|
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: 637.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGIT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 161 AENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLRPAFRPaD 240
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDK-D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 241 GSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 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: 597.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFgHASLQDSMIQDGLWDAFNDYHMGIT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 161 AENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPpRVVTDDEQPRPETSEQQLAQLRPAFRPaD 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKK-D 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 241 GSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:COG0183 238 GTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 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: 580.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 5 AIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVTV 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 85 NLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLqDSMIQDGLWDAFNDYHMGITAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 165 ADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQgKKPPRVVTDDEQPRPETSEQQLAQLRPAFRPaDGSVT 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPG-RKGPVVVDRDEGPRPDTTLEKLAKLKPAFKK-DGTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 245 AGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAFAVQ 324
Cdd:cd00751 238 AGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253174 325 ALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:cd00751 318 ALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-393 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 573.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGIT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 161 AENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLRPAFRpAD 240
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK-KD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 241 GSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| 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: 511.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 6 IVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVTVN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 86 LVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMH-GARDGLRFGHASLQDSMIQDgLWDAFNDYHMGITAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 165 ADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPqGKKPPRVVTDDEQPRPETSEQQLAQLRPAFRPaDGSVT 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVK-GRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDP-DGTVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 245 AGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAFAVQ 324
Cdd:TIGR01930 238 AGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQ 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253174 325 ALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:TIGR01930 318 VLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.43e-155 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 443.77 E-value: 1.43e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGIT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 161 AENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLRPAFRPaD 240
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDK-T 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 241 GSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-393 |
1.07e-152 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 436.70 E-value: 1.07e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVL-TAGCGQNPARQTALRAGLPVDT 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIqDGLWDAFNDYHMGI 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 160 TAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpQGKKPPRVVTDDEQPRPETSEQQLAQLRPAFRPA 239
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEI-KTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 240 DGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANE 319
Cdd:PRK09051 240 NGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253174 320 AFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-393 |
1.89e-146 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 420.65 E-value: 1.89e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 2 TDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPA 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 82 VTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGITA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 162 ENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGK-KPPRVVTDDEQPRPETSEqQLAQLRPAFRPAD 240
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRgRPSVIVDKDEGLGKFDPA-KLRKLRPSFKEDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 241 GSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-393 |
3.12e-145 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 417.85 E-value: 3.12e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQvlTAGCGQNPA--RQTALRAGLPVD 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQdGLWDAFNDYH-- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLAR-GRETAGGRRFpv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 157 ---MGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLR 233
Cdd:PRK06205 158 pggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 234 P--AFRPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDE 311
Cdd:PRK06205 238 PimGKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 312 VDLIEANEAFAVQALAVgqLLEW-----DSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQG 386
Cdd:PRK06205 318 IDLIELNEAFAAQVLAV--LKEWgfgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQG 395
|
....*..
gi 490253174 387 IAMTLQR 393
Cdd:PRK06205 396 LAAVFER 402
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-392 |
3.76e-141 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 407.11 E-value: 3.76e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 4 IAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVT 83
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 84 VNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNApylMHGA--RDGLRFGHASLQDSMIQDGLWDAFNDYHMGITA 161
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLG---MHGSyiRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 162 ENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQgKKPPRVVTDDEQPRPETSEQQLAQLRPAFrPADG 241
Cdd:PRK06633 162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI-KKTTSLFDHDETVRPDTSLEILSKLRPAF-DKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 242 SVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAF 321
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490253174 322 AVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-393 |
6.58e-137 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 396.63 E-value: 6.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLER-CQLPAAAVDELIFGQVLTAG-CGQNPARQTALRAGLPVD 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGeDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMhGARDGLRFGHASLQDSMIQdglWDAFNDY--- 155
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVM-GKADSAFSRQAEIFDTTIG---WRFVNPLmka 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 156 -----HMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLA 230
Cdd:PRK09050 157 qygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 231 QLRPAFRPaDGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLD 310
Cdd:PRK09050 237 KLKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 311 EVDLIEANEAFAVQALAVGQLLEW--DSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIA 388
Cdd:PRK09050 316 QFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIA 395
|
....*
gi 490253174 389 MTLQR 393
Cdd:PRK09050 396 LAIER 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-393 |
2.46e-127 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 371.99 E-value: 2.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-SFRGAFAPLSAVDLGAAVVRGLLER-CQLPAAAVDELIFGQVL-TAGCGQNPARQTALRAGLPV 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 78 DTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPyLMHGARDGLRFGHASLQDSMIqdglwdafndyhM 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-MNHGVDFHPGLSKNVAKAAGM------------M 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 158 GITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLRPAFR 237
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 238 PADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEA 317
Cdd:PRK08947 228 PVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253174 318 NEAFAVQALAVGQ---LLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK08947 308 NEAFAAQSLPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-392 |
3.33e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 351.50 E-value: 3.33e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 4 IAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVT 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 84 VNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQDGLWDAFNDYH-MGITAE 162
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 163 NLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPqGKKPPRVVTDDEQPRPETSEQqLAQLRPAFRPaDGS 242
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVA-GKKGDTVIDRDEQPFKANPEK-IPTLKPAFSK-TGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 243 VTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAFA 322
Cdd:PRK06954 246 VTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 323 VQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:PRK06954 326 VVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-393 |
3.50e-117 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 346.38 E-value: 3.50e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAG-CGQNPARQTALRAGLPVDT 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGeDSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGA-----RD--------GLRFGHASLQDSmiqd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAesafsRDakvfdttiGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 147 glwdaFNDYHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKK-PPRVVTDDEQPRPETS 225
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRKlPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 226 EQQLAQLRPAFrpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRA 305
Cdd:PRK08131 232 VEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 306 GWTLDEVDLIEANEAFAVQALAVGQLL--EWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGG 383
Cdd:PRK08131 310 GLTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGV 389
|
410
....*....|
gi 490253174 384 GQGIAMTLQR 393
Cdd:PRK08131 390 GQGLAMVIER 399
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-393 |
8.92e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 343.14 E-value: 8.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-SFRGAFAPLSAVDLGAAVVRGLLERC-QLPAAAVDELIFGQVLTAGC-GQNPARQTALRAGLPv 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 78 DTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPylmHGARDGL------RFGHASLQDSMIQDGLWDA 151
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFA---KGNSDSLpdtknpLFAEAQARTAARAEGGAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 152 FND-----------YHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKkpprVVTDDEQP 220
Cdd:PRK07851 157 WHDpredgllpdvyIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGT----VVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 221 RPETSEQQLAQLRPAFRPaDGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQ 300
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 301 ALQRAGWTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLC 380
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
|
410
....*....|...
gi 490253174 381 VGGGQGIAMTLQR 393
Cdd:PRK07851 392 VGGGQGMAMVLER 404
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-388 |
4.36e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 338.26 E-value: 4.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-SFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVL-TAGCGQNPARQTALRAGLPVD 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRfghaslqdsmiqdgLWDAFNDYHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRPNPR--------------LVEAAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 159 I--TAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSV----------PQGKKppRVVTDDEQPRPETSE 226
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgennkLQEET--ITFSQDEGVRADTTL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 227 QQLAQLRPAFRpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAG 306
Cdd:PRK07661 225 EILGKLRPAFN-VKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 307 WTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQG 386
Cdd:PRK07661 304 LELSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMG 383
|
..
gi 490253174 387 IA 388
Cdd:PRK07661 384 AA 385
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-264 |
7.59e-112 |
|
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: 327.72 E-value: 7.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 4 IAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 84 VNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLM-HGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGITAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALpTDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 163 NLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPrVVTDDEQPRPETSEQQLAQLRPAFRPaDGS 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDK-EGT 238
|
250 260
....*....|....*....|..
gi 490253174 243 VTAGNASSLNDGAAAVLLMRVD 264
Cdd:pfam00108 239 VTAGNASPINDGAAAVLLMSES 260
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-393 |
1.51e-110 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 329.66 E-value: 1.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-SFRGAFAPLSAVDLGAAVVRGLLERCQ-LPAAAVDELIFGQVL-TAGCGQNPARQTALRAGLPV 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 78 DTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPylMHGardglrfGHASLQDSMiqdglwdaFND--- 154
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP--MMG-------NKPSMSPAI--------FARden 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 155 ----YHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpQGKKP----------PRVVTDDEQP 220
Cdd:PRK09052 148 vgiaYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEI-TERFPdlatgevdvkTRTVDLDEGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 221 RPETSEQQLAQLRPAFRpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQ 300
Cdd:PRK09052 227 RADTSLEGLAKLKPVFA-NKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 301 ALQRAGWTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLC 380
Cdd:PRK09052 306 ALKQAGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMC 385
|
410
....*....|...
gi 490253174 381 VGGGQGIAMTLQR 393
Cdd:PRK09052 386 VGTGMGAAGIFER 398
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-393 |
3.65e-109 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 327.88 E-value: 3.65e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 3 DIAIVAAVRTPV-GSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQ-NPARQTALRAGLPVDTP 80
Cdd:PLN02287 47 DVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGARDGLRFGHASLQDSMIQdglwdafndyhMGIT 160
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 161 AENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSV-----PQGKKPPRVVTDDEQPRPETSEQQLAQLRPA 235
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpKTGEEKPIVISVDDGIRPNTTLADLAKLKPV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 236 FRpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLI 315
Cdd:PLN02287 276 FK-KNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 316 EANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRG--ASKGLATLCVGGGQGIAMTLQR 393
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.70e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 316.18 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGArdgLRFGHASL-------QDSMIQDGLWDAFN 153
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSD---LRWGPKHLlhknykiDDAMLVDGLIDAFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 154 DYHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpqgkkpprvVTDDEQPRpETSEQQLAQLR 233
Cdd:PRK06366 158 FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 234 PAFrPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVD 313
Cdd:PRK06366 228 PAF-DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYD 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253174 314 LIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:PRK06366 307 LVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
3-393 |
7.28e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 313.49 E-value: 7.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 3 DIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAV 82
Cdd:PRK08170 4 PVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 83 TVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYL-----------MHGARD-GLRFGH-ASLQDSMIQ---- 145
Cdd:PRK08170 84 TVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLfsekmvrwlagWYAAKSiGQKLAAlGKLRPSYLApvig 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 146 --DGLWDAFNDYHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREeIVPVSVPQGKkpprVVTDDEQPRPE 223
Cdd:PRK08170 164 llRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKE-VVPLFDRDGK----FYDHDDGVRPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 224 TSEQQLAQLRPAFRPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQ 303
Cdd:PRK08170 239 SSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 304 RAGWTLDEVDLIEANEAFAVQALAV-----------------GQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHE 366
Cdd:PRK08170 319 RHGLTLEDLDLWEINEAFAAQVLAClaawadeeycreqlgldGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHA 398
|
410 420
....*....|....*....|....*..
gi 490253174 367 MQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK08170 399 LKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-393 |
2.66e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 310.89 E-value: 2.66e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFR------GAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLtaGCGQN---PARQTAL 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 72 RAGLPVDTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYlmhGARDGLRFGHASLQDSMIQDglWDA 151
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPM---GDNPHIEPNPKLLTDPKYIE--YDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 152 FNDYHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVP-QGKKppRVVTDDEQPRPETSEQQLA 230
Cdd:PRK06445 154 TTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEvEGKK--KVVDVDQSVRPDTSLEKLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 231 QLRPAFRPaDGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLD 310
Cdd:PRK06445 232 KLPPAFKP-DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 311 EVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMT 390
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390
|
...
gi 490253174 391 LQR 393
Cdd:PRK06445 391 LER 393
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-393 |
6.89e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 292.17 E-value: 6.89e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFR--GAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAG-CGQNPARQTALRAGLPV 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 78 DTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHGArdglrfghASLQDSMIqdglwdAFNDYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGG--------AWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 158 --GITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKpprVVTDDEQPRPETSEQQLAQLRPA 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDQNGLT---ILDHDEHMRPGTTMESLAKLKPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 236 F-----RPADGSV---------------TAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPV 295
Cdd:PRK08242 224 FammgeMGGFDAValqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 296 SACRQALQRAGWTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKG 375
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTA 383
|
410
....*....|....*...
gi 490253174 376 LATLCVGGGQGIAMTLQR 393
Cdd:PRK08242 384 LITLCVGGGMGIATIIER 401
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-393 |
3.61e-95 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 291.12 E-value: 3.61e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 4 IAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 84 VNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPY-----LMHGARD-------GLR---FGHASLQDSMIQDgl 148
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIgvskkLARALVDlnkartlGQRlklFSRLRLRDLLPVP-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 149 wDAFNDY----HMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPprvVTDDEQPRPET 224
Cdd:PRK08963 165 -PAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP---LEEDNNIRGDS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 225 SEQQLAQLRPAFRPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDP-SVMGIGPVSACRQALQ 303
Cdd:PRK08963 241 TLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 304 RAGWTLDEVDLIEANEAFAVQALAVGQLL-----------------EWDSEKVNVNGGAIALGHPIGASGCRILVSLVHE 366
Cdd:PRK08963 321 RAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHE 400
|
410 420
....*....|....*....|....*..
gi 490253174 367 MQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK08963 401 LRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-393 |
4.62e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 289.30 E-value: 4.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGcGQ--NPARQTALRAGLPVD 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIG-PQagNIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPylMHGARD-GLRFGhasLQDSMIQDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 157 MG--ITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpqgkkpprvVTDDEQPRpETSEQQLAQLRP 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 235 AFRpaDGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDL 314
Cdd:PRK07801 225 LVE--GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253174 315 IEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-388 |
2.11e-94 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 287.82 E-value: 2.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-SFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGC-GQNPARQTALRAGLPVD 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLM--HGARDG-LRFGHASLQDSMIQdglwdafndy 155
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMnrHMLREGwLVEHKPEIYWSMLQ---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 156 hmgiTAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRV---------VTDDEQPRPETSE 226
Cdd:PRK07108 151 ----TAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKATgrlftkevtVSADEGIRPDTTL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 227 QQLAQLRPAFrpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAG 306
Cdd:PRK07108 227 EGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 307 WTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQG 386
Cdd:PRK07108 305 LKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQG 384
|
..
gi 490253174 387 IA 388
Cdd:PRK07108 385 AA 386
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-393 |
3.33e-92 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 282.00 E-value: 3.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAG-CGQNPARQTALRAGLPVDT 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYlmhGARDGLRFGHASLQDSMIqdglwDAFNDYHmgi 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL---GANAGPGRGLPRPDSWDI-----DMPNQFE--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 160 TAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPP------RVVTDDEQPRpETSEQQLAQLR 233
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGqptgetRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 234 PAFrpADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVD 313
Cdd:PRK07850 229 PVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 314 LIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK07850 307 LVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-389 |
2.85e-80 |
|
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: 251.64 E-value: 2.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 7 VAAVRTPVGSF---RGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTPAVT 83
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 84 VNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSnapylmhgardglrfghASLQDSMIQDGLWDAFNDYHMgitaen 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME-----------------TSAENNAKEKHIDVLINKYGM------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 164 ladafdisRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpQGKKPPRVVTDDE--QPRPETSEQQLAQLRPAFrPADG 241
Cdd:cd00826 138 --------RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGV-KGRKGDIHSDADEyiQFGDEASLDEIAKLRPAF-DKED 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 242 SVTAGNASSLNDGAAAVLLMRVDKARELGLPV-------LARIVSSAVAGVDPS----VMGIGPVSACRQALQRAGWTLD 310
Cdd:cd00826 208 FLTAGNACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 311 EVDLIEANEAFAVQALAVGQLLEWDSEK------------------VNVNGGAIALGHPIGASGCRILVSLVHEMQRR-- 370
Cdd:cd00826 288 DLDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEag 367
|
410 420
....*....|....*....|..
gi 490253174 371 ---GASKGLATLCVGGGQGIAM 389
Cdd:cd00826 368 krqGAGAGLALLCIGGGGGAAM 389
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-392 |
6.12e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 249.68 E-value: 6.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 5 AIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGL---LERcqlpaaAVDELIFGQVLtaGCGQNPARQTALRAGLPVDTPA 81
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFLskgMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 82 VTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYlmhgaRDGLRFGHaslqdsmiqdglwDAFNDYHMGITA 161
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-----QNRARFSP-------------ETIGDPDMGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 162 ENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVpqgkkpprvVTDDEQPRPETSEQQLAQLRPAFRpADG 241
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNG---------LLDESIKKEMNYERIIKRTKPAFL-HNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 242 SVTAGNASSLNDGAAAVLLMRVDKARELGL-PVLaRIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:PRK06690 208 TVTAGNSCGVNDGACAVLVMEEGQARKLGYkPVL-RFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253174 321 FAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQ 392
Cdd:PRK06690 287 FASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-385 |
3.79e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 246.18 E-value: 3.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAG-CGQNPARQTALRAGLPVDT 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMHG---ARDGlrFGHASlQDSMIQDGLWDAFNDYh 156
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPStlpAKNG--LGHYK-SPGMEERYPGIQFSQF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 157 MGitAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGKKPPRVVTDDEQPRPETSEQQLAQLRPAf 236
Cdd:PRK06504 157 TG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLI- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 237 rPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIE 316
Cdd:PRK06504 234 -AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253174 317 ANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQ 385
Cdd:PRK06504 313 VNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGM 381
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-393 |
4.80e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 241.60 E-value: 4.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG---SFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGC-GQNPARQTALRAGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 77 VDTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMS-NAPYLMHGARDGLR-----FGHASLQDSMIQDglwd 150
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGKPplgmgSGNLRLRALHPQS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 151 afndyHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVSVPQGkkppRVVTD-DEQPRPETSEQQL 229
Cdd:PRK06025 157 -----HQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDG----SVALDhEEFPRPQTTAEGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 230 AQLRPAFR-----PADGSVT--------------------AGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAG 284
Cdd:PRK06025 228 AALKPAFTaiadyPLDDKGTtyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 285 VDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLV 364
Cdd:PRK06025 308 DDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVL 387
|
410 420
....*....|....*....|....*....
gi 490253174 365 HEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK06025 388 DELERRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
271-393 |
8.12e-64 |
|
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: 199.79 E-value: 8.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 271 LPVLARIVSSAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAFAVQALAVGQLLEWDSEKVNVNGGAIALGH 350
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490253174 351 PIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-393 |
1.06e-60 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 202.05 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGAFAPLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPVDTP 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 81 AVTVNLVCGSGLKAVQQAVQAIRCG--DAGIviAGGQESMSNAPYlmhGARDGLR------------------FGHASLQ 140
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGqiDSGI--AGGVDTTSDAPI---AVNEGLRkillelnrakttgdrlkaLGKLRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 141 DSMIQ--------DGLwdafndyHMGITAENLADAFDISRERQDAFAASSQRKAAAAIAAGRFREEIVPVsvpqgkkppR 212
Cdd:PRK09268 161 HLAPEiprngeprTGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF---------L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 213 VVTDDEQPRPETSEQQLAQLRPAF-RPADGSVTAGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDpSVMG 291
Cdd:PRK09268 225 GLTRDNNLRPDSSLEKLAKLKPVFgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD-FVHG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 292 -----IGPVSACRQALQRAGWTLDEVDLIEANEAFAVQALAVgqLLEWDSE-------------------KVNVNGGAIA 347
Cdd:PRK09268 304 kegllMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLAT--LKAWEDEeycrerlgldaplgsidrsKLNVNGSSLA 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 490253174 348 LGHPIGASGCRILVSLVHEMQRRGASKGLATLCVGGGQGIAMTLQR 393
Cdd:PRK09268 382 AGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
245-391 |
4.33e-22 |
|
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: 94.43 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 245 AGNASSLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDPS----VMGIGPVSACRQALQRAGWTLDEVDLIEANEA 320
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 321 FAVQALAVGQLLEWDSEKV---NVNGGAIALGHPIGASGCRILVSLVHEMQ-------RRGASKGLATLCVGGGQGIAMT 390
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVrspAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253
|
.
gi 490253174 391 L 391
Cdd:cd00327 254 L 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
12-391 |
3.92e-18 |
|
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: 85.01 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 12 TPVGSFRGafapLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAGCGQNPARQTALRAGLPvDTPAVTVNLVCGSG 91
Cdd:cd00829 6 TPFGRRSD----RSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 92 LKAVQQAVQAIRCGDAGIVIAGGQESMSnapylmHGARDGLRFGHASLQDSMIQDGLWDAFNDYHMGITAENLADAFDIS 171
Cdd:cd00829 81 SAAVRAAAAAIASGLADVVLVVGAEKMS------DVPTGDEAGGRASDLEWEGPEPPGGLTPPALYALAARRYMHRYGTT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 172 RErqdAFAAssqrkaaaaiaagrfreeivpVSVPQ---GKKPPRVVTddeqPRPETSEQQLAQlRPAFRPadgsVTAGNA 248
Cdd:cd00829 155 RE---DLAK---------------------VAVKNhrnAARNPYAQF----RKPITVEDVLNS-RMIADP----LRLLDC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 249 SSLNDGAAAVLLMRVDKARELGLPvLARIVSSAVA-------GVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEANEAF 321
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDR-PVWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 322 AVQAL---------AVGQLLEWDSE---------KVNVNGGAIALGHPIGASGCRILVSLVH-------EMQRRGASKGL 376
Cdd:cd00829 281 TIAELlaledlgfcEKGEGGKLVREgdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRqlrgeagARQVPGARVGL 360
|
410
....*....|....*
gi 490253174 377 ATLCVGGGQGIAMTL 391
Cdd:cd00829 361 AHNIGGTGSAAVVTI 375
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-375 |
4.38e-15 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 76.09 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVG-----SFRgafaplsavDLGAAVVRGLLERCQLPAAAVDELIFGQVLTAG-CGQ-NPARQTALRA 73
Cdd:PRK06064 1 MRDVAIIGVGQTKFGelwdvSLR---------DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 74 GLPvDTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPylMHGARDGLrfghaslqdSMIQDGLWDAFn 153
Cdd:PRK06064 72 GLA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP--TPDATEAI---------ARAGDYEWEEF- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 154 dyhMGITAENLAdAFdISRERQDAFAASsqrkaaaaiaagrfREEIVPVSVPQ---GKKPPrvvtdDEQPRPETSEQQLA 230
Cdd:PRK06064 139 ---FGATFPGLY-AL-IARRYMHKYGTT--------------EEDLALVAVKNhynGSKNP-----YAQFQKEITVEQVL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 231 QLRPAFRPadgsVTAGNASSLNDGAAAVLLMRVDKARELGL-PVlaRIVSSAVA-------------GVDPSVMgigpvs 296
Cdd:PRK06064 195 NSPPVADP----LKLLDCSPITDGAAAVILASEEKAKEYTDtPV--WIKASGQAsdtialhdrkdftTLDAAVV------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 297 ACRQALQRAGWTLDEVDLIEANEAFAV-QALAV-----------GQLLEWDSEK------VNVNGGAIALGHPIGASGCR 358
Cdd:PRK06064 263 AAEKAYKMAGIEPKDIDVAEVHDCFTIaEILAYedlgfakkgegGKLAREGQTYiggdipVNPSGGLKAKGHPVGATGVS 342
|
410
....*....|....*..
gi 490253174 359 ILVSLVHEMqRRGASKG 375
Cdd:PRK06064 343 QAVEIVWQL-RGEAEKG 358
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-376 |
5.61e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 63.43 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 1 MTDIAIVAAVRTPVGSFRGafapLSAVDLGAAVVRGLLERCQLPAAAVDELIFGQvLTAGCgQNPARQTALRAGLPVD-- 78
Cdd:PRK07516 1 MMTASIVGWAHTPFGKLDA----ETLESLIVRVAREALAHAGIAAGDVDGIFLGH-FNAGF-SPQDFPASLVLQADPAlr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 79 -TPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPylmhGARDGLRFGHASLQ--DSMIQDGLWDAFndy 155
Cdd:PRK07516 75 fKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP----TAEVGDILLGASYLkeEGDTPGGFAGVF--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 156 hmGITAENLADAFdisRERQDAFAASSQRKAAAAiaagrfreeivpVSVPqgkkpprvvtddeqprpetseqqLAQLRPA 235
Cdd:PRK07516 148 --GRIAQAYFQRY---GDQSDALAMIAAKNHANG------------VANP-----------------------YAQMRKD 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 236 F------RPADGS-VTAG-----NASSLNDGAAAVLLMRVDKARELGLPVLARIVSSA-----VAGVDPSVMGiGPVSAC 298
Cdd:PRK07516 188 LgfefcrTVSEKNpLVAGplrrtDCSLVSDGAAALVLADAETARALQRAVRFRARAHVndflpLSRRDPLAFE-GPRRAW 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 299 RQALQRAGWTLDEVDLIEANEAFAVQAL---------AVGQ----LLEWDSEK-----VNVNGGAIALGHPIGASG---- 356
Cdd:PRK07516 267 QRALAQAGVTLDDLSFVETHDCFTIAELieyeamglaPPGQgaraIREGWTAKdgklpVNPSGGLKAKGHPIGATGvsmh 346
|
410 420
....*....|....*....|...
gi 490253174 357 ---CRILVSLVHEMQRRGASKGL 376
Cdd:PRK07516 347 vlaAMQLTGEAGGMQIPGAKLAG 369
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
239-364 |
5.47e-08 |
|
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: 54.49 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 239 ADGSVTAgnasslnDGAAAVLLMRVDKARELGLPVLARIVSSAVA--GVDPSVM---GIGPVSACRQALQRAGWTLDEVD 313
Cdd:cd00833 228 ADGYVRG-------EGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRTKGITapsGEAQAALIRRAYARAGVDPSDID 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253174 314 LIEA----------------NEAFA-----VQALAVGqllewdSEKVNVnggaialGHPIGASGcriLVSLV 364
Cdd:cd00833 301 YVEAhgtgtplgdpievealAKVFGgsrsaDQPLLIG------SVKSNI-------GHLEAAAG---LAGLI 356
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
48-371 |
5.72e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 54.08 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 48 VDELIFGQVLTAGCGQNPARQTALRAGLPVDTPaVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMS---NAPYL 124
Cdd:PRK12578 43 IELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTevdTSTSL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 125 MHGARDGlrfghaslqdsmiqDGLWDafndYHMGITAENLADAFDISR--------ERQDAFAASSQRKAAAAIAAGRFR 196
Cdd:PRK12578 122 AIGGRGG--------------NYQWE----YHFYGTTFPTYYALYATRhmavygttEEQMALVSVKAHKYGAMNPKAHFQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 197 EEIvpvsvpqgkkpprvvtddeqprpeTSEQQLAQlrpafRPADGSVTAGNASSLNDGAAAVLLMRVDKARELGL--PVL 274
Cdd:PRK12578 184 KPV------------------------TVEEVLKS-----RAISWPIKLLDSCPISDGSATAIFASEEKVKELKIdsPVW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 275 ARIV--SSAVAGVDPSVMGIG---PVSACRQALQRAGWTLDEVDLIEANEAFAVQALAV------------GQLLE-WDS 336
Cdd:PRK12578 235 ITGIgyANDYAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGyedlgftekgkgGKFIEeGQS 314
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490253174 337 EK-----VNVNGGAIALGHPIGASGcrilVSLVHEM--QRRG 371
Cdd:PRK12578 315 EKggkvgVNLFGGLKAKGHPLGATG----LSMIYEItkQLRD 352
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
28-383 |
8.56e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 53.92 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 28 DLGAAVVRGLLERCQLPAAAVDELIFGQV---LTAGCGQNPARQTALRAGLpVDTPAVTVNLVCGSGLKAVQQAVQAIRC 104
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 105 GDAGIVIAGGQESMSNAPylmhGARDGLRFGHASLQDSMIQDG--LW-DAFNDyhmgitaenLADAFD----ISRERQDA 177
Cdd:PRK06289 107 GRYDVALVVGVELMKTVP----GDVAAEHLGAAAWTGHEGQDArfPWpSMFAR---------VADEYDrrygLDEEHLRA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 178 FA----ASSQRKAAAAIAAGRFreeivpvsvpqgkkPPRVVTDDEQPRPetseqqlaqlrpafrPADGSVTAGNASSLND 253
Cdd:PRK06289 174 IAeinfANARRNPNAQTRGWAF--------------PDEATNDDDATNP---------------VVEGRLRRQDCSQVTD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 254 GAAAVLLMRVDKARELG----LPV------------LARIVSSAVAG--VDPSVMGigpvsACRQALQRAGWTLDEVDLI 315
Cdd:PRK06289 225 GGAGVVLASDAYLRDYAdarpIPRikgwghrtaplgLEQKLDRSAGDpyVLPHVRQ-----AVLDAYRRAGVGLDDLDGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 316 EANEAFAV------------------QALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVH-------EMQRR 370
Cdd:PRK06289 300 EVHDCFTPseylaidhigltgpgeswKAIENGEIAIGGRLPINPSGGLIGGGHPVGASGVRMLLDAAKqvtgtagDYQVE 379
|
410
....*....|...
gi 490253174 371 GASKGLaTLCVGG 383
Cdd:PRK06289 380 GAKTFG-TLNIGG 391
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
65-356 |
2.43e-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: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 65 PARQTALRAGLPvdTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNAPYLMhgardglrfGHASLQDsmi 144
Cdd:cd00834 140 AAGQVAIRLGLR--GPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLA---------GFAALRA--- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 145 qdglwdafndyhmgitaenladafdISRERQDAFAASsqrkaaaaiaagrfreeivpvsvpqgkkpprvvtddeqprpet 224
Cdd:cd00834 206 -------------------------LSTRNDDPEKAS------------------------------------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 225 seqqlaqlRPAFRPADGSVtagnassLNDGAAAVLLMRVDKARELGLPVLARIVSSAVAG-----VDPSVMGIGPVSACR 299
Cdd:cd00834 218 --------RPFDKDRDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMR 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490253174 300 QALQRAGWTLDEVDLI-------EANEafAVQALAVGQLLEWDSEKVNVNGGAIALGHPIGASG 356
Cdd:cd00834 283 AALADAGLSPEDIDYInahgtstPLND--AAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAG 344
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
80-379 |
5.93e-06 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 47.82 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSnaPYLMHGARDglrfghaslqdsmiqdglwdafndyhMGI 159
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPL--EEGLSGFAN--------------------------MGA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 160 TAENLADAFDISRerqdafaassqrkaaaaiaagrfreeivpvsvpqgkkpprvvtddeqprpetseqqlaqlrPAFRPA 239
Cdd:cd00828 206 LSTAEEEPEEMSR-------------------------------------------------------------PFDETR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 240 DGSVTAGnasslndGAAAVLLMRVDKARELGLPVLARIVSSAVAGVDP----SVMGIGPVSACRQALQRAGWTLDEVDLI 315
Cdd:cd00828 225 DGFVEAE-------GAGVLVLERAELALARGAPIYGRVAGTASTTDGAgrsvPAGGKGIARAIRTALAKAGLSLDDLDVI 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490253174 316 EA----------NEAFAVQALAVGQLLEW--DSEKVNVnggaialGHPIGASGcRILVSLVHEMQRRGASKGLATL 379
Cdd:cd00828 298 SAhgtstpandvAESRAIAEVAGALGAPLpvTAQKALF-------GHSKGAAG-ALQLIGALQSLEHGLIPPTANL 365
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
80-383 |
1.48e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 46.81 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNApylmhGARDGlrfghaslqdsmiqdglwdafndyhmgi 159
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTV-----SARVG---------------------------- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 160 tAENLADAFDISRERQ---DAFAASSQRKAAAAIAAGRFREE----IVPVSVPQGKKPP------RVVT-------DDEQ 219
Cdd:PTZ00455 159 -GDYLARAADYRRQRKlddFTFPCLFAKRMKYIQEHGHFTMEdtarVAAKAYANGNKNPlahmhtRKLSlefctgaSDKN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 220 PRPETSEQqlaqLRPAFRPADgsvtagnASSLNDGAAAVLLMRVDKARELGLP----VLARIVSSAVAG-------VDPS 288
Cdd:PTZ00455 238 PKFLGNET----YKPFLRMTD-------CSQVSDGGAGLVLASEEGLQKMGLSpndsRLVEIKSLACASgnlyedpPDAT 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 289 VMgIGPVSACRQALQRAGWTLDEVDLIEANEAFAVQALAVGQLL---EWDSEK---------------VNVNGGAIALGH 350
Cdd:PTZ00455 307 RM-FTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALgiaEYGHAKdlirngatalegripVNTGGGLLSFGH 385
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 490253174 351 PIGASGCRILVSLVHEM-------QRRGASKGLATLCVGG 383
Cdd:PTZ00455 386 PVGATGVKQIMEVYRQMkgqcgeyQMKNIPALGATLNMGG 425
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
80-118 |
2.56e-05 |
|
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: 45.32 E-value: 2.56e-05
10 20 30
....*....|....*....|....*....|....*....
gi 490253174 80 PAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESM 118
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
254-356 |
4.32e-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: 42.00 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 254 GAAAVLLMRVDKARELGLPVLARIV---SSAVA--GVDPSVMGIGPVSACRQALQRAGWTLDEVDLI-------EANEaf 321
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVgygASSDAyhITAPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstPLGD-- 309
|
90 100 110
....*....|....*....|....*....|....*..
gi 490253174 322 AVQALAVGQLLEWDSEKVNVNggAI--ALGHPIGASG 356
Cdd:COG0304 310 AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
233-368 |
4.55e-04 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 41.94 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 233 RPAFRPADGSVtagnassLNDGAAAVLLMRVDKARELGLPVLARI-----VSSAVAGVDPSVmgIGPVSACRQALQRAGW 307
Cdd:PRK07103 226 RPFDQDRDGFI-------YGEACGAVVLESAESARRRGARPYAKLlgwsmRLDANRGPDPSL--EGEMRVIRAALRRAGL 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 308 TLDEVDLIEANEAFAVQ--ALAVGQLLEWDSEKVNVNGGAIALGHPIGASGCRILVSLVHEMQ 368
Cdd:PRK07103 297 GPEDIDYVNPHGTGSPLgdETELAALFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMR 359
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
253-317 |
1.20e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.01 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490253174 253 DGAAAVLLMRVDKARELGLPVLARIVSSAV----------AgvdPSvmGIGPVSACRQALQRAGWTLDEVDLIEA 317
Cdd:COG3321 239 EGVGVVVLKRLSDALRDGDRIYAVIRGSAVnqdgrsngltA---PN--GPAQAAVIRRALADAGVDPATVDYVEA 308
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
243-391 |
1.54e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 40.28 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 243 VTAGNASSLNDGAAAVLLMRVDKAREL-GLPVLARIVSSAVAGVDPSVMGIGPVS------------------------- 296
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEItDKPVLIKAIGTGSDTLRLADRPFGEVPllpnespddykdlrypgvhsfragr 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 297 -ACRQALQRAGWT--LDEVDLIEANEAFAVQALAV------------GQLLEWDSEK------VNVNGGAIALGHPIGAS 355
Cdd:PRK06365 297 mAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTyedlglckygegGQFIESGKPElpgklpVNPSGGLLAAGHAVGAT 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490253174 356 GCRILVSLVHEMQRR-------------GASKGLATLCVGGGQGIAMTL 391
Cdd:PRK06365 377 GIMQAVFMFWQLQGRikkhfhddylqvkNAKRGLIHSHAGTGTYVTVTI 425
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
249-360 |
1.69e-03 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 40.40 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 249 SSLNDGAAAVLLMRVDKARELGL--PVLARIVSSAVAGVDPSvMGIG--------PVSACRQALQRAGWT--LDEVDLIE 316
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKkdPVYVKALQLAVSNGWEL-QYNGwdgsyfptTRIAARKAYREAGITdpREELSMAE 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490253174 317 ANEAFAVQALAVGQLLEWDSE------------------KVNVNGGAIALGHPIGASGCRIL 360
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
65-127 |
2.21e-03 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 39.69 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490253174 65 PARQTALRAGLPvdTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGGQESMSNaPYLMHG 127
Cdd:COG0304 140 AAGHVSIRFGLK--GPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT-PLGLAG 199
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
73-114 |
2.64e-03 |
|
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: 39.23 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490253174 73 AGLPVDTPAVTVNLVCGSGLKAVQQAVQAIRCGDAGIVIAGG 114
Cdd:smart00825 82 VGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
251-356 |
4.24e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.00 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 251 LNDGAAAVLLMRVDKARELGLPVLARIVSSAVAG-----VDPSVMGIGPVSACRQALQRAGWTLDEVDLIEA-------- 317
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYINAhgtstpag 309
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490253174 318 --NEAFAVQAlavgqLLEWDSEKVNVNGGAIALGHPIGASG 356
Cdd:PRK07314 310 dkAETQAIKR-----VFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
251-356 |
4.74e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 38.88 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 251 LNDGAAAVLLMRVDKARELGLPVLARIVS-----SAVAGVDPSVMGIGPVSACRQALQRAGWTLDEVDLIEAN------- 318
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGfgltcDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHgtatrln 287
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490253174 319 ---EAFAVQALAvgqllewdSEKVNVNGGAIALGHPIGASG 356
Cdd:PRK05952 288 dqrEANLIQALF--------PHRVAVSSTKGATGHTLGASG 320
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
253-356 |
6.49e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 38.34 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253174 253 DGAAAVLLMRVDKARELGLPVLARIV--------SSAVAGVDP-SVMGIG-PVSACRQALQRAGWTLDEVDLIEANEAFA 322
Cdd:PRK08256 215 CGAAAAIVCSEEFARKHGLDRAVEIVaqamttdtPSTFDGRSMiDLVGYDmTRAAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490253174 323 VQAL----AVGQLLEWDSEK--------------VNVNGGAIALGHPIGASG 356
Cdd:PRK08256 295 ANELltyeALGLCPEGEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| |
