|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
26-461 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 851.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 26 SYHSHRRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDLKMKSFDEETKLYTFDQLSSKVAAFVPYGSNPGEFD 105
Cdd:PLN02836 1 PPLPTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLKMKSEDEETQLYTLDQLPSRVAALVPRGTGPGDFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 106 EALWLNSKAVANFIGYAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILV 185
Cdd:PLN02836 81 EELWLNSRSSSRFIGYALCAADEALSDARWLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 186 NMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEA 265
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKFNSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 266 SRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQID 345
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 346 YVNAHATSTPIGDAVEARAIKTVFSEHATSGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFD 425
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEHATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFD 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 22325473 426 KRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLFASI 461
Cdd:PLN02836 401 DGFVPLTASKAMLIRAALSNSFGFGGTNASLLFTSP 436
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
31-458 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 587.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDLkmksfdeetklytfDQLSSKVAAFVPyGSNPGEFDEALwl 110
Cdd:PRK07314 2 RRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDT--------------SDLAVKIAGEVK-DFNPDDYMSRK-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVANFIGYAVCAADEALRDAEWLPTEEEeKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNMASG 190
Cdd:PRK07314 65 EARRMDRFIQYGIAAAKQAVEDAGLEITEEN-ADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 191 HVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfNSSPQEASRPFD 270
Cdd:PRK07314 144 HVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTR-NDDPERASRPFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 271 CDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAH 350
Cdd:PRK07314 223 KDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 351 ATSTPIGDAVEARAIKTVFSEHATsgTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMP 430
Cdd:PRK07314 303 GTSTPAGDKAETQAIKRVFGEHAY--KVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVP 380
|
410 420
....*....|....*....|....*...
gi 22325473 431 LtTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK07314 381 N-EARERKIDYALSNSFGFGGTNASLVF 407
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
31-458 |
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: 572.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTlddlkmkSFDEEtklytfdQLSSKVAAFVPygsnpgEFDEALWL 110
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPIT-------RFDAS-------DLPVKIAGEVK------DFDPEDYI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAV---ANFIGYAVCAADEALRDAEWlPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNM 187
Cdd:TIGR03150 61 DKKEArrmDRFIQYALAAAKEAVEDSGL-DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 188 ASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTkFNSSPQEASR 267
Cdd:TIGR03150 140 AAGQISIRYGAKGPNHAVVTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALST-RNDDPEKASR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 268 PFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYV 347
Cdd:TIGR03150 219 PFDKDRDGFVMGEGAGVLVLEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 348 NAHATSTPIGDAVEARAIKTVFSEHATSgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKR 427
Cdd:TIGR03150 299 NAHGTSTPLGDKAETKAIKKVFGDHAYK--LAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLD 376
|
410 420 430
....*....|....*....|....*....|.
gi 22325473 428 FMPLtTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:TIGR03150 377 YVPN-EAREAKIDYALSNSFGFGGTNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
31-458 |
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: 562.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRgltlddlKMKSFDEEtklytfdQLSSKVAAFVPygsnpgEFDEALWL 110
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIR-------PITRFDAS-------GLPVRIAGEVK------DFDPEEYL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVAN---FIGYAVCAADEALRDAEWLPTEEEeKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNM 187
Cdd:COG0304 61 DRKELRRmdrFTQYALAAAREALADAGLDLDEVD-PDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 188 ASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfNSSPQEASR 267
Cdd:COG0304 140 AAGHVSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTR-NDDPEKASR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 268 PFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYV 347
Cdd:COG0304 219 PFDKDRDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 348 NAHATSTPIGDAVEARAIKTVFSEHAtsGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKR 427
Cdd:COG0304 299 NAHGTSTPLGDAAETKAIKRVFGDHA--YKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLD 376
|
410 420 430
....*....|....*....|....*....|.
gi 22325473 428 FMPlTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:COG0304 377 YVP-NEAREAKIDYALSNSFGFGGHNASLVF 406
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
31-458 |
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: 560.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDlkmksfdeetklytFDQLSSKVAAFVPygsnpgEFDEALWL 110
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFD--------------ASGFPSRIAGEVP------DFDPEDYL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVA---NFIGYAVCAADEALRDAEWLPtEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNM 187
Cdd:cd00834 61 DRKELRrmdRFAQFALAAAEEALADAGLDP-EELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 188 ASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSsPQEASR 267
Cdd:cd00834 140 AAGQVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDD-PEKASR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 268 PFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYV 347
Cdd:cd00834 219 PFDKDRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 348 NAHATSTPIGDAVEARAIKTVFSEHATSgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKR 427
Cdd:cd00834 299 NAHGTSTPLNDAAESKAIKRVFGEHAKK--VPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLD 376
|
410 420 430
....*....|....*....|....*....|.
gi 22325473 428 FMPLtTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:cd00834 377 YVPN-EAREAPIRYALSNSFGFGGHNASLVF 406
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
29-458 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 518.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 29 SHRRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDLkmksfdeetklytfDQLSSKVAAFVPYGSNPGE--FDE 106
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPV--------------GDLATKIGGQVPDLAEDAEagFDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 107 ALWLNSK---AVANFIGYAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKI 183
Cdd:PRK06333 68 DRYLDPKdqrKMDRFILFAMAAAKEALAQAGWDPDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 184 LVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQ 263
Cdd:PRK06333 148 LTNMAAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRFNDAPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 264 EASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQ 343
Cdd:PRK06333 228 QASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 344 IDYVNAHATSTPIGDAVEARAIKTVFsehATSGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPI 423
Cdd:PRK06333 308 VQHLNAHATSTPVGDLGEVAAIKKVF---GHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPA 384
|
410 420 430
....*....|....*....|....*....|....*
gi 22325473 424 FDKRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK06333 385 AEGLDVVANKARPMDMDYALSNGFGFGGVNASILF 419
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
40-461 |
6.71e-177 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 501.92 E-value: 6.71e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 40 MVTPLGRGVETTWRRLIDGECGIRGLTLDDLKMKSFDEETKLYTFDQ--LSSKVAAFVPygsnPGEFDEALWLNSKAVAN 117
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKFLPDCIPEQKALENLVaaMPCQIAAEVD----QSEFDPSDFAPTKRESR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 118 FIGYAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNMASGHVSMKYG 197
Cdd:PTZ00050 77 ATHFAMAAAREALADAKLDILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 198 FQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFV 277
Cdd:PTZ00050 157 LKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKYNDDPQRASRPFDKDRAGFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 278 IGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCP-NQIDYVNAHATSTPI 356
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANINiNDVDYVNAHATSTPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 357 GDAVEARAIKTVFSEHATSgTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMPLTTSKK 436
Cdd:PTZ00050 317 GDKIELKAIKKVFGDSGAP-KLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHP 395
|
410 420
....*....|....*....|....*.
gi 22325473 437 ML-VRTAMSNSFGFGGTNASLLFASI 461
Cdd:PTZ00050 396 LQsIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
31-458 |
5.08e-137 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 399.88 E-value: 5.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLddlkmksFDEEtklytfdQLSSKVAAFVPygsnpgEFDEALWL 110
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITL-------FDAS-------DFPVQIAGEIT------DFDPTEVM 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVAN---FIGYAVCAADEALRDAEWLPtEEEEKERTGVSIGGGIGSICDIvEAAQLICEKR-LRRLSPFFIPKILVN 186
Cdd:PRK08439 62 DPKEVKKadrFIQLGLKAAREAMKDAGFLP-EELDAERFGVSSASGIGGLPNI-EKNSIICFEKgPRKISPFFIPSALVN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 187 MASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfNSSPQEAS 266
Cdd:PRK08439 140 MLGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTR-NDDPKKAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 267 RPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDgkGAVLAMTRALRQSGlcPNQIDY 346
Cdd:PRK08439 219 RPFDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAG--NPKIDY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 347 VNAHATSTPIGDAVEARAIKTVFSEHATSGTLafSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDK 426
Cdd:PRK08439 295 INAHGTSTPYNDKNETAALKELFGSKEKVPPV--SSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDL 372
|
410 420 430
....*....|....*....|....*....|..
gi 22325473 427 RFMPlTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK08439 373 DYIP-NVARKAELNVVMSNSFGFGGTNGVVIF 403
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
29-461 |
1.32e-129 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 381.27 E-value: 1.32e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 29 SHRRVVVTGLGMVTPLGRGVETTWRRLIDGECGIrgltlddLKMKSFDEEtklytfdQLSSKVAAFVPygsnpgEFDEAL 108
Cdd:PRK08722 2 SKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGI-------VNIEHFDTT-------NFSTRFAGLVK------DFNCEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 109 WLNSKAVAN---FIGYAVCAADEALRDAEWLPTEEEEKErtGVSIGGGIGSICDIVEAA-QLICEKRLRRLSPFFIPKIL 184
Cdd:PRK08722 62 YMSKKDARKmdlFIQYGIAAGIQALDDSGLEVTEENAHR--IGVAIGSGIGGLGLIEAGhQALVEKGPRKVSPFFVPSTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 185 VNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfNSSPQE 264
Cdd:PRK08722 140 VNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTR-NDEPQK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 265 ASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQI 344
Cdd:PRK08722 219 ASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 345 DYVNAHATSTPIGDAVEARAIKTVFSEHATSGTLAfSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIF 424
Cdd:PRK08722 299 GYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVLV-SSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGL 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 22325473 425 DKRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLFASI 461
Cdd:PRK08722 378 DIDLVPHTARKVESMEYAICNSFGFGGTNGSLIFKKM 414
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
141-458 |
4.24e-110 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 329.00 E-value: 4.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 141 EEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDAT 220
Cdd:PRK14691 23 EKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 221 RMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKI 300
Cdd:PRK14691 103 RMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHFNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 301 YAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEhatSGTLAF 380
Cdd:PRK14691 183 LAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE---SNALAI 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22325473 381 SSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNIIAGNAQPHDMTYALSNGFGFAGVNASILL 337
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
31-458 |
2.08e-97 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 298.51 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIrgltlddlkmkSFDEETKLYTFdqlSSKVAAFVPYgsNPGEfdealwL 110
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGI-----------TFSPEFAEMGM---RSQVWGNVKL--DPTG------L 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVANFIG----YAVCAADEALRDAEwLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKR-LRRLSPFFIPKILV 185
Cdd:PRK07967 60 IDRKVMRFMGdasaYAYLAMEQAIADAG-LSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPRgPKRVGPYAVTKAMA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 186 NMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAgFSRSRALSTKFNSSPQEA 265
Cdd:PRK07967 139 STVSACLATPFKIKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKYNDTPEKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 266 SRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPpeDGKGAVLAMTRALrqSGLcPNQID 345
Cdd:PRK07967 218 SRAYDANRDGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATV-DTPID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 346 YVNAHATSTPIGDAVEARAIKTVFSEHATsgtlAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFD 425
Cdd:PRK07967 293 YINTHGTSTPVGDVKELGAIREVFGDKSP----AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAA 368
|
410 420 430
....*....|....*....|....*....|....*
gi 22325473 426 KrfMPLTTSKK--MLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK07967 369 G--MPIVTETTdnAELTTVMSNSFGFGGTNATLVF 401
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
31-459 |
5.55e-97 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 301.90 E-value: 5.55e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIrgltlddlkmksfdeeTKLYTFD--QLSSKVAAFVPYGSNPGEFDEAL 108
Cdd:PLN02787 129 RRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGI----------------SEIERFDcsQFPTRIAGEIKSFSTDGWVAPKL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 109 wlnSKAVANFIGYAVCAADEALRDAEWlpTEEEEKERTGVSIGGGIGSIC-------DIVEAAQLicekRLRRLSPFFIP 181
Cdd:PLN02787 193 ---SKRMDKFMLYLLTAGKKALADGGI--TEDVMKELDKTKCGVLIGSAMggmkvfnDAIEALRI----SYRKMNPFCVP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 182 KILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfNSS 261
Cdd:PLN02787 264 FATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQR-NDD 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 262 PQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCP 341
Cdd:PLN02787 343 PTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 342 NQIDYVNAHATSTPIGDAVEARAIKTVFSEHAtsgTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPD 421
Cdd:PLN02787 423 EDVNYINAHATSTKAGDLKEYQALMRCFGQNP---ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPE 499
|
410 420 430
....*....|....*....|....*....|....*...
gi 22325473 422 PIFDKRFMPLTTSKKMLVRTAMSNSFGFGGTNASLLFA 459
Cdd:PLN02787 500 SGVDTKVLVGPKKERLDIKVALSNSFGFGGHNSSILFA 537
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
33-458 |
3.80e-96 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 295.87 E-value: 3.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 33 VVVTGLGMVTPLGRGVETTWRRLIDGECGIRglTLDDlkmkSFDEEtklytFDqLSSKVAafvpyGSNPGEFDEALwlnS 112
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIR--TLDD----PFVEE-----FD-LPVRIG-----GHLLEEFDHQL---T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 113 KAVANFIGY----AVCAADEALRDAEwlpTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVNMA 188
Cdd:PRK07910 74 RVELRRMSYlqrmSTVLGRRVWENAG---SPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 189 SGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRP 268
Cdd:PRK07910 151 AAAVGLERHAKAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMSTNNDDPAGACRP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 269 FDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVN 348
Cdd:PRK07910 231 FDKDRDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 349 AHATSTPIGDAVEARAIKTVFSEHATsgtlAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRF 428
Cdd:PRK07910 311 AHATGTSVGDVAEGKAINNALGGHRP----AVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDV 386
|
410 420 430
....*....|....*....|....*....|
gi 22325473 429 MPlTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK07910 387 VA-GEPRPGNYRYAINNSFGFGGHNVALAF 415
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
24-460 |
1.03e-90 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 281.90 E-value: 1.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 24 SSSYHSHR-R--VVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLT---LDDLK------MKSFDEETklYTFDQLSSKV 91
Cdd:PRK06501 1 MTAYRDHLgRpiVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITrfpTEGLRtriagtVDFLPESP--FGASALSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 92 A------AFVPYGSNPGEFDEALWLnskAVAnfigyavcaadealrdaewlPTEEEEKERTGVSIGGGIGsicDIVEAAQ 165
Cdd:PRK06501 79 ArlaaeeALAQAGIGKGDFPGPLFL---AAP--------------------PVELEWPARFALAAAVGDN---DAPSYDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 166 LICEKRLRRLSPFFiPKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSV 245
Cdd:PRK06501 133 LLRAARGGRFDALH-ERFQFGSIADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 246 AGFSRSRALSTKfNSSPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKG 325
Cdd:PRK06501 212 IRFSLLSALSTQ-NDPPEKASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 326 AVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATSgtLAFSSTKGATGHLLGAAGAVEAIFSILA 405
Cdd:PRK06501 291 AIGAIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAVFGERLAS--IPVSSNKSMIGHTLTAAGAVEAVFSLLT 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 22325473 406 IHHGVAPMTLNVKNPDPIFDKRFMPlTTSKKMLVRTAMSNSFGFGGTNASLLFAS 460
Cdd:PRK06501 369 IQTGRLPPTINYDNPDPAIPLDVVP-NVARDARVTAVLSNSFGFGGQNASLVLTA 422
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
31-458 |
3.52e-84 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 264.54 E-value: 3.52e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRgltlddlKMKSFDEetklytFDQLSSKVAAFVPYGSNPGEFdealwl 110
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVR-------RMPEWDR------YDGLNTRLAAPIDDFELPAHY------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVANfIG----YAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSICDIVEAAQLICEKRLRRLSPFFIPKILVN 186
Cdd:PRK09116 63 TRKKIRS-MGrvslMATRASELALEDAGLLGDPILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTYVRMMPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 187 MASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsIDALSVAGFSRSRALSTKfNSSPQEAS 266
Cdd:PRK09116 142 TTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEE-LCPTEAAVFDTLFATSTR-NDAPELTP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 267 RPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGavLAMTRALRQSGLCPNQIDY 346
Cdd:PRK09116 220 RPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 347 VNAHATSTPIGDAVEARAIKTVFSEHatsgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDK 426
Cdd:PRK09116 298 VNAHGTATDRGDIAESQATAAVFGAR-----MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACGA 372
|
410 420 430
....*....|....*....|....*....|..
gi 22325473 427 RFMPLTTSKKMLVRTAMSNSFGFGGTNASLLF 458
Cdd:PRK09116 373 LDYIMGEAREIDTEYVMSNNFAFGGINTSLIF 404
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
32-456 |
1.59e-80 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 254.21 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 32 RVVVTGLGMVTPLGrGVETTWRRLIDGECGIrgltlddlkmksfdeetKLYT-FDQLSSKVAAFVpyGSNPGEfdealwl 110
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGI-----------------KLHQpFPELPPLPLGLI--GNQPSS------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 nskaVANFIGYAVcaaDEALRDAEWLPTEEEekertgvsigggigsiCDIV----EAAQLICEKRLRRLSPFFIP----- 181
Cdd:PRK05952 56 ----LEDLTKTVV---TAALKDAGLTPPLTD----------------CGVVigssRGCQGQWEKLARQMYQGDDSpdeel 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 182 ------KILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALS 255
Cdd:PRK05952 113 dlenwlDTLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 256 tkfnsspQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALR 335
Cdd:PRK05952 193 -------KTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 336 QSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEhatsgTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTL 415
Cdd:PRK05952 266 RSGLTPEDIDYIHAHGTATRLNDQREANLIQALFPH-----RVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCV 340
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 22325473 416 NVKNPDpiFDKRFmpLTTSKKMLVRTAMSNSFGFGGTNASL 456
Cdd:PRK05952 341 GLQEPE--FDLNF--VRQAQQSPLQNVLCLSFGFGGQNAAI 377
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
197-459 |
1.52e-73 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 236.66 E-value: 1.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 197 GFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsIDALSVAGFSRSRALSTkfnsspqEASRPFDCDRDGF 276
Cdd:PRK09185 148 GLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLSP-------QPCRPFSANRDGI 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 277 VIGEGSGVIVLEeyehakrRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPI 356
Cdd:PRK09185 220 NIGEAAAFFLLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 357 GDAVEARAIKTVFSEHatsgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMpLTTSKK 436
Cdd:PRK09185 293 NDAMESRAVAAVFGDG-----VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYL-VENAQA 366
|
250 260
....*....|....*....|...
gi 22325473 437 MLVRTAMSNSFGFGGTNASLLFA 459
Cdd:PRK09185 367 LAIRYVLSNSFAFGGNNCSLIFG 389
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
31-457 |
9.25e-73 |
|
"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: 235.03 E-value: 9.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETT---WRRLIDGECGIRGLTLDDLKMKSFdeetklytfdqlsskVAAFVPYGSNPGEFdea 107
Cdd:cd00828 1 SRVVITGIGVVSPHGEGCDEVeefWEALREGRSGIAPVARLKSRFDRG---------------VAGQIPTGDIPGWD--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 108 lWLNSKAVANFIGYAVCAADEALRDAEWLPTEEEEKERTGVSIGGGIGSIcdivEAAQLICEKRLRRLSPFFIPK--ILV 185
Cdd:cd00828 63 -AKRTGIVDRTTLLALVATEEALADAGITDPYEVHPSEVGVVVGSGMGGL----RFLRRGGKLDARAVNPYVSPKwmLSP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 186 NMASGHVSMKYGF-QGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDaLSVAGFSRSRALSTKFNSsPQE 264
Cdd:cd00828 138 NTVAGWVNILLLSsHGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLE-EGLSGFANMGALSTAEEE-PEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 265 ASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPeDGKGAVLAMTRALRQSGLCPNQI 344
Cdd:cd00828 216 MSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPA-GGKGIARAIRTALAKAGLSLDDL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 345 DYVNAHATSTPIGDAVEARAIKTVFSEHATSgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIF 424
Cdd:cd00828 295 DVISAHGTSTPANDVAESRAIAEVAGALGAP--LPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV 372
|
410 420 430
....*....|....*....|....*....|....
gi 22325473 425 DKRFMP-LTTSKKMLVRTAMSNSFGFGGTNASLL 457
Cdd:cd00828 373 EHLSVVgLSRDLNLKVRAALVNAFGFGGSNAALV 406
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
32-457 |
1.85e-65 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 216.05 E-value: 1.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 32 RVVVTGLGMVTPLGRGVETTWRRLIDGECGIRgltlddlKMKSFDEETKLYTFDQLSSK-VAAFVPYGSNPGEFDEALW- 109
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFG-------VMRRPGRQVPDDAGAGLASAfIGAELDSLALPERLDAKLLr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 110 ---LNSKAvanfigyAVCAADEALRDAEWLPTEeeeKERTGVsigggigsicdIV--------EAAQLicEKRLRRLSPF 178
Cdd:PRK07103 76 rasLSAQA-------ALAAAREAWRDAALGPVD---PDRIGL-----------VVggsnlqqrEQALV--HETYRDRPAF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 179 FIPK-ILVNMASGHV---SMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRAL 254
Cdd:PRK07103 133 LRPSyGLSFMDTDLVglcSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 255 ST-KFNSSPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPpeDGKGAVLAMTRA 333
Cdd:PRK07103 213 GSdRFADEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 334 LRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATsgtlaFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPM 413
Cdd:PRK07103 291 LRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAHAW-----INATKSLTGHGLSAAGIVELIATLLQMRAGFLHP 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22325473 414 TLNVKNP-DPIFdkRFMPlTTSKKMLVRTAMSNSFGFGGTNASLL 457
Cdd:PRK07103 366 SRNLDEPiDERF--RWVG-STAESARIRYALSLSFGFGGINTALV 407
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
165-457 |
2.17e-65 |
|
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: 216.27 E-value: 2.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 165 QLICEKRLRRLSPFFIPKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALS 244
Cdd:cd00833 126 LELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDM 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 245 VAGFSRSRALStkfnssPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMS--GDAHHITQPpeD 322
Cdd:cd00833 206 FVGFSKAGMLS------PDGRCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITAP--S 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 323 GKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEH-ATSGTLAFSSTKGATGHLLGAAGAVEAIF 401
Cdd:cd00833 278 GEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSrSADQPLLIGSVKSNIGHLEAAAGLAGLIK 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22325473 402 SILAIHHGVAPMTLNVKNPDPIFD---KRFMPLTTSK----KMLVRTAMSNSFGFGGTNASLL 457
Cdd:cd00833 358 VVLALEHGVIPPNLHFETPNPKIDfeeSPLRVPTEARpwpaPAGPRRAGVSSFGFGGTNAHVI 420
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
121-457 |
1.02e-53 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 182.84 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 121 YAVCAADEALRDAEwLPTEEEEKERTGVSIGGGIGsicdiVEAAQLICEKRLRRLSPFFIPKILVNMASGHVSMKYGFQG 200
Cdd:cd00825 14 LGFEAAERAIADAG-LSREYQKNPIVGVVVGTGGG-----SPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 201 PNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRAlstkfnSSPQEASRPFDCDRDGFVIGE 280
Cdd:cd00825 88 PAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGAL------STPEKASRTFDAAADGFVFGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 281 GSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAV 360
Cdd:cd00825 162 GAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 361 EARAIKTVFSEHatsgTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFDKRFMPLTTSKkmlVR 440
Cdd:cd00825 242 ELKLLRSEFGDK----SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETTPRE---LR 314
|
330
....*....|....*..
gi 22325473 441 TAMSNSFGFGGTNASLL 457
Cdd:cd00825 315 TALLNGFGLGGTNATLV 331
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
31-457 |
2.07e-50 |
|
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: 176.01 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTlddlkmkSFDEEtklytfdQLSSKVAAFVPygsnpgEFDEALWL 110
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPIT-------RFDPS-------GYPARLAGEVP------DFDAAEHL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 111 NSKAVAN---FIGYAVCAADEALRDAEWLPTEEEEKERTgvsigggigsicdIVEAA------------QLICEKRLRRL 175
Cdd:cd00832 61 PGRLLPQtdrMTRLALAAADWALADAGVDPAALPPYDMG-------------VVTASaaggfefgqrelQKLWSKGPRHV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 176 SPF--FIPKILVNmaSGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGdADVMVAGGTESSIDALSVAGFSRSRA 253
Cdd:cd00832 128 SAYqsFAWFYAVN--TGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 254 LSTkfNSSPQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAhhitqPPEDGKGAVL--AMT 331
Cdd:cd00832 205 LST--SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDP-----PPGSGRPPGLarAIR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 332 RALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATSGTlafsSTKGATGHLLGAAGAVEAIFSILAIHHGVA 411
Cdd:cd00832 278 LALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFGPRGVPVT----APKTMTGRLYAGGAPLDVATALLALRDGVI 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 22325473 412 PMTLNVKNPDPIFDKRFMpLTTSKKMLVRTAMSNSFGFGGTNASLL 457
Cdd:cd00832 354 PPTVNVTDVPPAYGLDLV-TGRPRPAALRTALVLARGRGGFNSALV 398
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
31-293 |
2.69e-49 |
|
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: 168.58 E-value: 2.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 31 RRVVVTGLGMVTPLGRGVETTWRRLIDGECGIRGLTLDDlkmksfDEETKLYTFD-QLSSKVAAFVPYGSNPGEFDEALW 109
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPADR------WDPDKLYDPPsRIAGKIYTKWGGLDDIFDFDPLFF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 110 LNSKAVANFIG----YAVCAADEALRDAEWLPtEEEEKERTGVSIGGGIGsicDIVEAAQLICEKRLRRLSPFFIPKIlV 185
Cdd:pfam00109 75 GISPREAERMDpqqrLLLEAAWEALEDAGITP-DSLDGSRTGVFIGSGIG---DYAALLLLDEDGGPRRGSPFAVGTM-P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 186 NMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKfnsSPQEA 265
Cdd:pfam00109 150 SVIAGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD---GPCKA 226
|
250 260
....*....|....*....|....*...
gi 22325473 266 SRPFDcdrDGFVIGEGSGVIVLEEYEHA 293
Cdd:pfam00109 227 FDPFA---DGFVRGEGVGAVVLKRLSDA 251
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
301-418 |
9.44e-49 |
|
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: 162.74 E-value: 9.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 301 YAELCGYGMSGDAHHITQPPEDGKGAVLAMTRALRQSGLCPNQIDYVNAHATSTPIGDAVEARAIKTVFSEHATSGTLAF 380
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 22325473 381 SSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVK 418
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
186-454 |
2.97e-44 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 166.59 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 186 NMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALStkfnssPQEA 265
Cdd:COG3321 151 SVLAGRISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS------PDGR 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 266 SRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMS--GDAHHITQPpeDGKGAVLAMTRALRQSGLCPNQ 343
Cdd:COG3321 225 CRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRSNGLTAP--NGPAQAAVIRRALADAGVDPAT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 344 IDYVNAHATSTPIGDAVEARAIKTVFSEH-ATSGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDP 422
Cdd:COG3321 303 VDYVEAHGTGTPLGDPIEAAALTAAFGQGrPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNP 382
|
250 260 270
....*....|....*....|....*....|....*....
gi 22325473 423 -I-FDK-RFMPLTTSKKMLV----RTAMSNSFGFGGTNA 454
Cdd:COG3321 383 hIdFENsPFYVNTELRPWPAgggpRRAGVSSFGFGGTNA 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
181-453 |
1.45e-38 |
|
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: 149.77 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 181 PKILVNMASGHVSMKYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTkfns 260
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTT---- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 261 spQEASRPFDCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAH--HITQPPEDGKGAvlAMTRALRQSG 338
Cdd:TIGR02813 254 --NEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKfkSIYAPRPEGQAK--ALKRAYDDAG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 339 LCPNQIDYVNAHATSTPIGDAVEARAIKTVFSE-HATSGTLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNV 417
Cdd:TIGR02813 330 FAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQdNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINV 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 22325473 418 KNPDPIFDKRFMPLTTSKKM---------LVRTAMSNSFGFGGTN 453
Cdd:TIGR02813 410 DQPNPKLDIENSPFYLNTETrpwmqredgTPRRAGISSFGFGGTN 454
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
188-457 |
6.10e-33 |
|
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: 125.25 E-value: 6.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 188 ASGHVSMKYGFQ-GPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGGTESsidalsvagfsrsralstkfnsspqeas 266
Cdd:cd00327 46 AAGQLAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE---------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 267 rpfdcdrdgFVIGEGSGVIVLEEYEHAKRRGAKIYAELCGYGMSGDAHHItQPPEDGKGAVLAMTRALRQSGLCPNQIDY 346
Cdd:cd00327 98 ---------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 347 VNAHATSTPIGDAVEARAIKTVFSEHAtsgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTlnvknPDPIfdk 426
Cdd:cd00327 168 VEAHGTGTPIGDAVELALGLDPDGVRS----PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----PREP--- 235
|
250 260 270
....*....|....*....|....*....|.
gi 22325473 427 rfmplttskkmlvRTAMSNSFGFGGTNASLL 457
Cdd:cd00327 236 -------------RTVLLLGFGLGGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
207-457 |
4.72e-22 |
|
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: 95.86 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 207 TACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALStkfnssPQEASRPFDCDRDGFVIGEGSGVIV 286
Cdd:smart00825 95 TACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS------PDGRCKTFDASADGYVRGEGVGVVV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 287 LEEYEHAKRRGAKIYAELCGygmSGdahhITQppeDGKGAVLAMtralrqsglcPNqidyVNAHatstpigdavearaik 366
Cdd:smart00825 169 LKRLSDALRDGDPILAVIRG---SA----VNQ---DGRSNGITA----------PS----GPAQ---------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 367 tvfsehatsgtLAFSSTKGATGHLLGAAGAVEAIFSILAIHHGVAPMTLNVKNPDPIFD---KRFMPLTTSK----KMLV 439
Cdd:smart00825 209 -----------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDleeSPLRVPTELTpwppPGRP 277
|
250
....*....|....*...
gi 22325473 440 RTAMSNSFGFGGTNASLL 457
Cdd:smart00825 278 RRAGVSSFGFGGTNAHVI 295
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
159-347 |
5.72e-07 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 51.17 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 159 DIVEAAQLIC---EKRLRRLSPFfiPKILVNMASGHVSmkYGFQGPNHAAVTACATGAHSIGDATRMIQFGDADVMVAGG 235
Cdd:PRK06147 84 DASEAPLLLCvaeEERPGRPPDL--EERLLRELEARLG--LRLEPGSAVIARGRVSGAVALAQARRLIAAGGCPRVLVAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 236 TESSIDALSVAGFSRSRALSTKFNSspqeasrpfdcdrDGFVIGEGSGVIVLEEYEHAKRRGAKIYaelcGYGMSGDAHH 315
Cdd:PRK06147 160 VDSLLTGPTLAHYEARDRLLTSQNS-------------NGFIPGEAAAAVLLGRPAGGEAPGLPLL----GLGLGREPAP 222
|
170 180 190
....*....|....*....|....*....|....*
gi 22325473 316 ITQP---PEDGKGAVLAMTRALRQSGLCPNQIDYV 347
Cdd:PRK06147 223 VGESedlPLRGDGLTQAIRAALAEAGCGLEDMDYR 257
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
204-238 |
7.96e-06 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 47.75 E-value: 7.96e-06
10 20 30
....*....|....*....|....*....|....*...
gi 22325473 204 AAVT---ACATGAHSIGDATRMIQFGDADVMVAGGTES 238
Cdd:COG0183 80 PAVTvnrVCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
208-277 |
3.15e-05 |
|
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: 45.93 E-value: 3.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 208 ACATGAHSIGDATRMIQFGDADVMVAGGTESsidaLSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFV 277
Cdd:cd00751 83 VCGSGLQAVALAAQSIAAGEADVVVAGGVES----MSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFT 148
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
278-396 |
7.36e-05 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 44.70 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325473 278 IGEGSGVIVLEEYEHAKRRGAKIYAELCGYGmsgDAhhiTQPPEDGKGA-VLAMTRALRQSGLCPNQIDY--VNahatst 354
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGYA---DA---AQAPELFTTApALAIPKALKHAGLEASQVDYyeIN------ 317
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 22325473 355 pigdavEARAIKTVfsehATSGTLAFSSTK-----GAT--GHLLGAAGA 396
Cdd:PLN02644 318 ------EAFSVVAL----ANQKLLGLDPEKvnvhgGAVslGHPIGCSGA 356
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
270-304 |
1.51e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 43.79 E-value: 1.51e-04
10 20 30
....*....|....*....|....*....|....*
gi 22325473 270 DCDRDGFVIGEGSGVIVLEEYEHAKRRGAKIYAEL 304
Cdd:PRK06519 233 GEDGGGFILGSGGAFLVLESREHAEARGARPYARI 267
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
209-238 |
1.59e-04 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 43.99 E-value: 1.59e-04
10 20 30
....*....|....*....|....*....|
gi 22325473 209 CATGAHSIGDATRMIQFGDADVMVAGGTES 238
Cdd:PRK05790 88 CGSGLKAVALAAQAIRAGDADIVVAGGQES 117
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
208-282 |
1.46e-03 |
|
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: 40.67 E-value: 1.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22325473 208 ACATGAHSIGDATRMIQFGDADVMVAGGTESSIDALSVAGFSRSRALSTKFNSSPQEASRPFDCDRDGFVIGEGS 282
Cdd:TIGR01930 82 QCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDARLKDLTDANTGLPMGVTA 156
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
208-238 |
2.34e-03 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 39.59 E-value: 2.34e-03
10 20 30
....*....|....*....|....*....|.
gi 22325473 208 ACATGAHSIGDATRMIQFGDADVMVAGGTES 238
Cdd:pfam00108 84 VCGSGLKAVYLAAQSIASGDADVVLAGGVES 114
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
209-238 |
5.64e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 38.93 E-value: 5.64e-03
10 20 30
....*....|....*....|....*....|
gi 22325473 209 CATGAHSIGDATRMIQFGDADVMVAGGTES 238
Cdd:PRK08235 88 CASGLRAVTLADQIIRAGDASVIVAGGMES 117
|
|
| |
