|
Name |
Accession |
Description |
Interval |
E-value |
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-392 |
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: 552.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMgNGKLVDSMVHDGLWDHLNDFHMGMS 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 161 AELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLK-LSSPEALAALRPAFKKDGg 239
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRpDTTLEKLAKLKPAFKKDG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 240 TVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAF 319
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503023139 320 ASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-392 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 543.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVHDGLWDHLNDFHMGMS 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 161 AELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGLKL-SSPEALAALRPAFKKDg 238
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGdPVVVDTDEHPRPdTTAESLAKLRPAFDKD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 239 GTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEA 318
Cdd:PRK05790 240 GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503023139 319 FASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK05790 320 FAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-391 |
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: 528.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 5 VITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGCITV 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 85 NKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLvDSMVHDGLWDHLNDFHMGMSAELC 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 165 AEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLK-LSSPEALAALRPAFKKDGgTVTA 243
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRpDTTLEKLAKLKPAFKKDG-TVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 244 GNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSS 323
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503023139 324 LAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVEN 391
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-390 |
2.30e-167 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 473.81 E-value: 2.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 2 REVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGC 81
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 82 ITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVHDGLWDHLNDFHMGMSA 161
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 162 ELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG--PTVVEHDEGLKLSSPEALAALRPAFKKDGG 239
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGrpSVIVDKDEGLGKFDPAKLRKLRPSFKEDGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 240 TVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAF 319
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503023139 320 ASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVE 391
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-390 |
1.95e-159 |
|
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: 453.22 E-value: 1.95e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 6 ITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGCITVN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 86 KVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQA-RGGMRMGNGKLVDSMVHDgLWDHLNDFHMGMSAELC 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 165 AEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKL-SSPEALAALRPAFKKDGgTVTA 243
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPnTTLEKLAKLKPAFDPDG-TVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 244 GNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSS 323
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503023139 324 LAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-390 |
4.02e-152 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 434.91 E-value: 4.02e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVHDGLWDHLNDFHMGMS 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 161 AELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGL-KLSSPEALAALRPAFKKDg 238
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGdPIVVAKDEAPrKDTTIEKLAKLKPVFDKT- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 239 GTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEA 318
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503023139 319 FASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.81e-148 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 425.84 E-value: 1.81e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVHDGLWDHLNDFHMGMS 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 161 AELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGLKL-SSPEALAALRPAFKKDg 238
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGePLAFATDEQPRAgTTAESLAKLKPAFKKD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 239 GTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEA 318
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503023139 319 FASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK05656 320 FAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
3-390 |
1.33e-138 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 400.81 E-value: 1.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 3 EVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGCI 82
Cdd:PRK06954 8 PIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 83 TVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVHDGLWDHLNDFH-MGMSA 161
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 162 ELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKLSSPEALAALRPAFKKDgGTV 241
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKT-GTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 242 TAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFAS 321
Cdd:PRK06954 247 TAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503023139 322 SSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK06954 327 VTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-392 |
1.61e-137 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 397.79 E-value: 1.61e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGlgqnP-----ARQACLRAGL 75
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTE----PrdmylSRVAAINAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 76 PVEVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSMVhDGLWDHLNDF 155
Cdd:PRK09051 78 PQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMV-GALHDPFGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 156 HMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKLS-SPEALAALRPAF 234
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADtTLEDLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 235 KKDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHE 314
Cdd:PRK09051 237 KKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503023139 315 LNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK09051 317 ANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.27e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 339.27 E-value: 2.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGMRMGNGKLVDSM----VHDGLWDHLNDFH 156
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRLargrETAGGRRFPVPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 157 MGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGLKL-SSPEALAALRPAF 234
Cdd:PRK06205 161 MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGdPTVVDRDEHPRAdTTLESLAKLRPIM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 235 KKD--GGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDL 312
Cdd:PRK06205 241 GKQdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 313 HELNEAFASSSLAVQRTLGLDPA---RINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLV 389
Cdd:PRK06205 321 IELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVF 400
|
...
gi 503023139 390 ENI 392
Cdd:PRK06205 401 ERV 403
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
2.09e-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: 328.88 E-value: 2.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 4 VVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGCIT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 84 VNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQ-ARGGMRMGNGKLVDSMVHDGLWDHLNDFHMGMSAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTdARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 163 LCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLK-LSSPEALAALRPAFKKDgGTV 241
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRpPTTAEPLAKLKPAFDKE-GTV 239
|
250 260
....*....|....*....|.
gi 503023139 242 TAGNASTLNDGAAAVVLMSAE 262
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSES 260
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.44e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 331.99 E-value: 1.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMT---NAPYLvpqaRGGMRMGNGKLVDSMVHDGLWDHLNDFHM 157
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI----RAGAKFGDIKMVDLMQYDGLTDVFSGVFM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 158 GMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKL-SSPEALAALRPAFKK 236
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPdTSLEILSKLRPAFDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 237 DGgTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELN 316
Cdd:PRK06633 238 NG-VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVN 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503023139 317 EAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK06633 317 EAFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-392 |
4.00e-110 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 328.45 E-value: 4.00e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIAR-AGLAKDQVDEVIMGCVLPAGL-GQNPARQACLRAGLPVE 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 79 VGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARG-------------GMRMGNGKL-----V 140
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSafsrqaeifdttiGWRFVNPLMkaqygV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 141 DSMvhdglwdhlndfhmGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGL 219
Cdd:PRK09050 161 DSM--------------PETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGdPVVVDRDEHP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 220 KLS-SPEALAALRPAFKKdGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPK 298
Cdd:PRK09050 227 RPEtTLEALAKLKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 299 ACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGL--DPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMAS 376
Cdd:PRK09050 306 LLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCT 385
|
410
....*....|....*.
gi 503023139 377 LCLGGGEAVSLLVENI 392
Cdd:PRK09050 386 MCIGVGQGIALAIERV 401
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-382 |
3.90e-107 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 320.54 E-value: 3.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG-AFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLP-AGLGQNPARQACLRAGLPVE 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPeAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 79 VGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLvpqarGGMRMGNGKLVDSMvhdglwdhlNDFHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM-----GHVVRPNPRLVEAA---------PEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 159 M--SAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRK---------GPTVVEHDEGLKL-SSPEA 226
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTvgennklqeETITFSQDEGVRAdTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 227 LAALRPAFKKdGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGID 306
Cdd:PRK07661 227 LGKLRPAFNV-KGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503023139 307 PKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGG 382
Cdd:PRK07661 306 LSDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGG 381
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-390 |
2.88e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 313.10 E-value: 2.88e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVP-QARGGMRM---GNGKLVDSMVHDGLWDHLNDFH 156
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPsDLRWGPKHllhKNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 157 MGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSvagrkgptVVEHDEGLKLSSPEALAALRPAFKK 236
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRKTTMEDLAKLPPAFDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 237 DgGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELN 316
Cdd:PRK06366 233 N-GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503023139 317 EAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK06366 312 EAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-392 |
4.10e-96 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 292.25 E-value: 4.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFR-GAFASLSALDLGVVVLNEAIAR-AGLAKDQVDEVIMGCV---LPAGLgqNPARQACLRAGL 75
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKgGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVqqtLEQGF--NIARNAALLAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 76 PVEVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPylvpqarggmrMGNGklVDsmVHDGLWDHLND- 154
Cdd:PRK08947 79 PHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG--VD--FHPGLSKNVAKa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 155 -FHMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKG-PTVVEHDEGLKL-SSPEALAALR 231
Cdd:PRK08947 144 aGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGvLKLFDYDEVIRPeTTVEALAALR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 232 PAFKKDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDID 311
Cdd:PRK08947 224 PAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDID 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 312 LHELNEAFASSSLAVQRTLGLDPA---RINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLL 388
Cdd:PRK08947 304 VFELNEAFAAQSLPCLKDLGLLDKmdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATV 383
|
....
gi 503023139 389 VENI 392
Cdd:PRK08947 384 FERV 387
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-392 |
5.25e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 292.01 E-value: 5.25e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFR------GAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGlgQN---PARQACL 71
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVG--ENwlyGGRHPIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 72 RAGLPVEVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAP-YLVPQARGGMR-MGNGKLVDsmvhdglW 149
Cdd:PRK06445 79 LARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPmGDNPHIEPNPKlLTDPKYIE-------Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 150 DHLNDFHMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKL-SSPEALA 228
Cdd:PRK06445 152 DLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPdTSLEKLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 229 ALRPAFKKDGgTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPK 308
Cdd:PRK06445 232 KLPPAFKPDG-VITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 309 DIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLL 388
Cdd:PRK06445 311 DIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVV 390
|
....
gi 503023139 389 VENI 392
Cdd:PRK06445 391 LERV 394
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-382 |
1.21e-95 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 291.52 E-value: 1.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG-AFRGAFASLSALDLGVVVLNEAIARA-GLAKDQVDEVIMGCVLP-AGLGQNPARQACLRAGLPV 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPeAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 78 EVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYlvpqarggmrMGNGKLVDSMVHDGLWDHLNDFHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 158 GMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRK----------GPTVVEHDEGLKL-SSPEA 226
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFpdlatgevdvKTRTVDLDEGPRAdTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 227 LAALRPAFKkDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGID 306
Cdd:PRK09052 235 LAKLKPVFA-NKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLK 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503023139 307 PKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGG 382
Cdd:PRK09052 314 QDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTG 389
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-392 |
1.01e-93 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 285.85 E-value: 1.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPVEV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGeQSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAP--YLVPQARGGMRMGngklvdsmvhDGLWDHLNDFHm 157
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPlgANAGPGRGLPRPD----------SWDIDMPNQFE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 158 gmSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVS---VAGRKGPT----VVEHDEGLKLSSPEALAAL 230
Cdd:PRK07850 150 --AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapvLDEEGQPTgetrLVTRDQGLRDTTMEGLAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 231 RPAFkkDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDI 310
Cdd:PRK07850 228 KPVL--EGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 311 DLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK07850 306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
..
gi 503023139 391 NI 392
Cdd:PRK07850 386 RI 387
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.15e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 278.13 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPVEV 79
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAP----YLVPQARGgmrmgngkLVDSMVHDGLWDH---- 151
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPissaMTAGEQLG--------FTSPFAESKGWLHrygd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 152 --LNDFHmgmSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVsvAGrkgptvVEHDEGLKLSSPEALAA 229
Cdd:PRK07801 153 qeVSQFR---GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--GG------VTVDEGPRETSLEKMAG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 230 LRPAFkkDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKD 309
Cdd:PRK07801 222 LKPLV--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 310 IDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLV 389
Cdd:PRK07801 300 IDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTII 379
|
.
gi 503023139 390 E 390
Cdd:PRK07801 380 E 380
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-392 |
7.91e-89 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 273.96 E-value: 7.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGL-GQNPARQACLRAGLPVEV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARG-------------GMRMGNGKLVDSMVHD 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESafsrdakvfdttiGARFPNPKIVAQYGND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 147 GlwdhlndfhMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSV--AGRKGPTVVEHDEGLKLSSP 224
Cdd:PRK08131 161 S---------MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVpqGRKLPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 225 -EALAALRPAFkkDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKA 303
Cdd:PRK08131 232 vEALTKLKPLF--EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 304 GIDPKDIDLHELNEAFASSSLAVQRTLGL--DPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGG 381
Cdd:PRK08131 310 GLTLDDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGV 389
|
410
....*....|.
gi 503023139 382 GEAVSLLVENI 392
Cdd:PRK08131 390 GQGLAMVIERV 400
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-390 |
9.10e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 273.80 E-value: 9.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG-AFRGAFASLSALDLGVVVLNEAIARA-GLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPV 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 78 EVGCiTVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMT--------------NAPYLVPQARGGMRMGNGklvDSM 143
Cdd:PRK07851 81 LPGT-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtkNPLFAEAQARTAARAEGG---AEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 144 VHDGLWD-HLNDFH--MGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSvagRKGPTVVEHDEGLK 220
Cdd:PRK07851 157 WHDPREDgLLPDVYiaMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVT---LPDGTVVSTDDGPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 221 L-SSPEALAALRPAFKKDGgTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKA 299
Cdd:PRK07851 234 AgTTYEKVSQLKPVFRPDG-TVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 300 CAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCL 379
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|.
gi 503023139 380 GGGEAVSLLVE 390
Cdd:PRK07851 393 GGGQGMAMVLE 403
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-382 |
3.56e-88 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 273.95 E-value: 3.56e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 2 REVVITSACRTPV-GAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQ-NPARQACLRAGLPVEV 79
Cdd:PLN02287 46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYlvpQARGGMrmgNGKLVD-SMVHDGLwdhlndFHMG 158
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPM---AWEGGV---NPRVESfSQAQDCL------LPMG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 159 MSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSV------AGRKGPTVVEHDEGLKLSSPEA-LAALR 231
Cdd:PLN02287 194 ITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTkivdpkTGEEKPIVISVDDGIRPNTTLAdLAKLK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 232 PAFKKDGGTvTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDID 311
Cdd:PLN02287 274 PVFKKNGTT-TAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDID 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503023139 312 LHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMK--DQDAATGMASLCLGGG 382
Cdd:PLN02287 353 LFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKrrGKDCRFGVVSMCIGTG 425
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.29e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 270.22 E-value: 2.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFR--GAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPV 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 78 EVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTnapylvpqaRGGMRMGNGKL-VDSMVHDglwdHLNDFH 156
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMS---------RVPMGSDGGAWaMDPSTNF----PTYFVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 157 MGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSvaGRKGPTVVEHDEGLKL-SSPEALAALRPAFK 235
Cdd:PRK08242 148 QGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGLTILDHDEHMRPgTTMESLAKLKPSFA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 236 KDGGTV--------------------TAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLS 295
Cdd:PRK08242 226 MMGEMGgfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 296 IPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMA 375
Cdd:PRK08242 306 TRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALI 385
|
410
....*....|....*..
gi 503023139 376 SLCLGGGEAVSLLVENI 392
Cdd:PRK08242 386 TLCVGGGMGIATIIERV 402
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-390 |
2.14e-86 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 267.41 E-value: 2.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG-AFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPVE 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGaTGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 79 VGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTnapyLVPQARGGMRMGNGKLVDsmvhdglwdHLNDFHMG 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIS----CVQNEMNRHMLREGWLVE---------HKPEIYWS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 159 M--SAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSV-AGRKGPTV---------VEHDEGLKL-SSPE 225
Cdd:PRK07108 148 MlqTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVtAGVADKATgrlftkevtVSADEGIRPdTTLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 226 ALAALRPAFKkdGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGI 305
Cdd:PRK07108 228 GVSKIRSALP--GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 306 DPKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAV 385
Cdd:PRK07108 306 KVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGA 385
|
....*
gi 503023139 386 SLLVE 390
Cdd:PRK07108 386 AGLFE 390
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-390 |
2.53e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 264.67 E-value: 2.53e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAG-LGQNPARQACLRAGLPVEV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPqARGGMRMGNGklvdSMVHDGLWDHLND--FHM 157
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSP-STLPAKNGLG----HYKSPGMEERYPGiqFSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 158 GMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEH-DEGLKL-SSPEALAALRPAfk 235
Cdd:PRK06504 156 FTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIRFdATLEGIAGVKLI-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 236 KDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHEL 315
Cdd:PRK06504 234 AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEV 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503023139 316 NEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK06504 314 NEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.30e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 258.79 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQ-----------ARG---------GMRMGNGKLV 140
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmvrwlagwyaAKSigqklaalgKLRPSYLAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 141 DSMVHdGLWDHLNDFHMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKaQIAPVsvAGRKGpTVVEHDEGLK 220
Cdd:PRK08170 162 IGLLR-GLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL--FDRDG-KFYDHDDGVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 221 L-SSPEALAALRPAFKKDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKA 299
Cdd:PRK08170 237 PdSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 300 CAKAGIDPKDIDLHELNEAFASSSLAVQRT----------LGL-------DPARINIYGGGISIGHPIGASGARVLTTLI 362
Cdd:PRK08170 317 LQRHGLTLEDLDLWEINEAFAAQVLACLAAwadeeycreqLGLdgalgelDRERLNVDGGAIALGHPVGASGARIVLHLL 396
|
410 420 430
....*....|....*....|....*....|
gi 503023139 363 YAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK08170 397 HALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-390 |
2.36e-73 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 234.88 E-value: 2.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 2 REVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGC 81
Cdd:PRK08963 5 DRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 82 ITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLV--PQARGgmrmgngkLVDSMVHDGLWDHLNDFH--- 156
Cdd:PRK08963 85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskKLARA--------LVDLNKARTLGQRLKLFSrlr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 157 -------------------MGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPtvVEHDE 217
Cdd:PRK08963 157 lrdllpvppavaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQP--LEEDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 218 GL-KLSSPEALAALRPAFKKDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDP-KYVLVAPMLS 295
Cdd:PRK08963 235 NIrGDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 296 IPKACAKAGIDPKDIDLHELNEAFASSSLA----------VQRTLG-------LDPARINIYGGGISIGHPIGASGARVL 358
Cdd:PRK08963 315 TPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMI 394
|
410 420 430
....*....|....*....|....*....|..
gi 503023139 359 TTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK08963 395 TQTLHELRRRGGGLGLTTACAAGGLGAAMVLE 426
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
8-390 |
2.34e-71 |
|
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: 228.92 E-value: 2.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 8 SACRTPVGAF---RGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVGCITV 84
Cdd:cd00826 2 GAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 85 NKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARggmrmgngklvdsmvhdglwdHLndfhmgmsaELC 164
Cdd:cd00826 82 NNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEK---------------------HI---------DVL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 165 AEKYGvSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAGRKGPTVVEHDEGLKL---SSPEALAALRPAFKKDgGTV 241
Cdd:cd00826 132 INKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFgdeASLDEIAKLRPAFDKE-DFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 242 TAGNASTLNDGAAAVVLMSAEKAA-------ALGARPLVRVGAQAAAGIDPKYV-LVAPMLSIP---KACAKAGIDPKDI 310
Cdd:cd00826 210 TAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKVIkMVGGDGPIEaarKALEKAGLGIGDL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 311 DLHELNEAFASSSLAVQRTLGLDPAR------------------INIYGGGISIGHPIGASGARVLTTLIYAMK-----D 367
Cdd:cd00826 290 DLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKgeagkR 369
|
410 420
....*....|....*....|...
gi 503023139 368 QDAATGMASLCLGGGEAVSLLVE 390
Cdd:cd00826 370 QGAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-392 |
1.02e-69 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 223.49 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 3 EVVITSACRTPVGAFRGAFASLSALDLGVVVLNeaIARAGLaKDQVDEVIMGCVLpaGLGQNPARQACLRAGLPVEVGCI 82
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGM-EREIDDVILGNVV--GPGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 83 TVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYlvpQARGGMRMgngklvdsmvhdglwDHLNDFHMGMSAE 162
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF---QNRARFSP---------------ETIGDPDMGVAAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 163 LCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVSVAgrkgptvveHDEGLKLSSPEA--LAALRPAFKKDGgT 240
Cdd:PRK06690 139 YVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSFNGL---------LDESIKKEMNYEriIKRTKPAFLHNG-T 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 241 VTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFA 320
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503023139 321 SSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.19e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 206.94 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG---AFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGL-GQNPARQACLRAGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 77 VEVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMT-NAPYLVPQARGG---MRMGNGKLVDSMVHDglwdhl 152
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGkppLGMGSGNLRLRALHP------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 153 nDFHMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVsvAGRKGPTVVEHDEGLK-LSSPEALAALR 231
Cdd:PRK06025 155 -QSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVALDHEEFPRpQTTAEGLAALK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 232 PAFKK-------DGGTVT------------------AGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDPK 286
Cdd:PRK06025 232 PAFTAiadypldDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 287 YVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGARVLTTLIYAMK 366
Cdd:PRK06025 312 LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
|
410 420
....*....|....*....|....*.
gi 503023139 367 DQDAATGMASLCLGGGEAVSLLVENI 392
Cdd:PRK06025 392 RRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-390 |
4.38e-53 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 182.02 E-value: 4.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEVG 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVP--------QARGGMRMGN-----GKLVDSMV--- 144
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNeglrkillELNRAKTTGDrlkalGKLRPKHLape 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 145 -------HDGLwdhlndfHMGMSAELCAEKYGVSRQDQDQFAVESYAKSFEADAQGRFKAQIAPVsvagrKGptvVEHDE 217
Cdd:PRK09268 166 iprngepRTGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG---LTRDN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 218 GLKL-SSPEALAALRPAF-KKDGGTVTAGNASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQAAAGIDpkYV------L 289
Cdd:PRK09268 231 NLRPdSSLEKLAKLKPVFgKGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD--FVhgkeglL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 290 VAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSLAV----------QRTLGL-------DPARINIYGGGISIGHPIGA 352
Cdd:PRK09268 309 MAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATlkawedeeycRERLGLdaplgsiDRSKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*...
gi 503023139 353 SGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-390 |
6.54e-40 |
|
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: 138.16 E-value: 6.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 270 RPLVRVGAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDPARINIYGGGISIGHP 349
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 503023139 350 IGASGARVLTTLIYAMKDQDAATGMASLCLGGGEAVSLLVE 390
Cdd:pfam02803 82 LGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
19-389 |
1.41e-25 |
|
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: 106.58 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 19 GAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVeVGCITVNKVCGSGLKAVMLA 98
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 99 AQAIACGDAEVIVAGGMESMTNAPYLVPQarggmrmgnGKLVDSMVHDGLWDHLNDFHMGMSAELCA---EKYGVSRQDQ 175
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGDEA---------GGRASDLEWEGPEPPGGLTPPALYALAARrymHRYGTTREDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 176 DQFAVESYAksfeaDAQGRFKAQIapvsvagRKGPTVVEHDEGLKLSSPealaalrpafkkdggtVTAGNASTLNDGAAA 255
Cdd:cd00829 159 AKVAVKNHR-----NAARNPYAQF-------RKPITVEDVLNSRMIADP----------------LRLLDCCPVSDGAAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 256 VVLMSAEKAAALGARPlVRVGAQAAA-------GIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSLAVQR 328
Cdd:cd00829 211 VVLASEERARELTDRP-VWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 329 TLGLDP-------------AR-----INIYGGGISIGHPIGASGARVLTTLIYAMKDQ-------DAATGMASLCLGGGE 383
Cdd:cd00829 290 DLGFCEkgeggklvregdtAIggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEagarqvpGARVGLAHNIGGTGS 369
|
....*.
gi 503023139 384 AVSLLV 389
Cdd:cd00829 370 AAVVTI 375
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
29-389 |
2.06e-17 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 80.95 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 29 LGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPvEVGCITVNKVCGSGLKAVMLAAQAIACGDAE 108
Cdd:cd00327 10 LGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGKAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 109 VIVAGGMESmtnapylvpqarggmrmgngklvdsmvhdglwdhlndfhmgmsaelcaekygvsrqdqdqfavesyaksfe 188
Cdd:cd00327 89 IVLAGGSEE----------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 189 adaqgrfkaqiapvsvagrkgptvvehdeglklsspealaalrpafkkdggtvtagnaSTLNDGAAAVVLMSAEKAAALG 268
Cdd:cd00327 98 ----------------------------------------------------------FVFGDGAAAAVVESEEHALRRG 119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 269 ARPLVRVgAQAAAGIDPKYVLVAPMLS-----IPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDP---ARINIY 340
Cdd:cd00327 120 AHPQAEI-VSTAATFDGASMVPAVSGEglaraARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPAVS 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 503023139 341 GGGISIGHPIGASGARVLTTLIYAMK-------DQDAATGMASLCLGGGEAVSLLV 389
Cdd:cd00327 199 ATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-356 |
1.86e-15 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 77.24 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVG-----AFRgafaslsalDLGVVVLNEAIARAGLAKDQVDEVIMGCVLpAGL--GQ-NPARQACLR 72
Cdd:PRK06064 1 MRDVAIIGVGQTKFGelwdvSLR---------DLAVEAGLEALEDAGIDGKDIDAMYVGNMS-AGLfvSQeHIAALIADY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 73 AGLPvEVGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPylVPQARGGMrmgngklvdSMVHDGLWDHL 152
Cdd:PRK06064 71 AGLA-PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVP--TPDATEAI---------ARAGDYEWEEF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 153 NDFHM----GMSAELCAEKYGVSRQDQDQFAVESYAK-SFEADAQGRFKAQIAPVsvagRKGPTVVehdEGLKL--SSPe 225
Cdd:PRK06064 139 FGATFpglyALIARRYMHKYGTTEEDLALVAVKNHYNgSKNPYAQFQKEITVEQV----LNSPPVA---DPLKLldCSP- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 226 alaalrpafkkdggtvtagnastLNDGAAAVVLMSAEKAAALGARPL-VRVGAQAAAGI-----DPKYVLVAPMLSIPKA 299
Cdd:PRK06064 211 -----------------------ITDGAAAVILASEEKAKEYTDTPVwIKASGQASDTIalhdrKDFTTLDAAVVAAEKA 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503023139 300 CAKAGIDPKDIDLHELNEAFASSSL-------AVQRTLGLDPAR-----------INIYGGGISIGHPIGASGAR 356
Cdd:PRK06064 268 YKMAGIEPKDIDVAEVHDCFTIAEIlayedlgFAKKGEGGKLARegqtyiggdipVNPSGGLKAKGHPVGATGVS 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
36-368 |
8.49e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 72.19 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 36 EAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVEvGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGM 115
Cdd:PRK12578 31 EALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGK-VPLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 116 ESMTNAPYLVPQARGGmRMGNgklvdsmvhdGLWdhlnDFHM---------GMSAELCAEKYGVSRQDQDQFAVES--YA 184
Cdd:PRK12578 110 DKMTEVDTSTSLAIGG-RGGN----------YQW----EYHFygttfptyyALYATRHMAVYGTTEEQMALVSVKAhkYG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 185 KSFEadaqgrfKAQIapvsvagRKGPTVVEHDEGLKLSSPEALAalrpafkkdggtvtagNASTLNDGAAAVVLMSAEKA 264
Cdd:PRK12578 175 AMNP-------KAHF-------QKPVTVEEVLKSRAISWPIKLL----------------DSCPISDGSATAIFASEEKV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 265 AALGARPLVRVGAQAAAGiDPKYV--------LVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGL---- 332
Cdd:PRK12578 225 KELKIDSPVWITGIGYAN-DYAYVarrgewvgFKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFtekg 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 503023139 333 --------------DPARINIYGGGISIGHPIGASGarvlTTLIYAMKDQ 368
Cdd:PRK12578 304 kggkfieegqsekgGKVGVNLFGGLKAKGHPLGATG----LSMIYEITKQ 349
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
37-354 |
3.50e-13 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 70.31 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 37 AIARAGLAKDQVDEVIMGCVLpaglGQNPARQACLRA----GLPVevgcITVNKVCGSGLKAVMLAAQAIACGDAEVIVA 112
Cdd:PRK08256 33 ALADAGIDYDAVQQAYVGYVY----GDSTSGQRALYEvgmtGIPI----VNVNNNCSTGSTALFLARQAVRSGAADCALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 113 GGMESMTnapylvPQARGGMrmGNGKLVDSMVHDGLWDHLNDFHMGMSAelcAEKYGVsrqdqdqfAVESYAKSFEADAQ 192
Cdd:PRK08256 105 LGFEQMQ------PGALGSV--WDDRPSPLERFDKALAELQGFDPAPPA---LRMFGG--------AGREHMEKYGTTAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 193 grfkaQIAPVSVAGRK----GPTVVEHDEglkLSSPEALAAlRPAFkkdgGTVTAGNASTLNDGAAAVVLMSAEKAAALG 268
Cdd:PRK08256 166 -----TFAKIGVKARRhaanNPYAQFRDE---YTLEDVLAS-PMIW----GPLTRLQCCPPTCGAAAAIVCSEEFARKHG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 269 ARPLVRVGAQAA--------AGIDPKYVLVAPM--LSIPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGLDPAR-- 336
Cdd:PRK08256 233 LDRAVEIVAQAMttdtpstfDGRSMIDLVGYDMtrAAAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEALGLCPEGea 312
|
330 340 350
....*....|....*....|....*....|....
gi 503023139 337 ----------------INIYGGGISIGHPIGASG 354
Cdd:PRK08256 313 ekfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
25-358 |
1.90e-12 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 68.13 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 25 SALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPA---GLGQNPARQAcLRagLPvEVGCITVNKVCGSGLKAVMLAAQA 101
Cdd:PRK06157 26 GAEDLMVEAFLEALADAGIEPKDIDAAWFGTHYDEigsGKSGTPLSRA-LR--LP-NIPVTRVENFCATGSEAFRGAVYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 102 IACGDAEVIVAGGMESMTNAPY--LVPQARGG---MRMGNGKLVDSmvhdglwdhlndFHMGMSAElcAEKYGVSRQDqd 176
Cdd:PRK06157 102 VASGAYDIALALGVEKLKDTGYggLPVANPGTladMTMPNVTAPGN------------FAQLASAY--AAKYGVSRED-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 177 qfavesyaksfeadaqgrFKAQIAPVSVAgrkgptvvEHDEGLKlsSPEAlaALRPAFKKD---GGTVTAGN-----AST 248
Cdd:PRK06157 166 ------------------LKRAMAHVSVK--------SHANGAR--NPKA--HLRKAVTEEqvlKAPMIAGPlglfdCCG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 249 LNDGAAAVVLMSAEKAAALGARPLVRVGA-QAAAG-----IDPKY-VLVAPMLSIP--KACAKAGI-DP-KDIDLHELNE 317
Cdd:PRK06157 216 VSDGAAAAIVTTPEIARALGKKDPVYVKAlQLAVSngwelQYNGWdGSYFPTTRIAarKAYREAGItDPrEELSMAEVHD 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503023139 318 AFASSSLAVQRTLGLDPA------------------RINIYGGGISIGHPIGASGARVL 358
Cdd:PRK06157 296 CFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
27-358 |
4.25e-10 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 60.86 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 27 LDLGVVVLNEAIARAGLAKDQVDEVIMGCVLpaglGQNPARQACLrAGLPVEV-----GCITV--NKVCGSGLKAVMLAA 99
Cdd:PRK06289 27 ADLTREVVDGTLAAAGVDADDIEVVHVGNFF----GELFAGQGHL-GAMPATVhpalwGVPASrhEAACASGSVATLAAM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 100 QAIACGDAEVIVAGGMESMTNapylVPQARGGMRMGNGKLVDsmvHDG-----LWDHLndfhMGMSAELCAEKYGVSRQD 174
Cdd:PRK06289 102 ADLRAGRYDVALVVGVELMKT----VPGDVAAEHLGAAAWTG---HEGqdarfPWPSM----FARVADEYDRRYGLDEEH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 175 QDQFAVESYAKS-FEADAQGRFKAQIAPVSVAGRKGPTVVEhdeglklsspealAALRpafKKDGGTVTagnastlnDGA 253
Cdd:PRK06289 171 LRAIAEINFANArRNPNAQTRGWAFPDEATNDDDATNPVVE-------------GRLR---RQDCSQVT--------DGG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 254 AAVVLMSAEKAAAL-GARPLVRV------------GAQAAAGIDPKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFA 320
Cdd:PRK06289 227 AGVVLASDAYLRDYaDARPIPRIkgwghrtaplglEQKLDRSAGDPYVLPHVRQAVLDAYRRAGVGLDDLDGFEVHDCFT 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 503023139 321 SSSLAVQRTLGLDPA------------------RINIYGGGISIGHPIGASGARVL 358
Cdd:PRK06289 307 PSEYLAIDHIGLTGPgeswkaiengeiaiggrlPINPSGGLIGGGHPVGASGVRML 362
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
250-349 |
1.31e-08 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 56.19 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 250 NDGAAAVVLMSAEKAAALGARPLVRVGAQAAAG---ID--PKYVLVAPMLSIPKACAKAGIDPKDIDLHELNEAFASSSL 324
Cdd:PRK06158 209 TDGAGAVVMVRADRARDLPRPPVYVLGAAAATWhrqISsmPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINTI 288
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 503023139 325 AVQRTLGLDP----------ARI--------NIYGGGISIGHP 349
Cdd:PRK06158 289 LFLEDLGFCAkgeggafvegGRIapggrlpvNTNGGGLSCVHP 331
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
247-392 |
3.07e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 55.28 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 247 STLNDGAAAVVLMSAEKAAALGARP----LVRVGAQAAAG----IDPKYV--LVAPMLSIPKACAKAGIDPKDIDLHELN 316
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASgnlyEDPPDAtrMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 317 EAFASSSLAVQRTLGL-DPAR-----------------INIYGGGISIGHPIGASGARVLTTLIYAMKDQDAATGM---- 374
Cdd:PTZ00455 336 DCFTIAELLMYEALGIaEYGHakdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMknip 415
|
170 180
....*....|....*....|...
gi 503023139 375 ---ASLCLGGGE--AVSLLVENI 392
Cdd:PTZ00455 416 algATLNMGGDDktAVSTVLQNI 438
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
251-354 |
2.92e-06 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 48.92 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 251 DGAAAVVLMSAEKAAALGARPLVRVGaqAAAGIDPKYVLVAPMLSIPKACAKA----GIDPKDIDLHELNEAFASSSLAV 326
Cdd:PRK07937 206 DGAAAVVLAAGDRARELRERPAWITG--IEHRIESPSLGARDLTRSPSTALAAeaatGGDAGGVDVAELHAPFTHQELIL 283
|
90 100
....*....|....*....|....*....
gi 503023139 327 QRTLGL-DPARINIYGGGISiGHPIGASG 354
Cdd:PRK07937 284 REALGLgDKTKVNPSGGALA-ANPMFAAG 311
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
19-354 |
3.11e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 48.79 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 19 GAFASLSALDLGVVVLNEAIARAGLAKDQVDEVIMGcVLPAGLgQNPARQACLRAGLPVE---VGCITVNKVCGSGLKAV 95
Cdd:PRK07516 15 GKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLG-HFNAGF-SPQDFPASLVLQADPAlrfKPATRVENACATGSAAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 96 MLAAQAIACGDAEVIVAGGMESMTNAPylvpqarggmrmgngklvdsmvhdglwdhlndfhmgmSAELCAEKYGVSRQDQ 175
Cdd:PRK07516 93 YAALDAIEAGRARIVLVVGAEKMTATP-------------------------------------TAEVGDILLGASYLKE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 176 DQFAVESYAKSFEADAQGRFK---------AQIApvsvagrkgptVVEHDEGLklSSPeaLAALRpafkKDGG-----TV 241
Cdd:PRK07516 136 EGDTPGGFAGVFGRIAQAYFQrygdqsdalAMIA-----------AKNHANGV--ANP--YAQMR----KDLGfefcrTV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 242 TAGN-----------ASTLNDGAAAVVLMSAEKAAALGARPLVRVGAQA-----AAGIDPkYVLVAPMLSIPKACAKAGI 305
Cdd:PRK07516 197 SEKNplvagplrrtdCSLVSDGAAALVLADAETARALQRAVRFRARAHVndflpLSRRDP-LAFEGPRRAWQRALAQAGV 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503023139 306 DPKDIDLHELNEAFASSSLAVQRTLGLDP----AR--------------INIYGGGISIGHPIGASG 354
Cdd:PRK07516 276 TLDDLSFVETHDCFTIAELIEYEAMGLAPpgqgARairegwtakdgklpVNPSGGLKAKGHPIGATG 342
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
29-132 |
1.82e-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: 45.70 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 29 LGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQACLRAGLPVE-----VGC-------------------ITV 84
Cdd:pfam00109 90 LLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPRRgspfaVGTmpsviagrisyflglrgpsVTV 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 503023139 85 NKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNAPYLVPQARGGM 132
Cdd:pfam00109 170 DTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGM 217
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
29-355 |
1.12e-04 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 44.07 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 29 LGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQ------------------------------NPARQACLRAGLpvE 78
Cdd:cd00834 74 FALAAAEEALADAGLDPEELDPERIGVVIGSGIGGlatieeayrallekgprrvspffvpmalpnMAAGQVAIRLGL--R 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 79 VGCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMtnapylvpqarggmrmgngklvdsmvhdglwdhlndfhmg 158
Cdd:cd00834 152 GPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEAL---------------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 159 msaelcaekygvsrqdqdqfavesyaksfeadaqgrfkaqIAPVSVAGrkgptvvehdeglkLSSPEALA--------AL 230
Cdd:cd00834 192 ----------------------------------------ITPLTLAG--------------FAALRALStrnddpekAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 231 RPAFKKDGGTVtagnastLNDGAAAVVLMSAEKAAALGARPLVRV---GAQAAAgidpkYVLVAPM-------LSIPKAC 300
Cdd:cd00834 218 RPFDKDRDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEIlgyGASSDA-----YHITAPDpdgegaaRAMRAAL 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503023139 301 AKAGIDPKDID---LH----ELNEafASSSLAVQRTLGLDPARINIYGGGISIGHPIGASGA 355
Cdd:cd00834 286 ADAGLSPEDIDyinAHgtstPLND--AAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAGA 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
29-120 |
1.75e-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: 43.16 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 29 LGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGQNPARQA---CLRAGLPVEVG------------------------- 80
Cdd:COG0304 74 YALAAAREALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEayrALLEKGPRRVSpffvpmmmpnmaaghvsirfglkgp 153
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 503023139 81 CITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTN 120
Cdd:COG0304 154 NYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
251-334 |
2.66e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 42.98 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 251 DGAAAVVLMSAEKAAALGARP--LVRVGAQAAAGiDPKYVLVAPML--------SIPKACAKAGIDPKDIDLHELNEAFA 320
Cdd:PRK08257 244 DQGAAVLLTSVAKARRLGVPEdrWVYLHGGADAH-DPYDILERPDLhrspairaAGRRALALAGLGIDDIDAFDLYSCFP 322
|
90
....*....|....
gi 503023139 321 SSSLAVQRTLGLDP 334
Cdd:PRK08257 323 SAVQVAARELGLDL 336
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
252-355 |
6.68e-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: 41.62 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 252 GAAAVVLMSAEKAAALGARPLVRVGAQAAAGiDPkYVLVAP-------MLSIPKACAKAGIDPKDID----------LHE 314
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGASS-DA-YHITAPapdgegaARAMRAALKDAGLSPEDIDyinahgtstpLGD 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 503023139 315 LNEAfasssLAVQRTLGLDPARINIYgggiS----IGHPIGASGA 355
Cdd:COG0304 310 AAET-----KAIKRVFGDHAYKVPVS----StksmTGHLLGAAGA 345
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
249-368 |
7.83e-04 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 41.31 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 249 LNDGAAAVVLMSAEKAAALGARPLVRV---GAQAAAgidpkYVLVAP-------MLSIPKACAKAGIDPKDID------- 311
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVvgyGMTGDA-----YHMTAPapdgegaARAMKLALKDAGINPEDIDyinahgt 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503023139 312 ---LHELNEAfasssLAVQRTLGLDPARINIYGGGISIGHPIGASGA--RVLTTLiyAMKDQ 368
Cdd:PRK07314 305 stpAGDKAET-----QAIKRVFGEHAYKVAVSSTKSMTGHLLGAAGAveAIFSVL--AIRDQ 359
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
25-114 |
2.11e-03 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 39.71 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 25 SALDLGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLGqnPArQACL---RAGLPvEVGCITVNKVCGSGLKAVMLAAQA 101
Cdd:COG0332 50 TTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLF--PS-TACLvqhKLGAK-NAAAFDINAACSGFVYALSVAAAL 125
|
90
....*....|....
gi 503023139 102 IACGDAE-VIVAGG 114
Cdd:COG0332 126 IRSGQAKnVLVVGA 139
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
1-332 |
2.15e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 39.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 1 MREVVITSACRTPVGAFRGAFaslsaLDLGVVVLNEAIARAGLAKDQVDEVIMG----CVLPAGLGQNPARQACLRAGLP 76
Cdd:PRK06059 3 PEPVYILGAGMHPWGKWGRDF-----VEYGVVAARAALADAGLDWRDVQLVVGAdtirNGYPGFVAGATFAQALGWNGAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 77 vevgCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTNApYLVPQarGGMRMGNgklvdsmvHDGLWDHL---- 152
Cdd:PRK06059 78 ----VSSSYAACASGSQALQSARAQILAGLCDVALVVGADTTPKG-FFAPV--GGERPDD--------PDWLRFHLigat 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 153 NDFHMGMSAELCAEKYGVSRQDQDQFAVESyAKSFEADAQGRFKAqiaPVSVAGRKGPTVVehdeglklSSPEALAALrp 232
Cdd:PRK06059 143 NPVYFALLARRRMDLYGATVEDFAQVKVKN-ARHGLLNPNARYRK---EVTVEDVLASPVV--------SDPLRLLDI-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 233 afkkdggtvtagnaSTLNDGAAAVVLMSAEKA--AALGARPLVRVGAQAAA--------------GIDPKYVLVAPMLS- 295
Cdd:PRK06059 209 --------------CATSDGAAALIVASKSFArrHLGSVAGVPSVRAISTVtprypqhlpelpdiATDSTAAVPAPERVf 274
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 503023139 296 ----IPKACAKAGIDPKDIDLHELNEAFASSSLAVQRTLGL 332
Cdd:PRK06059 275 kdqiLDAAYAEAGIGPEDLSLAEVYDLSTALELDWYEHLGL 315
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
80-117 |
2.82e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.39 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|....*...
gi 503023139 80 GCITVNKVCGSGLKAVMLAAQAIACGDAEVIVAGGMES 117
Cdd:PRK07314 154 PNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEA 191
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
228-368 |
3.17e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 39.33 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 228 AALRPAFKKDGGTVtagnastLNDGAAAVVLMSAEKAAALGARPLVRVgaqAAAGIDPK-YVLVAP-------MLSIPKA 299
Cdd:PRK07910 226 GACRPFDKDRDGFV-------FGEGGALMVIETEEHAKARGANILARI---MGASITSDgFHMVAPdpngeraGHAMTRA 295
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503023139 300 CAKAGIDPKDIDlHELNEAFASS------SLAVQRTLGLDpaRINIYGGGISIGHPIGASGA--RVLTTLiyAMKDQ 368
Cdd:PRK07910 296 IELAGLTPGDID-HVNAHATGTSvgdvaeGKAINNALGGH--RPAVYAPKSALGHSVGAVGAveSILTVL--ALRDG 367
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
29-262 |
3.82e-03 |
|
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: 39.16 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 29 LGVVVLNEAIARAGLAKDQVDEVIMGCVLPAGLG-----------------------QNPARQACLRAGLPVEVGCITVN 85
Cdd:cd00825 14 LGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGsprfqvfgadamravgpyvvtkaMFPGASGQIATPLGIHGPAYDVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 86 KVCGSGLKAVMLAAQAIACGDAEVIVAGGMESMTnAPYLVPQARGGMRMGNGKlvDSMVHDGLWDHLNDFHMGMSAELCA 165
Cdd:cd00825 94 AACAGSLHALSLAADAVQNGKQDIVLAGGSEELA-APMDCEFDAMGALSTPEK--ASRTFDAAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 166 EKYGVSRQDQDQFAVESYAKSFEADAQGRFK---AQIAPV-----SVAG-RKGPT--VVEHDEGLKLSSPEALAALRPAF 234
Cdd:cd00825 171 LEHALARGAHIYAEIVGTAATIDGAGMGAFApsaEGLARAakealAVAGlTVWDIdyLVAHGTGTPIGDVKELKLLRSEF 250
|
250 260
....*....|....*....|....*...
gi 503023139 235 KKDGGTVTAGNASTLNDGAAAVVLMSAE 262
Cdd:cd00825 251 GDKSPAVSATKAMTGNLSSAAVVLAVDE 278
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
296-368 |
8.42e-03 |
|
Beta-ketoacyl synthase, C-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.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 36.01 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503023139 296 IPKACAKAGIDPKDIDLhelNEAFASSSL--------AVQRTLGLDPARINIYGGGI--SIGHPIGASGARVLTTLIYAM 365
Cdd:pfam02801 30 IRRALADAGVDPEDVDY---VEAHGTGTPlgdpieaeALKRVFGSGARKQPLAIGSVksNIGHLEGAAGAAGLIKVVLAL 106
|
...
gi 503023139 366 KDQ 368
Cdd:pfam02801 107 RHG 109
|
|
| |
