|
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: 756.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 3 KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 83 VQAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIAT 162
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 163 ACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 243 EYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSV 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 323 FGDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQvSGMEYALCNSFGFG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARE-RKIDYALSNSFGFG 399
|
410
....*....|.
gi 695765313 403 GTNGSLIFKKI 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: 705.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 164 CTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 324 GDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSgMEYALCNSFGFGG 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
|
....*...
gi 695765313 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: 666.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 164 CTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 324 GDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSgMEYALCNSFGFGG 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
|
410
....*....|
gi 695765313 404 TNGSLIFKKI 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: 653.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIV 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 81 AGVQAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISI 160
Cdd:PRK08722 81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 161 ATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 241 LEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 321 SVFGDAASR-VMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSGMEYALCNSF 399
Cdd:PRK08722 321 RALGEAGSKqVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSF 400
|
410
....*....|....
gi 695765313 400 GFGGTNGSLIFKKI 413
Cdd:PRK08722 401 GFGGTNGSLIFKKM 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: 621.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 164 CTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 324 GDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSgMEYALCNSFGFGG 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNSFGFGG 399
|
....*..
gi 695765313 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: 530.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKD--------FNCDDIISRKEQRKMD 72
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 73 AFIQYGIVAGVQAMQDSGL-EVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMF 151
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWdPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 152 GLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKDRDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 231 VLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPA 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 311 GDKAEAQAVKSVFGDAASrVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCD-LDFVPHEARQVS 389
Cdd:PRK06333 321 GDLGEVAAIKKVFGHVSG-LAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|...
gi 695765313 390 gMEYALCNSFGFGGTNGSLIFKK 412
Cdd:PRK06333 400 -MDYALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4-413 |
8.93e-174 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 491.56 E-value: 8.93e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 164 CTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMVVLEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSP-PEngaGAALAMVNAIRDAGIEPgqIAYVNAHGTSTPAGDKAEAQAVKSV 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPaPE---GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 323 FGDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSgMEYALCNSFGFG 402
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAE-LNVVMSNSFGFG 395
|
410
....*....|.
gi 695765313 403 GTNGSLIFKKI 413
Cdd:PRK08439 396 GTNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-413 |
6.53e-153 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 439.13 E-value: 6.53e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 13 MLSPVGNTVESTWKALLAGQSGISLIDHFDT----------------SAYATKFAGLVK--DFNCDDIISRKeqrKMDAF 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqsEFDPSDFAPTK---RESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 75 IQYGIVAGVQAMQDSGLEVTEE-NATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGL 153
Cdd:PTZ00050 78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 154 RGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKDRDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 233 GDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAG-IEPGQIAYVNAHGTSTPAG 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 312 DKAEAQAVKSVFGD-AASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQ-VS 389
Cdd:PTZ00050 318 DKIELKAIKKVFGDsGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHpLQ 397
|
410 420
....*....|....*....|....
gi 695765313 390 GMEYALCNSFGFGGTNGSLIFKKI 413
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4-410 |
1.01e-147 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 426.52 E-value: 1.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI-------DHFDTSAYA-------TKFAGLVKDFNCDDIISRK--- 66
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqddlkmKSEDEETQLytldqlpSRVAALVPRGTGPGDFDEElwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 67 EQRKMDAFIQYGIVAGVQAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGP-RKISPFFVPSTIVNMVAG 145
Cdd:PLN02836 86 NSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRlRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 146 HLTIMFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWD 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 225 KDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAH 304
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 305 GTSTPAGDKAEAQAVKSVFGD--AASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVP 382
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEhaTSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420
....*....|....*....|....*...
gi 695765313 383 HEARQVSGMEYALCNSFGFGGTNGSLIF 410
Cdd:PLN02836 406 LTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-410 |
2.16e-125 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 373.16 E-value: 2.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIV 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 81 AGVQAMQDSGL--EVTEE-NATRIGAAIGSGIGGLGLIEENHSSLtNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPS 157
Cdd:PLN02787 206 AGKKALADGGIteDVMKElDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPN 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 158 ISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAG 237
Cdd:PLN02787 285 YSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 238 MVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQ 317
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 318 AVKSVFGdAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQVSGMEYALCN 397
Cdd:PLN02787 445 ALMRCFG-QNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVALSN 523
|
410
....*....|...
gi 695765313 398 SFGFGGTNGSLIF 410
Cdd:PLN02787 524 SFGFGGHNSSILF 536
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4-411 |
3.80e-111 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 331.95 E-value: 3.80e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDT-SAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRyDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 83 VQAMQDSGLeVTEENAT--RIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPffvpSTIVNMV----AGHLTIMFGLRGP 156
Cdd:PRK09116 82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMphttAVNVGLFFGLKGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 157 SISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAStPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGA 236
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 237 GMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEA 316
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 317 QAVKSVFGDaasRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGC-DLDFVPHEARQVSgMEYAL 395
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREID-TEYVM 389
|
410
....*....|....*.
gi 695765313 396 CNSFGFGGTNGSLIFK 411
Cdd:PRK09116 390 SNNFAFGGINTSLIFK 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-412 |
1.61e-106 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 320.08 E-value: 1.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKdFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSL-TNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIAT 162
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMrGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 163 ACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGgFGAARALSTR-NDNPQAASRPWDKDRDGFVLGDGAGMVVL 241
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 242 EEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMVNAIrdAGIEpGQIAYVNAHGTSTPAGDKAEAQAVKS 321
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 322 VFGDAASrvMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDE-GCDLDFVpHEARQVSGMEYALCNSFG 400
Cdd:PRK07967 315 VFGDKSP--AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPqAAGMPIV-TETTDNAELTTVMSNSFG 391
|
410
....*....|..
gi 695765313 401 FGGTNGSLIFKK 412
Cdd:PRK07967 392 FGGTNATLVFRR 403
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-412 |
4.65e-106 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 319.37 E-value: 4.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 6 VVVTGLGMLSPVGNTVESTWKALLAGQSGI-----SLIDHFDTSayaTKFAG-LVKDFncDDIISRKEQRKMDAFIQYGI 79
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFDLP---VRIGGhLLEEF--DHQLTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 80 VAGVQAMQDSGleVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSIS 159
Cdd:PRK07910 89 VLGRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 160 IATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARA-LSTRNDNPQAASRPWDKDRDGFVLGDGAGM 238
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 239 VVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQA 318
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 319 VKSVFGdaASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQvSGMEYALCNS 398
Cdd:PRK07910 327 INNALG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP-GNYRYAINNS 403
|
410
....*....|....
gi 695765313 399 FGFGGTNGSLIFKK 412
Cdd:PRK07910 404 FGFGGHNVALAFGR 417
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
126-412 |
7.22e-101 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 303.57 E-value: 7.22e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 126 GPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGA 205
Cdd:PRK14691 53 GPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 206 ARALSTR-NDNPQAASRPWDKDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAM 284
Cdd:PRK14691 133 ARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 285 VNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVFGDAASrVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVP 364
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNA-LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 695765313 365 PTINLDNPDEGCD-LDFVPHEArQVSGMEYALCNSFGFGGTNGSLIFKK 412
Cdd:PRK14691 292 ATLNLENPDPAAKgLNIIAGNA-QPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
6-410 |
2.73e-98 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 299.62 E-value: 2.73e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 6 VVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVkDFNCDDIISRKEQRKMDAFIqygivAGVQA 85
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DFLPESPFGASALSEALARL-----AAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 86 MQDSGLEVT---------------EENATRIGAAIGSGIGGLGLieenHSSLTNGGPRKISPFFvPSTIVNMVAGHLTIM 150
Cdd:PRK06501 87 LAQAGIGKGdfpgplflaappvelEWPARFALAAAVGDNDAPSY----DRLLRAARGGRFDALH-ERFQFGSIADRLADR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 151 FGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGF 230
Cdd:PRK06501 162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 231 VLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPA 310
Cdd:PRK06501 242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 311 GDKAEAQAVKSVFGDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEAR--QV 388
Cdd:PRK06501 322 NDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARdaRV 401
|
410 420
....*....|....*....|..
gi 695765313 389 SGMeyaLCNSFGFGGTNGSLIF 410
Cdd:PRK06501 402 TAV---LSNSFGFGGQNASLVL 420
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-408 |
3.57e-78 |
|
"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: 247.35 E-value: 3.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGN---TVESTWKALLAGQSGISLIDHFdTSAYATKFAGLVKDFNCDDIISRKEqRKMDAFIQYGIV 80
Cdd:cd00828 1 SRVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 81 AGVQAMQDSGLEVTEEnatrigaaigsgigglGLIEENHSSLTNGG-------------PRKISPFFVPSTIV--NMVAG 145
Cdd:cd00828 79 ATEEALADAGITDPYE----------------VHPSEVGVVVGSGMgglrflrrggkldARAVNPYVSPKWMLspNTVAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 146 HLTIMFGL-RGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEkASTPLGVGGFGAARALSTRNDNPQAASRPWD 224
Cdd:cd00828 143 WVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 225 KDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPeNGAGAALAMVNAIRDAGIEPGQIAYVNAH 304
Cdd:cd00828 222 ETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 305 GTSTPAGDKAEAQAVKSVFGDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHE 384
Cdd:cd00828 301 GTSTPANDVAESRAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGL 380
|
410 420
....*....|....*....|....*
gi 695765313 385 ARQVSG-MEYALCNSFGFGGTNGSL 408
Cdd:cd00828 381 SRDLNLkVRAALVNAFGFGGSNAAL 405
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
5-408 |
3.53e-76 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 241.49 E-value: 3.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 5 RVVVTGLGMLSPVGNtVESTWKALLAGQSGISLIDHF-DTSAYATkfaGLVKDfncddiisrkEQRKMDAFIQygiVAGV 83
Cdd:PRK05952 3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPFpELPPLPL---GLIGN----------QPSSLEDLTK---TVVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENA--------------TRIGAAIGSGIGGLGLIEENHSSLTnggprkispfFVPSTIVNMVAGHLti 149
Cdd:PRK05952 66 AALKDAGLTPPLTDCgvvigssrgcqgqwEKLARQMYQGDDSPDEELDLENWLD----------TLPHQAAIAAARQI-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 150 mfGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnpQAASRPWDKDRDG 229
Cdd:PRK05952 134 --GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA------KTGAYPFDRQREG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 230 FVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTP 309
Cdd:PRK05952 206 LVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 310 AGDKAEAQAVKSVFGdaaSRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDegCDLDFVpHEARQvS 389
Cdd:PRK05952 286 LNDQREANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFV-RQAQQ-S 358
|
410
....*....|....*....
gi 695765313 390 GMEYALCNSFGFGGTNGSL 408
Cdd:PRK05952 359 PLQNVLCLSFGFGGQNAAI 377
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
151-410 |
1.67e-75 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 240.13 E-value: 1.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 151 FGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAS-TPLGvgGFGAARALSTRndnpqaASRPWDKDRDG 229
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCrLTLN--GFNSLESLSPQ------PCRPFSANRDG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 230 FVLGDGAGMVVLEeyehakkRGAKIYAEIVGFGMSSDAYHMTSP-PEnGAGAALAMVNAIRDAGIEPGQIAYVNAHGTST 308
Cdd:PRK09185 219 INIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPhPE-GLGAILAMQQALADAGLAPADIGYINLHGTAT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 309 PAGDKAEAQAVKSVFGDaasRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQv 388
Cdd:PRK09185 291 PLNDAMESRAVAAVFGD---GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQA- 366
|
250 260
....*....|....*....|..
gi 695765313 389 SGMEYALCNSFGFGGTNGSLIF 410
Cdd:PRK09185 367 LAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
5-409 |
2.53e-74 |
|
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: 237.84 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY----------ATKFAGLVKDFNCDDI----ISRKEQ 68
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpeDRWDADGYypdpgkpgktYTRRGGFLDDVDAFDAaffgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 69 RKMDA----FIQygiVAgVQAMQDSGLevteenaTRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPSTIVNMVA 144
Cdd:cd00833 82 EAMDPqqrlLLE---VA-WEALEDAGY-------SPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 145 GHLTIMFGLRGPSISIATACTSG---VHnigQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASR 221
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSlvaLH---LACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 222 PWDKDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAY--HMTSPpeNGAGAALAMVNAIRDAGIEPGQIA 299
Cdd:cd00833 223 PFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDID 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 300 YVNAHGTSTPAGDKAEAQAVKSVFG---DAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGC 376
Cdd:cd00833 301 YVEAHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKI 380
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 695765313 377 DLD----FVPHEAR---QVSGMEYALCNSFGFGGTNGSLI 409
Cdd:cd00833 381 DFEesplRVPTEARpwpAPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-412 |
6.61e-72 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 231.46 E-value: 6.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGI------------SLIDHFDTSAYATKFAGLVKDfncdDIISRKEQRKMD 72
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrqvpdDAGAGLASAFIGAELDSLALP----ERLDAKLLRRAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 73 AFIQYGIVAGVQAMQDSGLEVTEENatRIGAAIGSGIGGLGLIEENHSSLTNGgPRKISPFFVPSTIVNMVAGHLTIMFG 152
Cdd:PRK07103 79 LSAQAALAAAREAWRDAALGPVDPD--RIGLVVGGSNLQQREQALVHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 153 LRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRN--DNPQAASRPWDKDRDGF 230
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 231 VLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPA 310
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 311 GDKAEAQAvksVFGDAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNP-DEGCdlDFVPHEARQVS 389
Cdd:PRK07103 314 GDETELAA---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESAR 388
|
410 420
....*....|....*....|...
gi 695765313 390 gMEYALCNSFGFGGTNGSLIFKK 412
Cdd:PRK07103 389 -IRYALSLSFGFGGINTALVLER 410
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4-409 |
6.73e-70 |
|
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: 225.70 E-value: 6.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCDDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 84 QAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISP------FFVPSTivnmvaGHLTIMFGLRGPS 157
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAyqsfawFYAVNT------GQISIRHGMRGPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 158 ISIATACTSGVHNIGQAARMIAYGdADAMVAGGAEKASTPLGVGGFGAARALSTrNDNPQAASRPWDKDRDGFVLGDGAG 237
Cdd:cd00832 155 GVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 238 MVVLEEYEHAKKRGAKIYAEIVGFGMSsdayhMTSPPENGAGAALAmvNAIR----DAGIEPGQIAYVNAHGTSTPAGDK 313
Cdd:cd00832 233 ILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRPPGLA--RAIRlalaDAGLTPEDVDVVFADAAGVPELDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 314 AEAQAVKSVFGdaASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLDFVPHEARQvSGMEY 393
Cdd:cd00832 306 AEAAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRP-AALRT 382
|
410
....*....|....*.
gi 695765313 394 ALCNSFGFGGTNGSLI 409
Cdd:cd00832 383 ALVLARGRGGFNSALV 398
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-247 |
1.86e-60 |
|
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: 196.32 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY-----------ATKFAGLVKDFNCDDI---ISRKE 67
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLffgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 68 QRKMDAFIQYGIVAGVQAMQDSGLEVTEENATRIGAAIGSGIGGlgliEENHSSLTN-GGPRKISPFFVPsTIVNMVAGH 146
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD----YAALLLLDEdGGPRRGSPFAVG-TMPSVIAGR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 147 LTIMFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTrnDNPQAASRPWDkd 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231
|
250 260
....*....|....*....|.
gi 695765313 227 rDGFVLGDGAGMVVLEEYEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
119-405 |
1.51e-53 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 192.01 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 119 HSSLTNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATACTSG---VHnigQAARMIAYGDADAMVAGGAEKAS 195
Cdd:COG3321 129 YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSlvaVH---LACQSLRSGECDLALAGGVNLML 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 196 TPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSD-AYH-MTSP 273
Cdd:COG3321 206 TPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 274 peNGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVFG---DAASRVMVSSTKSMTGHLLGAAGAVE 350
Cdd:COG3321 281 --NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGqgrPADQPCAIGSVKSNIGHLEAAAGVAG 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765313 351 SIYSILALRDGVVPPTINLDNPDEGCDLD----FVPHEAR---QVSGMEYALCNSFGFGGTN 405
Cdd:COG3321 359 LIKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELRpwpAGGGPRRAGVSSFGFGGTN 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
77-409 |
5.36e-53 |
|
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: 179.75 E-value: 5.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 77 YGIVAGVQAMQDSGLEVTEENATRIGAAIGSGIGGLGLIEENHSSLTNGGPRKISPFFVPStivnmVAGHLTIMFGLRGP 156
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 157 SISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLGDGA 236
Cdd:cd00825 89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 237 GMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEA 316
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 317 QAVKSVFGDaaSRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEgcDLDFVPHEARQvSGMEYALC 396
Cdd:cd00825 244 KLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTP-RELRTALL 318
|
330
....*....|...
gi 695765313 397 NSFGFGGTNGSLI 409
Cdd:cd00825 319 NGFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
255-370 |
2.04e-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: 165.82 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 255 YAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEPGQIAYVNAHGTSTPAGDKAEAQAVKSVFGDAASR--VMV 332
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 695765313 333 SSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLD 370
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
136-412 |
3.43e-37 |
|
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: 144.38 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 136 PSTIVNMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDn 215
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 216 pqaaSRPWDKDRDGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMVNAIRDAGIEP 295
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 296 GQIAYVNAHGTSTPAGDKAEAQAVKSVFG---DAASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNP 372
Cdd:TIGR02813 333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 695765313 373 DEGCDLDFVPH----EAR----QVSGM-EYALCNSFGFGGTNGSLIFKK 412
Cdd:TIGR02813 413 NPKLDIENSPFylntETRpwmqREDGTpRRAGISSFGFGGTNFHMVLEE 461
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
143-409 |
1.54e-30 |
|
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: 117.93 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 143 VAGHLTIMFGLR-GPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKastplgvggfgaaralstrndnpqaasr 221
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 222 pwdkdrdgFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTsPPENGAGAALAMVNAIRDAGIEPGQIAYV 301
Cdd:cd00327 98 --------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 302 NAHGTSTPAGDKAEAQAVKSVFGDAAsrVMVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTinldnpdegcdldfv 381
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*...
gi 695765313 382 PHEARQVsgmeyaLCNSFGFGGTNGSLI 409
Cdd:cd00327 232 PREPRTV------LLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
157-409 |
6.09e-28 |
|
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: 111.65 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 157 SISIATACTSG---VHnigQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLG 233
Cdd:smart00825 90 SVTVDTACSSSlvaLH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 234 DGAGMVVLEEYEHAKKRGAKIYAEIVGFGMSSDayhmtsppenGAGAALAMVNAirdagiePGQIAyvnahgtstpagdk 313
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQD----------GRSNGITAPSG-------PAQLL-------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 314 aeaqavksvfgdaasrvmVSSTKSMTGHLLGAAGAVESIYSILALRDGVVPPTINLDNPDEGCDLD----FVPHEARQVS 389
Cdd:smart00825 211 ------------------IGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272
|
250 260
....*....|....*....|...
gi 695765313 390 GME---YALCNSFGFGGTNGSLI 409
Cdd:smart00825 273 PPGrprRAGVSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-260 |
4.08e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 58.04 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLidhfDTSAYATKFAGLVKDFNCDDIISRK-EQRKMDAFIQYGI 79
Cdd:PRK06519 3 MQPNDVVITGIGLVSSLGEGLDAHWNALSAGRPQPNV----DTETFAPYPVHPLPEIDWSQQIPKRgDQRQMETWQRLGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 80 VAGVQAMQDSGLEVTEENATRIGAAIGSgigglglieenhssltNGGPRKISpffVPSTIV------------------- 140
Cdd:PRK06519 79 YAAGLALDDAGIKGNEELLSTMDMIVAA----------------GGGERDIA---VDTAILnearkrndrgvllnerlmt 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 141 ------------NMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARA 208
Cdd:PRK06519 140 elrptlflaqlsNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPDMLLLYELGGL 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 695765313 209 LSTRNDNPQAASRPWDKDrdGFVLGDGAGMVVLEEYEHAKKRGAKIYAEIVG 260
Cdd:PRK06519 220 LLKGGWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARISG 269
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
136-301 |
7.02e-08 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 53.87 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 136 PSTIVNMVAGHLTimFGLRGPSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTrNDN 215
Cdd:PRK06147 107 EERLLRELEARLG--LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-SQN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 216 PqaasrpwdkdrDGFVLGDGAGMVVLEEYEHAKKRGAKIYAeiVGFGM-SSDAYHMTSPPENGAGAALAMVNAIRDAGIE 294
Cdd:PRK06147 184 S-----------NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGRePAPVGESEDLPLRGDGLTQAIRAALAEAGCG 250
|
....*..
gi 695765313 295 PGQIAYV 301
Cdd:PRK06147 251 LEDMDYR 257
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
221-361 |
3.34e-06 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 48.94 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 221 RPWDKDRDGFV-------LGDGAGMVVLEEYEHAKKRGAKIYAEIVGFGmssDAyhmTSPPENGAGA-ALAMVNAIRDAG 292
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYA---DA---AQAPELFTTApALAIPKALKHAG 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695765313 293 IEPGQIAY--VNahgtstpagdkaEAQAVKSV-----FGDAASRVMVSSTKSMTGHLLGAAGA--VESIYSILALRDG 361
Cdd:PLN02644 306 LEASQVDYyeIN------------EAFSVVALanqklLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKNG 371
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
156-244 |
1.07e-04 |
|
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: 44.29 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAST-PLGVGGFGAARALSTRNDNPQAASRPWDkDRDGFVLGD 234
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGE 158
|
90
....*....|
gi 695765313 235 GAGMVVlEEY 244
Cdd:COG0183 159 TAENVA-ERY 167
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
151-304 |
1.85e-04 |
|
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: 43.41 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 151 FGLRG-PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAST--------------------PLGVGGFGAARAL 209
Cdd:cd00829 63 LGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDvptgdeaggrasdlewegpePPGGLTPPALYAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 210 STR------------------------NDNPQA------------ASRP-WD--KDRDGFVLGDGAGMVVL--EEYehAK 248
Cdd:cd00829 143 AARrymhrygttredlakvavknhrnaARNPYAqfrkpitvedvlNSRMiADplRLLDCCPVSDGAAAVVLasEER--AR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695765313 249 KRGAKiYAEIVGFGMSSDAYHMTSPPENGA--GAALAMVNAIRDAGIEPGQIAYVNAH 304
Cdd:cd00829 221 ELTDR-PVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
156-244 |
1.90e-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: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAS-TPLGVGGfgaaRALSTRNDNPQAASRPWDKDRDGFVL-- 232
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSrAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTGls 151
|
90
....*....|...
gi 695765313 233 -GDGAGMVVlEEY 244
Cdd:cd00751 152 mGITAENVA-EKY 163
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
156-192 |
1.02e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 40.91 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*..
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAE 192
Cdd:PRK05790 80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
156-195 |
1.60e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 40.50 E-value: 1.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAS 195
Cdd:PRK07661 82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMS 121
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
156-195 |
4.36e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 39.17 E-value: 4.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAS 195
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMS 121
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
156-195 |
6.16e-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: 38.05 E-value: 6.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 695765313 156 PSISIATACTSGVHNIGQAARMIAYGDADAMVAGGAEKAS 195
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMS 116
|
|
| |
