|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
5-392 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 700.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 5 PPLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENP 84
Cdd:PLN03172 2 PSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 85 NMCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQ 164
Cdd:PLN03172 82 NMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 165 QGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMV 244
Cdd:PLN03172 162 QGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 245 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 324
Cdd:PLN03172 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033014183 325 EGKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 392
Cdd:PLN03172 321 EEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVP 388
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
19-388 |
2.42e-167 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 472.48 E-value: 2.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 19 PAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVT--EEFLKENPNMcaymAPSLDA 96
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 97 RQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRL 176
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 177 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGSDPDTSVGEKPIFEMVSAAQTILPDSDG 256
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 257 AIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPL--GISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRATRHV 334
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1033014183 335 MREYGNMSSA*VJFILDEMRKKSAKdgvattgEGLEWGVLFGFGPGLTVETVVL 388
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
7-231 |
1.59e-143 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 406.93 E-value: 1.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 7 LDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNM 86
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 87 CAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 166
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033014183 167 CFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDP 231
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
22-389 |
1.98e-97 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 294.36 E-value: 1.98e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 22 ILAIGTANPANYVIQAEYPDYyFRITNSGHMTDLkEKFKRMCDKSTIRKRHMHVTEEFLKENPnmcaymapSLDARQDIV 101
Cdd:COG3424 4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 102 VVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLA 181
Cdd:COG3424 74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 182 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVGekpiFEMVSAAQTILPDSDGAIDGH 261
Cdd:COG3424 154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 262 LREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRATRHVMREYGNM 341
Cdd:COG3424 229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNM 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1033014183 342 SSA*VJFILDE-MRKKSAKDGvattgeglEWGVLFGFGPGLTVETVVLH 389
Cdd:COG3424 309 SSATVLFVLERlLEEGAPAPG--------ERGLAMAFGPGFTAELVLLR 349
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
5-392 |
0e+00 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 700.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 5 PPLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENP 84
Cdd:PLN03172 2 PSIAEIRKAQRAEGPATILAIGKATPANCVSQADYPDYYFRITNSEHMTELKEKFKRMCDKSMIKKRYMHLTEEILKENP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 85 NMCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQ 164
Cdd:PLN03172 82 NMCAYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 165 QGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMV 244
Cdd:PLN03172 162 QGCFAGGTVLRLAKDLAENNAGSRVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAVIIGADPDTKI-ERPLFEIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 245 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLK 324
Cdd:PLN03172 241 SAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033014183 325 EGKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 392
Cdd:PLN03172 321 EEKLRATRHVLSDYGNMSSACVLFILDEMRKKSIEEGKGSTGEGLEWGVLFGFGPGLTVETVVLHSVP 388
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
1-393 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 694.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 1 MGDTPPLDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFL 80
Cdd:PLN03170 2 AGATVTVEEVRKAQRATGPATVLAIGTATPANCVHQADYPDYYFRITKSEHMTELKEKFKRMCDKSQIRKRYMHLTEEYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 81 KENPNMCAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRL 160
Cdd:PLN03170 82 AENPNMCAYMAPSLDARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 161 MMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPI 240
Cdd:PLN03170 162 MMYQQGCFAGGTVLRVAKDLAENNRGARVLVVCSEITAVTFRGPSESHLDSMVGQALFGDGAAAVIVGADPDERV-ERPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 241 FEMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIK 320
Cdd:PLN03170 241 FQLVSASQTILPDSEGAIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033014183 321 LGLKEGKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVPL 393
Cdd:PLN03170 321 VGLEKERMRATRHVLSEYGNMSSACVLFILDEMRKRSAEDGQATTGEGFDWGVLFGFGPGLTVETVVLHSVPI 393
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
7-391 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 690.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 7 LDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNM 86
Cdd:PLN03173 4 VDEIRKAQRAEGPATIMAIGTSTPPNCVDQSTYPDYYFRITNSEHKVELKEKFKRMCEKSMIKKRYMHLTEEILKENPSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 87 CAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 166
Cdd:PLN03173 84 CEYMAPSLDARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMYQQG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 167 CFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMVSA 246
Cdd:PLN03173 164 CFAGGTVLRLAKDLAENNKGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIIGSDPVLGV-EKPLFELVSA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 247 AQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEG 326
Cdd:PLN03173 243 AQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALKPE 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033014183 327 KMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSV 391
Cdd:PLN03173 323 KLRATRHVLSEYGNMSSACVLFILDEMRKKSAEDGLKSTGEGLEWGVLFGFGPGLTVETVVLHSV 387
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
11-392 |
0e+00 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 557.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 11 RKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNMCAYM 90
Cdd:PLN03168 7 RGQPRAEGPACVLGIGTAVPPAEFLQSEYPDFFFNITNCGEKEALKAKFKRICDKSGIRKRHMFLTEEVLKANPGICTYM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 91 APSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAG 170
Cdd:PLN03168 87 EPSLNVRHDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 171 GTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVgEKPIFEMVSAAQTI 250
Cdd:PLN03168 167 ASVLRVAKDLAENNKGARVLAVASEVTAVTYRAPSENHLDGLVGSALFGDGAGVYVVGSDPKPEV-EKALFEVHWAGETI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 251 LPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRA 330
Cdd:PLN03168 246 LPESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQG 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033014183 331 TRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 392
Cdd:PLN03168 326 SRDILSEFGNMSSASVLFVLDQIRQRSVKMGASTLGEGSEFGFFIGFGPGLTLEVLVLRAAA 387
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
7-390 |
8.36e-172 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 485.28 E-value: 8.36e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 7 LDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNM 86
Cdd:PLN03171 10 LGEICRAQRADGLAAVLAIGTANPANCVPQDEFPDFYFRATKSDHLTALKDKFKRICQELGVQKRYLHHTEELLSAHPEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 87 CAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 166
Cdd:PLN03171 90 LDHDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADITHLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLNG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 167 CFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSvgEKPIFEMVSA 246
Cdd:PLN03171 170 CFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDEGCFQTLLNQGLFGDGAAAVIVGADADAA--ERPLFEIVSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 247 AQTILPDSDGAIDGHLREVGLTFHL-LKDVPGLISKNIEKSLDEAFRPL----GISDWNSLFWIAHPGGPAILDQVEIKL 321
Cdd:PLN03171 248 AQAIIPESDDAINMHFTEGGLDGNIgTRQVPGLIGDNIERCLLDAFAPLlggdGGAEWNDLFWAVHPGSSAILDQVDAAL 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033014183 322 GLKEGKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKdgVATTGEGLEWGVLFGFGPGLTVETVVLHS 390
Cdd:PLN03171 328 GLEPEKLAASRRVLSDYGNMFGATVIFALDELRRQMEE--AAAAGAWPELGVMMAFGPGLTVDAMLLHA 394
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
19-388 |
2.42e-167 |
|
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.
Pssm-ID: 238427 [Multi-domain] Cd Length: 361 Bit Score: 472.48 E-value: 2.42e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 19 PAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVT--EEFLKENPNMcaymAPSLDA 96
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRLFSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPEM----SPSLDE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 97 RQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRL 176
Cdd:cd00831 77 RNDIALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 177 AKDLAENNRGARVLVVCSEITAVTFRGPSdtHLDSLVGQALFSDGAAALIVGSDPDTSVGEKPIFEMVSAAQTILPDSDG 256
Cdd:cd00831 157 AKDLLEANPGARVLVVSTELCSLWYRGPD--HRSMLVGNALFGDGAAAVLLSNDPRDRRRERPLFELVRAASTLLPDSED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 257 AIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPL--GISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRATRHV 334
Cdd:cd00831 235 AMGWHLGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1033014183 335 MREYGNMSSA*VJFILDEMRKKSAKdgvattgEGLEWGVLFGFGPGLTVETVVL 388
Cdd:cd00831 315 LRRYGNMSSSSVLYVLAYMEAKGRV-------KRGDRGLLIAFGPGFTCESAVW 361
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
7-231 |
1.59e-143 |
|
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.
Pssm-ID: 395142 Cd Length: 225 Bit Score: 406.93 E-value: 1.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 7 LDEIRKAQRADGPAGILAIGTANPANYVIQAEYPDYYFRITNSGHMTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNM 86
Cdd:pfam00195 1 SSEGRRAQRAEGKATLLAIGTATPEQCVPQETYVDYYFRDTKSEHMAELKEKFERLCDKSMIKKRYTHLTEEILDEHPEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 87 CAYMAPSLDARQDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQG 166
Cdd:pfam00195 81 CTEMAPSLDARLEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTTSGVRMPGADYQLAKLLGLRPSVKRVMLYFQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033014183 167 CFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDP 231
Cdd:pfam00195 161 CYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRGPSKDRLDSLVGAALFGDGAAAVIIGADP 225
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
18-391 |
1.39e-121 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 357.47 E-value: 1.39e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 18 GPAGILAIGTANPANYVIQAEYPDYYFRITNSGHmTDLKEKFKRMCDKSTIRKRHMHVTEEFLKENPNMCAYMAPSLDAR 97
Cdd:PLN03169 20 GKATILALGKAFPSQLVPQEYLVDGYFRDTKCDD-PALKEKLERLCKTTTVKTRYVVMSKEILDKYPELATEGTPTIKQR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 98 QDIVVVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLA 177
Cdd:PLN03169 99 LDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEARLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 178 KDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPdTSVGEKPIFEMVSAAQTILPDSDGA 257
Cdd:PLN03169 179 KDIAENNPGSRVLLTTSETTILGFRPPSPDRPYDLVGAALFGDGAAAVIIGADP-IPVSESPFFELHTAIQQFLPGTEKT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 258 IDGHLREVGLTFHLLKDVPGLISKNIE----KSLDEAfrPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRATRH 333
Cdd:PLN03169 258 IDGRLTEEGINFKLGRELPQKIEDNIEgfckKLMKKA--GLVEKDYNDLFWAVHPGGPAILNRLEKKLKLAPEKLECSRR 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033014183 334 VMREYGNMSSA*VJFILDEMRKKSAKDGvattGEGLEWGVLFGFGPGLTVETVVLHSV 391
Cdd:PLN03169 336 ALMDYGNVSSNTIVYVLEYMREELKKKG----EEDEEWGLILAFGPGITFEGILARNL 389
|
|
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
22-389 |
1.98e-97 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 294.36 E-value: 1.98e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 22 ILAIGTANPANYVIQAEYPDYyFRITNSGHMTDLkEKFKRMCDKSTIRKRHMHVTEEFLKENPnmcaymapSLDARQDIV 101
Cdd:COG3424 4 ILSIATAVPPHRYTQEEIAEF-AAELFGLDERDR-RRLRRLFENSGIETRHSVLPLEWYLEPP--------SFGERNALY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 102 VVEVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLA 181
Cdd:COG3424 74 IEEALELAEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 182 ENNRGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVGekpiFEMVSAAQTILPDSDGAIDGH 261
Cdd:COG3424 154 RADPDAVVLVVCVELCSLTFQ-RDDDSKDNLVANALFGDGAAAVVVSGDPRPGPG----PRILAFRSYLIPDTEDVMGWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 262 LREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRATRHVMREYGNM 341
Cdd:COG3424 229 VGDTGFRMVLSPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNM 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1033014183 342 SSA*VJFILDE-MRKKSAKDGvattgeglEWGVLFGFGPGLTVETVVLH 389
Cdd:COG3424 309 SSATVLFVLERlLEEGAPAPG--------ERGLAMAFGPGFTAELVLLR 349
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
242-392 |
6.93e-91 |
|
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in the N-terminal domain.
Pssm-ID: 397089 Cd Length: 151 Bit Score: 270.09 E-value: 6.93e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 242 EMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKL 321
Cdd:pfam02797 1 ELVSAAQTFLPNTDGVIDGHLTEEGLTFHLGRDVPQKIEENIEEFLKKAFEPLGISEWNSLFWIVHPGGPAILDRVETKL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033014183 322 GLKEGKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVLHSVP 392
Cdd:pfam02797 81 GLEPEKLEASRRALMDYGNVSSATVLFILDEMRKKSLKKGLATTGEGLDWGVLLAFGPGLTFETVVLRSVP 151
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
105-388 |
1.17e-54 |
|
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: 183.61 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 105 VPKLGKEAAVKAIKEWG----QLKSRITHLVFCTTSGVD----------------------MPGADYQLTKLLGLrpSVK 158
Cdd:cd00825 11 VSILGFEAAERAIADAGlsreYQKNPIVGVVVGTGGGSPrfqvfgadamravgpyvvtkamFPGASGQIATPLGI--HGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 159 RLMMYQqGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDT------------HLDSLVGQALFSDGAAALI 226
Cdd:cd00825 89 AYDVSA-ACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAmgalstpekasrTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 227 VGSDPDTSV-GEKPIFEMVSAAQTIlpdsDGAIDGHLREVGltfhllkdvpglisKNIEKSLDEAFRPLGISDWNSLFWI 305
Cdd:cd00825 168 VEELEHALArGAHIYAEIVGTAATI----DGAGMGAFAPSA--------------EGLARAAKEALAVAGLTVWDIDYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 306 AHPGGPAILDQVEIKLGLKE--GKMRATRHVMREYGNMSSA*VJFILDEMRKKSAKDGVA------------------TT 365
Cdd:cd00825 230 AHGTGTPIGDVKELKLLRSEfgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPpsihieeldeaglnivteTT 309
|
330 340
....*....|....*....|...
gi 1033014183 366 GEGLEWGVLFGFGPGLTVETVVL 388
Cdd:cd00825 310 PRELRTALLNGFGLGGTNATLVL 332
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
105-388 |
6.84e-54 |
|
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: 179.18 E-value: 6.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 105 VPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVD-MPGADYQLTKLLGLrPSVKRLMMYQqGCFAGGTVLRLAKDLAEN 183
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGeFSGAAGQLAYHLGI-SGGPAYSVNQ-ACATGLTALALAVQQVQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 184 NRGARVLVVCSEItavtfrgpsdthldslvgqALFSDGAAALIVGSDPDTSV-GEKPIFEMVSAAQTILPDSDgaidghl 262
Cdd:cd00327 85 GKADIVLAGGSEE-------------------FVFGDGAAAAVVESEEHALRrGAHPQAEIVSTAATFDGASM------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 263 revgltfhllkdVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMR--ATRHVMREYGN 340
Cdd:cd00327 139 ------------VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRspAVSATLIMTGH 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1033014183 341 MSSA*VJFILDEMRKKSAKDGVATTGEGLEWGVLFGFGPGLTVETVVL 388
Cdd:cd00327 207 PLGAAGLAILDELLLMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
19-388 |
1.62e-35 |
|
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.
Pssm-ID: 238423 [Multi-domain] Cd Length: 324 Bit Score: 132.56 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 19 PAGILAIGTANPANYVIQAEYPDYYFRITNsghmtdlkeKFKRMcdkstIRKRHMhvteEFLKENpnmcaymapsldarq 98
Cdd:cd00827 1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPG---------KYTTG-----IGQRHM----AGDDED--------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 99 divvveVPKLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVD-MPGADYQLTKLLGLRPSvkRLMMYQQGCFAGGTVLRLA 177
Cdd:cd00827 48 ------VPTMAVEAARRALERAGIDPDDIGLLIVATESPIDkGKSAATYLAELLGLTNA--EAFDLKQACYGGTAALQLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 178 KDLAENNRGARVLVVCSEItavtFRGPSDTHLDslvGQALFSDGAAALIVGSDPDtsvgeKPIFEMVSAAQTILPDSD-- 255
Cdd:cd00827 120 ANLVESGPWRYALVVASDI----ASYLLDEGSA---LEPTLGDGAAAMLVSRNPG-----ILAAGIVSTHSTSDPGYDfs 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 256 --GAIDGHLREVGLTFHLL--------KDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKE 325
Cdd:cd00827 188 pyPVMDGGYPKPCKLAYAIrltaepagRAVFEAAHKLIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLGGPP 267
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033014183 326 GKMRATRH-VMREYGNMSSA*VJFILDEMRKKsakdGVATTGEGLewgVLFGFGPGLTVETVVL 388
Cdd:cd00827 268 EKASQTRWiLLRRVGNMYAASILLGLASLLES----GKLKAGDRV---LLFSYGSGFTAEAFVL 324
|
|
| PksG |
COG3425 |
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ... |
98-232 |
1.17e-14 |
|
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 442651 [Multi-domain] Cd Length: 382 Bit Score: 74.83 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 98 QDIVVvevpkLGKEAAVKAIKEWGQLKSRITHLVFCTTSGVDM--PGADYqLTKLLGLRPSVkRLMMYQQGCFAGGTVLR 175
Cdd:COG3425 49 EDAVT-----MAANAARRALDRAGIDPSDIGAVYVGTESGPDAskPIATY-VHGALGLPPNC-RAFELKFACYAGTAALQ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033014183 176 LAKDLAENNRGARVLVVCSEItavtfrgpSDTHLDSlVGQALFSDGAAALIVGSDPD 232
Cdd:COG3425 122 AALGWVASGPNKKALVIASDI--------ARYGPGS-AGEYTQGAGAVAMLVGADPR 169
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
108-388 |
1.94e-11 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 64.48 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 108 LGKEAAVKAIKEWGQLKSRITHLVFCTTSGVD-MPGADYQLTKLLGLrpsvKRLMMY--QQGC--FAGGtvLRLAKDLAE 182
Cdd:cd00830 53 LAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGA----KNAAAFdiNAACsgFLYG--LSTAAGLIR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 183 NNRGARVLVVCSEITA--VTFRGPSdTHLdslvgqaLFSDGAAALIVGSDPDT---------SVGEKPIFEMVSAAQTIL 251
Cdd:cd00830 127 SGGAKNVLVVGAETLSriLDWTDRS-TAV-------LFGDGAGAVVLEATEEDpgildsvlgSDGSGADLLTIPAGGSRS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 252 PDSDGAIDGHL-----REVgltfhlLKDVPGLISKNIEKSLDEAfrplGIS----DWnslFWIaHPGGPAILDQVEIKLG 322
Cdd:cd00830 199 PFEDAEGGDPYlvmdgREV------FKFAVRLMPESIEEALEKA----GLTpddiDW---FVP-HQANLRIIEAVAKRLG 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033014183 323 LKEGKMratRHVMREYGNMSSA*VJFILDEM-RKKSAKDGvattgeglEWGVLFGFGPGLTVETVVL 388
Cdd:cd00830 265 LPEEKV---VVNLDRYGNTSAASIPLALDEAiEEGKLKKG--------DLVLLLGFGAGLTWGAALL 320
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
108-372 |
4.57e-08 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 54.35 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 108 LGKEAAVKAIKEWGQLKSRITHLVFCTTSGvDM--PGADYQLTKLLGLRpsvkrlmmyqqGCFA-------GGTV--LRL 176
Cdd:COG0332 54 LAVEAARKALEAAGIDPEDIDLIIVATVTP-DYlfPSTACLVQHKLGAK-----------NAAAfdinaacSGFVyaLSV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 177 AKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGSDPDT---------SVGEKPIFEMVSA 246
Cdd:COG0332 122 AAALIRSGQAKNVLVVGAETlSRIVDWTDRSTCV-------LFGDGAGAVVLEASEEGpgilgsvlgSDGSGADLLVVPA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 247 AQTILPDSDGAIDGHL-----REVgltfhlLKDVPGLISKNIEKSLDEAfrplGIS----DWnslfWIAHPGGPAILDQV 317
Cdd:COG0332 195 GGSRNPPSPVDEGDHYlrmdgREV------FKFAVRNLPEVIREALEKA----GLTlddiDW----FIPHQANLRIIEAV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 318 EIKLGLKEGKMRATrhvMREYGNMSSA*VJFILDEM-RKKSAKDG----VATTGEGLEWG 372
Cdd:COG0332 261 AKRLGLPEEKVVVN---IDRYGNTSAASIPLALDEAlREGRIKPGdlvlLAGFGAGLTWG 317
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
217-382 |
1.17e-06 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 49.86 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 217 LFSDGAAALIVGSDPDT---------SVGEKPIFEMVSAAQTILPDSDGAIDGHLREVGLTfhLLKDVPGLISKNIEKSL 287
Cdd:PRK12879 158 LFGDGAGAVVLEATENEpgfidyvlgTDGDGGDILYRTGLGTTMDRDALSGDGYIVQNGRE--VFKWAVRTMPKGARQVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 288 DEAfrplGIS----DWnslfWIAHPGGPAILDQVEIKLGLKEGKmraTRHVMREYGNMSSA*VJFILDEMRkksaKDGVA 363
Cdd:PRK12879 236 EKA----GLTkddiDW----VIPHQANLRIIESLCEKLGIPMEK---TLVSVEYYGNTSAATIPLALDLAL----EQGKI 300
|
170
....*....|....*....
gi 1033014183 364 TTGEGLewgVLFGFGPGLT 382
Cdd:PRK12879 301 KPGDTL---LLYGFGAGLT 316
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
153-378 |
1.93e-06 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 49.57 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 153 LRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLdsLVGQALFSDGAAALIVGSDPD 232
Cdd:PLN02854 236 LRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVVVSTENITLNWYFGNDRSM--LLCNCIFRMGGAAVLLSNKAR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 233 TSVGEKpiFEMVSAAQTilpdSDGAIDGHLR------------EVGLTFHLLKDVPGLISKNI----------------- 283
Cdd:PLN02854 314 DRKRSK--YQLVHTVRT----HKGADDKNYNcvyqreddkgtiGVSLARELMAVAGDALKTNIttlgplvlplseqfmff 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 284 -----EKSLDEAFRPLgISDWNSLF--WIAHPGGPAILDQVEIKLGLKEGKMRATRHVMREYGNMSSA*VJFildEMRKK 356
Cdd:PLN02854 388 vtlvrRKLLKAKVKPY-IPDFKLAFehFCIHAGGRAVLDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWY---ELAYT 463
|
250 260
....*....|....*....|..
gi 1033014183 357 SAKdGVATTGEGLeWGVLFGFG 378
Cdd:PLN02854 464 EAK-GRVSAGDRV-WQIAFGSG 483
|
|
| PRK07204 |
PRK07204 |
beta-ketoacyl-ACP synthase III; |
108-388 |
4.12e-06 |
|
beta-ketoacyl-ACP synthase III;
Pssm-ID: 235964 Cd Length: 329 Bit Score: 48.29 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 108 LGKEAAVKAIKEWGQLKSRITHLV-FCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRG 186
Cdd:PRK07204 55 MGAEAAKKAVEDAKLTLDDIDCIIcASGTIQQAIPCTASLIQEQLGLQHSGIPCFDINSTCLSFITALDTISYAIECGRY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 187 ARVLVVCSEITAVtfrGPSDTHLDSLVgqaLFSDGAAALIVGSDPDTS---------VGEKPIFEMVSAAQTILPDSDGA 257
Cdd:PRK07204 135 KRVLIISSEISSV---GLNWGQNESCI---LFGDGAAAVVITKGDHSSrilashmetYSSGAHLSEIRGGGTMIHPREYS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 258 IDghlREVGLTFHLL-KDVPGLISKNIEKSLDEAFRPLGISDWNSLFWIAHPGGPAILDQVEIKLGLKEGKMRAtrhVMR 336
Cdd:PRK07204 209 EE---RKEDFLFDMNgRAIFKLSSKYLMKFIDKLLMDAGYTLADIDLIVPHQASGPAMRLIRKKLGVDEERFVT---IFE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1033014183 337 EYGNMSSA*VJFILDEMRKKSAkdgvattgegLEWG---VLFGFGPGLTVETVVL 388
Cdd:PRK07204 283 DHGNMIAASIPVALFEAIKQKK----------VQRGnkiLLLGTSAGLSIGGILL 327
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
298-388 |
4.37e-05 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 41.72 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 298 DWnslFWIaHPGGPAILDQVEIKLGLKEGKMRATrhvMREYGNMSSA*VJFILDEM-RKKSAKDGvattgeglEWGVLFG 376
Cdd:pfam08541 12 DW---FVP-HQANLRIIDAVAKRLGLPPEKVVVN---LDEYGNTSAASIPLALDEAvEEGKLKPG--------DLVLLVG 76
|
90
....*....|..
gi 1033014183 377 FGPGLTVETVVL 388
Cdd:pfam08541 77 FGAGLTWGAALL 88
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
152-244 |
3.23e-04 |
|
FAE1/Type III polyketide synthase-like protein; The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding.
Pssm-ID: 429970 Cd Length: 290 Bit Score: 42.23 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033014183 152 GLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSE-ITAVTFRGpSDTHLdsLVGQALFSDGAAALIVGSD 230
Cdd:pfam08392 130 KLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYALVVSTEnITPNWYFG-NDRSM--LLPNCLFRMGGAAVLLSNR 206
|
90
....*....|....
gi 1033014183 231 PDTSVGEKpiFEMV 244
Cdd:pfam08392 207 PADRRRAK--YELV 218
|
|
| ACP_syn_III |
pfam08545 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl- ... |
164-236 |
3.49e-04 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430064 [Multi-domain] Cd Length: 80 Bit Score: 39.04 E-value: 3.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033014183 164 QQGCfAGGTV-LRLAKDLAENNRGARVLVVCSEI-TAVTFRGPSDTHLdslvgqaLFSDGAAALIVGSDPDTSVG 236
Cdd:pfam08545 4 NAAC-SGFVYaLSTAAALIRSGRAKNVLVIGAETlSKILDWTDRSTAV-------LFGDGAGAVVLEATDEPGAR 70
|
|
| |
