------------------------------QKASRPWDK----------------------------- 226
Cdd:COG0183 141 PminpgltdpytglsmgetaenvaerygisreeqdafalrshQRAAAAIAAgrfddeivpvevpdrkgevvvdrdegprp 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 227 --------------DRDGFV-------LGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGdayhmtAPPSD-GDGGARA 284
Cdd:COG0183 221 dttleklaklkpafKKDGTVtagnasgINDGAAALLLMSEEAAKELGLKPLARIVAYAVAG------VDPEImGIGPVPA 294
|
250
....*....|....*...
gi 743523938 285 MKNAIKDAGIAPEQIGYI 302
Cdd:COG0183 295 TRKALARAGLTLDDIDLI 312
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
157-233 |
3.32e-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: 42.47 E-value: 3.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743523938 157 PNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKAS-TPMGMGGfaaaKALSTRNDEPQKASRPWDKDRDGFVL 233
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSrAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTG 149
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
186-361 |
1.52e-03 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 40.46 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 186 VMVAGGAEKASTPM----GMGGFAAAKAlstrndepqKASRPWDKDRDGFV-------LGDGAGVLVLEEYEHAKARGAK 254
Cdd:PLN02644 201 VEVPGGRGRPSVIVdkdeGLGKFDPAKL---------RKLRPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 255 IYAELVGFGMSGDA--YHMTAPpsdgdggARAMKNAIKDAGIAPEQIGY--INAHGTSTPLGDvaelrgmKKVFGEHASA 330
Cdd:PLN02644 272 VIAKIRGYADAAQApeLFTTAP-------ALAIPKALKHAGLEASQVDYyeINEAFSVVALAN-------QKLLGLDPEK 337
|
170 180 190
....*....|....*....|....*....|...
gi 743523938 331 LMVSSTKSMTGHLLGAAGA--IEAIITVLSLRD 361
Cdd:PLN02644 338 VNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKN 370
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
157-202 |
1.87e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 39.59 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 743523938 157 PNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKAS-TPMGMG 202
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMShAPYALP 123
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
75-305 |
2.08e-03 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 39.94 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 75 FIQYGVAAGVQALEDSGLIINEENAERVGVAIGSGIGGlglieqnhsslinggprklspffVPSTIINMVSGhlsiMKGm 154
Cdd:cd00829 16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQS-----------------------FPGALIAEYLG----LLG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 155 qGPNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKAS--------------------------TPMGMGGFAA-- 206
Cdd:cd00829 68 -KPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSdvptgdeaggrasdlewegpeppgglTPPALYALAArr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 207 ------------------AKALSTRNDEPQ----------KASRP-WD--KDRDGFVLGDGAGVLVL--EEYehAKARGA 253
Cdd:cd00829 147 ymhrygttredlakvavkNHRNAARNPYAQfrkpitvedvLNSRMiADplRLLDCCPVSDGAAAVVLasEER--ARELTD 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 743523938 254 KiYAELVGFGMSGDAYHMTAPPSDG--DGGARAMKNAIKDAGIAPEQIGYINAH 305
Cdd:cd00829 225 R-PVWILGVGAASDTPSLSERDDFLslDAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
163-305 |
2.30e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 39.85 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 163 TACTTGTHAIGMAGRMIAYGDA-DVMVAGgaekastpmgmggfaaAKALSTRNDepqkasrpWDkDRDGFVL-GDGAGVL 240
Cdd:PRK12879 112 AACAGFLYGLETANGLITSGLYkKVLVIG----------------AERLSKVTD--------YT-DRTTCILfGDGAGAV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 241 VLEEYEHAkarGAKIYAELVGFGMSGDAYHMTAPPSDGDGGA-----------------------RAMKNAIKDAGIAPE 297
Cdd:PRK12879 167 VLEATENE---PGFIDYVLGTDGDGGDILYRTGLGTTMDRDAlsgdgyivqngrevfkwavrtmpKGARQVLEKAGLTKD 243
|
....*...
gi 743523938 298 QIGYINAH 305
Cdd:PRK12879 244 DIDWVIPH 251
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
136-302 |
2.85e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 39.75 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 136 VPSTIINMVsghlsimkgmqgpniavttaCTTGTHAIGMAGRMIAYGDADVMVAGGAEKAS------------TPMG--- 200
Cdd:PRK05790 79 VPALTINKV--------------------CGSGLKAVALAAQAIRAGDADIVVAGGQESMSqaphvlpgsrwgQKMGdve 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 201 ------------------MG------------------GFAAA---KALSTRN-----DE------PQKASRP--WDKD- 227
Cdd:PRK05790 139 lvdtmihdgltdafngyhMGitaenlaeqygitreeqdEFALAsqqKAEAAIKagrfkDEivpvtiKQRKGDPvvVDTDe 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 228 -------------------RDGFV-------LGDGAGVLVLEEYEHAKARGAKIYAELVGFGMSGdayhmTAPPSDGDGG 281
Cdd:PRK05790 219 hprpdttaeslaklrpafdKDGTVtagnasgINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAG-----VDPAIMGIGP 293
|
250 260
....*....|....*....|.
gi 743523938 282 ARAMKNAIKDAGIAPEQIGYI 302
Cdd:PRK05790 294 VPAIRKALEKAGWSLADLDLI 314
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
146-273 |
3.41e-03 |
|
nondecarboxylating condensing enzymes; In general, thiolases 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. 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: 238422 [Multi-domain] Cd Length: 393 Bit Score: 39.40 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523938 146 GHLSIMK--GMQG-PNIAVTTACTTGTHAIGMAGRMIAYGDADVMVAGGAEKASTpmgmggfaaakalSTRNDEPQKASR 222
Cdd:cd00826 63 AQQAAMHagGLQEaPAIGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMET-------------SAENNAKEKHID 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 743523938 223 PWDKDRDGFVLGDGAGVLVLEEYEHAKARGAKIyAELVGFGMSGDAYHMTA 273
Cdd:cd00826 130 VLINKYGMRACPDAFALAGQAGAEAAEKDGRFK-DEFAKFGVKGRKGDIHS 179
|
|
| |
