|
Name |
Accession |
Description |
Interval |
E-value |
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
1-352 |
3.55e-155 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 439.58 E-value: 3.55e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 1 MTRIAAVHGALAPHRRAQSEITDMVARTCLPEGTDRRVLDRLHRGARVDSRHMTLPLDQYRELDGFGAANDVFIAAATDL 80
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERDRRRLRRLFENSGIETRHSVLPLEWYLEPPSFGERNALYIEEALEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 81 GGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHV 160
Cdd:COG3424 81 AEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFLRADPDAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 161 AVLLSVELCSLTFQRNDATMANLVATGLFGDGAAAVVgfGSHRPAETAGPTIVDTRSHLYPDTGRLLGWDVRDTGFRVVL 240
Cdd:COG3424 161 VLVVCVELCSLTFQRDDDSKDNLVANALFGDGAAAVV--VSGDPRPGPGPRILAFRSYLIPDTEDVMGWDVGDTGFRMVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 241 DPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVLR 320
Cdd:COG3424 239 SPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNMSSATVLFVLE 318
|
330 340 350
....*....|....*....|....*....|..
gi 2351511137 321 DTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:COG3424 319 RLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
1-350 |
2.61e-100 |
|
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: 300.30 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 1 MTRIAAVHGALAPHRRAQSEITDMVAR--TCLPEGTDRRVLDRLHRGARVDSRHMTLP--LDQYRELD----GFGAANDV 72
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRlfSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPemspSLDERNDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 73 FIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDY 152
Cdd:cd00831 81 ALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDLAKDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 153 LVGRPDHVAVLLSVELCSLTFQRNDaTMANLVATGLFGDGAAAVV--GFGSHRPAETAGPTIVDTRSHLYPDTGRLLGWD 230
Cdd:cd00831 161 LEANPGARVLVVSTELCSLWYRGPD-HRSMLVGNALFGDGAAAVLlsNDPRDRRRERPLFELVRAASTLLPDSEDAMGWH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 231 VRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDH--GLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVG 308
Cdd:cd00831 240 LGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2351511137 309 NLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00831 320 NMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFTCESAVW 361
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
68-350 |
3.92e-26 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 107.47 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLA 147
Cdd:PLN03173 93 ARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMYQQGCFAGGTVLR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 148 RMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVATGLFGDGAAAVVgFGSHRPAETAGP--TIVDTRSHLYPDTG 224
Cdd:PLN03173 173 LAKDLAENNKGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFGDGAAAII-IGSDPVLGVEKPlfELVSAAQTILPDSD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 225 RLLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHL 304
Cdd:PLN03173 252 GAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALKPEKLRATRHVL 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2351511137 305 AEVGNLSSSSVLHVL----RDTLADHRPPPGTP---GVLLAMGPGFACELVLL 350
Cdd:PLN03173 332 SEYGNMSSACVLFILdemrKKSAEDGLKSTGEGlewGVLFGFGPGLTVETVVL 384
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
68-352 |
3.10e-16 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 78.19 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAaatDLGGRAVRDALRMAGLSAADVDLLIFTSVS-GISTPSIDARLAVRLGLRRdvrrLPMFGLGCAGG--AA 144
Cdd:TIGR00747 45 AADDETSS---TMGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG----IPAFDLSAACAgfIY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 145 GLARMHDYLVGRPDHVAVLLSVELCSLTFQRNDatMANLVatgLFGDGAAAVVGFGSHRPAEtagptIVDTRSHLYPDTG 224
Cdd:TIGR00747 118 ALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTD--RGTCV---LFGDGAGAVVLGESEDPGG-----IISTHLGADGTQG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 225 RLL----GW--DVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALD 298
Cdd:TIGR00747 188 EALylpaGGrpTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVV 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2351511137 299 VTwrhLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:TIGR00747 268 KT---VHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
36-197 |
4.84e-14 |
|
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: 70.65 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 36 RRVLDRLHRGARVDSRHMTLP---LDQYRELDGFGAAN-----DVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSV 107
Cdd:pfam00195 50 KEKFERLCDKSMIKKRYTHLTeeiLDEHPELCTEMAPSldarlEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 108 SGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVAT 186
Cdd:pfam00195 130 SGVRMPGADYQLAKLLGLRPSVKRVMLYFQGCYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRgPSKDRLDSLVGA 209
|
170
....*....|.
gi 2351511137 187 GLFGDGAAAVV 197
Cdd:pfam00195 210 ALFGDGAAAVI 220
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BH0617 |
COG3424 |
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and ... |
1-352 |
3.55e-155 |
|
Predicted naringenin-chalcone synthase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442650 [Multi-domain] Cd Length: 351 Bit Score: 439.58 E-value: 3.55e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 1 MTRIAAVHGALAPHRRAQSEITDMVARTCLPEGTDRRVLDRLHRGARVDSRHMTLPLDQYRELDGFGAANDVFIAAATDL 80
Cdd:COG3424 1 SARILSIATAVPPHRYTQEEIAEFAAELFGLDERDRRRLRRLFENSGIETRHSVLPLEWYLEPPSFGERNALYIEEALEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 81 GGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHV 160
Cdd:COG3424 81 AEEAARRALDKAGLDPEDIDHLVTVSCTGFAAPGLDARLINRLGLRPDVRRLPVGGMGCAAGAAGLRRAADFLRADPDAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 161 AVLLSVELCSLTFQRNDATMANLVATGLFGDGAAAVVgfGSHRPAETAGPTIVDTRSHLYPDTGRLLGWDVRDTGFRVVL 240
Cdd:COG3424 161 VLVVCVELCSLTFQRDDDSKDNLVANALFGDGAAAVV--VSGDPRPGPGPRILAFRSYLIPDTEDVMGWDVGDTGFRMVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 241 DPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVLR 320
Cdd:COG3424 239 SPEVPDLIAEHLAPAVEPLLARHGLTIEDIDHWAVHPGGPKVLDAVEEALGLPPEALAHSREVLREYGNMSSATVLFVLE 318
|
330 340 350
....*....|....*....|....*....|..
gi 2351511137 321 DTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:COG3424 319 RLLEEGAPAPGERGLAMAFGPGFTAELVLLRW 350
|
|
| CHS_like |
cd00831 |
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ... |
1-350 |
2.61e-100 |
|
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: 300.30 E-value: 2.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 1 MTRIAAVHGALAPHRRAQSEITDMVAR--TCLPEGTDRRVLDRLHRGARVDSRHMTLP--LDQYRELD----GFGAANDV 72
Cdd:cd00831 1 AATILAIGTAVPPHRVPQSELVDFYRRlfSSDHLPELKEKLKRLCAKTGIETRYLVLPggEETYAPRPemspSLDERNDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 73 FIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDY 152
Cdd:cd00831 81 ALEEARELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAMLINRLGLRPDVKRYNLGGMGCSAGAIALDLAKDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 153 LVGRPDHVAVLLSVELCSLTFQRNDaTMANLVATGLFGDGAAAVV--GFGSHRPAETAGPTIVDTRSHLYPDTGRLLGWD 230
Cdd:cd00831 161 LEANPGARVLVVSTELCSLWYRGPD-HRSMLVGNALFGDGAAAVLlsNDPRDRRRERPLFELVRAASTLLPDSEDAMGWH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 231 VRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDH--GLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVG 308
Cdd:cd00831 240 LGEEGLTFVLSRDVPRLVEKNLERVLRKLLARLgiGLFKLAFDHWCVHPGGRAVLDAVEKALGLSPEDLEASRMVLRRYG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2351511137 309 NLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00831 320 NMSSSSVLYVLAYMEAKGRVKRGDRGLLIAFGPGFTCESAVW 361
|
|
| PLN03173 |
PLN03173 |
chalcone synthase; Provisional |
68-350 |
3.92e-26 |
|
chalcone synthase; Provisional
Pssm-ID: 178717 [Multi-domain] Cd Length: 391 Bit Score: 107.47 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLA 147
Cdd:PLN03173 93 ARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRSSVKRFMMYQQGCFAGGTVLR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 148 RMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVATGLFGDGAAAVVgFGSHRPAETAGP--TIVDTRSHLYPDTG 224
Cdd:PLN03173 173 LAKDLAENNKGARVLVVCSEITAVTFRgPSDTHLDSLVGQALFGDGAAAII-IGSDPVLGVEKPlfELVSAAQTILPDSD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 225 RLLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHL 304
Cdd:PLN03173 252 GAIDGHLREVGLTFHLLKDVPGLISKNVEKSLTEAFKPLGISDWNSLFWIAHPGGPAILDQVEAKLALKPEKLRATRHVL 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2351511137 305 AEVGNLSSSSVLHVL----RDTLADHRPPPGTP---GVLLAMGPGFACELVLL 350
Cdd:PLN03173 332 SEYGNMSSACVLFILdemrKKSAEDGLKSTGEGlewGVLFGFGPGLTVETVVL 384
|
|
| PLN03169 |
PLN03169 |
chalcone synthase family protein; Provisional |
39-351 |
3.80e-25 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 215612 [Multi-domain] Cd Length: 391 Bit Score: 104.78 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 39 LDRLHRGARVDSRHMTLP---LDQYRELDGFGAAN-----DVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGI 110
Cdd:PLN03169 60 LERLCKTTTVKTRYVVMSkeiLDKYPELATEGTPTikqrlDIANEAVTQMAVEASLACIKEWGRPVSDITHLVYVSSSEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 111 STPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAVLLSVELCSLTFQR-NDATMANLVATGLF 189
Cdd:PLN03169 140 RLPGGDLYLAKQLGLSPDVQRVMLYFLGCSGGVAGLRVAKDIAENNPGSRVLLTTSETTILGFRPpSPDRPYDLVGAALF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 190 GDGAAAVV-GFGSHRPAETAGPTIVDTRSHLYPDTGRLLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTK 268
Cdd:PLN03169 220 GDGAAAVIiGADPIPVSESPFFELHTAIQQFLPGTEKTIDGRLTEEGINFKLGRELPQKIEDNIEGFCKKLMKKAGLVEK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 269 DVAA--WVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVL---RDTLADHRPPPGTPGVLLAMGPGF 343
Cdd:PLN03169 300 DYNDlfWAVHPGGPAILNRLEKKLKLAPEKLECSRRALMDYGNVSSNTIVYVLeymREELKKKGEEDEEWGLILAFGPGI 379
|
....*...
gi 2351511137 344 ACELVLLR 351
Cdd:PLN03169 380 TFEGILAR 387
|
|
| PLN03172 |
PLN03172 |
chalcone synthase family protein; Provisional |
68-350 |
4.22e-25 |
|
chalcone synthase family protein; Provisional
Pssm-ID: 178716 Cd Length: 393 Bit Score: 104.75 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLA 147
Cdd:PLN03172 93 ARQDMVVVEVPKLGKEAAAKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLKPSVKRFMMYQQGCFAGGTVLR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 148 RMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVATGLFGDGAAAV-VGFGSHRPAETAGPTIVDTRSHLYPDTGR 225
Cdd:PLN03172 173 LAKDLAENNAGSRVLVVCSEITAVTFRgPSDTHLDSLVGQALFGDGAAAViIGADPDTKIERPLFEIVSAAQTILPDSDG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 226 LLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLA 305
Cdd:PLN03172 253 AIDGHLREVGLTFHLLKDVPGLISKNIEKSLVEAFAPIGINDWNSIFWIAHPGGPAILDQVEIKLDLKEEKLRATRHVLS 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2351511137 306 EVGNLSSSSVLHVL----RDTLADHRPPPGTP---GVLLAMGPGFACELVLL 350
Cdd:PLN03172 333 DYGNMSSACVLFILdemrKKSIEEGKGSTGEGlewGVLFGFGPGLTVETVVL 384
|
|
| PLN03170 |
PLN03170 |
chalcone synthase; Provisional |
68-350 |
2.24e-24 |
|
chalcone synthase; Provisional
Pssm-ID: 178714 [Multi-domain] Cd Length: 401 Bit Score: 102.87 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLA 147
Cdd:PLN03170 97 ARQDIVVVEVPKLGKAAAQKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKMLGLRPSVNRLMMYQQGCFAGGTVLR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 148 RMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVATGLFGDGAAAV-VGFGSHRPAETAGPTIVDTRSHLYPDTGR 225
Cdd:PLN03170 177 VAKDLAENNRGARVLVVCSEITAVTFRgPSESHLDSMVGQALFGDGAAAViVGADPDERVERPLFQLVSASQTILPDSEG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 226 LLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLA 305
Cdd:PLN03170 257 AIDGHLREVGLTFHLLKDVPGLISKNIERSLEEAFKPLGITDYNSIFWVAHPGGPAILDQVEAKVGLEKERMRATRHVLS 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2351511137 306 EVGNLSSSSVLHVL----RDTLADHRPPPGTP---GVLLAMGPGFACELVLL 350
Cdd:PLN03170 337 EYGNMSSACVLFILdemrKRSAEDGQATTGEGfdwGVLFGFGPGLTVETVVL 388
|
|
| PLN03171 |
PLN03171 |
chalcone synthase-like protein; Provisional |
21-350 |
1.48e-22 |
|
chalcone synthase-like protein; Provisional
Pssm-ID: 178715 [Multi-domain] Cd Length: 399 Bit Score: 97.38 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 21 ITDMVARTCLPEGTDRRVLdrlHRGARVDSRHMTLpLDqyRELDGFGAANDVFIAAATDLGGRAVRDALRMAGLSAADVD 100
Cdd:PLN03171 58 LKDKFKRICQELGVQKRYL---HHTEELLSAHPEF-LD--HDAPSLDARLDIAADAVPELAAEAAKKAIAEWGRPAADIT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 101 LLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAVLLSVELCSLTFQRND-AT 179
Cdd:PLN03171 132 HLVVTTNSGAHIPGVDFRLVPLLGLRPSVRRTMLHLNGCFAGAAALRLAKDLAENNRGARVLVVAAEITLLLFNGPDeGC 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 180 MANLVATGLFGDGAAAVVGFGSHRPAETAGPTIVDTRSHLYPDTGRLLGWDVRDTGFRVVLDPR-VP----DVIRRHLAD 254
Cdd:PLN03171 212 FQTLLNQGLFGDGAAAVIVGADADAAERPLFEIVSAAQAIIPESDDAINMHFTEGGLDGNIGTRqVPgligDNIERCLLD 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 255 DVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVLrDTLADHRPPPGTP- 333
Cdd:PLN03171 292 AFAPLLGGDGGAEWNDLFWAVHPGSSAILDQVDAALGLEPEKLAASRRVLSDYGNMFGATVIFAL-DELRRQMEEAAAAg 370
|
330 340
....*....|....*....|..
gi 2351511137 334 -----GVLLAMGPGFACELVLL 350
Cdd:PLN03171 371 awpelGVMMAFGPGLTVDAMLL 392
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
76-352 |
1.88e-20 |
|
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: 90.55 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 76 AATDLGGRAVRDALRMAGLSAADVDLLIFTSVSG-ISTPSIDARLAVRLGLRR----DVR-----------------RLp 133
Cdd:COG0332 50 TTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPdYLFPSTACLVQHKLGAKNaaafDINaacsgfvyalsvaaaliRS- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 134 mfglgcaggaaglarmhdylvGRPDHVAVlLSVELCS--LTFQRNDATManlvatgLFGDGAAAVVgFGshrpAETAGPT 211
Cdd:COG0332 129 ---------------------GQAKNVLV-VGAETLSriVDWTDRSTCV-------LFGDGAGAVV-LE----ASEEGPG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 212 IVDTRSHLYPDTGRLLGWDVRDTGFRVVLDPRVPDVIR-----------RHLADDVKGFLEDHGLKTKDVAAWVCHPGGP 280
Cdd:COG0332 175 ILGSVLGSDGSGADLLVVPAGGSRNPPSPVDEGDHYLRmdgrevfkfavRNLPEVIREALEKAGLTLDDIDWFIPHQANL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351511137 281 KVLEAVAEALDLPcdaLDVTWRHLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:COG0332 255 RIIEAVAKRLGLP---EEKVVVNIDRYGNTSAASIPLALDEALREGRIKPGDLVLLAGFGAGLTWGAAVLRW 323
|
|
| PLN03168 |
PLN03168 |
chalcone synthase; Provisional |
70-351 |
6.13e-20 |
|
chalcone synthase; Provisional
Pssm-ID: 178712 [Multi-domain] Cd Length: 389 Bit Score: 89.71 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 70 NDVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARM 149
Cdd:PLN03168 94 HDIVVVQVPKLAAEAAQKAIKEWGGRKSDITHIVFATTSGVNMPGADHALAKLLGLKPTVKRVMMYQTGCFGGASVLRVA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 150 HDYLVGRPDHVAVLLSVELCSLTFQR-NDATMANLVATGLFGDGAAA-VVGFGSHRPAET-------AGPTIVdtrshly 220
Cdd:PLN03168 174 KDLAENNKGARVLAVASEVTAVTYRApSENHLDGLVGSALFGDGAGVyVVGSDPKPEVEKalfevhwAGETIL------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 221 PDTGRLLGWDVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVT 300
Cdd:PLN03168 247 PESDGAIDGHLTEAGLIFHLMKDVPGLISKNIEKFLNEARKCVGSPDWNEMFWAVHPGGPAILDQVEAKLKLTKDKMQGS 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351511137 301 WRHLAEVGNLSSSSVLHVLrDTLADHRPPPGTP--------GVLLAMGPGFACELVLLR 351
Cdd:PLN03168 327 RDILSEFGNMSSASVLFVL-DQIRQRSVKMGAStlgegsefGFFIGFGPGLTLEVLVLR 384
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
77-350 |
1.41e-19 |
|
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: 87.98 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 77 ATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGIS-TPSIDARLAVRLGLRR----DV------------------RRlp 133
Cdd:cd00830 50 TSDLAVEAAKKALEDAGIDADDIDLIIVATSTPDYlFPATACLVQARLGAKNaaafDInaacsgflyglstaagliRS-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 134 mfglgcaggaaglarmhdylvGRPDHVAVlLSVELCSLTFQRNDATMAnlvatGLFGDGAAAVVGfgshRPAEtAGPTIV 213
Cdd:cd00830 128 ---------------------GGAKNVLV-VGAETLSRILDWTDRSTA-----VLFGDGAGAVVL----EATE-EDPGIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 214 DTRSHLYPDTGRLLGWDVRDTGFRVVLDPRVPDVIR-----------RHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKV 282
Cdd:cd00830 176 DSVLGSDGSGADLLTIPAGGSRSPFEDAEGGDPYLVmdgrevfkfavRLMPESIEEALEKAGLTPDDIDWFVPHQANLRI 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351511137 283 LEAVAEALDLPCDALDVTwrhLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00830 256 IEAVAKRLGLPEEKVVVN---LDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLGFGAGLTWGAALL 320
|
|
| fabH |
TIGR00747 |
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II ... |
68-352 |
3.10e-16 |
|
3-oxoacyl-(acyl-carrier-protein) synthase III; FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 273249 [Multi-domain] Cd Length: 318 Bit Score: 78.19 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 68 AANDVFIAaatDLGGRAVRDALRMAGLSAADVDLLIFTSVS-GISTPSIDARLAVRLGLRRdvrrLPMFGLGCAGG--AA 144
Cdd:TIGR00747 45 AADDETSS---TMGFEAAKRAIENAGISKDDIDLIIVATTTpDHAFPSAACMVQAYLGIKG----IPAFDLSAACAgfIY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 145 GLARMHDYLVGRPDHVAVLLSVELCSLTFQRNDatMANLVatgLFGDGAAAVVGFGSHRPAEtagptIVDTRSHLYPDTG 224
Cdd:TIGR00747 118 ALSVAKQYIESGKYKTVLVVGAEKLSSTLDWTD--RGTCV---LFGDGAGAVVLGESEDPGG-----IISTHLGADGTQG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 225 RLL----GW--DVRDTGFRVVLDPRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALD 298
Cdd:TIGR00747 188 EALylpaGGrpTSGPSPFITMEGNEVFKHAVRKMGDVVEETLEANGLDPEDIDWFVPHQANLRIIEALAKRLELDMSQVV 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2351511137 299 VTwrhLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:TIGR00747 268 KT---VHKYGNTSAASIPLALDELLRTGRIKPGDLLLLVAFGGGLTWGAALVRF 318
|
|
| Chal_sti_synt_N |
pfam00195 |
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ... |
36-197 |
4.84e-14 |
|
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: 70.65 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 36 RRVLDRLHRGARVDSRHMTLP---LDQYRELDGFGAAN-----DVFIAAATDLGGRAVRDALRMAGLSAADVDLLIFTSV 107
Cdd:pfam00195 50 KEKFERLCDKSMIKKRYTHLTeeiLDEHPELCTEMAPSldarlEIANAEVPELGAEAALKAIKEWGQPKSKITHLVFCTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 108 SGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAVLLSVELCSLTFQ-RNDATMANLVAT 186
Cdd:pfam00195 130 SGVRMPGADYQLAKLLGLRPSVKRVMLYFQGCYGGATVLRTAKDIAENNPGARVLVVCSEITVLGFRgPSKDRLDSLVGA 209
|
170
....*....|.
gi 2351511137 187 GLFGDGAAAVV 197
Cdd:pfam00195 210 ALFGDGAAAVI 220
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
76-352 |
9.37e-14 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 70.87 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 76 AATDLGGRAVRDALRMAGLSAADVDLLIF-TSVSGISTPSIDARLAVRLGLRRdvrrLPMFglgcaggaaglarmhdylv 154
Cdd:PRK09352 51 TTSDLATEAAKKALEAAGIDPEDIDLIIVaTTTPDYAFPSTACLVQARLGAKN----AAAF------------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 155 grpDHVAVllsvelCS-----LtfqrndATMANLVATG--------------------------LFGDGAAAVVgfgsHR 203
Cdd:PRK09352 108 ---DLSAA------CSgfvyaL------STADQFIRSGayknvlvigaeklsrivdwtdrstcvLFGDGAGAVV----LG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 204 PAETAGptIVDTrsHLYPDtGRllGWDVRDTGFRVVLDPRVPDVIR-----------RHLADDVKGFLEDHGLKTKDVAA 272
Cdd:PRK09352 169 ASEEPG--ILST--HLGSD-GS--YGDLLYLPGGGSRGPASPGYLRmegrevfkfavRELAKVAREALEAAGLTPEDIDW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 273 WVCHPGGPKVLEAVAEALDLPCDALDVTwrhLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:PRK09352 242 LVPHQANLRIIDATAKKLGLPMEKVVVT---VDKYGNTSAASIPLALDEAVRDGRIKRGDLVLLEGFGGGLTWGAALVRW 318
|
|
| Chal_sti_synt_C |
pfam02797 |
Chalcone and stilbene synthases, C-terminal domain; This domain of chalcone synthase is ... |
221-351 |
2.34e-13 |
|
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: 66.71 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 221 PDTGRLLGWDVRDTGFRVVLDPRVPDVIrrhlADDVKGFLEDH----GLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDA 296
Cdd:pfam02797 11 PNTDGVIDGHLTEEGLTFHLGRDVPQKI----EENIEEFLKKAfeplGISEWNSLFWIVHPGGPAILDRVETKLGLEPEK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351511137 297 LDVTWRHLAEVGNLSSSSVLHVL---RDTLADHRPPPGTP----GVLLAMGPGFACELVLLR 351
Cdd:pfam02797 87 LEASRRALMDYGNVSSATVLFILdemRKKSLKKGLATTGEgldwGVLLAFGPGLTFETVVLR 148
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
77-352 |
9.19e-12 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 65.27 E-value: 9.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 77 ATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGIS-TPSIDARLAVRLGLRR----DVRrlpmfglGCAGGAAGLARMHD 151
Cdd:PRK12879 53 TSDLAIKAAERALARAGLDAEDIDLIIVATTTPDYlFPSTASQVQARLGIPNaaafDIN-------AACAGFLYGLETAN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 152 YLV--GRPDHVAVLlSVELCSltfQRNDATMANLVAtgLFGDGAAAVVgfgsHRPAETAgPTIVDTRSHLYPDTGRLL-- 227
Cdd:PRK12879 126 GLItsGLYKKVLVI-GAERLS---KVTDYTDRTTCI--LFGDGAGAVV----LEATENE-PGFIDYVLGTDGDGGDILyr 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 228 --GWDVRD-----TGFRVVLDPRvpDVIR---RHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPcdaL 297
Cdd:PRK12879 195 tgLGTTMDrdalsGDGYIVQNGR--EVFKwavRTMPKGARQVLEKAGLTKDDIDWVIPHQANLRIIESLCEKLGIP---M 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2351511137 298 DVTWRHLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:PRK12879 270 EKTLVSVEYYGNTSAATIPLALDLALEQGKIKPGDTLLLYGFGAGLTWAALLVKW 324
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
77-350 |
1.00e-07 |
|
"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: 52.82 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 77 ATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGIST-PSIDARLAVRLGLRR----DVR----------RLPMfglgcag 141
Cdd:cd00827 48 VPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKgKSAATYLAELLGLTNaeafDLKqacyggtaalQLAA------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 142 gaaglarmhDYL-VGRPDHVAVllsveLCSLTFQRNDATMANLVATglFGDGAAAVV-----GFGSHRPAETAGPTIVDT 215
Cdd:cd00827 121 ---------NLVeSGPWRYALV-----VASDIASYLLDEGSALEPT--LGDGAAAMLvsrnpGILAAGIVSTHSTSDPGY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 216 RSHLYPDTGRLLGWDVRDTGF-RVVLDPRVPDVIRRH---LADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALD 291
Cdd:cd00827 185 DFSPYPVMDGGYPKPCKLAYAiRLTAEPAGRAVFEAAhklIAKVVRKALDRAGLSEDIDYFVPHQPNGKKILEAVAKKLG 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 292 LPCDALDVT-WRHLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00827 265 GPPEKASQTrWILLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSYGSGFTAEAFVL 324
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
76-350 |
5.41e-05 |
|
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: 43.97 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 76 AATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGIST-PSIDARLAVRLGlrrdVRRLPMFGLGCAGGAAGlarmhdylv 154
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEfSGAAGQLAYHLG----ISGGPAYSVNQACATGL--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 155 grpdhVAVLLSVELcsltFQRNDATMANLVATG--LFGDGAAA-VVGFGSH--RPAETAGPTIVDTRSHLYPDTgrllgw 229
Cdd:cd00327 73 -----TALALAVQQ----VQNGKADIVLAGGSEefVFGDGAAAaVVESEEHalRRGAHPQAEIVSTAATFDGAS------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 230 dvrdtgfrvvldpRVPDVIRRHLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTWRH--LAEV 307
Cdd:cd00327 138 -------------MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVRSPAVSatLIMT 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2351511137 308 GNLSSSSVLH-------VLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00327 205 GHPLGAAGLAildelllMLEHEFIPPTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
171-350 |
2.00e-04 |
|
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: 42.62 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 171 LTFQRNDATMANLVATGLFGDGAAA-VVGFGSH--RPAETAGPTIVDTRSHLYPDTGRLLGWDVRDtgfrvvldprvpdv 247
Cdd:cd00825 141 STPEKASRTFDAAADGFVFGDGAGAlVVEELEHalARGAHIYAEIVGTAATIDGAGMGAFAPSAEG-------------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 248 irrhLADDVKGFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALDVTW--RHLAEVGNLSSSSVL--------- 316
Cdd:cd00825 207 ----LARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFGDKSPAvsATKAMTGNLSSAAVVlavdeavlm 282
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351511137 317 ----------------HVLRDTLADHRPPPGTPGVLLAMGPGFACELVLL 350
Cdd:cd00825 283 lehgfippsihieeldEAGLNIVTETTPRELRTALLNGFGLGGTNATLVL 332
|
|
| PLN02854 |
PLN02854 |
3-ketoacyl-CoA synthase |
84-345 |
1.59e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 215459 Cd Length: 521 Bit Score: 40.33 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 84 AVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAVL 163
Cdd:PLN02854 195 ALDSLFSKTGVKPRDIGILIVNCSLFNPTPSLSAMIVNHYKLRTDIKSYNLGGMGCSAGLISIDLANDLLKANPNSYAVV 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 164 LSVELCSLT-FQRNDATManLVATGLFGDGAAAVVGFGSHRPAETAGPTIVDT-RSHLYPD------------------- 222
Cdd:PLN02854 275 VSTENITLNwYFGNDRSM--LLCNCIFRMGGAAVLLSNKARDRKRSKYQLVHTvRTHKGADdknyncvyqreddkgtigv 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 223 ---------TGRLLGWDVRDTG-----------FRVVLdprvpdVIRRHLADDVKGFLEDHGLKTKDvaaWVCHPGGPKV 282
Cdd:PLN02854 353 slarelmavAGDALKTNITTLGplvlplseqfmFFVTL------VRRKLLKAKVKPYIPDFKLAFEH---FCIHAGGRAV 423
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351511137 283 LEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVLRDTLADHRPPPGTPGVLLAMGPGFAC 345
Cdd:PLN02854 424 LDELQKNLQLSDWHMEPSRMTLHRFGNTSSSSLWYELAYTEAKGRVSAGDRVWQIAFGSGFKC 486
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
44-117 |
1.97e-03 |
|
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: 39.69 E-value: 1.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351511137 44 RGARVdsrhmtlpldqYRELDGFGAANDVFIAAATDLGG----RAVRDALRMAGLSAADVDLLiftSVSGISTPSIDA 117
Cdd:COG0304 247 RGAKI-----------YAEVVGYGASSDAYHITAPAPDGegaaRAMRAALKDAGLSPEDIDYI---NAHGTSTPLGDA 310
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
77-130 |
2.24e-03 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 39.70 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2351511137 77 ATDLGGRAVRDALRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRL-GLRRDVR 130
Cdd:PRK08235 26 ATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAaGIPWEVQ 80
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
42-100 |
3.49e-03 |
|
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: 39.06 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351511137 42 LHRGARVdsrhmtlpldqYRELDGFGAANDVFIAAATDLGG----RAVRDALRMAGLSAADVD 100
Cdd:cd00834 245 KARGAKI-----------YAEILGYGASSDAYHITAPDPDGegaaRAMRAALADAGLSPEDID 296
|
|
| PLN00415 |
PLN00415 |
3-ketoacyl-CoA synthase |
62-351 |
4.14e-03 |
|
3-ketoacyl-CoA synthase
Pssm-ID: 177808 Cd Length: 466 Bit Score: 38.90 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 62 ELDGFGAANDVFiaaatdlggravrdalRMAGLSAADVDLLIFTSVSGISTPSIDARLAVRLGLRRDVRRLPMFGLGCAG 141
Cdd:PLN00415 135 ELVIFGALNSLF----------------KKTGIEPREVGIFIVNCSLFNPNPSLSSMIVNRYKLKTDVKTYNLSGMGCSA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 142 GAAGLARMHDYLVGRPDHVAVLLSVELCSLTFQR-NDATManLVATGLFGDGAAAV------------------------ 196
Cdd:PLN00415 199 GAISVDLATNLLKANPNTYAVIVSTENMTLSMYRgNDRSM--LVPNCLFRVGGAAVmlsnrsqdrvrskyelthivrthk 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 197 -------------------VGFG-SHRPAETAGPTIVDTRSHLYP------DTGRLLGWDVRDTGFRVVLDPRVPD--VI 248
Cdd:PLN00415 277 gssdkhytcaeqkedskgiVGVAlSKELTVVAGDTLKTNLTALGPlvlplsEKLRFILFLVKSKLFRLKVSPYVPDfkLC 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 249 RRHladdvkgfledhglktkdvaaWVCHPGGPKVLEAVAEALDLPCDALDVTWRHLAEVGNLSSSSVLHVLRDTLADHRP 328
Cdd:PLN00415 357 FKH---------------------FCIHAGGRALLDAVEKGLGLSEFDLEPSRMTLHRFGNTSSSSLWYELAYVEAKCRV 415
|
330 340
....*....|....*....|...
gi 2351511137 329 PPGTPGVLLAMGPGFACELVLLR 351
Cdd:PLN00415 416 KRGDRVWQLAFGSGFKCNSIVWR 438
|
|
| FAE1_CUT1_RppA |
pfam08392 |
FAE1/Type III polyketide synthase-like protein; The members of this family are described as ... |
84-196 |
4.99e-03 |
|
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: 38.38 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 84 AVRDALRMAGLSAADVDLLIfTSVSGIS-TPSIDARLAVRLGLRRDVRRLPMFGLGCAGGAAGLARMHDYLVGRPDHVAV 162
Cdd:pfam08392 90 AVDDLFAKTGVSPRDIDILV-VNCSLFNpTPSLSAMIVNRYKLRSDIKSYNLSGMGCSAGLISIDLAKNLLQVHPNTYAL 168
|
90 100 110
....*....|....*....|....*....|....*
gi 2351511137 163 LLSVELCSLTFQR-NDATManLVATGLFGDGAAAV 196
Cdd:pfam08392 169 VVSTENITPNWYFgNDRSM--LLPNCLFRMGGAAV 201
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
243-352 |
6.00e-03 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 38.00 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351511137 243 RVPDVIRRhladdvkgFLEDHGLKTKDVAAWVCHPGGPKVLEAVAEALDLPCDALdVTwrHLAEVGNLSSSSVLHVLRDT 322
Cdd:CHL00203 227 QVPAVIIK--------CLNALNISIDEVDWFILHQANKRILEAIANRLSVPNSKM-IT--NLEKYGNTSAASIPLALDEA 295
|
90 100 110
....*....|....*....|....*....|
gi 2351511137 323 LADHRPPPGTPGVLLAMGPGFACELVLLRW 352
Cdd:CHL00203 296 IQNNKIQPGQIIVLSGFGAGLTWGAIVLKW 325
|
|
| |
