|
Name |
Accession |
Description |
Interval |
E-value |
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
2-408 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 740.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSA 161
Cdd:TIGR03150 81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 162 CATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLEE 241
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 242 YESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVF 321
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 322 KDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGGT 401
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400
|
....*..
gi 77545124 402 NASLLFR 408
Cdd:TIGR03150 401 NASLVFK 407
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
1-410 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 698.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAA 80
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 81 DEAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVS 160
Cdd:PRK07314 81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 161 ACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLE 240
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 241 EYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTV 320
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 321 FKDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGG 400
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
|
410
....*....|
gi 77545124 401 TNASLLFRKV 410
Cdd:PRK07314 401 TNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
2-410 |
0e+00 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 691.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSA 161
Cdd:COG0304 81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 162 CATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLEE 241
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 242 YESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVF 321
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 322 KDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGGT 401
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 77545124 402 NASLLFRKV 410
Cdd:COG0304 401 NASLVFKRY 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
2-407 |
0e+00 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 644.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSA 161
Cdd:cd00834 81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 162 CATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLEE 241
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 242 YESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVF 321
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 322 KDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGGT 401
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 77545124 402 NASLLF 407
Cdd:cd00834 401 NASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
1-409 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 540.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRD--------FNAEDYIEKKETRKMDLF 72
Cdd:PRK06333 3 KKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMDRF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 73 IQYALAAADEAVKDSKLVIDD-DNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGA 151
Cdd:PRK06333 83 ILFAMAAAKEALAQAGWDPDTlEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 152 KGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTR-NDDPQAASRPFEKNRDGFVM 230
Cdd:PRK06333 163 KGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 231 AEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFND 310
Cdd:PRK06333 243 GEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 311 LYETMAIKTVFKdHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECD-LDYVPNEARRVVVE 389
Cdd:PRK06333 323 LGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMD 401
|
410 420
....*....|....*....|
gi 77545124 390 SALSNSFGFGGTNASLLFRK 409
Cdd:PRK06333 402 YALSNGFGFGGVNASILFRR 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
1-410 |
0e+00 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 538.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAA 80
Cdd:PRK08439 1 MKRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 81 DEAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVS 160
Cdd:PRK08439 81 REAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 161 ACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLE 240
Cdd:PRK08439 161 ACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 241 EYESARARGAHIYAELVGYGLTSDAHHLTAPAPggEGAARCMAMALKNSGMQAEDvtYINAHGTSTHFNDLYETMAIKTV 320
Cdd:PRK08439 241 EYESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAGNPKID--YINAHGTSTPYNDKNETAALKEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 321 FKDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGG 400
Cdd:PRK08439 317 FGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGG 396
|
410
....*....|
gi 77545124 401 TNASLLFRKV 410
Cdd:PRK08439 397 TNGVVIFKKV 406
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
12-410 |
1.91e-167 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 475.72 E-value: 1.91e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 12 ISALGNGVEKNWQSLLAGKSGIDRITRFDA----------------SDFPSQIAGEVR--DFNAEDYiekKETRKMDLFI 73
Cdd:PTZ00050 2 VTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqsEFDPSDF---APTKRESRAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 74 QYALAAADEAVKDSKLVIDDD-NAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAK 152
Cdd:PTZ00050 79 HFAMAAAREALADAKLDILSEkDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 153 GPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTR-NDDPQAASRPFEKNRDGFVMA 231
Cdd:PTZ00050 159 GPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 232 EGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSG-MQAEDVTYINAHGTSTHFND 310
Cdd:PTZ00050 239 EGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 311 LYETMAIKTVFKDH-ARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVV-- 387
Cdd:PTZ00050 319 KIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLqs 398
|
410 420
....*....|....*....|...
gi 77545124 388 VESALSNSFGFGGTNASLLFRKV 410
Cdd:PTZ00050 399 IDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
2-410 |
6.55e-159 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 454.08 E-value: 6.55e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:PRK08722 4 RRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSA 161
Cdd:PRK08722 84 QALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 162 CATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLEE 241
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 242 YESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVF 321
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 322 -KDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRV-VVESALSNSFGFG 399
Cdd:PRK08722 324 gEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVeSMEYAICNSFGFG 403
|
410
....*....|.
gi 77545124 400 GTNASLLFRKV 410
Cdd:PRK08722 404 GTNGSLIFKKM 414
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
2-407 |
1.72e-152 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 438.46 E-value: 1.72e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDA--------------SDFPSQIAGEV-RDFNAEDYIEKK-- 64
Cdd:PLN02836 6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVpRGTGPGDFDEELwl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 65 ETRKMDLFIQYALAAADEAVKDSK-LVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPG 143
Cdd:PLN02836 86 NSRSSSRFIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 144 QISMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTR-NDDPQAASRPFE 222
Cdd:PLN02836 166 HVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 223 KNRDGFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAH 302
Cdd:PLN02836 246 CDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 303 GTSTHFNDLYETMAIKTVFKDHAR--KLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVP 380
Cdd:PLN02836 326 ATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVP 405
|
410 420
....*....|....*....|....*...
gi 77545124 381 -NEARRVVVESALSNSFGFGGTNASLLF 407
Cdd:PLN02836 406 lTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
2-407 |
1.28e-126 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 376.24 E-value: 1.28e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLTAGK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKL---VIDDDNAERVGVLVGAGLGGLPTIEKYHSAyLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSS 158
Cdd:PLN02787 209 KALADGGItedVMKELDKTKCGVLIGSAMGGMKVFNDAIEA-LRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSI 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 159 VSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGAGIVV 238
Cdd:PLN02787 288 STACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 239 LEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIK 318
Cdd:PLN02787 368 LEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALM 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 319 TVFKDHArKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLD-YVPNEARRVVVESALSNSFG 397
Cdd:PLN02787 448 RCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSNSFG 526
|
410
....*....|
gi 77545124 398 FGGTNASLLF 407
Cdd:PLN02787 527 FGGHNSSILF 536
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-407 |
4.70e-118 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 350.08 E-value: 4.70e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 4 VVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVrdfnaeDYIEKKETRKMDLFIQYALAAADEA 83
Cdd:PRK06501 13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV------DFLPESPFGASALSEALARLAAEEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 84 VKDSKLVIDDDNA-----------ERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPgQISMRFGAK 152
Cdd:PRK06501 87 LAQAGIGKGDFPGplflaappvelEWPARFALAAAVGDNDAPSYDRLLRAARGGRFDALHERFQFGSIAD-RLADRFGTR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 153 GPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAE 232
Cdd:PRK06501 166 GLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFVMAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 233 GAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLY 312
Cdd:PRK06501 246 GAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKM 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 313 ETMAIKTVFKDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESAL 392
Cdd:PRK06501 326 EYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVTAVL 405
|
410
....*....|....*
gi 77545124 393 SNSFGFGGTNASLLF 407
Cdd:PRK06501 406 SNSFGFGGQNASLVL 420
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
1-410 |
4.55e-114 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 339.34 E-value: 4.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVrDFNAEDYIEKKETRKMDLFIQYALAAA 80
Cdd:PRK07967 1 MRRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNV-KLDPTGLIDRKVMRFMGDASAYAYLAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 81 DEAVKDSKLVIDDDNAERVGVLVGAGLGGLPTI-EKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSV 159
Cdd:PRK07967 80 EQAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQvEAADAMRGPRGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 160 SACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGgFNVMRALSTR-NDDPQAASRPFEKNRDGFVMAEGAGIVV 238
Cdd:PRK07967 160 SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 239 LEEYESARARGAHIYAELVGYGLTSDAHHLTAPApgGEGAARCMAMALknSGMQAeDVTYINAHGTSTHFNDLYETMAIK 318
Cdd:PRK07967 239 VEELEHALARGAKIYAEIVGYGATSDGYDMVAPS--GEGAVRCMQMAL--ATVDT-PIDYINTHGTSTPVGDVKELGAIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 319 TVFKDHARKlmVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPE-CDLDYVPNEARRVVVESALSNSFG 397
Cdd:PRK07967 314 EVFGDKSPA--ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNSFG 391
|
410
....*....|...
gi 77545124 398 FGGTNASLLFRKV 410
Cdd:PRK07967 392 FGGTNATLVFRRY 404
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
1-408 |
4.01e-109 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 326.56 E-value: 4.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNgvekNWQS----LLAGKSGIDRITRFD-ASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQY 75
Cdd:PRK09116 1 MRRVVVTGMGGVTALGE----DWQTiaarLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 76 ALAAADEAVKDSKLvIDDD---NAERVGVLVGAGLGGLPTIEkYHSAYLKGGYKKISP-FFIPMLiTNLAPGQISMRFGA 151
Cdd:PRK09116 77 ATRASELALEDAGL-LGDPiltDGRMGIAYGSSTGSTDPIGA-FGTMLLEGSMSGITAtTYVRMM-PHTTAVNVGLFFGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 152 KGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAEStITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMA 231
Cdd:PRK09116 154 KGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 232 EGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPggEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDL 311
Cdd:PRK09116 233 EGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQA--ETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 312 YETMAIKTVFKDharKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPEC-DLDYVPNEARRVVVES 390
Cdd:PRK09116 311 AESQATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEY 387
|
410
....*....|....*...
gi 77545124 391 ALSNSFGFGGTNASLLFR 408
Cdd:PRK09116 388 VMSNNFAFGGINTSLIFK 405
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
4-409 |
1.09e-101 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 308.20 E-value: 1.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 4 VVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITR--FDASDFPSQIAGEVRDfNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDpfVEEFDLPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKlvIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSA 161
Cdd:PRK07910 93 RVWENAG--SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 162 CATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRA-LSTRNDDPQAASRPFEKNRDGFVMAEGAGIVVLE 240
Cdd:PRK07910 171 CASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALMVIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 241 EYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTV 320
Cdd:PRK07910 251 TEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 321 FKDHarKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSNSFGFGG 400
Cdd:PRK07910 331 LGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGFGG 408
|
....*....
gi 77545124 401 TNASLLFRK 409
Cdd:PRK07910 409 HNVALAFGR 417
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
1-409 |
1.07e-90 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 278.86 E-value: 1.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNgVEKNWQSLLAGKSGIDRITRFdaSDFPSQIAGEVrdfnaedyieKKETRKMDLFIQYALaaa 80
Cdd:PRK05952 1 MMKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPF--PELPPLPLGLI----------GNQPSSLEDLTKTVV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 81 DEAVKDSKL---------VIDDDNA-----ERVGVLVGAGLGGLPTIEKYHSaYLKggykkispfFIPMLITNLAPGQIs 146
Cdd:PRK05952 65 TAALKDAGLtppltdcgvVIGSSRGcqgqwEKLARQMYQGDDSPDEELDLEN-WLD---------TLPHQAAIAAARQI- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 147 mrfGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALStrnddpQAASRPFEKNRD 226
Cdd:PRK05952 134 ---GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA------KTGAYPFDRQRE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 227 GFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTST 306
Cdd:PRK05952 205 GLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 307 HFNDLYETMAIKTVFkdhARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEpdPECDLDYVpNEARRV 386
Cdd:PRK05952 285 RLNDQREANLIQALF---PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNFV-RQAQQS 358
|
410 420
....*....|....*....|...
gi 77545124 387 VVESALSNSFGFGGTNASLLFRK 409
Cdd:PRK05952 359 PLQNVLCLSFGFGGQNAAIALGK 381
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
124-409 |
6.39e-90 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 275.45 E-value: 6.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 124 GYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNV 203
Cdd:PRK14691 53 GPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 204 MRALSTR-NDDPQAASRPFEKNRDGFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCM 282
Cdd:PRK14691 133 ARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 283 AMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVFKDhARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVP 362
Cdd:PRK14691 213 KIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVP 291
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 77545124 363 PTINYSEPDPECD-LDYVPNEARRVVVESALSNSFGFGGTNASLLFRK 409
Cdd:PRK14691 292 ATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
2-406 |
3.51e-85 |
|
"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: 265.46 E-value: 3.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNG---VEKNWQSLLAGKSGIDRITRFDaSDFPSQIAGEVRDFNAEDYIEKKeTRKMDLFIQYALA 78
Cdd:cd00828 1 SRVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGWDAKR-TGIVDRTTLLALV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 79 AADEAVKDSKLVIDD-DNAERVGVLVGAGLGGlpTIEKYHsaYLKGGYKKISPFFIP--MLITNLAPGQISMRF-GAKGP 154
Cdd:cd00828 79 ATEEALADAGITDPYeVHPSEVGVVVGSGMGG--LRFLRR--GGKLDARAVNPYVSPkwMLSPNTVAGWVNILLlSSHGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 155 NVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAEStITPLAVGGFNVMRALSTRNDDPQAASRPFEKNRDGFVMAEGA 234
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 235 GIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGeGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYET 314
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGK-GIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 315 MAIKTVFKDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEAR--RVVVESAL 392
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAAL 392
|
410
....*....|....
gi 77545124 393 SNSFGFGGTNASLL 406
Cdd:cd00828 393 VNAFGFGGSNAALV 406
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
2-406 |
1.05e-76 |
|
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: 243.42 E-value: 1.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQIAGEVRDFNAEDYIEKKETRKMDLFIQYALAAAD 81
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 82 EAVKDSKL-VIDDDNAERVGVLVGAGLGGLPTIEKYHSAYLKGG-----YKKISPFFIpmlitnLAPGQISMRFGAKGPN 155
Cdd:cd00832 81 WALADAGVdPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPrhvsaYQSFAWFYA------VNTGQISIRHGMRGPS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 156 VSSVSACATGTHSIGDAYHVIRRGdADVMIAGGAESTITPLAVGGFNVMRALSTrNDDPQAASRPFEKNRDGFVMAEGAG 235
Cdd:cd00832 155 GVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 236 IVVLEEYESARARGAHIYAELVGYGLTSDAhhltAPAPG-GEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYET 314
Cdd:cd00832 233 ILVLEDAAAARERGARVYGEIAGYAATFDP----PPGSGrPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 315 MAIKTVFKdhARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVVESALSN 394
Cdd:cd00832 309 AALAAVFG--PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVL 386
|
410
....*....|..
gi 77545124 395 SFGFGGTNASLL 406
Cdd:cd00832 387 ARGRGGFNSALV 398
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
1-409 |
7.67e-76 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 241.47 E-value: 7.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 1 MRRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRITRFDASDFPSQ--------IAGEVRDFNAEDYIEKKETRKMDLF 72
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAgaglasafIGAELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 73 IQYALAAADEAVKDSKLviDDDNAERVGVLVGAGLGGLPTIEKYHSAYlKGGYKKISP-FFIPMLITNLApGQISMRFGA 151
Cdd:PRK07103 81 AQAALAAAREAWRDAAL--GPVDPDRIGLVVGGSNLQQREQALVHETY-RDRPAFLRPsYGLSFMDTDLV-GLCSEQFGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 152 KGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTRN--DDPQAASRPFEKNRDGFV 229
Cdd:PRK07103 157 RGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 230 MAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEgaARCMAMALKNSGMQAEDVTYINAHGTSTHFN 309
Cdd:PRK07103 237 YGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 310 DLYETMAIKTVFKDHARklmVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEP-DPECdlDYVPNEARRVVV 388
Cdd:PRK07103 315 DETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESARI 389
|
410 420
....*....|....*....|.
gi 77545124 389 ESALSNSFGFGGTNASLLFRK 409
Cdd:PRK07103 390 RYALSLSFGFGGINTALVLER 410
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
149-407 |
2.32e-69 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 223.95 E-value: 2.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 149 FGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAEStITPLAVGGFNVMRALSTRnddpqaASRPFEKNRDGF 228
Cdd:PRK09185 147 LGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSPQ------PCRPFSANRDGI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 229 VMAEGAGIVVLEEYESARARgahiyaeLVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHF 308
Cdd:PRK09185 220 NIGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 309 NDLYETMAIKTVFKDHarkLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLDYVPNEARRVVV 388
Cdd:PRK09185 293 NDAMESRAVAAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAI 369
|
250
....*....|....*....
gi 77545124 389 ESALSNSFGFGGTNASLLF 407
Cdd:PRK09185 370 RYVLSNSFAFGGNNCSLIF 388
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
3-406 |
8.74e-61 |
|
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: 202.40 E-value: 8.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 3 RVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRIT--RFDASDFPSQ----------IAGEVRDFNAED----YIEKKET 66
Cdd:cd00833 2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYPDpgkpgktytrRGGFLDDVDAFDaaffGISPREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 67 RKMDLFIQYALAAADEAVKDSKLVIDDDNAERVGVLVGAGLGGLPTIEKYHSAYlkggykkISPFFIPMLITNLAPGQIS 146
Cdd:cd00833 82 EAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDE-------IDAYAATGTSRAFLANRIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 147 MRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALStrnddPQAASRPFEKNRD 226
Cdd:cd00833 155 YFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFDADAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 227 GFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTST 306
Cdd:cd00833 230 GYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 307 HFNDLYETMAIKTVF---KDHARKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPECDLD----YV 379
Cdd:cd00833 310 PLGDPIEVEALAKVFggsRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRV 389
|
410 420 430
....*....|....*....|....*....|....*.
gi 77545124 380 PNEA---------RRVVVesalsNSFGFGGTNASLL 406
Cdd:cd00833 390 PTEArpwpapagpRRAGV-----SSFGFGGTNAHVI 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
75-406 |
1.47e-56 |
|
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: 189.00 E-value: 1.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 75 YALAAADEAVKDSKLVIDDDNAERVGVLVGAGLGglpTIEKYHSAylKGGYKKISPFFIPMLITNLAPGQISMRFGAKGP 154
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGG---SPRFQVFG--ADAMRAVGPYVVTKAMFPGASGQIATPLGIHGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 155 NVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAvGGFNVMRALSTrnddPQAASRPFEKNRDGFVMAEGA 234
Cdd:cd00825 89 AYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMD-CEFDAMGALST----PEKASRTFDAAADGFVFGDGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 235 GIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYET 314
Cdd:cd00825 164 GALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKEL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 315 MAIKTVFKDHARklMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINYSEPDPecDLDYVPNEARRVVVESALSN 394
Cdd:cd00825 244 KLLRSEFGDKSP--AVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTALLN 319
|
330
....*....|..
gi 77545124 395 SFGFGGTNASLL 406
Cdd:cd00825 320 GFGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
2-245 |
1.07e-55 |
|
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: 183.99 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKSGIDRI--TRFDASDF---PSQIAGEVR----------DFNAE-DYIEKKE 65
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLfFGISPRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 66 TRKMDLFIQYALAAADEAVKDSKLVIDDDNAERVGVLVGAGLGGLptiEKYHSAYLKGGYKKISPFFIPMlITNLAPGQI 145
Cdd:pfam00109 81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDY---AALLLLDEDGGPRRGSPFAVGT-MPSVIAGRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 146 SMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTrnDDPQAASRPFeknR 225
Cdd:pfam00109 157 SYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF---A 231
|
250 260
....*....|....*....|
gi 77545124 226 DGFVMAEGAGIVVLEEYESA 245
Cdd:pfam00109 232 DGFVRGEGVGAVVLKRLSDA 251
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
253-367 |
7.32e-47 |
|
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: 156.57 E-value: 7.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 253 YAELVGYGLTSDAHHLTAPAPGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVFKDHARK--LMV 330
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 77545124 331 SSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTINY 367
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
117-403 |
7.15e-46 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 169.67 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 117 HSAYLKGGYKKISPFFIPMLITNLAPGQISMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITPL 196
Cdd:COG3321 129 YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 197 AVGGFNVMRALStrnddPQAASRPFEKNRDGFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHH--LTapAPG 274
Cdd:COG3321 209 SFILFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSngLT--APN 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 275 GEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVFKDH---ARKLMVSSTKSMTGHALGAAG--GLea 349
Cdd:COG3321 282 GPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFGQGrpaDQPCAIGSVKSNIGHLEAAAGvaGL-- 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77545124 350 VYSVLAIDRGEVPPTINYSEPDPECDLD----YVPNEA---------RRVVVesalsNSFGFGGTNA 403
Cdd:COG3321 360 IKAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTELrpwpagggpRRAGV-----SSFGFGGTNA 421
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
141-406 |
2.35e-34 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 127.95 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 141 APGQISMRFG-AKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAEStitplavggfnvmralstrnddpqaasr 219
Cdd:cd00327 46 AAGQLAYHLGiSGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 220 pfeknrdgFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLtAPAPGGEGAARCMAMALKNSGMQAEDVTYI 299
Cdd:cd00327 98 --------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 300 NAHGTSTHFNDLYETMAIKTVFKDHArkLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPTinysepdpecdldyv 379
Cdd:cd00327 169 EAHGTGTPIGDAVELALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT--------------- 231
|
250 260
....*....|....*....|....*..
gi 77545124 380 PNEARrvvveSALSNSFGFGGTNASLL 406
Cdd:cd00327 232 PREPR-----TVLLLGFGLGGTNAAVV 253
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
113-402 |
2.85e-34 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 135.52 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 113 IEKYHSAYLkgGYKKISpffIPMLITNLAPGQISMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAEST 192
Cdd:TIGR02813 162 IKKFQDQYI--HWEENS---FPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 193 ITPLAVGGFNVMRALSTRNDdpqaaSRPFEKNRDGFVMAEGAGIVVLEEYESARARGAHIYAELVGYGLTSDAHHLTAPA 272
Cdd:TIGR02813 237 NSPFMYMSFSKTPAFTTNED-----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 273 PGGEGAARCMAMALKNSGMQAEDVTYINAHGTSTHFNDLYETMAIKTVF---KDHARKLMVSSTKSMTGHALGAAGGLEA 349
Cdd:TIGR02813 312 PRPEGQAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFsqdNDQKQHIALGSVKSQIGHTKSTAGTAGM 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77545124 350 VYSVLAIDRGEVPPTINYSEPDPECDLD----YVPNEARRVVVES------ALSNSFGFGGTN 402
Cdd:TIGR02813 392 IKAVLALHHKVLPPTINVDQPNPKLDIEnspfYLNTETRPWMQREdgtprrAGISSFGFGGTN 454
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
176-406 |
3.30e-26 |
|
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: 107.03 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 176 IRRGDADVMIAGGAESTITPLAVGGFNVMRALStrnddPQAASRPFEKNRDGFVMAEGAGIVVLEEYESARARGAHIYAE 255
Cdd:smart00825 111 LRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLKRLSDALRDGDPILAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 256 LVGYGLTSDAHH--LTAPapggegaarcmamalkNSGMQaedvtyinahgtsthfndlyetmaiktvfkdharkLMVSST 333
Cdd:smart00825 186 IRGSAVNQDGRSngITAP----------------SGPAQ-----------------------------------LLIGSV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 334 KSMTGHALGAAG--GLeaVYSVLAIDRGEVPPTINYSEPDPECDLD----YVPNEA---------RRVVVesalsNSFGF 398
Cdd:smart00825 215 KSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELtpwpppgrpRRAGV-----SSFGF 287
|
....*...
gi 77545124 399 GGTNASLL 406
Cdd:smart00825 288 GGTNAHVI 295
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
2-388 |
3.50e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 54.96 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 2 RRVVVTGIGTISALGNGVEKNWQSLLAGKsgidRITRFDASDF---PSQIAGEVrDFNAEdyIEKK-ETRKMDLFiQ--- 74
Cdd:PRK06519 6 NDVVITGIGLVSSLGEGLDAHWNALSAGR----PQPNVDTETFapyPVHPLPEI-DWSQQ--IPKRgDQRQMETW-Qrlg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 75 -YA--LAAADEAVKDSK-------LVIDDDNAERVGVLVgaglgglptiekyhSAYLKGGYKKISP-------------- 130
Cdd:PRK06519 78 tYAagLALDDAGIKGNEellstmdMIVAAGGGERDIAVD--------------TAILNEARKRNDRgvllnerlmtelrp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 131 -FFIPMLiTNLAPGQISMRFGAKGPNVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAESTITP-----LAVGGFNvm 204
Cdd:PRK06519 144 tLFLAQL-SNLLAGNISIVHKVTGSSRTFMGEESAGVSAIEIAFARIASGQSDHALVGGAYNAERPdmlllYELGGLL-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 205 ralsTRNDDPQAASRPFEKNrDGFVMAEGAGIVVLEEYESARARGAHIYAELVgyGLTSDahhLTAPAPGgeGAARCMAM 284
Cdd:PRK06519 221 ----LKGGWAPVWSRGGEDG-GGFILGSGGAFLVLESREHAEARGARPYARIS--GVESD---RARRAPG--DLEASLER 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 285 ALKNSGMQAEDVTYINAhgtSTHFNDLyeTMAIKTVFKDHArKLMVSSTKSMTGHALGAAGGLEAVYSVLAIDRGEVPPT 364
Cdd:PRK06519 289 LLKPAGGLAAPTAVISG---ATGAHPA--TAEEKAALEAAL-AGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPP 362
|
410 420
....*....|....*....|....
gi 77545124 365 INysePDPECDLDyvpNEARRVVV 388
Cdd:PRK06519 363 FD---ASGEKPMS---GAAREAVV 380
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
165-299 |
3.04e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 45.78 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 165 GTHSIGDAYHVIRRGDADVMIAGGAESTITPLAVGGFNVMRALSTrnddpqaasrpfEKNRDGFVMAEGAGIVVLEEYES 244
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPRVLVAGVDSLLTGPTLAHYEARDRLLT------------SQNSNGFIPGEAAAAVLLGRPAG 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 77545124 245 ARARGAHIYAelVGYGLTSDAHHLTAPAPG-GEGAARCMAMALKNSGMQAEDVTYI 299
Cdd:PRK06147 204 GEAPGLPLLG--LGLGREPAPVGESEDLPLrGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
161-242 |
1.42e-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: 43.52 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77545124 161 ACATGTHSIGDAYHVIRRGDADVMIAGGAES-TITPLAVGGFNVMRALSTRNDDPQAASRpFEKNRDGFVMAEGAGIVVl 239
Cdd:COG0183 87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESmSRAPMLLPKARWGYRMNAKLVDPMINPG-LTDPYTGLSMGETAENVA- 164
|
...
gi 77545124 240 EEY 242
Cdd:COG0183 165 ERY 167
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
161-192 |
6.34e-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: 41.70 E-value: 6.34e-04
10 20 30
....*....|....*....|....*....|..
gi 77545124 161 ACATGTHSIGDAYHVIRRGDADVMIAGGAEST 192
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVESM 114
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
161-192 |
7.25e-04 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 41.44 E-value: 7.25e-04
10 20 30
....*....|....*....|....*....|..
gi 77545124 161 ACATGTHSIGDAYHVIRRGDADVMIAGGAEST 192
Cdd:TIGR01930 82 QCASGLQAVILAAQLIRAGEADVVVAGGVESM 113
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
149-200 |
3.90e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 39.06 E-value: 3.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 77545124 149 FGAKGPnVSSVSACATGTHSIGDAYHVIRRGDADVMIAGGAES-----TITPLAVGG 200
Cdd:PRK12578 70 LTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKmtevdTSTSLAIGG 125
|
|
| |
