|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
1-416 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 684.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 1 MSQPSTANGGFPSVVVTAVTATTSISPDIESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRLDMRRM 80
Cdd:PRK07910 1 MMTELTTGKGFPNVVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFDLPVRIGGHLLEEFDHQLTRVELRRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 81 SYVQRMGKLLGGQLWESAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGA 160
Cdd:PRK07910 81 SYLQRMSTVLGRRVWENAGSPEVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 161 RAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRA-MSTRNDEPERASRPFDKDRDGFVF 239
Cdd:PRK07910 161 KAGVITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 240 GEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGD 319
Cdd:PRK07910 241 GEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 320 AAEANAIRVA-GCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAV 398
Cdd:PRK07910 321 VAEGKAINNAlGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAI 400
|
410
....*....|....*...
gi 523437855 399 NNSFGFGGHNVALAFGRY 416
Cdd:PRK07910 401 NNSFGFGGHNVALAFGRY 418
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
24-416 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 607.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 24 SISPDIESTWKGLLAGESGIHALEDEFVtkWDLAVKIGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGSP- 101
Cdd:PRK07314 14 PLGNDVESTWKNLLAGKSGIGPITHFDT--SDLAVKIAGEVKDfNPDDYMSRKEARRMDRFIQYGIAAAKQAVEDAGLEi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 102 -EVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAH 180
Cdd:PRK07314 92 tEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 181 AWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAK 260
Cdd:PRK07314 172 AARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 261 PLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVA---GCDQAAVY 337
Cdd:PRK07314 252 IYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVfgeHAYKVAVS 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523437855 338 APKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PRK07314 332 STKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGGTNASLVFKRY 410
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
25-416 |
4.24e-178 |
|
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: 502.32 E-value: 4.24e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISP---DIESTWKGLLAGESGIHALEDEFVTkwDLAVKIGGHLKDP-VDSHMGRLDMRRMSYVQRMGKLLGGQLWESAG- 99
Cdd:COG0304 11 VSPlgnGVEEFWEALLAGRSGIRPITRFDAS--GLPVRIAGEVKDFdPEEYLDRKELRRMDRFTQYALAAAREALADAGl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 100 -SPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAI 178
Cdd:COG0304 89 dLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACASGAHAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 179 AHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARG 258
Cdd:COG0304 169 GEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEELEHAKARG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 259 AKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIR-VAG--CDQAA 335
Cdd:COG0304 249 AKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKrVFGdhAYKVP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 336 VYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGR 415
Cdd:COG0304 329 VSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGHNASLVFKR 408
|
.
gi 523437855 416 Y 416
Cdd:COG0304 409 Y 409
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
25-413 |
4.92e-171 |
|
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: 484.35 E-value: 4.92e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISP---DIESTWKGLLAGESGIHALEDEFVTkwDLAVKIGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAGS 100
Cdd:cd00834 11 VTPlgnGVEEFWEALLAGRSGIRPITRFDAS--GFPSRIAGEVPDfDPEDYLDRKELRRMDRFAQFALAAAEEALADAGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 101 --PEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAI 178
Cdd:cd00834 89 dpEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTACASGAHAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 179 AHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARG 258
Cdd:cd00834 169 GDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLESLEHAKARG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 259 AKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQA---A 335
Cdd:cd00834 249 AKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVFGEHAkkvP 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523437855 336 VYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAF 413
Cdd:cd00834 329 VSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGHNASLVF 406
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
25-414 |
1.10e-156 |
|
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: 448.09 E-value: 1.10e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISP---DIESTWKGLLAGESGIhaledEFVTKWD---LAVKIGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWES 97
Cdd:TIGR03150 11 VTPlgnGVEEFWENLLAGKSGI-----GPITRFDasdLPVKIAGEVKDfDPEDYIDKKEARRMDRFIQYALAAAKEAVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 98 AGSP--EVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGS 175
Cdd:TIGR03150 86 SGLDieEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTACATGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 176 EAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAK 255
Cdd:TIGR03150 166 HAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEELEHAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 256 ARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQA- 334
Cdd:TIGR03150 246 ARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVFGDHAy 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 335 --AVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALA 412
Cdd:TIGR03150 326 klAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGTNASLV 405
|
..
gi 523437855 413 FG 414
Cdd:TIGR03150 406 FK 407
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
25-416 |
4.81e-125 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 368.17 E-value: 4.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISP---DIESTWKGLLAGESGIHALEDEFVTkwDLAVKIGGHLKDPV---------DSHMGRLDMRRMSYVQRMGKLLGG 92
Cdd:PRK06333 14 VSPlgcGVETFWQRLLAGQSGIRTLTDFPVG--DLATKIGGQVPDLAedaeagfdpDRYLDPKDQRKMDRFILFAMAAAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 93 QLWESAG---SPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVS 169
Cdd:PRK06333 92 EALAQAGwdpDTLEDRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRYGFKGPLGAPVT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 170 ACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTR-NDEPERASRPFDKDRDGFVFGEAGALMLI 248
Cdd:PRK06333 172 ACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGFVMGEGAGILVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 249 ETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIR- 327
Cdd:PRK06333 252 ETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKk 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 328 VAGCDQA-AVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEID-LDVVAGEPRYGDYRYAVNNSFGFG 405
Cdd:PRK06333 332 VFGHVSGlAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMDYALSNGFGFG 411
|
410
....*....|.
gi 523437855 406 GHNVALAFGRY 416
Cdd:PRK06333 412 GVNASILFRRW 422
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
25-416 |
1.02e-109 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 328.96 E-value: 1.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISP---DIESTWKGLLAGESGIHAL----------------EDEFVTKwdLAVKIGGHLK----DPVDSHMGRLDMRRMS 81
Cdd:PTZ00050 2 VTPlgvGAESTWEALIAGKSGIRKLtefpkflpdcipeqkaLENLVAA--MPCQIAAEVDqsefDPSDFAPTKRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 82 YVQRMGKLlggQLWESA--GSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLG 159
Cdd:PTZ00050 80 FAMAAARE---ALADAKldILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 160 ARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTR-NDEPERASRPFDKDRDGFV 238
Cdd:PTZ00050 157 LKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 239 FGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSL-ELAGLSPADIDHVNAHGTATPI 317
Cdd:PTZ00050 237 MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALkDGANININDVDYVNAHATSTPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 318 GDAAEANAI----RVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPR--Y 391
Cdd:PTZ00050 317 GDKIELKAIkkvfGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpL 396
|
410 420
....*....|....*....|....*
gi 523437855 392 GDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PTZ00050 397 QSIDAVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
24-416 |
5.94e-95 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 290.87 E-value: 5.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 24 SISPDIESTWKGLLAGESGIHALEDEFVTkwDLAVKIGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAG--S 100
Cdd:PRK08439 14 SLGLNKESSFKAICNGECGIKKITLFDAS--DFPVQIAGEITDfDPTEVMDPKEVKKADRFIQLGLKAAREAMKDAGflP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 101 PEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAH 180
Cdd:PRK08439 92 EELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTACAAGTHAIIE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 181 AWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGE-AGALMLiETEEHAKARGA 259
Cdd:PRK08439 172 AVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEgAGALVL-EEYESAKKRGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 260 KPLARLLGAGITSDAFHMVAPAADGvrAGRAMTRSLELAGLSPadIDHVNAHGTATPIGDAAEANAIRVAGCDQAA---V 336
Cdd:PRK08439 251 KIYAEIIGFGESGDANHITSPAPEG--PLRAMKAALEMAGNPK--IDYINAHGTSTPYNDKNETAALKELFGSKEKvppV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 337 YAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PRK08439 327 SSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGTNGVVIFKKV 406
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
29-413 |
2.03e-93 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 287.84 E-value: 2.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 29 IESTWKGLLAGESGIHALEDEFVTKWDLAVKIGGHLKDPVDSHMGRL--------DMRRMSY--VQRMGKLLGGQL---- 94
Cdd:PLN02836 23 VETTWRRLIAGECGVRALTQDDLKMKSEDEETQLYTLDQLPSRVAALvprgtgpgDFDEELWlnSRSSSRFIGYALcaad 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 95 -------WesAGSPEVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTP 167
Cdd:PLN02836 103 ealsdarW--LPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAAGHVSIRYGFQGPNHAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 168 VSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTR-NDEPERASRPFDKDRDGFVFGEAGALM 246
Cdd:PLN02836 181 VTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASRPFDCDRDGFVIGEGAGVL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 247 LIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAI 326
Cdd:PLN02836 261 VLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVNAHATSTPLGDAVEARAI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 327 RVAGCDQA-----AVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVA-GEPRYGDYRYAVNN 400
Cdd:PLN02836 341 KTVFSEHAtsgglAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDGFVPlTASKAMLIRAALSN 420
|
410
....*....|...
gi 523437855 401 SFGFGGHNVALAF 413
Cdd:PLN02836 421 SFGFGGTNASLLF 433
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
29-415 |
5.34e-92 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 283.43 E-value: 5.34e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 29 IESTWKGLLAGESGIHALEDEFVTkwDLAVKIGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAG--SPEVDP 105
Cdd:PRK08722 21 VESSWKALLAGQSGIVNIEHFDTT--NFSTRFAGLVKDfNCEEYMSKKDARKMDLFIQYGIAAGIQALDDSGleVTEENA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 106 DRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQI 185
Cdd:PRK08722 99 HRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 186 VMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARL 265
Cdd:PRK08722 179 AYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 266 LGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVA----GCDQAAVYAPKS 341
Cdd:PRK08722 259 VGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRAlgeaGSKQVLVSSTKS 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523437855 342 ALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPR-YGDYRYAVNNSFGFGGHNVALAFGR 415
Cdd:PRK08722 339 MTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARkVESMEYAICNSFGFGGTNGSLIFKK 413
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
106-416 |
1.74e-89 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 274.68 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 106 DRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQI 185
Cdd:PRK14691 26 ERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 186 VMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTR-NDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLAR 264
Cdd:PRK14691 106 RNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 265 LLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIR--VAGCDQAAVYAPKSA 342
Cdd:PRK14691 186 IVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKhlFGESNALAITSTKSA 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523437855 343 LGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEID-LDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PRK14691 266 TGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKRW 340
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
36-414 |
1.81e-79 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 250.68 E-value: 1.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 36 LLAGESGIHALEDefvtkWDLAVKIGGHLKDPVD-----SHMGRLDMRRMSYVQRMGKLLGGQLWESAG---SPEVDPDR 107
Cdd:PRK09116 26 LKAGRNAVRRMPE-----WDRYDGLNTRLAAPIDdfelpAHYTRKKIRSMGRVSLMATRASELALEDAGllgDPILTDGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 108 FAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLA-VQMiMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIV 186
Cdd:PRK09116 101 MGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATTyVRM-MPHTTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 187 MGDADVAVCGGVE--GPIEAlpiAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLAR 264
Cdd:PRK09116 180 YGYQTVMLAGGAEelCPTEA---AVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 265 LLGAGITSDAFHMVAPAADGVRagRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIrvagcdqAAVYAP----- 339
Cdd:PRK09116 257 IVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQAT-------AAVFGArmpis 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523437855 340 --KSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEI-DLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFG 414
Cdd:PRK09116 328 slKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMSNNFAFGGINTSLIFK 405
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
167-416 |
2.96e-73 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 235.30 E-value: 2.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 167 PVS---ACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGE-A 242
Cdd:PRK06501 168 PISlstACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDRDGFVMAEgA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 243 GALMLiETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAE 322
Cdd:PRK06501 248 GALVL-ESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKME 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 323 ANAIRVAGCDQAA---VYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVN 399
Cdd:PRK06501 327 YLGLSAVFGERLAsipVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVTAVLS 406
|
250
....*....|....*..
gi 523437855 400 NSFGFGGHNVALAFGRY 416
Cdd:PRK06501 407 NSFGFGGQNASLVLTAE 423
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
28-416 |
2.69e-70 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 231.02 E-value: 2.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 28 DIESTWKGLLAGESGIHALEdEFVTKwDLAVKIGGHLKDP-----VDSHMGRLDMRRMSYVQRMGK--LLGGQLWESAGS 100
Cdd:PLN02787 145 DPDVFYNNLLEGVSGISEIE-RFDCS-QFPTRIAGEIKSFstdgwVAPKLSKRMDKFMLYLLTAGKkaLADGGITEDVMK 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 101 pEVDPDRFAVVVGTGLGGAERIVESYDLMNAGgPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAH 180
Cdd:PLN02787 223 -ELDKTKCGVLIGSAMGGMKVFNDAIEALRIS-YRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILN 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 181 AWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAK 260
Cdd:PLN02787 301 AANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGAN 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 261 PLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAI-RVAGCD-QAAVYA 338
Cdd:PLN02787 381 IYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALmRCFGQNpELRVNS 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523437855 339 PKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAG-EPRYGDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PLN02787 461 TKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGpKKERLDIKVALSNSFGFGGHNSSILFAPY 539
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
145-415 |
1.07e-68 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 222.23 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 145 IMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMStrndePE 224
Cdd:PRK05952 120 TLPHQAAIAAARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALA-----KT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 225 RASrPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPAD 304
Cdd:PRK05952 195 GAY-PFDRQREGLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPED 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 305 IDHVNAHGTATPIGDAAEANAIRVAGCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETpdPEIDLDV 384
Cdd:PRK05952 274 IDYIHAHGTATRLNDQREANLIQALFPHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQE--PEFDLNF 351
|
250 260 270
....*....|....*....|....*....|.
gi 523437855 385 VAgEPRYGDYRYAVNNSFGFGGHNVALAFGR 415
Cdd:PRK05952 352 VR-QAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
24-415 |
5.20e-68 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 221.44 E-value: 5.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 24 SISPDIESTWKGLLAGESGIHALEDEF--VTKWDLAVK----IGGHLKD-PVDSHMGRLDMRRMSYVQRMGKLLGGQLWE 96
Cdd:PRK07103 14 AIGQGRPSFAAALLAGRHAFGVMRRPGrqVPDDAGAGLasafIGAELDSlALPERLDAKLLRRASLSAQAALAAAREAWR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 97 SAGSPEVDPDRFAVVV-GTGLGGAE--RIVESYdlmnAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSS 173
Cdd:PRK07103 94 DAALGPVDPDRIGLVVgGSNLQQREqaLVHETY----RDRPAFLRPSYGLSFMDTDLVGLCSEQFGIRGEGFTVGGASAS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 174 GSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRN--DEPERASRPFDKDRDGFVFGEAGALMLIETE 251
Cdd:PRK07103 170 GQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGFIYGEACGAVVLESA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 252 EHAKARGAKPLARLLGAGITSDAFHMVAPAADGvrAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGC 331
Cdd:PRK07103 250 ESARRRGARPYAKLLGWSMRLDANRGPDPSLEG--EMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 332 DQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETP-DPEIDLdvVAGEPRYGDYRYAVNNSFGFGGHNVA 410
Cdd:PRK07103 328 AHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFRW--VGSTAESARIRYALSLSFGFGGINTA 405
|
....*
gi 523437855 411 LAFGR 415
Cdd:PRK07103 406 LVLER 410
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
102-416 |
2.47e-65 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 214.15 E-value: 2.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 102 EVDPDRFAVVVGTGLGGAERIVESYDLMNAG-GPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAH 180
Cdd:PRK07967 92 QVSNPRTGLIAGSGGGSTRNQVEAADAMRGPrGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYSISSACATSAHCIGN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 181 AWRQIVMGDADVAVCGGVEGPIEALPiAAFSMMRAMSTR-NDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGA 259
Cdd:PRK07967 172 AVEQIQLGKQDIVFAGGGEELDWEMS-CLFDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGVVVVEELEHALARGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 260 KPLARLLGAGITSDAFHMVAPAADGvrAGRAMTRSleLAGLSpADIDHVNAHGTATPIGDAAEANAIR-VAGCDQAAVYA 338
Cdd:PRK07967 251 KIYAEIVGYGATSDGYDMVAPSGEG--AVRCMQMA--LATVD-TPIDYINTHGTSTPVGDVKELGAIReVFGDKSPAISA 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523437855 339 PKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEI-DLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:PRK07967 326 TKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAaGMPIVTETTDNAELTTVMSNSFGFGGTNATLVFRRY 404
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
105-415 |
2.42e-64 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 211.24 E-value: 2.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 105 PDRFAVVVGT---GLGGAERIVESYDLMNAGGP-----RKVSPLAVqmimPNGAAAVIGLQLGAragvMTPVSACSSGSE 176
Cdd:PRK09185 94 ADRIGVVLGTstsGILEGELAYRRRDPAHGALPadyhyAQQELGSL----ADFLRAYLGLSGPA----YTISTACSSSAK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 177 AIAHAWRQIVMGDADVAVCGGVEGpIEALPIAAFSMMRAMStrndepERASRPFDKDRDGFVFGEAGALMLIEteehaka 256
Cdd:PRK09185 166 VFASARRLLEAGLCDAAIVGGVDS-LCRLTLNGFNSLESLS------PQPCRPFSANRDGINIGEAAAFFLLE------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 257 RGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQAAV 336
Cdd:PRK09185 232 REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVPC 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523437855 337 YAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVALAFGR 415
Cdd:PRK09185 312 SSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIFGR 390
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
27-411 |
3.24e-62 |
|
"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: 206.14 E-value: 3.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 27 PDIESTWKGLLAGESGIHALEDEfvtKWDLAVKIGGHLKDPVDSHMGRLDMRRMSYVQRMGKLLGGQLWESAG---SPEV 103
Cdd:cd00828 19 DEVEEFWEALREGRSGIAPVARL---KSRFDRGVAGQIPTGDIPGWDAKRTGIVDRTTLLALVATEEALADAGitdPYEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 104 DPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSPLAvqMIMPNGAAAVIGLQLGARAG-VMTPVSACSSGSEAIAHAW 182
Cdd:cd00828 96 HPSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKW--MLSPNTVAGWVNILLLSSHGpIKTPVGACATALEALDLAV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 183 RQIVMGDADVAVCGGVEGPIEaLPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGAKPL 262
Cdd:cd00828 174 EAIRSGKADIVVVGGVEDPLE-EGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 263 ARLLGAGITSDAFHMVAPAADGVrAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAI-RVAG--CDQAAVYAP 339
Cdd:cd00828 253 GRVAGTASTTDGAGRSVPAGGKG-IARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIaEVAGalGAPLPVTAQ 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523437855 340 KSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPR--YGDYRYAVNNSFGFGGHNVAL 411
Cdd:cd00828 332 KALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAALVNAFGFGGSNAAL 405
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
96-411 |
1.74e-48 |
|
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: 170.43 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 96 ESAG-SPE-VDPDRFAVVVGTGLggaerivESYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSACSS 173
Cdd:cd00833 100 EDAGySPEsLAGSRTGVFVGASS-------SDYLELLARDPDEIDAYAATGTSRAFLANRISYFFDLRGPSLTVDTACSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 174 GSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMStrndePERASRPFDKDRDGFVFGEAGALMLIETEEH 253
Cdd:cd00833 173 SLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDGRCRPFDADADGYVRGEGVGVVVLKRLSD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 254 AKARGAKPLARLLGAGITSDAF--HMVAPAADGvrAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIrvagc 331
Cdd:cd00833 248 ALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEA--QAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEAL----- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 332 dqAAVYAP-------------KSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLD----VVAGE----PR 390
Cdd:cd00833 321 --AKVFGGsrsadqplligsvKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEarpwPA 398
|
330 340
....*....|....*....|.
gi 523437855 391 YGDYRYAVNNSFGFGGHNVAL 411
Cdd:cd00833 399 PAGPRRAGVSSFGFGGTNAHV 419
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
81-412 |
1.81e-48 |
|
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: 167.81 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 81 SYVQRMGKLLGGQLWESAG-SPEVDPD-RFAVVVGTGLGGAERIVESYDLMnaggpRKVSPLAVQMIMPNGAAAVIGLQL 158
Cdd:cd00825 9 SYVSILGFEAAERAIADAGlSREYQKNpIVGVVVGTGGGSPRFQVFGADAM-----RAVGPYVVTKAMFPGASGQIATPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 159 GARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEgpieaLPIAAFSMMRAMSTRNDEPERASRPFDKDRDGFV 238
Cdd:cd00825 84 GIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSE-----ELAAPMDCEFDAMGALSTPEKASRTFDAAADGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 239 FGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIG 318
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 319 DAAEANAIRVA-GCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPeiDLDVVAGEPRYGDYRYA 397
Cdd:cd00825 239 DVKELKLLRSEfGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRTA 316
|
330
....*....|....*
gi 523437855 398 VNNSFGFGGHNVALA 412
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
25-253 |
1.16e-45 |
|
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: 158.18 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 25 ISPDIESTWKGLLAGESGIHALED---EFVTKWDLAVKIGGHLKDPV---------DSHMGRLDMR---RMSYVQRMGKL 89
Cdd:pfam00109 14 GGNDPEEFWENLLEGRDGISEIPAdrwDPDKLYDPPSRIAGKIYTKWgglddifdfDPLFFGISPReaeRMDPQQRLLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 90 LGGQLWESAGSP--EVDPDRFAVVVGTGLGGAErivESYDLMNAGGPRKVSPLAVQMiMPNGAAAVIGLQLGARAGVMTP 167
Cdd:pfam00109 94 AAWEALEDAGITpdSLDGSRTGVFIGSGIGDYA---ALLLLDEDGGPRRGSPFAVGT-MPSVIAGRISYFLGLRGPSVTV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 168 VSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTrnDEPERASRPFDkdrDGFVFGE-AGALM 246
Cdd:pfam00109 170 DTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA---DGFVRGEgVGAVV 244
|
....*..
gi 523437855 247 LIETEEH 253
Cdd:pfam00109 245 LKRLSDA 251
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
30-411 |
4.02e-44 |
|
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: 158.29 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 30 ESTWKGLLAGESGIHAledefVTKWDLA---VKIGGHLKDPVDSHmgRLDMRRMSYVQRMGKL-LGGQLW----ESAGSP 101
Cdd:cd00832 19 EEYWKAVLDGRSGLGP-----ITRFDPSgypARLAGEVPDFDAAE--HLPGRLLPQTDRMTRLaLAAADWaladAGVDPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 102 EVDPDRFAVVVGTGLGGAERIVESYDLMNAGGPRKVSplAVQMIMPNGAAAV--IGLQLGARAGVMTPVSACSSGSEAIA 179
Cdd:cd00832 92 ALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVS--AYQSFAWFYAVNTgqISIRHGMRGPSGVVVAEQAGGLDALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 180 HAWRQIVMGdADVAVCGGVEGPIEALPIAAFSMMRAMSTrNDEPERASRPFDKDRDGFVFGEAGALMLIETEEHAKARGA 259
Cdd:cd00832 170 QARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILVLEDAAAARERGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 260 KPLARLLGAGITSDAfhmvaPAADGVRAG--RAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAI-RVAGCDQAAV 336
Cdd:cd00832 248 RVYGEIAGYAATFDP-----PPGSGRPPGlaRAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALaAVFGPRGVPV 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523437855 337 YAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDVVAGEPRYGDYRYAVNNSFGFGGHNVAL 411
Cdd:cd00832 323 TAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGFNSAL 397
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
262-374 |
5.10e-39 |
|
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: 136.16 E-value: 5.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 262 LARLLGAGITSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAIRVAGCDQA-----AV 336
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGArkqplAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 523437855 337 YAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYE 374
Cdd:pfam02801 81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
96-409 |
1.89e-32 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 130.38 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 96 ESAGspeVDPDRFA-----VVVGTGLGGaerivesYDLMNAGGPRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSA 170
Cdd:COG3321 104 EDAG---YDPESLAgsrtgVFVGASSND-------YALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRGPSVTVDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 171 CSSGSEAIAHAWRQIVMGDADVAVCGGVEgpIEALPIA--AFSMMRAMStrndePERASRPFDKDRDGFVFGEAGALMLI 248
Cdd:COG3321 174 CSSSLVAVHLACQSLRSGECDLALAGGVN--LMLTPESfiLFSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 249 ETEEHAKARGAKPLARLLGAGITSD--AFHMVAPAADGVRagRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAEANAI 326
Cdd:COG3321 247 KRLSDALRDGDRIYAVIRGSAVNQDgrSNGLTAPNGPAQA--AVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAAL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 327 rvagcdqAAVYAP-------------KSALGHSIGAVGALeSVL-TVLTLRDGVIPPTLNYETPDPEIDLD----VVAGE 388
Cdd:COG3321 325 -------TAAFGQgrpadqpcaigsvKSNIGHLEAAAGVA-GLIkAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTE 396
|
330 340
....*....|....*....|....*
gi 523437855 389 ----PRYGDYRYAVNNSFGFGGHNV 409
Cdd:COG3321 397 lrpwPAGGGPRRAGVSSFGFGGTNA 421
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
169-416 |
1.11e-23 |
|
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: 104.32 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 169 SACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMSTRNDeperaSRPFDKDRDGFVFGEAGALMLI 248
Cdd:TIGR02813 204 AACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED-----IQPFDIDSKGMMIGEGIGMMAL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 249 ETEEHAKARGAKPLARLLGAGITSDA-FHMV-APAADGvrAGRAMTRSLELAGLSPADIDHVNAHGTATPIGDAAE---A 323
Cdd:TIGR02813 279 KRLEDAERDGDRIYAVIKGVGASSDGkFKSIyAPRPEG--QAKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEfggL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 324 NAIRVAGCDQA---AVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNYETPDPEIDLDvvaGEPRY--------- 391
Cdd:TIGR02813 357 VSVFSQDNDQKqhiALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIE---NSPFYlntetrpwm 433
|
250 260
....*....|....*....|....*....
gi 523437855 392 ----GDYRYAVNNSFGFGGHNVALAFGRY 416
Cdd:TIGR02813 434 qredGTPRRAGISSFGFGGTNFHMVLEEY 462
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
146-411 |
7.92e-23 |
|
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: 96.74 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 146 MPNGAAAVIGLQLGARAGVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEGpiealpiaafsmmramstrndeper 225
Cdd:cd00327 43 FSGAAGQLAYHLGISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 226 asrpfdkdrdgFVFGEAGALMLIETEEHAKARGAKPLARLLGAGITSDAFHMV-APAADGvrAGRAMTRSLELAGLSPAD 304
Cdd:cd00327 98 -----------FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVpAVSGEG--LARAARKALEGAGLTPSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 305 IDHVNAHGTATPIGDAAEANAIRVA-GCDQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPtlnyeTPDPEidld 383
Cdd:cd00327 165 IDYVEAHGTGTPIGDAVELALGLDPdGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP-----TPREP---- 235
|
250 260
....*....|....*....|....*...
gi 523437855 384 vvageprygdyRYAVNNSFGFGGHNVAL 411
Cdd:cd00327 236 -----------RTVLLLGFGLGGTNAAV 252
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
170-411 |
1.19e-20 |
|
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: 91.24 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 170 ACSSGSEAIAHAWRQIVMGDADVAVCGGVEGPIEALPIAAFSMMRAMStrndePERASRPFDKDRDGFVFGEAGALMLIE 249
Cdd:smart00825 96 ACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 250 TEEHAKARGAKPLARLLGAGITSDafhmvapaadgvraGRAmtrslelAGLspadidhvnahgTAtPIGDAaeanairva 329
Cdd:smart00825 171 RLSDALRDGDPILAVIRGSAVNQD--------------GRS-------NGI------------TA-PSGPA--------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 330 gcdQAAVYAPKSALGHSIGAVGaLESVL-TVLTLRDGVIPPTLNYETPDPEIDLD----VVAGEPR----YGDYRYAVNN 400
Cdd:smart00825 208 ---QLLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTpwppPGRPRRAGVS 283
|
250
....*....|.
gi 523437855 401 SFGFGGHNVAL 411
Cdd:smart00825 284 SFGFGGTNAHV 294
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
233-388 |
3.13e-07 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 52.26 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 233 DRDGFVFGEAGALMLIETEEHAKARGAKPLARLlgAGITSDAfhmvAPAADGVRAGRaMTRSLELAGLSPADiDHVNAHG 312
Cdd:PRK06519 235 DGGGFILGSGGAFLVLESREHAEARGARPYARI--SGVESDR----ARRAPGDLEAS-LERLLKPAGGLAAP-TAVISGA 306
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523437855 313 TATPIGDAAEANAIRVAGcdQAAVYAPKSALGHSIGAVGALESVLTVLTLRDGVIPPTLNyetPDPEIDLDVVAGE 388
Cdd:PRK06519 307 TGAHPATAEEKAALEAAL--AGPVRGIGTLFGHTMEAQFPLGLALAALSVSKGALFPPFD---ASGEKPMSGAARE 377
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
242-356 |
1.85e-06 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 49.57 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 242 AGALMLIEtEEHAKARGAKPLARLLGAGITSdafhmVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHgtatpigDAA 321
Cdd:PRK09051 255 AAAVVLAE-ADAAEARGLKPLARLVGYAHAG-----VDPEYMGIGPVPATQKALERAGLTVADLDVIEAN-------EAF 321
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 523437855 322 EANAIRVA---GCDQAAVYAPKS--ALGHSIGAVGALESV 356
Cdd:PRK09051 322 AAQACAVTrelGLDPAKVNPNGSgiSLGHPVGATGAIITV 361
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
146-352 |
8.91e-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: 47.37 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 146 MPNGAAAVIGLQLGARAGVmtPVS--------ACSSGSEAIAHAWRQIVMGDADVAVCGGVE------------------ 199
Cdd:COG0183 57 LQAGQGQNPARQAALLAGL--PESvpavtvnrVCGSGLQAVALAAQAIAAGDADVVIAGGVEsmsrapmllpkarwgyrm 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 200 ---------GPIEALPIAAFSM--------------------------MRAMSTRND------------EPERASRPFDK 232
Cdd:COG0183 135 naklvdpmiNPGLTDPYTGLSMgetaenvaerygisreeqdafalrshQRAAAAIAAgrfddeivpvevPDRKGEVVVDR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 233 D---RDGF----------VFGEAG--------------ALMLIETEEHAKARGAKPLARLLGAgitsdAFHMVAPAADGV 285
Cdd:COG0183 215 DegpRPDTtleklaklkpAFKKDGtvtagnasgindgaAALLLMSEEAAKELGLKPLARIVAY-----AVAGVDPEIMGI 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 286 RAGRAMTRSLELAGLSPADIDHVNAHgtatpigdaaEANAIRVAGCDQA-------------AVyapksALGHSIGAVGA 352
Cdd:COG0183 290 GPVPATRKALARAGLTLDDIDLIEIN----------EAFAAQVLAVLRElgldpdkvnvnggAI-----ALGHPLGASGA 354
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
146-352 |
1.06e-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: 47.09 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 146 MPNGAAAVIGLQLGARAGVMTPVSA------CSSGSEAIAHAWRQIVMGDADVAVCGGVE----GPIeALPIAAFSMMRA 215
Cdd:cd00751 53 LQAGEGQNPARQAALLAGLPESVPAttvnrvCGSGLQAVALAAQSIAAGEADVVVAGGVEsmsrAPY-LLPKARRGGRLG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 216 MSTRNDEP---------------------------------------ERASR-----------------------PFDKD 233
Cdd:cd00751 132 LNTLDGMLddgltdpftglsmgitaenvaekygisreeqdefalrshQRAAAaqeagrfkdeivpvevpgrkgpvVVDRD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 234 ---RDGF----------VFGEAG--------------ALMLIETEEHAKARGAKPLARLLGAGITSdafhmVAPAADGVR 286
Cdd:cd00751 212 egpRPDTtleklaklkpAFKKDGtvtagnasgindgaAAVLLMSEEKAKELGLKPLARIVGYAVAG-----VDPAIMGIG 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523437855 287 AGRAMTRSLELAGLSPADIDHVNAHgtatpigdaaEANAIRVAGC--------DQAAVYAPKSALGHSIGAVGA 352
Cdd:cd00751 287 PVPAIPKALKRAGLTLDDIDLIEIN----------EAFAAQALAClkelgldpEKVNVNGGAIALGHPLGASGA 350
|
|
| PRK06816 |
PRK06816 |
StlD/DarB family beta-ketosynthase; |
145-247 |
5.03e-05 |
|
StlD/DarB family beta-ketosynthase;
Pssm-ID: 235866 Cd Length: 378 Bit Score: 45.29 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 145 IMPNGAAAVIGLqLGARA-GVMTPVSACSSGSEAIAHAWRQIVMGDADVAVCGGVEgpiealpiAAFSMMRAmSTRNDEP 223
Cdd:PRK06816 98 LMPGHASMVHGE-LGAPPiEVVSSAGVCAAGMMALKYAYLSVKAGESRNAVATASE--------LASRWFRA-SRFEAEE 167
|
90 100 110
....*....|....*....|....*....|....*..
gi 523437855 224 ERASR-------PFDKD------RDGfvfgeAGALML 247
Cdd:PRK06816 168 EKLAEleenpeiAFEKDflrwmlSDG-----AGAVLL 199
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
137-199 |
8.20e-05 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 44.37 E-value: 8.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523437855 137 VSPLAVQ-MIMPN----GAAAVIGLQLGARAGVMTPVSA------CSSGSEAIAHAWRQIVMGDADVAVCGGVE 199
Cdd:PRK05790 43 VPPEQVDeVIMGQvlqaGAGQNPARQAALKAGLPVEVPAltinkvCGSGLKAVALAAQAIRAGDADIVVAGGQE 116
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
134-199 |
9.63e-05 |
|
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: 43.83 E-value: 9.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523437855 134 PRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSA------CSSGSEAIAHAWRQIVMGDADVAVCGGVE 199
Cdd:pfam00108 42 PEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAvtinkvCGSGLKAVYLAAQSIASGDADVVLAGGVE 113
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
242-352 |
1.41e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 43.93 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 242 AGALMLIEtEEHAKARGAKPLARLLGAGITSDAFHMVAPAAdgvraGRAMTRSLELAGLSPADIDHVNahgtatpIGDAA 321
Cdd:PRK08235 254 AAALVLMS-EDRAKQEGRKPLATILAHTAIAVEAKDFPRTP-----GYAINALLEKTGKTVEDIDLFE-------INEAF 320
|
90 100 110
....*....|....*....|....*....|....*.
gi 523437855 322 EANAI---RVAGCD--QAAVYAPKSALGHSIGAVGA 352
Cdd:PRK08235 321 AAVALastEIAGIDpeKVNVNGGAVALGHPIGASGA 356
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
151-199 |
6.87e-04 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 41.48 E-value: 6.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 523437855 151 AAVIGLQLGARAGVMTPV-SACSSGSEAIAHAWRQIVMGDADVAVCGGVE 199
Cdd:cd00829 56 GALIAEYLGLLGKPATRVeAAGASGSAAVRAAAAAIASGLADVVLVVGAE 105
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
241-365 |
7.48e-04 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 41.51 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 241 EAGALMLIETEEHAKARGAKPLARLLGAGITSdafhmVAPAADGVRAGRAMTRSLELAGLSPADIDHVNAHgtatpigda 320
Cdd:PRK06205 259 DAAAACLVTTEDKAEELGLRPLARLVSWAVAG-----VEPSRMGIGPVPATEKALARAGLTLDDIDLIELN--------- 324
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 523437855 321 aEANAIRVAGC-----------DQAAVYAPKSALGHSIGAVGA--LESVLTVLTLRDG 365
Cdd:PRK06205 325 -EAFAAQVLAVlkewgfgaddeERLNVNGSGISLGHPVGATGGriLATLLRELQRRQA 381
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
136-199 |
1.67e-03 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 40.52 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523437855 136 KVSPLAVQ-MIM----PNGA-AAVIGLQLGARAGVMTPVSA------CSSGSEAIAHAWRQIVMGDADVAVCGGVE 199
Cdd:PRK07108 43 KLDPAEVEdVIMgcanPEGAtGANIARQIALRAGLPVTVPGmtvnrfCSSGLQTIALAAQRVIAGEGDVFVAGGVE 118
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
134-255 |
5.35e-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: 38.75 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 134 PRKVSPLAVQMIMPNGAAAVIGLQLGARAGVMTPVSA------CSSGSEAIAHAWRQIVMGDADVAVCGGVEgpiealpi 207
Cdd:TIGR01930 40 PELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAytvnrqCASGLQAVILAAQLIRAGEADVVVAGGVE-------- 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 523437855 208 aafSMMRA-MSTRNDEPERASRPFDKDRDGFVFGEAGAL----MLIETEEHAK 255
Cdd:TIGR01930 112 ---SMSRVpYGVPRSLRWGVKPGNAELEDARLKDLTDANtglpMGVTAENLAK 161
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
242-352 |
6.83e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 38.58 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523437855 242 AGALMLIETEEhAKARGAKPLARLLgagitSDAFHMVAPAADGVRAGRAMTRSLELAGLSPADID--HVNAHGTATPIGd 319
Cdd:PRK07661 252 AAAVLLMDREK-AESDGLKPLAKFR-----SFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGlfELNEAFASQSIQ- 324
|
90 100 110
....*....|....*....|....*....|....*
gi 523437855 320 aaeanAIRVAGCDQAAVYAPKS--ALGHSIGAVGA 352
Cdd:PRK07661 325 -----VIRELGLDEEKVNVNGGaiALGHPLGCTGA 354
|
|
| |
