|
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: 755.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 3 KRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 83 VQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIAT 162
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 163 ACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIVLE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 243 EYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSI 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 323 FGESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNSFGFG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARE-RKIDYALSNSFGFG 399
|
410
....*....|.
gi 556426225 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 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 164 CTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIVLEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 324 GESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
|
....*...
gi 556426225 404 TNGSLIFK 411
Cdd:TIGR03150 400 TNASLVFK 407
|
|
| 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: 664.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIV 80
Cdd:PRK08722 1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 81 AGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISI 160
Cdd:PRK08722 81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 161 ATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 241 LEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 321 SIFGESASR-VMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSF 399
Cdd:PRK08722 321 RALGEAGSKqVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESMEYAICNSF 400
|
410
....*....|....
gi 556426225 400 GFGGTNGSLIFKKI 413
Cdd:PRK08722 401 GFGGTNGSLIFKKM 414
|
|
| 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: 664.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 164 CTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIVLEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 324 GESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAK-IDYALSNSFGFGG 399
|
410
....*....|
gi 556426225 404 TNGSLIFKKI 413
Cdd:COG0304 400 HNASLVFKRY 409
|
|
| 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: 624.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 164 CTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIVLEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 324 GESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFGG 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAP-IRYALSNSFGFGG 399
|
....*..
gi 556426225 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: 527.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKD--------FNCEDIISRKEQRKMD 72
Cdd:PRK06333 1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 73 AFIQYGIVAGVQAMQDSGLEI-TEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMF 151
Cdd:PRK06333 81 RFILFAMAAAKEALAQAGWDPdTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 152 GLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKDRDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 231 VLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPA 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 311 GDKAEAQAVKSIFGeSASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCD-LDFVPHEARQVS 389
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|...
gi 556426225 390 gMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK06333 400 -MDYALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
4-413 |
2.75e-173 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 490.01 E-value: 2.75e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATA 163
Cdd:PRK08439 82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 164 CTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGAGMIVLEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 244 YEHAKKRGAKIYAEIVGFGMSSDAYHMTSP-PEngaGAALAMENAIRDAGITPaqIGYVNAHGTSTPAGDKAEAQAVKSI 322
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPaPE---GPLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 323 FGESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSgMEYTLCNSFGFG 402
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAE-LNVVMSNSFGFG 395
|
410
....*....|.
gi 556426225 403 GTNGSLIFKKI 413
Cdd:PRK08439 396 GTNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
13-413 |
3.04e-153 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 439.90 E-value: 3.04e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 13 MLSPVGNTVESTWKALLAGQSGISLIDHFDT----------------SAYATKFAGLVK--DFNCEDIISRKeqrKMDAF 74
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqsEFDPSDFAPTK---RESRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 75 IQYGIVAGVQAMQDSGLEITEE-NATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGL 153
Cdd:PTZ00050 78 THFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 154 RGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWDKDRDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 233 GDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAG-ITPAQIGYVNAHGTSTPAG 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 312 DKAEAQAVKSIFGESASR-VMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQ-VS 389
Cdd:PTZ00050 318 DKIELKAIKKVFGDSGAPkLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHpLQ 397
|
410 420
....*....|....*....|....
gi 556426225 390 GMEYTLCNSFGFGGTNGSLIFKKI 413
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
4-410 |
9.52e-145 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 418.81 E-value: 9.52e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI-------DHFDTSAYA-------TKFAGLVKDFNCEDIISRK--- 66
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqddlkmKSEDEETQLytldqlpSRVAALVPRGTGPGDFDEElwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 67 EQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGP-RKISPFFVPSTIVNMVAG 145
Cdd:PLN02836 86 NSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRlRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 146 HLTIMFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTR-NDNPQAASRPWD 224
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 225 KDRDGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAH 304
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 305 GTSTPAGDKAEAQAVKSIFGESAS--RVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVP 382
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420
....*....|....*....|....*...
gi 556426225 383 HEARQVSGMEYTLCNSFGFGGTNGSLIF 410
Cdd:PLN02836 406 LTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
1-410 |
7.92e-125 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 371.62 E-value: 7.92e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 1 MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIV 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 81 AGVQAMQDSGleITEE-----NATRIGAAIGSGIGGLGLIEENHTSLmNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRG 155
Cdd:PLN02787 206 AGKKALADGG--ITEDvmkelDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSAMLAMDLGWMG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDG 235
Cdd:PLN02787 283 PNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 236 AGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAE 315
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 316 AQAVKSIFGESaSRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTL 395
Cdd:PLN02787 443 YQALMRCFGQN-PELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLDIKVAL 521
|
410
....*....|....*
gi 556426225 396 CNSFGFGGTNGSLIF 410
Cdd:PLN02787 522 SNSFGFGGHNSSILF 536
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
4-411 |
1.58e-112 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 335.42 E-value: 1.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDT-SAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAG 82
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDRyDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 83 VQAMQDSGLeITEENAT--RIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPffvpSTIVNMV----AGHLTIMFGLRGP 156
Cdd:PRK09116 82 ELALEDAGL-LGDPILTdgRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMMphttAVNVGLFFGLKGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 157 SISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAStPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGA 236
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 237 GMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEA 316
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQP--QAETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 317 QAVKSIFGEsasRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGC-DLDFVPHEARQVSgMEYTL 395
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREID-TEYVM 389
|
410
....*....|....*.
gi 556426225 396 CNSFGFGGTNGSLIFK 411
Cdd:PRK09116 390 SNNFAFGGINTSLIFK 405
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
4-412 |
3.72e-103 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 311.61 E-value: 3.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKdFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIG-AAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIAT 162
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGlIAGSGGGSTRNQVEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 163 ACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGgFGAARALSTR-NDNPQAASRPWDKDRDGFVLGDGAGMIVL 241
Cdd:PRK07967 161 ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 242 EEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMENAIrdAGITpAQIGYVNAHGTSTPAGDKAEAQAVKS 321
Cdd:PRK07967 240 EELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTPVGDVKELGAIRE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 322 IFGESASRvmVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDE-GCDLDFVpHEARQVSGMEYTLCNSFG 400
Cdd:PRK07967 315 VFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPqAAGMPIV-TETTDNAELTTVMSNSFG 391
|
410
....*....|..
gi 556426225 401 FGGTNGSLIFKK 412
Cdd:PRK07967 392 FGGTNATLVFRR 403
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
126-412 |
4.81e-103 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 308.97 E-value: 4.81e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 126 GPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGA 205
Cdd:PRK14691 53 GPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 206 ARALSTR-NDNPQAASRPWDKDRDGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAM 284
Cdd:PRK14691 133 ARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 285 ENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIFGESASrVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVP 364
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGESNA-LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 556426225 365 PTINLDNPDEGCD-LDFVPHEArQVSGMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK14691 292 ATLNLENPDPAAKgLNIIAGNA-QPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
6-412 |
1.25e-102 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 310.51 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 6 VVVTGLGMLSPVGNTVESTWKALLAGQSGI-----SLIDHFDTSayaTKFAG-LVKDFncEDIISRKEQRKMDAFIQYGI 79
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIrtlddPFVEEFDLP---VRIGGhLLEEF--DHQLTRVELRRMSYLQRMST 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 80 VAGVQAMQDSGleITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSIS 159
Cdd:PRK07910 89 VLGRRVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 160 IATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARA-LSTRNDNPQAASRPWDKDRDGFVLGDGAGM 238
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 239 IVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQA 318
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 319 VKSIFGesASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTLCNS 398
Cdd:PRK07910 327 INNALG--GHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRP-GNYRYAINNS 403
|
410
....*....|....
gi 556426225 399 FGFGGTNGSLIFKK 412
Cdd:PRK07910 404 FGFGGHNVALAFGR 417
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
6-410 |
3.95e-99 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 301.93 E-value: 3.95e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 6 VVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVkDFNCEDIISRKEQRKMDAFIqygivAGVQA 85
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DFLPESPFGASALSEALARL-----AAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 86 MQDSGLEIT---------------EENATRIGAAIGSGIGglgliEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIM 150
Cdd:PRK06501 87 LAQAGIGKGdfpgplflaappvelEWPARFALAAAVGDND-----APSYDRLLRAARGGRFDALHERFQFGSIADRLADR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 151 FGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGF 230
Cdd:PRK06501 162 FGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 231 VLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPA 310
Cdd:PRK06501 242 VMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 311 GDKAEAQAVKSIFGESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEAR--QV 388
Cdd:PRK06501 322 NDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARdaRV 401
|
410 420
....*....|....*....|..
gi 556426225 389 SGMeytLCNSFGFGGTNGSLIF 410
Cdd:PRK06501 402 TAV---LSNSFGFGGQNASLVL 420
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
5-408 |
9.00e-81 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 253.44 E-value: 9.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 5 RVVVTGLGMLSPVGNtVESTWKALLAGQSGISLIDHF-DTSAYATkfaGLV--KDFNCEDIIsrkEQRKMDAFIQYGIVA 81
Cdd:PRK05952 3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPFpELPPLPL---GLIgnQPSSLEDLT---KTVVTAALKDAGLTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 82 gvqAMQDSGLEITEENATRIGAAIGSGigglglieENHTSLMNGGPRKISPFFVpSTIVNMVAGHLTIMFGLRGPSISIA 161
Cdd:PRK05952 76 ---PLTDCGVVIGSSRGCQGQWEKLAR--------QMYQGDDSPDEELDLENWL-DTLPHQAAIAAARQIGTQGPVLAPM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 162 TACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnpQAASRPWDKDRDGFVLGDGAGMIVL 241
Cdd:PRK05952 144 AACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA------KTGAYPFDRQREGLVLGEGGAILVL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 242 EEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKS 321
Cdd:PRK05952 218 ESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 322 IFGesaSRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDegCDLDFVpHEARQvSGMEYTLCNSFGF 401
Cdd:PRK05952 298 LFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFV-RQAQQ-SPLQNVLCLSFGF 370
|
....*..
gi 556426225 402 GGTNGSL 408
Cdd:PRK05952 371 GGQNAAI 377
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
4-408 |
8.36e-77 |
|
"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: 243.89 E-value: 8.36e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGN---TVESTWKALLAGQSGISLIDHFdTSAYATKFAGLVKDFNCEDIISRKEqRKMDAFIQYGIV 80
Cdd:cd00828 1 SRVVITGIGVVSPHGEgcdEVEEFWEALREGRSGIAPVARL-KSRFDRGVAGQIPTGDIPGWDAKRT-GIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 81 AGVQAMQDSGLEI-TEENATRIGAAIGSGIGGLGLIEenHTSLMNGgpRKISPFFVPSTIV--NMVAGHLTIMFGL-RGP 156
Cdd:cd00828 79 ATEEALADAGITDpYEVHPSEVGVVVGSGMGGLRFLR--RGGKLDA--RAVNPYVSPKWMLspNTVAGWVNILLLSsHGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 157 SISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEkASTPLGVGGFGAARALSTRNDNPQAASRPWDKDRDGFVLGDGA 236
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 237 GMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPeNGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEA 316
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 317 QAVKSIFGESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYT-L 395
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLKVRAaL 392
|
410
....*....|...
gi 556426225 396 CNSFGFGGTNGSL 408
Cdd:cd00828 393 VNAFGFGGSNAAL 405
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
151-410 |
1.84e-74 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 237.43 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 151 FGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAS-TPLGvgGFGAARALSTRndnpqaASRPWDKDRDG 229
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCrLTLN--GFNSLESLSPQ------PCRPFSANRDG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 230 FVLGDGAGMIVLEeyehakkRGAKIYAEIVGFGMSSDAYHMTSP-PEnGAGAALAMENAIRDAGITPAQIGYVNAHGTST 308
Cdd:PRK09185 219 INIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPhPE-GLGAILAMQQALADAGLAPADIGYINLHGTAT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 309 PAGDKAEAQAVKSIFGEsasRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQv 388
Cdd:PRK09185 291 PLNDAMESRAVAAVFGD---GVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQA- 366
|
250 260
....*....|....*....|..
gi 556426225 389 SGMEYTLCNSFGFGGTNGSLIF 410
Cdd:PRK09185 367 LAIRYVLSNSFAFGGNNCSLIF 388
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
5-409 |
3.62e-72 |
|
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: 232.45 E-value: 3.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY----------ATKFAGLVKDFNCEDI----ISRKEQ 68
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIpeDRWDADGYypdpgkpgktYTRRGGFLDDVDAFDAaffgISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 69 RKMDA----FIQygiVAgVQAMQDSGLeiteenaTRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVA 144
Cdd:cd00833 82 EAMDPqqrlLLE---VA-WEALEDAGY-------SPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 145 GHLTIMFGLRGPSISIATACTSG---VHnigQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASR 221
Cdd:cd00833 151 NRISYFFDLRGPSLTVDTACSSSlvaLH---LACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 222 PWDKDRDGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAY--HMTSPpeNGAGAALAMENAIRDAGITPAQIG 299
Cdd:cd00833 223 PFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAP--SGEAQAALIRRAYARAGVDPSDID 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 300 YVNAHGTSTPAGDKAEAQAVKSIFGES---ASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGC 376
Cdd:cd00833 301 YVEAHGTGTPLGDPIEVEALAKVFGGSrsaDQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKI 380
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 556426225 377 DLD----FVPHEAR---QVSGMEYTLCNSFGFGGTNGSLI 409
Cdd:cd00833 381 DFEesplRVPTEARpwpAPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
5-412 |
5.94e-72 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 231.46 E-value: 5.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 5 RVVVTGLGMLSPVGNTVESTWKALLAGQSGI------------SLIDHFDTSAYATKFAGLVKdfncEDIISRKEQRKMD 72
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFgvmrrpgrqvpdDAGAGLASAFIGAELDSLAL----PERLDAKLLRRAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 73 AFIQYGIVAGVQAMQDSGLEitEENATRIGAAIGSGIGGLGLIEENHTSLMNGgPRKISPFFVPSTIVNMVAGHLTIMFG 152
Cdd:PRK07103 79 LSAQAALAAAREAWRDAALG--PVDPDRIGLVVGGSNLQQREQALVHETYRDR-PAFLRPSYGLSFMDTDLVGLCSEQFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 153 LRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRN--DNPQAASRPWDKDRDGF 230
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 231 VLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPpeNGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPA 310
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 311 GDKAEAQAvksIFGESASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNP-DEGCdlDFVPHEARQVS 389
Cdd:PRK07103 314 GDETELAA---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESAR 388
|
410 420
....*....|....*....|...
gi 556426225 390 gMEYTLCNSFGFGGTNGSLIFKK 412
Cdd:PRK07103 389 -IRYALSLSFGFGGINTALVLER 410
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
4-409 |
1.60e-69 |
|
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: 224.93 E-value: 1.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGV 83
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 84 QAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISP------FFVPSTivnmvaGHLTIMFGLRGPS 157
Cdd:cd00832 81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAyqsfawFYAVNT------GQISIRHGMRGPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 158 ISIATACTSGVHNIGQAARIIAYGdADAMVAGGAEKASTPLGVGGFGAARALSTrNDNPQAASRPWDKDRDGFVLGDGAG 237
Cdd:cd00832 155 GVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 238 MIVLEEYEHAKKRGAKIYAEIVGFGMSsdayhMTSPPENGAGAAL--AMENAIRDAGITPAQIGYVNAHGTSTPAGDKAE 315
Cdd:cd00832 233 ILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRPPGLarAIRLALADAGLTPEDVDVVFADAAGVPELDRAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 316 AQAVKSIFGesASRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQvSGMEYTL 395
Cdd:cd00832 308 AAALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRP-AALRTAL 384
|
410
....*....|....
gi 556426225 396 CNSFGFGGTNGSLI 409
Cdd:cd00832 385 VLARGRGGFNSALV 398
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
4-247 |
9.80e-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: 194.78 E-value: 9.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 4 RRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLI--DHFDTSAY-----------ATKFAGLVKDFNCEDI---ISRKE 67
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydppsriagkiYTKWGGLDDIFDFDPLffgISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 68 QRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLgliEENHTSLMNGGPRKISPFFVPsTIVNMVAGHL 147
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVG-TMPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 148 TIMFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTrnDNPQAASRPWDkdr 227
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA--- 231
|
250 260
....*....|....*....|
gi 556426225 228 DGFVLGDGAGMIVLEEYEHA 247
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
119-405 |
1.24e-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: 192.39 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 119 HTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMFGLRGPSISIATACTSG---VHnigQAARIIAYGDADAMVAGGAEKAS 195
Cdd:COG3321 129 YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSlvaVH---LACQSLRSGECDLALAGGVNLML 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 196 TPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSD-AYH-MTSP 273
Cdd:COG3321 206 TPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 274 peNGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIFGESASR---VMVSSTKSMTGHLLGAAGAVE 350
Cdd:COG3321 281 --NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVAG 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426225 351 SIYSILALRDQAVPPTINLDNPDEGCDLD----FVPHEARQVSGMEYTLC---NSFGFGGTN 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 |
5.49e-52 |
|
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: 177.06 E-value: 5.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 77 YGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPStivnmVAGHLTIMFGLRGP 156
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPG-----ASGQIATPLGIHGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 157 SISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLGDGA 236
Cdd:cd00825 89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 237 GMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEA 316
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 317 QAVKSIFGEsaSRVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEgcDLDFVPHEARQvSGMEYTLC 396
Cdd:cd00825 244 KLLRSEFGD--KSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTP-RELRTALL 318
|
330
....*....|...
gi 556426225 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 |
1.48e-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: 166.20 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 255 YAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITPAQIGYVNAHGTSTPAGDKAEAQAVKSIFGESASR--VMV 332
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 556426225 333 SSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLD 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 |
1.79e-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: 145.15 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 136 PSTIVNMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTRNDn 215
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 216 pqaaSRPWDKDRDGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTSPPENGAGAALAMENAIRDAGITP 295
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 296 AQIGYVNAHGTSTPAGDKAEAQAVKSIFGESASR---VMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNP 372
Cdd:TIGR02813 333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 556426225 373 DEGCDLDFVPH----EAR----QVSGMEYTL-CNSFGFGGTNGSLIFKK 412
Cdd:TIGR02813 413 NPKLDIENSPFylntETRpwmqREDGTPRRAgISSFGFGGTNFHMVLEE 461
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
143-409 |
1.14e-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: 118.32 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 143 VAGHLTIMFGLR-GPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKastplgvggfgaaralstrndnpqaasr 221
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 222 pwdkdrdgFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAYHMTsPPENGAGAALAMENAIRDAGITPAQIGYV 301
Cdd:cd00327 98 --------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 302 NAHGTSTPAGDKAEAQAVKSIFGESAsrVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTinldnpdegcdldfv 381
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*...
gi 556426225 382 PHEARQVsgmeytLCNSFGFGGTNGSLI 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 |
2.24e-25 |
|
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: 104.72 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 157 SISIATACTSG---VHnigQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALStrndnPQAASRPWDKDRDGFVLG 233
Cdd:smart00825 90 SVTVDTACSSSlvaLH---LACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 234 DGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAyhmtsppengagaalamenaiRDAGITpaqigyvnahgtsTPAGdk 313
Cdd:smart00825 162 EGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG---------------------RSNGIT-------------APSG-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 314 aEAQavksifgesasrVMVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLD----FVPHEARQVS 389
Cdd:smart00825 206 -PAQ------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWP 272
|
250 260
....*....|....*....|...
gi 556426225 390 GMEYTLC---NSFGFGGTNGSLI 409
Cdd:smart00825 273 PPGRPRRagvSSFGFGGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-346 |
1.13e-09 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 59.58 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 1 MSKRRVVVTGLGMLSPVGNTVESTWkALLAGQSGISLIDhfdtsayATKFA-----GLVK-DFNCEdIISRKEQRKMDAF 74
Cdd:PRK06519 3 MQPNDVVITGIGLVSSLGEGLDAHW-NALSAGRPQPNVD-------TETFApypvhPLPEiDWSQQ-IPKRGDQRQMETW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 75 IQYGIVAGVQAMQDSGLEITEEnatrigaaigsgigglglieenHTSLMN------GGPRKISpffVPSTIV-------- 140
Cdd:PRK06519 74 QRLGTYAAGLALDDAGIKGNEE----------------------LLSTMDmivaagGGERDIA---VDTAILnearkrnd 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 141 -----------------------NMVAGHLTIMFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTP 197
Cdd:PRK06519 129 rgvllnerlmtelrptlflaqlsNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 198 LGVGGFGAARALSTRNDNPQAASRPWDKDrdGFVLGDGAGMIVLEEYEHAKKRGAKIYAEIVgfGMSSDayhmTSPPENG 277
Cdd:PRK06519 209 DMLLLYELGGLLLKGGWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARIS--GVESD----RARRAPG 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426225 278 AGAAlAMENAIRDAGITPAQiGYVNAHGTSTPAGDKAEAQAVksifgESASRVMVSSTKSMTGHLLGAA 346
Cdd:PRK06519 281 DLEA-SLERLLKPAGGLAAP-TAVISGATGAHPATAEEKAAL-----EAALAGPVRGIGTLFGHTMEAQ 342
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
136-301 |
1.77e-08 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 55.80 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 136 PSTIVNMVAGHLTimFGLRGPSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKASTPLGVGGFGAARALSTrNDN 215
Cdd:PRK06147 107 EERLLRELEARLG--LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT-SQN 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 216 PqaasrpwdkdrDGFVLGDGAGMIVLEEYEHAKKRGAKIYAeiVGFGM-SSDAYHMTSPPENGAGAALAMENAIRDAGIT 294
Cdd:PRK06147 184 S-----------NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LGLGRePAPVGESEDLPLRGDGLTQAIRAALAEAGCG 250
|
....*..
gi 556426225 295 PAQIGYV 301
Cdd:PRK06147 251 LEDMDYR 257
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
221-360 |
4.68e-06 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 48.55 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 221 RPWDKDRDGFV-------LGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGmssDAyhmTSPPENGAGA-ALAMENAIRDAG 292
Cdd:PLN02644 232 RPSFKEDGGSVtagnassISDGAAALVLVSGEKALELGLQVIAKIRGYA---DA---AQAPELFTTApALAIPKALKHAG 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426225 293 ITPAQIGY--VNahgtstpagdkaEAQAVKS-----IFGESASRVMVSSTKSMTGHLLGAAGA--VESIYSILALRD 360
Cdd:PLN02644 306 LEASQVDYyeIN------------EAFSVVAlanqkLLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKN 370
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
151-304 |
1.33e-05 |
|
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: 46.87 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 151 FGLRG-PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAST--------------------PLGVGGFGAARAL 209
Cdd:cd00829 63 LGLLGkPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDvptgdeaggrasdlewegpePPGGLTPPALYAL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 210 STR------------------------NDNPQA------------ASRP-WD--KDRDGFVLGDGAGMIVL--EEYehAK 248
Cdd:cd00829 143 AARrymhrygttredlakvavknhrnaARNPYAqfrkpitvedvlNSRMiADplRLLDCCPVSDGAAAVVLasEER--AR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556426225 249 KRGAKiYAEIVGFGMSSDAYHMTSPPENGA--GAALAMENAIRDAGITPAQIGYVNAH 304
Cdd:cd00829 221 ELTDR-PVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
156-301 |
5.02e-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: 41.98 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAST-PLGV----GGFGAARALSTRNDNP-------------- 216
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLpkarWGYRMNAKLVDPMINPgltdpytglsmget 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 217 -----------------------QAASRPWDK-------------------------------------------DRDGF 230
Cdd:COG0183 160 aenvaerygisreeqdafalrshQRAAAAIAAgrfddeivpvevpdrkgevvvdrdegprpdttleklaklkpafKKDGT 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556426225 231 V-------LGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSdayhmtSPPEN-GAGAALAMENAIRDAGITPAQIGYV 301
Cdd:COG0183 240 VtagnasgINDGAAALLLMSEEAAKELGLKPLARIVAYAVAG------VDPEImGIGPVPATRKALARAGLTLDDIDLI 312
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
234-348 |
1.11e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 40.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 234 DGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSSDAyhmtsPPENGAGAALAMENAIRDAGITPAQIGYVNAHgtstpagdk 313
Cdd:cd00751 246 DGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVD-----PAIMGIGPVPAIPKALKRAGLTLDDIDLIEIN--------- 311
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 556426225 314 aEAQAVKSI-----FGESASRVMVS-STKSMtGHLLGAAGA 348
Cdd:cd00751 312 -EAFAAQALaclkeLGLDPEKVNVNgGAIAL-GHPLGASGA 350
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
156-199 |
2.40e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 39.73 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAS-TPLG 199
Cdd:PRK07661 82 PAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSlVPMM 126
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
156-232 |
2.73e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 39.77 E-value: 2.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAS-TPLGVGGfgaaRALSTRNDNPQAASRPWDKDRDGFVL 232
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSrAPYLLPK----ARRGGRLGLNTLDGMLDDGLTDPFTG 149
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
156-192 |
3.61e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 39.37 E-value: 3.61e-03
10 20 30
....*....|....*....|....*....|....*..
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAE 192
Cdd:PRK05790 80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
156-195 |
4.47e-03 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 39.17 E-value: 4.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 556426225 156 PSISIATACTSGVHNIGQAARIIAYGDADAMVAGGAEKAS 195
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMS 121
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
226-348 |
4.74e-03 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 38.98 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426225 226 DRDGFV-------LGDGAGMIVLEEYEHAKKRGAKIYAEIVGFGMSS--DAYhMtsppenGAGAALAMENAIRDAGITPA 296
Cdd:PRK05790 237 DKDGTVtagnasgINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGvdPAI-M------GIGPVPAIRKALEKAGWSLA 309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 556426225 297 QIGYVNAHgtstpagdkaEA---QAVKSI--FGESASRVMVSSTKSMTGHLLGAAGA 348
Cdd:PRK05790 310 DLDLIEIN----------EAfaaQALAVEkeLGLDPEKVNVNGGAIALGHPIGASGA 356
|
|
| |
