|
Name |
Accession |
Description |
Interval |
E-value |
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
6-390 |
0e+00 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 773.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 6 PRDVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVARN-QFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPK 84
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 85 TVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAKASNMMGLTAEMLGRMNGI 164
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 165 SREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDPKGGTVTAATSSA 244
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 245 LSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSVMK 324
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491207493 325 GLGIYDK-QDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK08947 321 DLGLLDKmDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
8-390 |
0e+00 |
|
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]
Pssm-ID: 131498 Cd Length: 385 Bit Score: 588.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVARN-QFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNpKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAKASNMMGLTAEMLGRMNGISR 166
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAKAAGMMGLTAEMLGKMHGISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 167 EEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDPKGGTVTAATSSALS 246
Cdd:TIGR02445 161 EQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKNGTVTAGTSSALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 247 DGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGL 326
Cdd:TIGR02445 241 DGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491207493 327 GIYDKQD-IINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:TIGR02445 321 GLLDKMDeKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
7-390 |
0e+00 |
|
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: 508.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTlEQGMNIGRNIGLLADLPKTV 86
Cdd:COG0183 2 REVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQA-GQGQNPARQAALLAGLPESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGM-----MHGIDLNPEASKHYAKAS-------NMMGLT 154
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMllpkaRWGYRMNAKLVDPMINPGltdpytgLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 155 AEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILcDIDEVIRPDANLEAFKALRPVFDpKG 234
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVV-DRDEGPRPDTTLEKLAKLKPAFK-KD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 235 GTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEA 314
Cdd:COG0183 238 GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491207493 315 FAAQGLSVMKGLGIYDkqDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:COG0183 318 FAAQVLAVLRELGLDP--DKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
10-389 |
5.93e-175 |
|
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: 492.38 E-value: 5.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 10 VIVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEqGMNIGRNIGLLADLPKTVAGQ 89
Cdd:cd00751 1 VIVSAVRTPIGR-FGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 90 TVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMH------------GIDLNPEASKHYAKASNMMGLTAEM 157
Cdd:cd00751 79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLpkarrggrlglnTLDGMLDDGLTDPFTGLSMGITAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 158 LGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGfKILCDIDEVIRPDANLEAFKALRPVFDpKGGTV 237
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG-PVVVDRDEGPRPDTTLEKLAKLKPAFK-KDGTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 238 TAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAA 317
Cdd:cd00751 237 TAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491207493 318 QGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:cd00751 317 QALACLKELGL--DPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
11-388 |
3.90e-158 |
|
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: 449.76 E-value: 3.90e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 11 IVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQgMNIGRNIGLLADLPKTVAGQT 90
Cdd:TIGR01930 1 IVAAARTPIGK-FGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 91 VNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAKASNM-------------MGLTAEM 157
Cdd:TIGR01930 79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKPGNAELEDArlkdltdantglpMGVTAEN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 158 LGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILcDIDEVIRPDANLEAFKALRPVFDPKGgTV 237
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTV-SSDEGIRPNTTLEKLAKLKPAFDPDG-TV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 238 TAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAA 317
Cdd:TIGR01930 237 TAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207493 318 QGLSVMKGLGIYDkqDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIE 388
Cdd:TIGR01930 317 QVLACIKELGLDL--EKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
6-390 |
1.79e-141 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 408.00 E-value: 1.79e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 6 PRDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTlEQGMNIGRNIGLLADLPKT 85
Cdd:PRK05790 1 MKDVVIVSAARTPIGKF-GGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQA-GAGQNPARQAALKAGLPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMG---HV------GMMHGidlNPEASKHYAK-----ASN-- 149
Cdd:PRK05790 79 VPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSqapHVlpgsrwGQKMG---DVELVDTMIHdgltdAFNgy 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 150 MMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPV 229
Cdd:PRK05790 156 HMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 230 FDpKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTI 309
Cdd:PRK05790 236 FD-KDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 310 ELNEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:PRK05790 315 EINEAFAAQALAVEKELGL--DPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
.
gi 491207493 390 V 390
Cdd:PRK05790 393 P 393
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
7-390 |
1.29e-127 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 372.90 E-value: 1.29e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTK-----NGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLAD 81
Cdd:PRK06445 2 EDVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 82 LPKTVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHG--IDLNP-----EASKHYAKASNM-MGL 153
Cdd:PRK06445 82 LPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphIEPNPklltdPKYIEYDLTTGYvMGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 154 TAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGhDANGFKILCDIDEVIRPDANLEAFKALRPVFDPk 233
Cdd:PRK06445 162 TAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKP- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 234 GGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNE 313
Cdd:PRK06445 240 DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491207493 314 AFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK06445 320 AFAVVVLYAIKELGL--DPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
7-390 |
2.47e-125 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 366.97 E-value: 2.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARN-QFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKT 85
Cdd:PRK09050 2 TEAFICDAIRTPIGRY-GGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHG------------ID-------LNPEASKHYAK 146
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGkadsafsrqaeiFDttigwrfVNPLMKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 147 ASnmMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKAL 226
Cdd:PRK09050 161 DS--MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 227 RPVFDPkGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADI 306
Cdd:PRK09050 239 KPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 307 QTIELNEAFAAQGLSVMKGLGIYDKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATV 386
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLADDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397
|
....
gi 491207493 387 IERV 390
Cdd:PRK09050 398 IERV 401
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
7-390 |
4.73e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 363.69 E-value: 4.73e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVAR-NQFDVNeVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKT 85
Cdd:PRK07661 2 REAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRaGNYEGP-IDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMM-HGIDLNPEASKHYAKASNMMGLTAEMLGRMNGI 164
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMgHVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 165 SREEQDAFGVESHRRAWAATQEGRFKNEIVGV--------EGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDPKGgT 236
Cdd:PRK07661 161 SREDQDAFAVRSHQRAAKALAEGKFADEIVPVdvtlrtvgENNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKG-S 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 237 VTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFA 316
Cdd:PRK07661 240 VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491207493 317 AQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK07661 320 SQSIQVIRELGL--DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
8-390 |
6.39e-124 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 363.55 E-value: 6.39e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVARNQ-FDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK09052 7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNSV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMM-HGIDLNPEAskhYAKASNM-----MGLTAEMLGR 160
Cdd:PRK09052 87 GGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgNKPSMSPAI---FARDENVgiaygMGLTAEKVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 161 MNGISREEQDAFGVESHRRAWAATQEGRFKNEIV---------GVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFD 231
Cdd:PRK09052 164 QWKVSREDQDAFALESHQKAIAAQQAGEFKDEITpyeiterfpDLATGEVDVKTRTVDLDEGPRADTSLEGLAKLKPVFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 232 PKGgTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIEL 311
Cdd:PRK09052 244 NKG-SVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIEL 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491207493 312 NEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK09052 323 NEAFAAQSLAVIRDLGL--DPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
8-390 |
3.88e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 353.80 E-value: 3.88e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKTK-NGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK08242 3 EAYIYDAVRTPRGKGKkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMmhGID-----LNPEASKHyakaSNMM--GLTAEMLG 159
Cdd:PRK08242 83 PGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM--GSDggawaMDPSTNFP----TYFVpqGISADLIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 160 RMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEghDANGFKILcDIDEVIRPDANLEAFKALRPVFDPKGGTV-- 237
Cdd:PRK08242 157 TKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGLTIL-DHDEHMRPGTTMESLAKLKPSFAMMGEMGgf 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 238 ------------------TAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRA 299
Cdd:PRK08242 234 davalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 300 GLTMADIQTIELNEAFAAQGLSVMKGLGIYDkqDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGL 379
Cdd:PRK08242 314 GLTVDDIDLFELNEAFASVVLRFMQALDIPH--DKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGG 391
|
410
....*....|.
gi 491207493 380 GQGIATVIERV 390
Cdd:PRK08242 392 GMGIATIIERV 402
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
6-390 |
2.42e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 351.98 E-value: 2.42e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 6 PRDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMnIGRNIGLLADLPKT 85
Cdd:PRK06205 1 MRDAVICEPVRTPVGRF-GGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPA-IGRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHM----------------GHVGMMHGIDLNPEAS--KHYAKA 147
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMsnvefyttdmrwgvrgGGVQLHDRLARGRETAggRRFPVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 148 SNMMGlTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALR 227
Cdd:PRK06205 159 GGMIE-TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 228 PV---FDPkGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMA 304
Cdd:PRK06205 238 PImgkQDP-EATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 305 DIQTIELNEAFAAQGLSVMKGLGIyDKQDI--INLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQG 382
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWGF-GADDEerLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQG 395
|
....*...
gi 491207493 383 IATVIERV 390
Cdd:PRK06205 396 LAAVFERV 403
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
7-390 |
1.14e-116 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 345.23 E-value: 1.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARN-QFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKT 85
Cdd:TIGR02430 1 REAYICDAIRTPIGRY-GGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGID-------------------LNPEASKHYAK 146
Cdd:TIGR02430 80 VPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKAdsafsrsakiedttigwrfINPLMKALYGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 147 ASnmMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKAL 226
Cdd:TIGR02430 160 DS--MPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 227 RPVFDPkGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADI 306
Cdd:TIGR02430 238 KPVVRP-DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 307 QTIELNEAFAAQGLSVMKGLGIYDKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATV 386
Cdd:TIGR02430 317 DVIELNEAFAAQALAVLRELGLADDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALA 396
|
....
gi 491207493 387 IERV 390
Cdd:TIGR02430 397 IERV 400
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
7-390 |
2.29e-113 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 336.55 E-value: 2.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGkTKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK09051 3 REVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGH-------------------VGMMHGIDLNPEASKHyaka 147
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRapyllpaarwgarmgdaklVDMMVGALHDPFGTIH---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 148 snmMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILcDIDEVIRPDANLEAFKALR 227
Cdd:PRK09051 158 ---MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVF-DTDEHVRADTTLEDLAKLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 228 PVFDPKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQ 307
Cdd:PRK09051 234 PVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 308 TIELNEAFAAQGLSVMKGLGIYDKQdiINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVI 387
Cdd:PRK09051 314 VIEANEAFAAQACAVTRELGLDPAK--VNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIF 391
|
...
gi 491207493 388 ERV 390
Cdd:PRK09051 392 ERL 394
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
8-389 |
1.74e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 329.27 E-value: 1.74e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVAR-NQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPkTV 86
Cdd:PRK07851 3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKvPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDL----NP---EASKHYAKASN---------- 149
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtkNPlfaEAQARTAARAEggaeawhdpr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 150 ----------MMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANgfkiLCDIDEVIRPDAN 219
Cdd:PRK07851 162 edgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGT----VVSTDDGPRAGTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 220 LEAFKALRPVFDPkGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRA 299
Cdd:PRK07851 238 YEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 300 GLTMADIQTIELNEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGL 379
Cdd:PRK07851 317 GMSIDDIDLVEINEAFAAQVLPSARELGI--DEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|
gi 491207493 380 GQGIATVIER 389
Cdd:PRK07851 395 GQGMAMVLER 404
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
11-390 |
8.10e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 327.07 E-value: 8.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 11 IVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTVAGQT 90
Cdd:PRK06504 6 IVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGTS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 91 VNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMH----------GIDLNPEASKHYAKA--SNMMGltAEML 158
Cdd:PRK06504 85 IDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSpstlpaknglGHYKSPGMEERYPGIqfSQFTG--AEMM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 159 GRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDpkGGTVT 238
Cdd:PRK06504 163 AKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE--GGRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 239 AATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQ 318
Cdd:PRK06504 241 AATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASV 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491207493 319 GLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK06504 321 PLAWLKATGA--DPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
6-389 |
1.86e-106 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 320.94 E-value: 1.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 6 PRDVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKT 85
Cdd:PLN02287 45 GDDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPET 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEAsKHYAKASNM---MGLTAEMLGRMN 162
Cdd:PLN02287 125 VPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRV-ESFSQAQDCllpMGITSENVAERF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 163 GISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDAN-----GFKILCDIDEVIRPDANLEAFKALRPVFDpKGGTV 237
Cdd:PLN02287 204 GVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDpktgeEKPIVISVDDGIRPNTTLADLAKLKPVFK-KNGTT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 238 TAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAA 317
Cdd:PLN02287 283 TAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFAS 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491207493 318 QGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQ--QDTQIGLATMCIGLGQGIATVIER 389
Cdd:PLN02287 363 QFVYCCKKLGL--DPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgKDCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
11-390 |
7.78e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 314.34 E-value: 7.78e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 11 IVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTVAGQT 90
Cdd:PRK07801 6 IVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 91 VNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHV----GMMHGIDL---NPEAS-----KHYAKASNMMGLTAEML 158
Cdd:PRK07801 85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIpissAMTAGEQLgftSPFAEskgwlHRYGDQEVSQFRGAELI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 159 GRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGhdangfkilCDIDEVIRpDANLEAFKALRPVFDpkGGTVT 238
Cdd:PRK07801 165 AEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKPLVE--GGRLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 239 AATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQ 318
Cdd:PRK07801 233 AAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491207493 319 GLSVMKGLGiYDKQDiINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK07801 313 VLAWLKETG-ADPAK-VNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIERL 382
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
10-390 |
3.95e-101 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 304.72 E-value: 3.95e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 10 VIVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTVAGQ 89
Cdd:PRK07850 5 VIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 90 TVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMmhGIDLNPEASKHYAKASNM-MG---LTAEMLGRMNGIS 165
Cdd:PRK07850 84 TIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL--GANAGPGRGLPRPDSWDIdMPnqfEAAERIAKRRGIT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 166 REEQDAFGVESHRRAWAATQEGRFKNEIVGV------EGHDANGFKILCDIDEVIRpDANLEAFKALRPVFDpkGGTVTA 239
Cdd:PRK07850 162 REDVDAFGLRSQRRAAQAWAEGRFDREISPVqapvldEEGQPTGETRLVTRDQGLR-DTTMEGLAGLKPVLE--GGIHTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 240 ATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQG 319
Cdd:PRK07850 239 GTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFASVV 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207493 320 LSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK07850 319 LSWAQVHEP--DMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
8-390 |
9.37e-101 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 304.39 E-value: 9.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTVA 87
Cdd:PRK08131 3 DAYIYDGLRSPFGR-HAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 88 GQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGI-------DL------------NPEASKHYAKAS 148
Cdd:PRK08131 82 GQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKaesafsrDAkvfdttigarfpNPKIVAQYGNDS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 149 nmMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDAN-GFKILCDIDEVIRPDANLEAFKALR 227
Cdd:PRK08131 162 --MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRkLPPKLVAEDEHPRPSSTVEALTKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 228 PVFDpkGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQ 307
Cdd:PRK08131 240 PLFE--GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 308 TIELNEAFAAQGLSVMKGLGIYDKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVI 387
Cdd:PRK08131 318 IIEINEAFASQVLGCLKGLGVDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVI 397
|
...
gi 491207493 388 ERV 390
Cdd:PRK08131 398 ERV 400
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
7-389 |
8.61e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 286.40 E-value: 8.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTKnGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVnQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK05656 2 QDVVIVAATRTAIGSFQ-GSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQV-LTAGAGQNPARQAAIKAGLPHSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMG-----------HVGMMHGIDLNPEASKHYAKASN--MMGL 153
Cdd:PRK05656 80 PAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSlapyvlpgartGLRMGHAQLVDSMITDGLWDAFNdyHMGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 154 TAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDpK 233
Cdd:PRK05656 160 TAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK-K 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 234 GGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNE 313
Cdd:PRK05656 239 DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491207493 314 AFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:PRK05656 319 AFAAQSLAVGKELGW--DAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
8-388 |
2.37e-89 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 275.11 E-value: 2.37e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRSAMGKTKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKTVA 87
Cdd:PRK07108 3 EAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 88 GQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVG--MMHGIDLNPEASKHYAKASNMMGLTAEMLGRMNGIS 165
Cdd:PRK07108 83 GMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQneMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRYGIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 166 REEQDAFGVESHRRAWAATQEGRFKNEIV------GVEGHDANGF---KILCDIDEVIRPDANLEAFKALRPVFdpKGGT 236
Cdd:PRK07108 163 KERQDEYGVQSQQRAAAAQAAGRFDDEIVpitvtaGVADKATGRLftkEVTVSADEGIRPDTTLEGVSKIRSAL--PGGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 237 VTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFA 316
Cdd:PRK07108 241 ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491207493 317 AQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIE 388
Cdd:PRK07108 321 VQVLYCRDTLGI--PMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
5-390 |
2.48e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 276.13 E-value: 2.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 5 NPRDVVIVDGVRSAMGKTKNGMFRNVRADsLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQgMNIGRNIGLLADLPK 84
Cdd:PRK08170 1 MARPVYIVDGARTPFLKARGGPGPFSASD-LAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDE-ANIARVVALRLGCGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 85 TVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHV-------------------GMMHGIDLNPEASKHYA 145
Cdd:PRK08170 79 KVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHApllfsekmvrwlagwyaakSIGQKLAALGKLRPSYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 146 K-------------ASNMMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKnEIVGVEGHDANGFkilcDIDE 212
Cdd:PRK08170 159 ApvigllrgltdpvVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGKFY----DHDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 213 VIRPDANLEAFKALRPVFDPKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPAT 292
Cdd:PRK08170 234 GVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 293 QKALKRAGLTMADIQTIELNEAFAAQGLSVM----------------KGLGIYDkQDIINLNGGAIALGHPLGCSGARIT 356
Cdd:PRK08170 314 TPLLQRHGLTLEDLDLWEINEAFAAQVLACLaawadeeycreqlgldGALGELD-RERLNVDGGAIALGHPVGASGARIV 392
|
410 420 430
....*....|....*....|....*....|....
gi 491207493 357 TTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK08170 393 LHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
7-390 |
3.95e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 256.50 E-value: 3.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTKnGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVnQTLEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK06633 3 KPVYITHAKRTAFGSFM-GSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQV-ITGGSGQNPARQTLIHAGIPKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVgmMHGIDLNPEASKHYAKASNMM--------------G 152
Cdd:PRK06633 81 PGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLG--MHGSYIRAGAKFGDIKMVDLMqydgltdvfsgvfmG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 153 LTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEgHDANGFKILCDIDEVIRPDANLEAFKALRPVFDp 232
Cdd:PRK06633 159 ITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIE-VTIKKTTSLFDHDETVRPDTSLEILSKLRPAFD- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 233 KGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELN 312
Cdd:PRK06633 237 KNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 313 EAFAAQGLSVMKGLgiydKQDI--INLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK06633 317 EAFAAQSIYVNREM----KWDMekVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
7-390 |
6.29e-82 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 255.79 E-value: 6.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTleqgmNIG----RNIGLLADL 82
Cdd:PLN02644 1 RDVCIVGVARTPIGGF-LGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSA-----NLGqapaRQAALGAGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 83 PKTVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHM----------------GHV----GMMHGIDLNPEASK 142
Cdd:PLN02644 75 PPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMsnapkylpearkgsrlGHDtvvdGMLKDGLWDVYNDF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 143 HyakasnmMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFK-ILCDIDEviRPDA-NL 220
Cdd:PLN02644 155 G-------MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPsVIVDKDE--GLGKfDP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 221 EAFKALRPVFDPKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAG 300
Cdd:PLN02644 226 AKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 301 LTMADIQTIELNEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLG 380
Cdd:PLN02644 306 LEASQVDYYEINEAFSVVALANQKLLGL--DPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGG 383
|
410
....*....|
gi 491207493 381 QGIATVIERV 390
Cdd:PLN02644 384 GASAIVVELM 393
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
9-258 |
7.92e-82 |
|
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: 251.07 E-value: 7.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 9 VVIVDGVRSAMGKtKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTlEQGMNIGRNIGLLADLPKTVAG 88
Cdd:pfam00108 1 VVIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQA-GEGQNPARQAALKAGIPDSAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 89 QTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAKASNM--------------MGLT 154
Cdd:pfam00108 79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLlipdgltdafngyhMGLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 155 AEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGfKILCDIDEVIRPDANLEAFKALRPVFDpKG 234
Cdd:pfam00108 159 AENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKG-KPTVDKDEGIRPPTTAEPLAKLKPAFD-KE 236
|
250 260
....*....|....*....|....
gi 491207493 235 GTVTAATSSALSDGASAMLLMSAE 258
Cdd:pfam00108 237 GTVTAGNASPINDGAAAVLLMSES 260
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
3-389 |
6.73e-81 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 254.14 E-value: 6.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 3 TLNPRDVVIVDGVRSAMGKTKNGmFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEqGMNIGRNIGLLADL 82
Cdd:PRK08963 1 TRQGDRIAIVSGLRTPFAKQATA-FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPE-APNIAREIVLGTGM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 83 PKTVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHV------GMMHG-IDLN------------------ 137
Cdd:PRK08963 79 NVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLpigvskKLARAlVDLNkartlgqrlklfsrlrlr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 138 -----PEASKHYAKASNMmGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDangFKILCDIDE 212
Cdd:PRK08963 159 dllpvPPAVAEYSTGLRM-GDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPP---YKQPLEEDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 213 VIRPDANLEAFKALRPVFDPKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDA-AIMGYGPVPA 291
Cdd:PRK08963 235 NIRGDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 292 TQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGIYD---------------KQDIINLNGGAIALGHPLGCSGARIT 356
Cdd:PRK08963 315 TPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFASERfareklgrsqaigevDMSKFNVLGGSIAYGHPFAATGARMI 394
|
410 420 430
....*....|....*....|....*....|...
gi 491207493 357 TTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:PRK08963 395 TQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
8-390 |
8.06e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 253.93 E-value: 8.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 8 DVVIVDGVRS--AMGKTKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMNIGRNIGLLADLPKT 85
Cdd:PRK06025 3 EAYIIDAVRTprGIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 86 VAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAKASNM----------MGLTA 155
Cdd:PRK06025 83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPLGMGSGNLrlralhpqshQGVCG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 156 EMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANgfkILCDIDEVIRPDANLEAFKALRPVF----- 230
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGS---VALDHEEFPRPQTTAEGLAALKPAFtaiad 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 231 ---DPKGGTVT-----------------AATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVP 290
Cdd:PRK06025 240 yplDDKGTTYRglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 291 ATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQI 370
Cdd:PRK06025 320 AAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDL--DRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKR 397
|
410 420
....*....|....*....|
gi 491207493 371 GLATMCIGLGQGIATVIERV 390
Cdd:PRK06025 398 GLVTMCAAGGMAPAIIIERV 417
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
7-388 |
2.11e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 249.24 E-value: 2.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTkNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTlEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK08235 2 SKTVIVSAARTPFGKF-GGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQG-GQGQIPSRQAARAAGIPWEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGH-----------VGMMHG--IDLNPEASKHYAKASNMMGL 153
Cdd:PRK08235 80 QTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNapyilpgarwgYRMGDNevIDLMVADGLTCAFSGVHMGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 154 TAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGFKILCDIDEVIRPDANLEAFKALRPVFDPK 233
Cdd:PRK08235 160 YGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 234 GgTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNE 313
Cdd:PRK08235 240 G-TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491207493 314 AFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIE 388
Cdd:PRK08235 319 AFAAVALASTEIAGI--DPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
10-390 |
2.07e-66 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 214.63 E-value: 2.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 10 VIVDGVRSAMGKtKNGMFRNVRADSLSAELVRALvARNQFDvnEVEDLIWGCVnqtLEQGMNIGRNIGLLADLPKTVAGQ 89
Cdd:PRK06690 4 VIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLTFL-SKGMER--EIDDVILGNV---VGPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 90 TVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAkasnmMGLTAEMLGRMNGISREEQ 169
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-----MGVAAEYVAERYNITREMQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 170 DAFGVESHRRAWAATQEGRFKNEIVGVEGHdangfkilcdIDEVIRPDANLEAF-KALRPVFDpKGGTVTAATSSALSDG 248
Cdd:PRK06690 152 DEYACLSYKRTLQALEKGYIHEEILSFNGL----------LDESIKKEMNYERIiKRTKPAFL-HNGTVTAGNSCGVNDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 249 ASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGI 328
Cdd:PRK06690 221 ACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQI 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491207493 329 -YDKqdiINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIERV 390
Cdd:PRK06690 301 pYEK---LNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
7-390 |
1.75e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 210.64 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 7 RDVVIVDGVRSAMGKTKNGmFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTlEQGMNIGRNIGLLADLPKTV 86
Cdd:PRK06366 2 KDVYIVSAKRTAIGKFGRS-FSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQA-GVGQNPAGQAAYHAGLPFGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 87 AGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLN--PEA--SKHYAKASNM------------ 150
Cdd:PRK06366 80 TKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgPKHllHKNYKIDDAMlvdglidafyfe 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 151 -MGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDAngfkilcdiDEVIRpDANLEAFKALRPV 229
Cdd:PRK06366 160 hMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLDR---------DEGIR-KTTMEDLAKLPPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 230 FDpKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTI 309
Cdd:PRK06366 230 FD-KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 310 ELNEAFAAQGLSVMKGLGIYDKQdiINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:PRK06366 309 EHNEAFSIASIIVRDQLKIDNER--FNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEM 386
|
.
gi 491207493 390 V 390
Cdd:PRK06366 387 V 387
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-388 |
1.63e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 203.20 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 1 MATLNPRDVVIVDGVRSAMGKTKnGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVnQTLEQGMNIGRNIGLLA 80
Cdd:PRK06954 1 MTAVDQDPIVIASAARTPMAAFQ-GEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCV-LPAGQGQAPARQAALGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 81 DLPKTVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHM-----------GHVGMMHGIDLN----PEASKHYA 145
Cdd:PRK06954 79 GLPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMtnapyllpkarGGMRMGHGQVLDhmflDGLEDAYD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 146 KAsNMMGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDANGfKILCDIDEVIRpDANLEAFKA 225
Cdd:PRK06954 159 KG-RLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKG-DTVIDRDEQPF-KANPEKIPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 226 LRPVFDpKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMAD 305
Cdd:PRK06954 236 LKPAFS-KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 306 IQTIELNEAFAAQGLSVMKGLGIydKQDIINLNGGAIALGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIAT 385
Cdd:PRK06954 315 VDLFEINEAFAVVTMAAMKEHGL--PHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAM 392
|
...
gi 491207493 386 VIE 388
Cdd:PRK06954 393 GIE 395
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
265-389 |
4.96e-58 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 185.15 E-value: 4.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 265 LKPRAVIRSMAVAGCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGI-YDKqdiINLNGGAIA 343
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIdPEK---VNVNGGAIA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 491207493 344 LGHPLGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:pfam02803 78 LGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
16-388 |
3.11e-54 |
|
nondecarboxylating condensing enzymes; In general, thiolases 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. 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: 238422 [Multi-domain] Cd Length: 393 Bit Score: 184.23 E-value: 3.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 16 RSAMGK--TKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEqGMNIGRNIGLLADLPKTVAGQTVNR 93
Cdd:cd00826 5 MTAFGKfgGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPAIGMNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 94 LCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVgmmhgiDLNPEASKHYAKASNMMGltaemlgrmngiSREEQDAFG 173
Cdd:cd00826 84 LCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAKEKHIDVLINKYG------------MRACPDAFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 174 VESHRRAWAATQEGRFKNEIV--GVEGHDANgfkILCDIDEVIR--PDANLEAFKALRPVFDpKGGTVTAATSSALSDGA 249
Cdd:cd00826 146 LAGQAGAEAAEKDGRFKDEFAkfGVKGRKGD---IHSDADEYIQfgDEASLDEIAKLRPAFD-KEDFLTAGNACGLNDGA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 250 SAMLLMSAERAQALGLKPRAV-------IRSMAVAGCD----AAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQ 318
Cdd:cd00826 222 AAAILMSEAEAQKHGLQSKAReiqalemITDMASTFEDkkviKMVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFAAN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 319 GLSVMKGLGI----------------YDKQDIINLNGGAIALGHPLGCSGARITTTLLNVM-----EQQDTQIGLATMCI 377
Cdd:cd00826 302 ACATNEALGLcpegqggalvdrgdntYGGKSIINPNGGAIAIGHPIGASGAAICAELCFELkgeagKRQGAGAGLALLCI 381
|
410
....*....|.
gi 491207493 378 GLGQGIATVIE 388
Cdd:cd00826 382 GGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-389 |
6.16e-43 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 155.06 E-value: 6.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 1 MATLNPRDVVIVDGVRSAMGKTkNGMFRNV-RADSLSAELvRALVARNQFDVNEVEDLIWGCVnQTLEQGMNIGRNIGLL 79
Cdd:PRK09268 1 MTMPTVRRVAILGGNRIPFARS-NGAYADAsNQDMLTAAL-DGLVDRFGLQGERLGEVVAGAV-LKHSRDFNLTRECVLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 80 ADLPKTVAGQTVNRLCGSSMQALHTAAAQIATNQGDIFIIGGV-----------EHMGHV-----------------GMM 131
Cdd:PRK09268 78 SALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVdttsdapiavnEGLRKIllelnrakttgdrlkalGKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 132 HGIDLNPEASKHYAKASNM-MGLTAEMLGRMNGISREEQDAFGVESHRRAWAATQEGRFKNEIVGVEGHDAngfkilcdi 210
Cdd:PRK09268 158 RPKHLAPEIPRNGEPRTGLsMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 211 DEVIRPDANLEAFKALRPVFD-PKGGTVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVA------GCDAAI 283
Cdd:PRK09268 229 DNNLRPDSSLEKLAKLKPVFGkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAavdfvhGKEGLL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 284 MGygPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKG----------------LGIYDKqDIINLNGGAIALGHP 347
Cdd:PRK09268 309 MA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgldapLGSIDR-SKLNVNGSSLAAGHP 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 491207493 348 LGCSGARITTTLLNVMEQQDTQIGLATMCIGLGQGIATVIER 389
Cdd:PRK09268 386 FAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
242-387 |
4.45e-17 |
|
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: 80.18 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 242 SSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDA----AIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAA 317
Cdd:cd00327 97 EFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGAsmvpAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTP 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491207493 318 QGLSVMKGLGI-YDKQDIINLNGGAIALGHPLGCSGARITTTLLNVME-------QQDTQIGLATMCIGLGQGIATVI 387
Cdd:cd00327 177 IGDAVELALGLdPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
18-354 |
1.25e-16 |
|
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: 80.39 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 18 AMGKTKNGMFRNVRADSLSAELVRALVARNQFDVNEVEDLIWGCVNQTLEQGMnIGRNIGLLADLPKTVAgQTVNRLCGS 97
Cdd:cd00829 2 GVGMTPFGRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSF-PGALIAEYLGLLGKPA-TRVEAAGAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 98 SMQALHTAAAQIATNQGDIFIIGGVEHMGHVG-----MMHGIDLNPEASKHYAkASNMMGLTAEMLGRM---NGISREEQ 169
Cdd:cd00829 80 GSAAVRAAAAAIASGLADVVLVVGAEKMSDVPtgdeaGGRASDLEWEGPEPPG-GLTPPALYALAARRYmhrYGTTREDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 170 DAFGVESHRRAwAATQEGRFKNEIvgveghdangfkilcDIDEVIrpdanleafkALRPVFDPkggtVTAATSSALSDGA 249
Cdd:cd00829 159 AKVAVKNHRNA-ARNPYAQFRKPI---------------TVEDVL----------NSRMIADP----LRLLDCCPVSDGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 250 SAMLLMSAERAQALGLKPrAVIRSMAVA-------GCDAAIMGYGPVPATQKALKRAGLTMADIQTIELNEAFAAQGLSV 322
Cdd:cd00829 209 AAVVLASEERARELTDRP-VWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLA 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 491207493 323 MKGLGIYDKQDI----------------INLNGGAIALGHPLGCSGAR 354
Cdd:cd00829 288 LEDLGFCEKGEGgklvregdtaiggdlpVNTSGGLLSKGHPLGATGLA 335
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
95-354 |
1.16e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 74.93 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 95 CGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGmmhgidlNPEASKHYAKASN-----MMGLT----AEMLGR--MN- 162
Cdd:PRK06064 85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP-------TPDATEAIARAGDyeweeFFGATfpglYALIARryMHk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 163 -GISREEQDAFGVESHRRAwAATQEGRFKNEIvgveghdangfkilcDIDEVIRPdanleafkalRPVFDPkggtVTAAT 241
Cdd:PRK06064 158 yGTTEEDLALVAVKNHYNG-SKNPYAQFQKEI---------------TVEQVLNS----------PPVADP----LKLLD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 242 SSALSDGASAMLLMSAERAQALGLKPrAVIRSMAVA-------------GCDAAIMgygpvpATQKALKRAGLTMADIQT 308
Cdd:PRK06064 208 CSPITDGAAAVILASEEKAKEYTDTP-VWIKASGQAsdtialhdrkdftTLDAAVV------AAEKAYKMAGIEPKDIDV 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491207493 309 IELNEAFAAQGLSVMKGLGIYDK---------------QDI-INLNGGAIALGHPLGCSGAR 354
Cdd:PRK06064 281 AEVHDCFTIAEILAYEDLGFAKKgeggklaregqtyigGDIpVNPSGGLKAKGHPVGATGVS 342
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
243-375 |
6.12e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 54.13 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 243 SALSDGASAMLLMSAERAQALGLKP---RAV-IRSMAVAGC-------DAAIMgYGPVPATQKALKRAGLTMADIQTIEL 311
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsRLVeIKSLACASGnlyedppDATRM-FTSRAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 312 NEAFAAQGLSVMKGLGI----------------YDKQDIINLNGGAIALGHPLGCSGARittTLLNVMEQQDTQIGLATM 375
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaeyghakdlirngataLEGRIPVNTGGGLLSFGHPVGATGVK---QIMEVYRQMKGQCGEYQM 411
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
243-352 |
1.04e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 50.33 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 243 SALSDGASAMLLMSAERAQALglkPRAV-IRSMAVAGcDAAIMGY-------GPVPATQKALKRAGLTMADIQTIELNEA 314
Cdd:PRK07516 213 SLVSDGAAALVLADAETARAL---QRAVrFRARAHVN-DFLPLSRrdplafeGPRRAWQRALAQAGVTLDDLSFVETHDC 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491207493 315 FA--------AQGLS--------VMKGLGIYDKQDIINLNGGAIALGHPLGCSG 352
Cdd:PRK07516 289 FTiaelieyeAMGLAppgqgaraIREGWTAKDGKLPVNPSGGLKAKGHPIGATG 342
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
243-354 |
1.03e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 47.33 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 243 SALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYG---------PVPATQKALKRAGLT--MADIQTIEL 311
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQYNgwdgsyfptTRIAARKAYREAGITdpREELSMAEV 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 491207493 312 NEAFAAQGLSVMKGLGIYDK----QDI------------INLNGGAIALGHPLGCSGAR 354
Cdd:PRK06157 294 HDCFSITELVTMEDLGLSERgqawRDVldgffdadgglpCQIDGGLKCFGHPIGASGLR 352
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
91-352 |
1.04e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 47.15 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 91 VNRLCGSSMQALHTAAAQIATNQGDIFIIGGVEHMGHVGMMHGIDLNPEASKHYAK---------ASNMMGLTAEMlgRM 161
Cdd:PRK12578 78 VEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVDTSTSLAIGGRGGNYQWEyhfygttfpTYYALYATRHM--AV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 162 NGISREEQDAFGVESHRRAwAATQEGRFKNEIVgveghdangfkilcdIDEVIRPdanleafkalRPVFDPkggtVTAAT 241
Cdd:PRK12578 156 YGTTEEQMALVSVKAHKYG-AMNPKAHFQKPVT---------------VEEVLKS----------RAISWP----IKLLD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 242 SSALSDGASAMLLMSAERAQALGLKPRAVIRSMAVAGCDAAIMGYG-------PVPATQKALKRAGLTMADIQTIELNEA 314
Cdd:PRK12578 206 SCPISDGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVARRGewvgfkaTQLAARQAYNMAKVTPNDIEVATVHDA 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 491207493 315 FAAQGLSVMKGLGIYDKQD----------------IINLNGGAIALGHPLGCSG 352
Cdd:PRK12578 286 FTIAEIMGYEDLGFTEKGKggkfieegqsekggkvGVNLFGGLKAKGHPLGATG 339
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
220-352 |
1.07e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 47.20 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 220 LEAFKALRPVFDPkggtVTAATSSALSDGASAMLLMSAERAQALGLKPRAVIRSMAV--------AGCDAA-IMGYG-PV 289
Cdd:PRK08256 192 LEDVLASPMIWGP----LTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMttdtpstfDGRSMIdLVGYDmTR 267
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491207493 290 PATQKALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGI----------------YDKQDIINLNGGAIALGHPLGCSG 352
Cdd:PRK08256 268 AAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLcpegeaekfiddgdntYGGRWVVNPSGGLLSKGHPLGATG 346
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
243-355 |
1.91e-05 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 46.22 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 243 SALSDGASAMLLMSAERAQALGlKPRAVIRsMAVAGCDAAIMGYGP-----------VP----ATQKALKRAGLTMADIQ 307
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYA-DARPIPR-IKGWGHRTAPLGLEQkldrsagdpyvLPhvrqAVLDAYRRAGVGLDDLD 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491207493 308 TIELNEAFAAQGLSVMKGLGI---------YDKQDI-------INLNGGAIALGHPLGCSGARI 355
Cdd:PRK06289 298 GFEVHDCFTPSEYLAIDHIGLtgpgeswkaIENGEIaiggrlpINPSGGLIGGGHPVGASGVRM 361
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
245-366 |
5.05e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 45.04 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 245 LSDGASAMLLMSAERAQALGLKPRAVIRSMAVAgCDAAIM------GYGPVPATQKALKRAGLTMADIQTI-------EL 311
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLT-CDAYHMsapepdGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRL 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491207493 312 NEAFAAQ----------GLSVMKGlgiydkqdiinlnggaiALGHPLGCSGA-RITTTLLNVMEQQ 366
Cdd:PRK05952 287 NDQREANliqalfphrvAVSSTKG-----------------ATGHTLGASGAlGVAFSLLALRHQQ 335
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
219-309 |
2.67e-04 |
|
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: 42.91 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 219 NLEAFKALRPvFDPK-GGTVtaatssaLSDGASAMLLMSAERAQALGLKPRAVIRSMAVAgCDAAIM------GYGPVPA 291
Cdd:cd00834 210 NDDPEKASRP-FDKDrDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDAYHItapdpdGEGAARA 280
|
90
....*....|....*...
gi 491207493 292 TQKALKRAGLTMADIQTI 309
Cdd:cd00834 281 MRAALADAGLSPEDIDYI 298
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
243-355 |
7.09e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 41.21 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 243 SALSDGASAMLLMSAERAQALGLKPrAVIRSMAvAGCDAAIMG---YGPVPATQKALKRA-GLTMADIQTIELNEAFAAQ 318
Cdd:PRK07937 202 APITDGAAAVVLAAGDRARELRERP-AWITGIE-HRIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQ 279
|
90 100 110
....*....|....*....|....*....|....*...
gi 491207493 319 GLSVMKGLGIYDKQdIINLNGGAIAlGHPLGCSG-ARI 355
Cdd:PRK07937 280 ELILREALGLGDKT-KVNPSGGALA-ANPMFAAGlERI 315
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
225-347 |
1.01e-03 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 40.78 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 225 ALRPVFDPkggtVTAATSSALSDGASAMLLMSAERAQALGLKPRAV-----------IRSMAVAGCDAAIMGyGPvpatq 293
Cdd:PRK06158 192 AARMVSDP----LSVRDCCLVTDGAGAVVMVRADRARDLPRPPVYVlgaaaatwhrqISSMPDLTVTAAAES-GP----- 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 294 KALKRAGLTMADIQTIELNEAFAAQGLSVMKGLGIYDK-------QD---------IINLNGGAIALGHP 347
Cdd:PRK06158 262 RAFAMAGLTPADIDVVELYDAFTINTILFLEDLGFCAKgeggafvEGgriapggrlPVNTNGGGLSCVHP 331
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
246-310 |
2.27e-03 |
|
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: 39.85 E-value: 2.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491207493 246 SDGASAMLLMSAERAQALGLKPRAVIRSMAVAgCD-AAIMGYGPVPATQ-----KALKRAGLTMADIQTIE 310
Cdd:cd00833 234 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVN-QDgRTKGITAPSGEAQaalirRAYARAGVDPSDIDYVE 303
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
246-345 |
4.36e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 38.81 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491207493 246 SDGASAMLLMSAERAQALGLKPrAVIRSMAV-AGCDAAIMG--YGPVPAT--------QKALKRAGLTMADIQTIELNEA 314
Cdd:PRK07855 216 SDGAVALVVTSAERARDLKQRP-AVIKAAAQgSGADQYMMTsyYRDDITGlpemglvaRQLWAQSGLGPADIDTAILYDH 294
|
90 100 110
....*....|....*....|....*....|....
gi 491207493 315 FAAQGLSVMKGLGIYDK---QDIInlNGGAIALG 345
Cdd:PRK07855 295 FTPFVLMQLEELGFCGRgeaKDFI--ADGALELG 326
|
|
| |
