|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 676.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYHMGIT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 161 AENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRPAFLpKE 240
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFD-KD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 241 GTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1613180472 321 FAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVKN 393
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-393 |
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: 644.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLgNSQLIDTLVHDGLTDAFNNYHMGIT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 161 AENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDpLIVTTDEYPKVDTSLEKLQQLRPAFlPKE 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAF-KKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 241 GTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:COG0183 238 GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1613180472 321 FAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVKN 393
Cdd:COG0183 318 FAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-393 |
0e+00 |
|
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: 628.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 5 VIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFTL 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 85 DMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLiDTLVHDGLTDAFNNYHMGITAENV 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 165 AQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRrKDPLIVTTDEYPKVDTSLEKLQQLRPAFlPKEGTVT 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGR-KGPVVVDRDEGPRPDTTLEKLAKLKPAF-KKDGTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 245 AGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFAAQ 324
Cdd:cd00751 238 AGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1613180472 325 SLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVKN 393
Cdd:cd00751 318 ALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-392 |
0e+00 |
|
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: 536.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 6 IVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFTLD 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 86 MVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAY-VSTQHRFGQRLGNSQLIDTLVHDgLTDAFNNYHMGITAENV 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYgVPRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 165 AQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKdPLIVTTDEYPKVDTSLEKLQQLRPAFLPKeGTVT 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPD-GTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 245 AGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFAAQ 324
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1613180472 325 SLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVK 392
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-394 |
2.12e-178 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 501.73 E-value: 2.12e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYHMGIT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 161 AENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRPAFlPKE 240
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAF-KKD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 241 GTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1613180472 321 FAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVKNN 394
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-390 |
5.23e-177 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 498.33 E-value: 5.23e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPEDK 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEpRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVhDGLTDAFNNYHMGI 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 160 TAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRrKDPLIVTTDEYPKVDTSLEKLQQLRPAFLPK 239
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTR-KGEVVFDTDEHVRADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 240 EGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNE 319
Cdd:PRK09051 240 NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1613180472 320 AFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAI 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.30e-169 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 478.82 E-value: 2.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYHMGIT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 161 AENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRPAFlPKE 240
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVF-DKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 241 GTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1613180472 321 FAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVK 392
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-393 |
2.15e-168 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 476.79 E-value: 2.15e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNY----H 156
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLARGRETAGGRRFpvpgG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 157 MGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRP-- 234
Cdd:PRK06205 161 MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLRPim 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 235 AFLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDL 314
Cdd:PRK06205 241 GKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 315 VESNEAFAAQSLAVLKDLKLNP---EIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK06205 321 IELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVF 400
|
..
gi 1613180472 392 KN 393
Cdd:PRK06205 401 ER 402
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-391 |
6.26e-153 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 437.22 E-value: 6.26e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 2 KNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 82 FTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYHMGITA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 162 ENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRR-KDPLIVTTDEYP-KVDtsLEKLQQLRPAFLPK 239
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRgRPSVIVDKDEGLgKFD--PAKLRKLRPSFKED 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 240 EGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNE 319
Cdd:PLN02644 239 GGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1613180472 320 AFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PLN02644 319 AFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVV 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-391 |
2.10e-148 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 425.91 E-value: 2.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKT-QVKPEMVDEVILGNVLHAGL-GQNVARQVAVHSGIPED 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 79 KTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYV--STQHRFGQrlgNSQLIDT-----LVHDGLTDA 151
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVmgKADSAFSR---QAEIFDTtigwrFVNPLMKAQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 152 FNNYHMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQ 231
Cdd:PRK09050 158 YGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 232 LRPAFLPkEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISD 311
Cdd:PRK09050 238 LKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 312 LDLVESNEAFAAQSLAVLKDLKL--NPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAV 389
Cdd:PRK09050 317 FDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIAL 396
|
..
gi 1613180472 390 IV 391
Cdd:PRK09050 397 AI 398
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-392 |
6.09e-148 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 424.44 E-value: 6.09e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMS---QAAYVstqhRFGQRLGNSQLIDTLVHDGLTDAFNNYHM 157
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI----RAGAKFGDIKMVDLMQYDGLTDVFSGVFM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 158 GITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIvTTDEYPKVDTSLEKLQQLRPAFl 237
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAF- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 238 PKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVES 317
Cdd:PRK06633 236 DKNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEV 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1613180472 318 NEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIVK 392
Cdd:PRK06633 316 NEAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-390 |
2.55e-134 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 389.71 E-value: 2.55e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDKT-QVKPEMVDEVILGNV---LHAGLgqNVARQVAVHSGI 75
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVqqtLEQGF--NIARNAALLAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 76 PEDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMsqaAYVSTQHRfgqrlgnsqlIDTLVHDGLTDAFNNY 155
Cdd:PRK08947 79 PHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM---GHVPMNHG----------VDFHPGLSKNVAKAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 156 HMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRPA 235
Cdd:PRK08947 146 MMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 236 FLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLV 315
Cdd:PRK08947 226 FDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1613180472 316 ESNEAFAAQSLAVLKDLKL---NPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:PRK08947 306 ELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATV 383
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-392 |
4.06e-133 |
|
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: 387.22 E-value: 4.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 2 KNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKT-QVKPEMVDEVILGNVLHAGL-GQNVARQVAVHSGIPEDK 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARNpQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYV--STQHRFGQrlgNSQLIDT-----LVHDGLTDAF 152
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVmgKADSAFSR---SAKIEDTtigwrFINPLMKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 153 NNYHMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQL 232
Cdd:TIGR02430 158 GVDSMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 233 RPAFLPkEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDL 312
Cdd:TIGR02430 238 KPVVRP-DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 313 DLVESNEAFAAQSLAVLKDLKL--NPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:TIGR02430 317 DVIELNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALA 396
|
..
gi 1613180472 391 VK 392
Cdd:TIGR02430 397 IE 398
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-388 |
3.38e-130 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 379.48 E-value: 3.38e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVL-HAGLGQNVARQVAVHSGIPED 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 79 KTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRfgqrlGNSQLIDTLvhdgltdafNNYHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVR-----PNPRLVEAA---------PEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 159 I--TAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDP--------LIVTTDEYPKVDTSLEK 228
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetITFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 229 LQQLRPAFLPKeGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLT 308
Cdd:PRK07661 227 LGKLRPAFNVK-GSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 309 ISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTA 388
Cdd:PRK07661 306 LSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAA 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-393 |
1.28e-122 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 360.19 E-value: 1.28e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGS------FKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLhaGLGQNVA---RQVAV 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENWLyggRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 72 HSGIPEDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHrfgQRLGNSQLIDT-LVHDGLTD 150
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNPH---IEPNPKLLTDPkYIEYDLTT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 151 AFNnyhMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVpQRRKDPLIVTTDEYPKVDTSLEKLQ 230
Cdd:PRK06445 156 GYV---MGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTSLEKLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 231 QLRPAFLPkEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTIS 310
Cdd:PRK06445 232 KLPPAFKP-DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 311 DLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390
|
...
gi 1613180472 391 VKN 393
Cdd:PRK06445 391 LER 393
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.81e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 357.01 E-value: 3.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDKT-QVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPE 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 78 DKTAfTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSqaayvstqhRFGQrlGNSqlidtlvhDGLTDAFN---- 153
Cdd:PRK07851 81 LPGT-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVS---------RFAK--GNS--------DSLPDTKNplfa 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 154 ---------------NYH--------------MGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSV 204
Cdd:PRK07851 141 eaqartaaraeggaeAWHdpredgllpdvyiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 205 PqrrkDPLIVTTDEYPKVDTSLEKLQQLRPAFLPkEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAG 284
Cdd:PRK07851 221 P----DGTVVSTDDGPRAGTTYEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 285 VAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLI 364
Cdd:PRK07851 296 LSPEIMGLGPVEASKQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLL 375
|
410 420
....*....|....*....|....*..
gi 1613180472 365 HEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK07851 376 NNLQTHDKTFGLETMCVGGGQGMAMVL 402
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-264 |
5.58e-121 |
|
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: 350.83 E-value: 5.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 4 IVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 84 LDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAY-VSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYHMGITAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYaLPTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 163 NVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPlIVTTDEYPKVDTSLEKLQQLRPAFlPKEGT 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAF-DKEGT 238
|
250 260
....*....|....*....|..
gi 1613180472 243 VTAGNASGINDGAALLMLMTEE 264
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSES 260
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-390 |
9.19e-121 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 355.46 E-value: 9.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDKTQ-VKPEMVDEVILGNVL-HAGLGQNVARQVAVHSGIPE 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 78 DKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYvstqhrfgqrLGNSQLIDTLVHDGLTDAFNNYHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 158 GITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDP---------LIVTTDEYPKVDTSLEK 228
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktRTVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 229 LQQLRPAFLPKeGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLT 308
Cdd:PRK09052 235 LAKLKPVFANK-GSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 309 ISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTA 388
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAA 393
|
..
gi 1613180472 389 VI 390
Cdd:PRK09052 394 GI 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-386 |
6.43e-120 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 353.16 E-value: 6.43e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYV-STQHRFGQR---LGNSQLIDTLVHDGLTDAFNNYH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlPSDLRWGPKhllHKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 157 MGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRrkdplivttDEYPKvDTSLEKLQQLRPAF 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLDR---------DEGIR-KTTMEDLAKLPPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 237 lPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVE 316
Cdd:PRK06366 231 -DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 317 SNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQG 386
Cdd:PRK06366 310 HNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGA 379
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-389 |
2.90e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 351.89 E-value: 2.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 4 IVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 84 LDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNNYH-MGITAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 163 NVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDpLIVTTDEYPKvDTSLEKLQQLRPAFlPKEGT 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPF-KANPEKIPTLKPAF-SKTGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 243 VTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFA 322
Cdd:PRK06954 246 VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFA 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1613180472 323 AQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAV 389
Cdd:PRK06954 326 VVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAM 392
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-393 |
1.11e-114 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 340.22 E-value: 1.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGL-GQNVARQVAVHSGIPEDK 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYV-----STQHR--------FGQRLGNSQLIDTlvhd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVmgkaeSAFSRdakvfdttIGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 147 gltdaFNNYHMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKD-PLIVTTDEYPKVDTS 225
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKLpPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 226 LEKLQQLRPAFlpKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKA 305
Cdd:PRK08131 232 VEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 306 GLTISDLDLVESNEAFAAQSLAVLKDLKL--NPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGG 383
Cdd:PRK08131 310 GLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGV 389
|
410
....*....|
gi 1613180472 384 GQGTAVIVKN 393
Cdd:PRK08131 390 GQGLAMVIER 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-391 |
3.48e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 338.78 E-value: 3.48e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAF--GGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPE 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGkkDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 78 DKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTqhrfgqrlGNSQLIDTLVhdgltdAFNNYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSD--------GGAWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 158 --GITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVsvpqrrKDP---LIVTTDEYPKVDTSLEKLQQL 232
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV------KDQnglTILDHDEHMRPGTTMESLAKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 233 RPAF-------------LPKEGTV-------TAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGT 292
Cdd:PRK08242 221 KPSFammgemggfdavaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 293 GPIPATQKALKKAGLTISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQV 372
Cdd:PRK08242 301 GPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGK 380
|
410
....*....|....*....
gi 1613180472 373 TRGLATLCIGGGQGTAVIV 391
Cdd:PRK08242 381 RTALITLCVGGGMGIATII 399
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-390 |
3.68e-114 |
|
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: 338.46 E-value: 3.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 3 NIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDK-TQVKPEMVDEVILGNVLHA-GLGQNVARQVAVHSGIPEDK 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTlEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMsqaAYVSTQHRfgqrlgnsqlIDTLVHDGLTDAFNNYHMGI 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHM---GHVPMMHG----------VDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 160 TAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRPAFLPK 239
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 240 EGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNE 319
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1613180472 320 AFAAQSLAVLKDLKLNPEI---VNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:TIGR02445 308 AFAAQALPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATV 381
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.02e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 334.37 E-value: 1.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPEDK 79
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQ-----AAYVSTQHRFGQRLGNSQLIDTLVHDGLTDAFNN 154
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipissAMTAGEQLGFTSPFAESKGWLHRYGDQEVSQFRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 155 yhmgitAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVpqrrkdpliVTTDEYPKvDTSLEKLQQLRP 234
Cdd:PRK07801 161 ------AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 235 afLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDL 314
Cdd:PRK07801 225 --LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1613180472 315 VESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTII 379
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-391 |
2.01e-110 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 330.96 E-value: 2.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 3 NIVIVEALRTPI-GAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQ-NVARQVAVHSGIPEDKT 80
Cdd:PLN02287 47 DVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQRLGNSQLIDTLVHdgltdafnnyhMGIT 160
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 161 AENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVpqRRKDP-------LIVTTDEYPKVDTSLEKLQQLR 233
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHT--KIVDPktgeekpIVISVDDGIRPNTTLADLAKLK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 234 PAFlPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLD 313
Cdd:PLN02287 274 PVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDID 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 314 LVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKR-QVTR-GLATLCIGGGQGTAVIV 391
Cdd:PLN02287 353 LFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgKDCRfGVVSMCIGTGMGAAAVF 432
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-393 |
3.41e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 309.25 E-value: 3.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKT 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQA------------AYVSTQHRFGQRL--------GNSQLI 140
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHApllfsekmvrwlAGWYAAKSIGQKLaalgklrpSYLAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 141 DTLVHdGLTDAFNNYHMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFAdEIVPVSVPQRRkdplIVTTDEYP 220
Cdd:PRK08170 162 IGLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDRDGK----FYDHDDGV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 221 KVDTSLEKLQQLRPAFLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQK 300
Cdd:PRK08170 236 RPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 301 ALKKAGLTISDLDLVESNEAFAAQSLAVLKDLK-----------------LNPEIVNVNGGAIALGHPIGASGARILVTL 363
Cdd:PRK08170 316 LLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLHL 395
|
410 420 430
....*....|....*....|....*....|
gi 1613180472 364 IHEMKKRQVTRGLATLCIGGGQGTAVIVKN 393
Cdd:PRK08170 396 LHALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
4.85e-102 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 307.42 E-value: 4.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPEDK 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAY-VSTQHRFGQRLGNSQLIDtlvhdgLTDAFNnyhmg 158
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLgANAGPGRGLPRPDSWDID------MPNQFE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 159 iTAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDP------LIVTTDEYPKvDTSLEKLQQL 232
Cdd:PRK07850 150 -AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGqptgetRLVTRDQGLR-DTTMEGLAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 233 RPAFlpKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDL 312
Cdd:PRK07850 228 KPVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1613180472 313 DLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK07850 306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTII 384
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.01e-99 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 300.88 E-value: 2.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPEDK 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 80 TAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRFGQR-LGNSQlidtlvHDGLTDAFNNYH-- 156
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNgLGHYK------SPGMEERYPGIQfs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 157 --MGitAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDPLIVTTDEYPKVDTSLEKLQQLRP 234
Cdd:PRK06504 155 qfTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 235 afLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDL 314
Cdd:PRK06504 233 --IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1613180472 315 VESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK06504 311 YEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIV 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-391 |
3.78e-99 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 301.52 E-value: 3.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 4 IVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 84 LDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMS----------QAAYVSTQ--HRFGQRLgnsQLIDTLvhdGLTD- 150
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSvlpigvskklARALVDLNkaRTLGQRL---KLFSRL---RLRDl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 151 -----AFNNY----HMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKdplIVTTDEYPK 221
Cdd:PRK08963 161 lpvppAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ---PLEEDNNIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 222 VDTSLEKLQQLRPAFLPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPE---LMgtGPIPAT 298
Cdd:PRK08963 238 GDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWqdmLL--GPAYAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 299 QKALKKAGLTISDLDLVESNEAFAAQSLAVLKDL-----------------KLNPEIVNVNGGAIALGHPIGASGARILV 361
Cdd:PRK08963 316 PLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMIT 395
|
410 420 430
....*....|....*....|....*....|
gi 1613180472 362 TLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK08963 396 QTLHELRRRGGGLGLTTACAAGGLGAAMVL 425
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-388 |
1.36e-92 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 283.58 E-value: 1.36e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIG-AFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAG-LGQNVARQVAVHSGIPED 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 79 KTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTQHRfgqrlgnsqlidtlvhdgLTDAFNNYH-- 156
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHM------------------LREGWLVEHkp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 157 -----MGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDP---------LIVTTDEYPKV 222
Cdd:PRK07108 143 eiywsMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKatgrlftkeVTVSADEGIRP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 223 DTSLEKLQQLRPAFlpKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKAL 302
Cdd:PRK07108 223 DTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 303 KKAGLTISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIG 382
Cdd:PRK07108 301 KQAGLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIG 380
|
....*.
gi 1613180472 383 GGQGTA 388
Cdd:PRK07108 381 GGQGAA 386
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-392 |
6.18e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 274.73 E-value: 6.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTP--IGAFG-GSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGL-GQNVARQVAVHSGIP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPrgIGKVGkGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 77 EDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAyvSTQHRFGQRLGNSQLIDTlVHDGLTDAFNNYH 156
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTA--AMAAEDMAAGKPPLGMGS-GNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 157 MGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVsvpQRRKDPLIVTTDEYPKVDTSLEKLQQLRPAF 236
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV---YRDDGSVALDHEEFPRPQTTAEGLAALKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 237 -------LPKEGTV------------------TAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMG 291
Cdd:PRK06025 235 taiadypLDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 292 TGPIPATQKALKKAGLTISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQ 371
Cdd:PRK06025 315 NAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRG 394
|
410 420
....*....|....*....|.
gi 1613180472 372 VTRGLATLCIGGGQGTAVIVK 392
Cdd:PRK06025 395 LKRGLVTMCAAGGMAPAIIIE 415
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-391 |
1.72e-86 |
|
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: 267.82 E-value: 1.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 7 VEALRTPIGAFGG---SFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFT 83
Cdd:cd00826 1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 84 LDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAyvstqhrfgQRLGNSQLIDTLVHdgltdafnnyhmgitaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA---------ENNAKEKHIDVLIN------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 164 vaqKYGiSREEQDQFALESQEKAAKALENHRFADEIVPVSVPQRRKDpLIVTTDEYPK--VDTSLEKLQQLRPAFlPKEG 241
Cdd:cd00826 134 ---KYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEYIQfgDEASLDEIAKLRPAF-DKED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 242 TVTAGNASGINDGAALLMLMTEEKALELGLT-------PLVTIESYASAGVAPE----LMGTGPIPATQKALKKAGLTIS 310
Cdd:cd00826 208 FLTAGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 311 DLDLVESNEAFAAQSLAVLKDLKLNPE------------------IVNVNGGAIALGHPIGASGARILVTLIHEMK---- 368
Cdd:cd00826 288 DLDLIEAHDAFAANACATNEALGLCPEgqggalvdrgdntyggksIINPNGGAIAIGHPIGASGAAICAELCFELKgeag 367
|
410 420
....*....|....*....|....
gi 1613180472 369 KRQVTR-GLATLCIGGGQGTAVIV 391
Cdd:cd00826 368 KRQGAGaGLALLCIGGGGGAAMCI 391
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-390 |
3.72e-85 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 263.16 E-value: 3.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 3 NIVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKIldkTQVKPEMVDEVILGNVLhaGLGQNVARQVAVHSGIPEDKTAF 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL---SKGMEREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 83 TLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYvSTQHRFGqrlgnsqlidtlvhdglTDAFNNYHMGITAE 162
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-QNRARFS-----------------PETIGDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 163 NVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVSVpqrrkdplivTTDEYPKVDTSLEKL-QQLRPAFLpKEG 241
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG----------LLDESIKKEMNYERIiKRTKPAFL-HNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 242 TVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAF 321
Cdd:PRK06690 208 TVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1613180472 322 AAQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVI 390
Cdd:PRK06690 288 ASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALL 356
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
271-391 |
2.32e-63 |
|
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: 199.02 E-value: 2.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 271 LTPLVTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFAAQSLAVLKDLKLNPEIVNVNGGAIALGH 350
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1613180472 351 PIGASGARILVTLIHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMII 121
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
4-391 |
1.67e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 196.27 E-value: 1.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 4 IVIVEALRTPIGAFGGSFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPEDKTAFT 83
Cdd:PRK09268 9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 84 LDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAY-VSTQHR-----------FGQRLgnSQLIDTLVHDGLTDA 151
Cdd:PRK09268 89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIaVNEGLRkillelnraktTGDRL--KALGKLRPKHLAPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 152 FNN------YHMGITAENVAQKYGISREEQDQFALESQEKAAKALENHRFADEIVPVsvpqrrkdpLIVTTDEYPKVDTS 225
Cdd:PRK09268 167 PRNgeprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF---------LGLTRDNNLRPDSS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 226 LEKLQQLRPAF-LPKEGTVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYASAGV----APELMGTGPIPATQK 300
Cdd:PRK09268 238 LEKLAKLKPVFgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVdfvhGKEGLLMAPAYAVPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 301 ALKKAGLTISDLDLVESNEAFAAQSLAVLK--------------DLKL---NPEIVNVNGGAIALGHPIGASGARILVTL 363
Cdd:PRK09268 318 LLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycrerlglDAPLgsiDRSKLNVNGSSLAAGHPFAATGGRIVATL 397
|
410 420
....*....|....*....|....*...
gi 1613180472 364 IHEMKKRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK09268 398 AKLLAEKGSGRGLISICAAGGQGVTAIL 425
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-391 |
7.96e-31 |
|
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: 121.22 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 12 TPIGAFGGsfksVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPeDKTAFTLDMVCGSG 91
Cdd:cd00829 6 TPFGRRSD----RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 92 LKAIQLAAQSIMLGDADIVIAGGVENMSQaayVSTQHRFGQRLGNSQLIDTLVHDGLT--DAFNNY---HMgitaenvaQ 166
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMSD---VPTGDEAGGRASDLEWEGPEPPGGLTppALYALAarrYM--------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 167 KYGISREeqdQFALEsqekaakALENHRFAdeivpVSVP--QRRKDpliVTTDEypkVDTSleklqqlRPAFLPkegtVT 244
Cdd:cd00829 150 RYGTTRE---DLAKV-------AVKNHRNA-----ARNPyaQFRKP---ITVED---VLNS-------RMIADP----LR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 245 AGNASGINDGAALLMLMTEEKALELGLTPlVTIESYASAGVAPELMG-------TGPIPATQKALKKAGLTISDLDLVES 317
Cdd:cd00829 198 LLDCCPVSDGAAAVVLASEERARELTDRP-VWILGVGAASDTPSLSErddflslDAARLAARRAYKMAGITPDDIDVAEL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 318 NEAFAAQSLAVLKDLKL-----------NPEI-------VNVNGGAIALGHPIGASGARILVTLIHEMK----KRQV--- 372
Cdd:cd00829 277 YDCFTIAELLALEDLGFcekgeggklvrEGDTaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRgeagARQVpga 356
|
410
....*....|....*....
gi 1613180472 373 TRGLATLciGGGQGTAVIV 391
Cdd:cd00829 357 RVGLAHN--IGGTGSAAVV 373
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
245-391 |
9.74e-27 |
|
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: 107.14 E-value: 9.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 245 AGNASGINDGAALLMLMTEEKALELGLTPLVTIESYAS----AGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 321 FAAQSLAVLKDLKLNPEIV---NVNGGAIALGHPIGASGARILVTLIHEMKKRQV-------TRGLATLCIGGGQGTAVI 390
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIpptprepRTVLLLGFGLGGTNAAVV 253
|
.
gi 1613180472 391 V 391
Cdd:cd00327 254 L 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-390 |
5.80e-21 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 93.42 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 1 MKNIVIVEALRTPIGAFGG-SFKSVsAVELGttvlKKILDKTQVKPEMVDEVILGNVLhAGL--GQ-NVARQVAVHSGIP 76
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDvSLRDL-AVEAG----LEALEDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADYAGLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 77 eDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAY---VSTQHRFGQRLGNSQLIDTLVhdGLTDAFN 153
Cdd:PRK06064 75 -PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTpdaTEAIARAGDYEWEEFFGATFP--GLYALIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 154 NYHMgitaenvaQKYGISREEQDQFALESQEKAAKalenHRFAdeivpvsvpQRRKDpliVTTDEYPKVDTSLEKLQQLr 233
Cdd:PRK06064 152 RRYM--------HKYGTTEEDLALVAVKNHYNGSK----NPYA---------QFQKE---ITVEQVLNSPPVADPLKLL- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 234 paflpkegtvtagNASGINDGAALLMLMTEEKALELGLTPlVTIESYASAGVAPEL-----MGT--GPIPATQKALKKAG 306
Cdd:PRK06064 207 -------------DCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGQASDTIALhdrkdFTTldAAVVAAEKAYKMAG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 307 LTISDLDLVESNEAFAAQSLAVLKDL-----------------KLNPEI-VNVNGGAIALGHPIGASGARILVTLIHEMK 368
Cdd:PRK06064 273 IEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeggklaregqtYIGGDIpVNPSGGLKAKGHPVGATGVSQAVEIVWQLR 352
|
410 420 430
....*....|....*....|....*....|.
gi 1613180472 369 ------KRQVTR---GLaTLCIGGGQGTAVI 390
Cdd:PRK06064 353 geaekgRQQVIGagyGL-THNVGGTGHTAVV 382
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
24-370 |
3.94e-16 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 79.12 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 24 VSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIpEDKTAFTLDMVCGSGLKAIQLAAQSIM 103
Cdd:PRK12578 19 VSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGL-TGKVPLRVEAMCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 104 LGDADIVIAGGVENMSQAAyVSTQHRFGQRLGNSQLidTLVHDGLTdaFNNYHMGITAENVAqKYGISREEQDQFALESQ 183
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVD-TSTSLAIGGRGGNYQW--EYHFYGTT--FPTYYALYATRHMA-VYGTTEEQMALVSVKAH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 184 EKAAKALENHrFADEIvpvsvpqrrkdplivttdeypkvdtSLEKLQQLRPAFLPkegtVTAGNASGINDGAALLMLMTE 263
Cdd:PRK12578 172 KYGAMNPKAH-FQKPV-------------------------TVEEVLKSRAISWP----IKLLDSCPISDGSATAIFASE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 264 EKALELGLTPLVTIES--YAS--AGVAPELMGTG---PIPATQKALKKAGLTISDLDLVESNEAFAAQSLAVLKDL---- 332
Cdd:PRK12578 222 EKVKELKIDSPVWITGigYANdyAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLgfte 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1613180472 333 -----KLNPE---------IVNVNGGAIALGHPIGASGarilVTLIHEMKKR 370
Cdd:PRK12578 302 kgkggKFIEEgqsekggkvGVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
28-393 |
1.17e-13 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 72.23 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 28 ELGTTVLKKILDKTQV--KPEMVDEVILGNVLHAGLGQ--NVARQVAVHSGIPEDKTAFT------LDMVCGSGLKAIQL 97
Cdd:PTZ00455 50 ELLATAIQGTLENTGLdgKAALVDKVVVGNFLGELFSSqgHLGPAAVGSLGQSGASNALLykpamrVEGACASGGLAVQS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 98 AAQSIMLGDADIVIAGGVEnmsqaayvsTQHRFGQRLGNSQLIDT--LVHDGLTDAFNNYHMGITAENVAQKYGisreeq 175
Cdd:PTZ00455 130 AWEALLAGTSDIALVVGVE---------VQTTVSARVGGDYLARAadYRRQRKLDDFTFPCLFAKRMKYIQEHG------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 176 dQFALESQEK-AAKALENHRFAdeivPVSVPQRRKDPLIVTTDEYPKvdtsleklqqlRPAFLPKEGT---VTAGNASGI 251
Cdd:PTZ00455 195 -HFTMEDTARvAAKAYANGNKN----PLAHMHTRKLSLEFCTGASDK-----------NPKFLGNETYkpfLRMTDCSQV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 252 NDGAALLMLMTEEKALELGLTP----LVTIESYASAGV-----APEL--MGTGpIPATQKALKKAGLTISDLDLVESNEA 320
Cdd:PTZ00455 259 SDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASGnlyedPPDAtrMFTS-RAAAQKALSMAGVKPSDLQVAEVHDC 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 321 FAAQSLAV-----------LKDLKLNPEI-------VNVNGGAIALGHPIGASGARILVTLIHEMKKR----QVTRGL-- 376
Cdd:PTZ00455 338 FTIAELLMyealgiaeyghAKDLIRNGATalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQcgeyQMKNIPal 417
|
410 420
....*....|....*....|
gi 1613180472 377 -ATLCIGGGQGTAV--IVKN 393
Cdd:PTZ00455 418 gATLNMGGDDKTAVstVLQN 437
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
88-360 |
1.10e-12 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 68.90 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 88 CGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVstqhrfGQRLGNSQLIDTLVHDGLTdAFNNYHMGITAenVAQK 167
Cdd:PRK06157 88 CATGSEAFRGAVYAVASGAYDIALALGVEKLKDTGYG------GLPVANPGTLADMTMPNVT-APGNFAQLASA--YAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 168 YGISREEQD----QFALESQEKAAKALENHRFAdeivPVSVPQRRKDPLIVttdeypkvdtsleklqqlrpaflpkeGTV 243
Cdd:PRK06157 159 YGVSREDLKramaHVSVKSHANGARNPKAHLRK----AVTEEQVLKAPMIA--------------------------GPL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 244 TAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYA-SAGVAPELMGTG----PIPAT----QKALKKAGLT--ISDL 312
Cdd:PRK06157 209 GLFDCCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQlAVSNGWELQYNGwdgsYFPTTriaaRKAYREAGITdpREEL 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1613180472 313 DLVESNEAFAAQSLAVLKDLKLNPE------------------IVNVNGGAIALGHPIGASGARIL 360
Cdd:PRK06157 289 SMAEVHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
43-373 |
1.07e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 65.74 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 43 VKPEMVDEVILGnVLHAGLGQNVARQVAVHSGIPE--DKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQ 120
Cdd:PRK07516 39 IAAGDVDGIFLG-HFNAGFSPQDFPASLVLQADPAlrFKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 121 AAyvstqhrfGQRLGNSQLIDTLVHD------GLTDAFnnyhmGITAENVAQKYGisreeqDQfaleSQEKAAKALENHR 194
Cdd:PRK07516 118 TP--------TAEVGDILLGASYLKEegdtpgGFAGVF-----GRIAQAYFQRYG------DQ----SDALAMIAAKNHA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 195 FAdeivpVSVP--QRRKDPLI----VTTDEYPKVDTSLEKLqqlrpaflpkegtvtagNASGINDGAALLMLMTEEKALE 268
Cdd:PRK07516 175 NG-----VANPyaQMRKDLGFefcrTVSEKNPLVAGPLRRT-----------------DCSLVSDGAAALVLADAETARA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 269 LglTPLVTIESYASAG----------VAPElmgtGPIPATQKALKKAGLTISDLDLVESNEAFA--------AQSLA--- 327
Cdd:PRK07516 233 L--QRAVRFRARAHVNdflplsrrdpLAFE----GPRRAWQRALAQAGVTLDDLSFVETHDCFTiaelieyeAMGLAppg 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1613180472 328 ----------VLKDLKLnPeiVNVNGGAIALGHPIGASGarilVTLiHEMKKRQVT 373
Cdd:PRK07516 307 qgarairegwTAKDGKL-P--VNPSGGLKAKGHPIGATG----VSM-HVLAAMQLT 354
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
38-389 |
2.34e-11 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 64.71 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 38 LDKTQVKPEMVDEVILGNV---LHAGLGQNVARQVAVHSGIpEDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGG 114
Cdd:PRK06289 38 LAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRAGRYDVALVVG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 115 VENMSQaayVSTQhRFGQRLGNSQLIDtlvHDGLTDAFNNYHM-GITAENVAQKYGISREeqdQFALESQEKAAKALENH 193
Cdd:PRK06289 117 VELMKT---VPGD-VAAEHLGAAAWTG---HEGQDARFPWPSMfARVADEYDRRYGLDEE---HLRAIAEINFANARRNP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 194 RfadeivpvsvPQRRK----DPLIVTTDEY-PKVDTSLEKLqqlrpaflpkegtvtagNASGINDGAALLMLMTEEKALE 268
Cdd:PRK06289 187 N----------AQTRGwafpDEATNDDDATnPVVEGRLRRQ-----------------DCSQVTDGGAGVVLASDAYLRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 269 L-GLTPLVTIESY--------------ASAG---VAPELMGtgpipATQKALKKAGLTISDLDLVESNEAFAAQSLAVLK 330
Cdd:PRK06289 240 YaDARPIPRIKGWghrtaplgleqkldRSAGdpyVLPHVRQ-----AVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAID 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 331 DLKLNP-----------EI-------VNVNGGAIALGHPIGASGARILVTLIhemkkRQVT-----------RGLATLCI 381
Cdd:PRK06289 315 HIGLTGpgeswkaiengEIaiggrlpINPSGGLIGGGHPVGASGVRMLLDAA-----KQVTgtagdyqvegaKTFGTLNI 389
|
....*...
gi 1613180472 382 GGGQGTAV 389
Cdd:PRK06289 390 GGSTTTTV 397
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
88-391 |
9.14e-10 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 59.91 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 88 CGSGLKAIQLAAQSIMLGDADIVIAGGVENMSQAAYVSTqhrFGQRlgNSQLIDtlvHDGLTDAFNNYHM--------GI 159
Cdd:PRK08256 80 CSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSV---WDDR--PSPLER---FDKALAELQGFDPappalrmfGG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 160 TAENVAQKYGISREeqdQFAlesqEKAAKAlenHRFAdeivpvsvpqrRKDPLIVTTDEYpkvdtSLEKLQQLRPAFLPk 239
Cdd:PRK08256 152 AGREHMEKYGTTAE---TFA----KIGVKA---RRHA-----------ANNPYAQFRDEY-----TLEDVLASPMIWGP- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 240 egtVTAGNASGINDGAALLMLMTEEKALELGLTPLVTIESYA---------SAGVAPELMGTG-PIPATQKALKKAGLTI 309
Cdd:PRK08256 205 ---LTRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAmttdtpstfDGRSMIDLVGYDmTRAAAQQVYEQAGIGP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 310 SDLDLVESNEAFAAQSLAVLKDLKLNPE------------------IVNVNGGAIALGHPIGASGARILVTLIHEMK--- 368
Cdd:PRK08256 282 EDIDVVELHDCFSANELLTYEALGLCPEgeaekfiddgdntyggrwVVNPSGGLLSKGHPLGATGLAQCAELTWQLRgta 361
|
330 340
....*....|....*....|....
gi 1613180472 369 -KRQVTRGLATLCIGGGQGTAVIV 391
Cdd:PRK08256 362 gARQVEGARLALQHNLGLGGACVV 385
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
90-356 |
7.11e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 54.15 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 90 SGLKAIQLAAQSIMLGDADIVIAGGVENMSQaayVSTQHrfgqrlGNSQLI---DTLVHDGLTDAFNNYHmGITAENVAQ 166
Cdd:PRK06365 101 TGGLAFQAGYEEIASGRMDCVAVYGFETMSH---VNTWK------GNEFIAlasDTNFDYPLGGFYTGYY-AMMAVRHMY 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 167 KYGISREeqdQFALESQEKAAKALENhRFADEIVPVSVPQRRKDPLIvttdEYPkvdtsleklqqlrpaflpkegtVTAG 246
Cdd:PRK06365 171 EFGTTVE---QLAKVSVKNHGNAIHN-PFAQSPMKITVEDVRKSPMV----SYP----------------------LTRL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 247 NASGINDGAALLMLMTEEKALELGLTPlVTIESYASAG--VAPELMGTGPIP--------------------------AT 298
Cdd:PRK06365 221 DVCAMSDGAACAILASEDKAFEITDKP-VLIKAIGTGSdtLRLADRPFGEVPllpnespddykdlrypgvhsfragrmAA 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1613180472 299 QKALKKAGLT--ISDLDLVESNEAFAAQSLAVLKDLKL-------------NPEI-----VNVNGGAIALGHPIGASG 356
Cdd:PRK06365 300 KEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgKPELpgklpVNPSGGLLAAGHAVGATG 377
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
88-357 |
2.45e-07 |
|
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: 52.16 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 88 CGSGLKAIQLAAQSIMLGDADIVIAGGVEnmsqaayvstqhrfgqrlgnsqlidTLVHDGLTDAFNnyhmgitaenvaqk 167
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAE-------------------------ALITPLTLAGFA-------------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 168 ygisreeqdqfalesqekAAKALeNHRFADeivpvsvPQRrkdplivttdeypkvdtsleklqQLRPAFLPKEGTVtagn 247
Cdd:cd00834 202 ------------------ALRAL-STRNDD-------PEK-----------------------ASRPFDKDRDGFV---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 248 asgINDGAALLMLMTEEKALELGLTPLVTIESYASAG-----VAPELMGTGPIPATQKALKKAGLTISDLDLV------- 315
Cdd:cd00834 229 ---LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDYInahgtst 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1613180472 316 ---ESNEAFAAQslAVLKDLKLNPeIVNVNGGAIalGHPIGASGA 357
Cdd:cd00834 306 plnDAAESKAIK--RVFGEHAKKV-PVSSTKSMT--GHLLGAAGA 345
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
81-118 |
4.40e-07 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 50.71 E-value: 4.40e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGVENM 118
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
253-357 |
3.41e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 48.51 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 253 DGAALLMLMTEEKALELGLTPLVTIESY-----ASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVES-------NEA 320
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlNDQ 289
|
90 100 110
....*....|....*....|....*....|....*..
gi 1613180472 321 FAAQSLAvlkdlKLNPEIVNVNGGAIALGHPIGASGA 357
Cdd:PRK05952 290 REANLIQ-----ALFPHRVAVSSTKGATGHTLGASGA 321
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
81-115 |
1.02e-05 |
|
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: 47.17 E-value: 1.02e-05
10 20 30
....*....|....*....|....*....|....*
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGV 115
Cdd:cd00833 163 SLTVDTACSSSLVALHLACQSLRSGECDLALVGGV 197
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
88-116 |
3.87e-05 |
|
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: 45.47 E-value: 3.87e-05
10 20
....*....|....*....|....*....
gi 1613180472 88 CGSGLKAIQLAAQSIMLGDADIVIAGGVE 116
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
81-115 |
4.73e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 45.63 E-value: 4.73e-05
10 20 30
....*....|....*....|....*....|....*
gi 1613180472 81 AFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGV 115
Cdd:COG3321 167 SVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV 201
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
67-115 |
7.67e-05 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 44.24 E-value: 7.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1613180472 67 RQVAVHSGIPEDKTAFTLDMVCGSGLKAIQLAAQSIMLGDADIVIAGGV 115
Cdd:smart00825 76 SRTGVFVGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGV 124
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
251-368 |
9.43e-05 |
|
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: 44.16 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 251 INDGAALLMLMTEEKALELGLTPLVTIESYA-----SAGVAPELMGTGPIPATQKALKKAGLTISDLDLVES---NEAFA 322
Cdd:cd00825 159 FGDGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAhgtGTPIG 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1613180472 323 AQSLAVLKDLKLNPEIVNVNGGAIALGHPIGASGARILVTLIHEMK 368
Cdd:cd00825 239 DVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
253-357 |
1.06e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 43.95 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 253 DGAALLMLMTEEKALELGLTPLVTI--ESYASAG---VAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFA----- 322
Cdd:PRK07910 242 EGGALMVIETEEHAKARGANILARImgASITSDGfhmVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTsvgdv 321
|
90 100 110
....*....|....*....|....*....|....*
gi 1613180472 323 AQSLAVLKDLKLNPEIVNVNGGaiALGHPIGASGA 357
Cdd:PRK07910 322 AEGKAINNALGGHRPAVYAPKS--ALGHSVGAVGA 354
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
88-116 |
2.62e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 42.85 E-value: 2.62e-04
10 20
....*....|....*....|....*....
gi 1613180472 88 CGSGLKAIQLAAQSIMLGDADIVIAGGVE 116
Cdd:PRK07314 162 CATGAHAIGDAARLIAYGDADVMVAGGAE 190
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
86-116 |
4.94e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 42.02 E-value: 4.94e-04
10 20 30
....*....|....*....|....*....|.
gi 1613180472 86 MVCGSGLKAIQLAAQSIMLGDADIVIAGGVE 116
Cdd:PRK07910 169 SACASGSEAIAQAWRQIVLGEADIAICGGVE 199
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
251-390 |
6.50e-04 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 41.55 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 251 INDGAALLMLMTEEKALELGLTPL-----VTIESYASAGVAPELMGTGPIPATQKALKKAGLTISDLDLVESNEAFAAQS 325
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPPVyvlgaAAATWHRQISSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 326 LAVLKDLKLNPE------------------IVNVNGGAIALGHPiGASGARILV----TLIHEMKKRQVTRGLATLCIGG 383
Cdd:PRK06158 288 ILFLEDLGFCAKgeggafveggriapggrlPVNTNGGGLSCVHP-GMYGLFLLIeavrQLRGEAGERQVAGAEVALAHGN 366
|
170
....*....|..
gi 1613180472 384 G-----QGTAVI 390
Cdd:PRK06158 367 GgvlssQATAIL 378
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
253-357 |
6.57e-04 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 41.60 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 253 DGAALLMLMTEEKALELGLTPLVTIESYASAG-----VAPELMGTGPIPATQKALKKAG-LTISDLDLVESN-------- 318
Cdd:PTZ00050 239 EGAGILVLEELEHALRRGAKIYAEIRGYGSSSdahhiTAPHPDGRGARRCMENALKDGAnININDVDYVNAHatstpigd 318
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1613180472 319 --EAFAAQSlaVLKDLKLNPEIVNVNGGAIalGHPIGASGA 357
Cdd:PTZ00050 319 kiELKAIKK--VFGDSGAPKLYVSSTKGGL--GHLLGAAGA 355
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
247-357 |
7.51e-04 |
|
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: 41.23 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 247 NASGIN--DGAALLMLMTEEKALELGLTPLVTIESYASAG-----VAPELMGTGPIPATQKALKKAGLTISDLDLV---- 315
Cdd:COG0304 223 DRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDYInahg 302
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1613180472 316 ---ESNEAFAAQSL-AVLKDlklNPEIVNVNggAI--ALGHPIGASGA 357
Cdd:COG0304 303 tstPLGDAAETKAIkRVFGD---HAYKVPVS--STksMTGHLLGAAGA 345
|
|
| init_cond_enzymes |
cd00827 |
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
20-115 |
1.50e-03 |
|
"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: 40.11 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 20 SFKSVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNVARQVAVHSGIPeDKTAFTLDMVCGSGLKAIQLAA 99
Cdd:cd00827 42 AGDDEDVPTMAVEAARRALERAGIDPDDIGLLIVATESPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAA 120
|
90
....*....|....*...
gi 1613180472 100 QSIMLGDAD--IVIAGGV 115
Cdd:cd00827 121 NLVESGPWRyaLVVASDI 138
|
|
| fabH |
CHL00203 |
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional |
23-206 |
5.20e-03 |
|
3-oxoacyl-acyl-carrier-protein synthase 3; Provisional
Pssm-ID: 164577 [Multi-domain] Cd Length: 326 Bit Score: 38.39 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 23 SVSAVELGTTVLKKILDKTQVKPEMVDEVILGNVLHAGLGQNvARQVAVHSGIPEdKTAFTLDMVCGSGLKAIQLAAQSI 102
Cdd:CHL00203 48 STSLTKLAAEAANKALDKAHMDPLEIDLIILATSTPDDLFGS-ASQLQAEIGATR-AVAFDITAACSGFILALVTATQFI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 103 MLGDADIVIAGGVENMSQaaYVSTQHR-----FGQRLGNSQLIDTLVHDGL-----TDAFNNYHMGIT-AENVAQKYGIS 171
Cdd:CHL00203 126 QNGSYKNILVVGADTLSK--WIDWSDRktcilFGDGAGAAIIGASYENSILgfklcTDGKLNSHLQLMnKPVNNQSFGTT 203
|
170 180 190
....*....|....*....|....*....|....*
gi 1613180472 172 REEQDQFalesQEKAAKALENHRFADEIVPVSVPQ 206
Cdd:CHL00203 204 KLPQGQY----QSISMNGKEVYKFAVFQVPAVIIK 234
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
253-357 |
8.03e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 38.23 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1613180472 253 DGAALLMLMTEEKALELGLTPLVTIESYASAG-----VAPELMGTGPIPATQKALKKAGLTISDLDLV----------ES 317
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstpagDK 311
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1613180472 318 NEAFAAQSlaVLKDlklNPEIVNVNGGAIALGHPIGASGA 357
Cdd:PRK07314 312 AETQAIKR--VFGE---HAYKVAVSSTKSMTGHLLGAAGA 346
|
|
| |
