|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
3-388 |
0e+00 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 552.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 3 EVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDCT 82
Cdd:PLN02644 2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 83 TVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHY-NLLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNAAE 161
Cdd:PLN02644 82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYlPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 162 MCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGE--TIVNNDEDIFKVIPEKVSKLNPVFVKN-GT 238
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGKFDPAKLRKLRPSFKEDgGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 239 ITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYA 318
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 319 AVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVE 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-389 |
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 500641576 5 YIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDCTTV 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 85 NKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNAAEMCV 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 165 EKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFK-VIPEKVSKLNPVFVKNGTITAAN 243
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPdTTLEKLAKLKPAFKKDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 244 ASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVLA 323
Cdd:cd00751 241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641576 324 NQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIEN 389
Cdd:cd00751 321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-390 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 526.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHynLLRKPV--KFGDANCIDGLLNDGLTDVYNNFHMGN 158
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPM--LLPKARwgYRMNAKLVDPMINPGLTDPYTGLSMGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 159 AAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFK-VIPEKVSKLNPVFVKNG 237
Cdd:COG0183 159 TAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPdTTLEKLAKLKPAFKKDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 238 TITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAY 317
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500641576 318 AAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-390 |
2.14e-166 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 471.17 E-value: 2.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHynLLRKP---VKFGDANCIDGLLNDGLTDVYNNFHMG 157
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPH--VLPGSrwgQKMGDVELVDTMIHDGLTDAFNGYHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 158 NAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETI-VNNDEDI-FKVIPEKVSKLNPVFVK 235
Cdd:PRK05790 159 ITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVvVDTDEHPrPDTTAESLAKLRPAFDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 236 NGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINE 315
Cdd:PRK05790 239 DGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINE 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500641576 316 AYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK05790 319 AFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-388 |
1.29e-162 |
|
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: 461.31 E-value: 1.29e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 6 IIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDCTTVN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 86 KVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHY--NLLRKPVKFGDANCIDGLLNDgLTDVYNNFHMGNAAEMC 163
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvpRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 164 VEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFK-VIPEKVSKLNPVFVKNGTITAA 242
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPnTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 243 NASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVL 322
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641576 323 ANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-388 |
5.28e-143 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 411.80 E-value: 5.28e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHY-NLLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNA 159
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYIlPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 160 AEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETI-VNNDEDIFK-VIPEKVSKLNPVFVKNG 237
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIvVAKDEAPRKdTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 238 TITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAY 317
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500641576 318 AAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-388 |
5.12e-129 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 376.54 E-value: 5.12e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHynLL---RKPVKFGDANCIDGLLNDGLTDVYNNFH-M 156
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPY--LLpkaRGGMRMGHGQVLDHMFLDGLEDAYDKGRlM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 157 GNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFKVIPEKVSKLNPVFVKN 236
Cdd:PRK06954 164 GTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 237 GTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEA 316
Cdd:PRK06954 244 GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500641576 317 YAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-388 |
3.05e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 343.53 E-value: 3.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHynLLRKPVKFGDANCI-------DGLLNDGLTDVYNN 153
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPF--LLPSDLRWGPKHLLhknykidDAMLVDGLIDAFYF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 154 FHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIkinhktgeTIVNNDEDIFKVIPEKVSKLNPVF 233
Cdd:PRK06366 159 EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF--------NDLDRDEGIRKTTMEDLAKLPPAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 234 VKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEI 313
Cdd:PRK06366 231 DKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEH 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500641576 314 NEAY--AAVVLANQkiLDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK06366 311 NEAFsiASIIVRDQ--LKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-390 |
3.08e-115 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 341.17 E-value: 3.08e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVL-----SANLgqspARQASIFAGI 75
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpteprDMYL----SRVAAINAGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 76 SENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNL-LRKPVKFGDANCIDGLLNdGLTDVYNNF 154
Cdd:PRK09051 78 PQETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPaARWGARMGDAKLVDMMVG-ALHDPFGTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 155 HMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDI-FKVIPEKVSKLNPVF 233
Cdd:PRK09051 157 HMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVrADTTLEDLAKLKPVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 234 VK-NGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFE 312
Cdd:PRK09051 237 KKeNGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500641576 313 INEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK09051 317 ANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.12e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 339.70 E-value: 1.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNAA 160
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 161 EMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFKVIP-EKVSKLNPVFVKNGTI 239
Cdd:PRK06633 162 ENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSlEILSKLRPAFDKNGVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 240 TAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAA 319
Cdd:PRK06633 242 TAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500641576 320 VVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK06633 322 QSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-388 |
4.17e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 325.69 E-value: 4.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPH-YNLLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNA 159
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYvLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 160 AEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIV--NNDEDIFKVIPEKVSKLNPVFVKNG 237
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAfaTDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 238 TITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAY 317
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500641576 318 AAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-388 |
2.23e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 297.77 E-value: 2.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNV-----LSANLgqspARQASIFAGI 75
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVdtigpQAGNI----ARTSWLAAGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 76 SENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGDANCIDGllNDGLTDVY---- 151
Cdd:PRK07801 77 PEEVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGFTSPFAE--SKGWLHRYgdqe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 152 -NNFHmgnAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKinhktgetIVNNDEDIFKVIPEKVSKLN 230
Cdd:PRK07801 155 vSQFR---GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVG--------GVTVDEGPRETSLEKMAGLK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 231 PVfVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDY 310
Cdd:PRK07801 224 PL-VEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDV 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500641576 311 FEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK07801 303 VEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-260 |
6.87e-98 |
|
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: 292.28 E-value: 6.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 4 VYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDCTT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 84 VNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYN--LLRKPVKFGDANCIDGLLNDGLTDVYNNFHMGNAAE 161
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALptDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 162 MCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDI-FKVIPEKVSKLNPVFVKNGTIT 240
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIrPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 500641576 241 AANASNLNDSAAALLLASKE 260
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.46e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 296.25 E-value: 1.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAE------FSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQS-PARQASIFA 73
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKDPQkdvfnnIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 74 GISENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYN---LLRKPVKFGDANCIDGLLNDGltdv 150
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDnphIEPNPKLLTDPKYIEYDLTTG---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 151 ynnFHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDIFKVIP-EKVSKL 229
Cdd:PRK06445 157 ---YVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSlEKLAKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 230 NPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDID 309
Cdd:PRK06445 234 PPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 310 YFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIEN 389
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLER 393
|
.
gi 500641576 390 I 390
Cdd:PRK06445 394 V 394
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.36e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 288.04 E-value: 2.36e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVlSANlGQSPA--RQASIFAGISEN 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQG-YPN-GEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 79 TDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNL-LRKPVKFGDANCIDGLLNDGLTDVYNNF--- 154
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDRLARGRETAGGRRFpvp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 155 -HMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGE-TIVNNDEDI-FKVIPEKVSKLNP 231
Cdd:PRK06205 159 gGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPrADTTLESLAKLRP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 232 VFVK---NGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDI 308
Cdd:PRK06205 239 IMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 309 DYFEINEAYAAVVLA---NQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAI 385
Cdd:PRK06205 319 DLIELNEAFAAQVLAvlkEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAA 398
|
....*.
gi 500641576 386 IIENIN 391
Cdd:PRK06205 399 VFERVN 404
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-390 |
2.46e-92 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 283.00 E-value: 2.46e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQ-SVGIDPNAICSVYMGnvlSANLG----QSPARQASIFAGI 75
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYG---CANQAgednRNVARMSALLAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 76 SENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhYNLLRKPVKFG-DANCIDG-----LLNDGLTD 149
Cdd:PRK09050 78 PVSVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAP-FVMGKADSAFSrQAEIFDTtigwrFVNPLMKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 150 VYNNFHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGE-TIVNNDEDI-FKVIPEKVS 227
Cdd:PRK09050 157 QYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPrPETTLEALA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 228 KLNPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLND 307
Cdd:PRK09050 237 KLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 308 IDYFEINEAYAAVVLANQKILDL--DSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAI 385
Cdd:PRK09050 317 FDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIAL 396
|
....*
gi 500641576 386 IIENI 390
Cdd:PRK09050 397 AIERV 401
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-388 |
1.32e-91 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 281.12 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG----GFLGNLaefSATQLGAIAIKEAYQSV-GIDPNAICSVYMGNVL-SANLGQSPARQASIFAG 74
Cdd:PRK09052 5 LQDAYIVAATRTPVGkaprGMFKNT---RPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 75 ISENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhynllrkpvKFGDANCIDGLLNDGLTDVYNNF 154
Cdd:PRK09052 82 LPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP---------MMGNKPSMSPAIFARDENVGIAY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 155 HMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKI-----NHKTGET-----IVNNDE----Difk 220
Cdd:PRK09052 153 GMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEIterfpDLATGEVdvktrTVDLDEgpraD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 221 VIPEKVSKLNPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQ 300
Cdd:PRK09052 230 TSLEGLAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 301 AKLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGG 380
Cdd:PRK09052 310 AGLKQDDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTG 389
|
....*...
gi 500641576 381 GASAIIIE 388
Cdd:PRK09052 390 MGAAGIFE 397
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-388 |
1.38e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 273.14 E-value: 1.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSAnlGQSP---ARQASIFAGISE 77
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQV--GEQAtnvARNAVLASKLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 78 NTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGDANcidgLLNDGLTDVYNN--FH 155
Cdd:PRK06504 79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGH----YKSPGMEERYPGiqFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 156 MGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNN-DEDI-FKVIPEKVSKLNPVf 233
Cdd:PRK06504 155 QFTGAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTvDEGIrFDATLEGIAGVKLI- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 234 VKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEI 313
Cdd:PRK06504 234 AEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEV 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500641576 314 NEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK06504 314 NEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-388 |
4.31e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 271.62 E-value: 4.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG-GFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVL-SANLGQSPARQASIFAGISEN 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 79 TDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPvkfgdancidgllNDGLTDVYNNFHM-- 156
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHVVRP-------------NPRLVEAAPEYYMgm 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 157 GNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKI-------NHKTGET--IVNNDEDI-FKVIPEKV 226
Cdd:PRK07661 148 GHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVtlrtvgeNNKLQEEtiTFSQDEGVrADTTLEIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 227 SKLNPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLN 306
Cdd:PRK07661 228 GKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 307 DIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAII 386
Cdd:PRK07661 308 DIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGV 387
|
..
gi 500641576 387 IE 388
Cdd:PRK07661 388 FE 389
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-390 |
5.08e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 264.05 E-value: 5.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFL--GNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLS-ANLGQSPARQASIFAGISE 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPvGDQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 78 NTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhynllrkpvkFGDanciDG--LLNDGLTDVYNNF- 154
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP----------MGS----DGgaWAMDPSTNFPTYFv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 155 HMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIK-INhktGETIVNNDEDIFK-VIPEKVSKLNPV 232
Cdd:PRK08242 147 PQGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKdQN---GLTILDHDEHMRPgTTMESLAKLKPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 233 FVKNGTI---------------------TAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPS 291
Cdd:PRK08242 224 FAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 292 IAITKALKQAKLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYG 371
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTA 383
|
410
....*....|....*....
gi 500641576 372 VASICNGGGGASAIIIENI 390
Cdd:PRK08242 384 LITLCVGGGMGIATIIERV 402
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
4-390 |
1.27e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 258.79 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 4 VYIIAAKRTPiggFL---GNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTD 80
Cdd:PRK08170 5 VYIVDGARTP---FLkarGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 81 CTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhynLL--RKPVK-FGDANCIDGL--------------- 142
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAP---LLfsEKMVRwLAGWYAAKSIgqklaalgklrpsyl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 143 -----LNDGLTDVYNNFHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFtNEIIPIkinHKTGETIVNNDED 217
Cdd:PRK08170 159 apvigLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPL---FDRDGKFYDHDDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 218 IFK-VIPEKVSKLNPVF-VKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAIT 295
Cdd:PRK08170 235 VRPdSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 296 KALKQAKLSLNDIDYFEINEAYAAVVLANQKILD-----------------LDSKKINIYGGAVAMGHPLGASGARIICT 358
Cdd:PRK08170 315 PLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgalgeLDRERLNVDGGAIALGHPVGASGARIVLH 394
|
410 420 430
....*....|....*....|....*....|..
gi 500641576 359 LISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK08170 395 LLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-390 |
2.81e-82 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 256.43 E-value: 2.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG----GFLGNL-AE-FSATQLGAIAIKEAyqsvGIDPNAICSVYMGNVL-SANLGQSPARQASIFA 73
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrskgGAFRNVrAEdLSAHLMRSLLARNP----ALDPAEIDDIIWGCVQqTLEQGFNIARNAALLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 74 GISENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhynllrkpvkfgdancidglLNDGLtdvynN 153
Cdd:PRK08947 77 GIPHSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP--------------------MNHGV-----D 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 154 FH-------------MGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGE-TIVNNDEDI- 218
Cdd:PRK08947 132 FHpglsknvakaagmMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVlKLFDYDEVIr 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 219 FKVIPEKVSKLNPVFV-KNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKA 297
Cdd:PRK08947 212 PETTVEALAALRPAFDpVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 298 LKQAKLSLNDIDYFEINEAYAA---VVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVAS 374
Cdd:PRK08947 292 LKRAGLSISDIDVFELNEAFAAqslPCLKDLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLAT 371
|
410
....*....|....*.
gi 500641576 375 ICNGGGGASAIIIENI 390
Cdd:PRK08947 372 MCIGLGQGIATVFERV 387
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-386 |
3.23e-82 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 258.54 E-value: 3.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 2 NEVYIIAAKRTPI-----GGFLGNLAEfsatQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQ-SPARQASIFAGI 75
Cdd:PLN02287 46 DDVVIVAAYRTPIckakrGGFKDTYPD----DLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 76 SENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGD-ANCIDGLLNDGLTdvynnf 154
Cdd:PLN02287 122 PETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESfSQAQDCLLPMGIT------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 155 hmgnaAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIK---INHKTGE---TIVNNDEDIF-KVIPEKVS 227
Cdd:PLN02287 196 -----SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHtkiVDPKTGEekpIVISVDDGIRpNTTLADLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 228 KLNPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLND 307
Cdd:PLN02287 271 KLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDD 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 308 IDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEG--GKYGVASICNGGG-GASA 384
Cdd:PLN02287 351 IDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGmGAAA 430
|
..
gi 500641576 385 II 386
Cdd:PLN02287 431 VF 432
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-390 |
1.09e-78 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 247.77 E-value: 1.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANL-GQSPARQASIFAGISENT 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 80 DCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhYNLLRKPVKFG-DANCIDGLL-----NDGLTDVYNN 153
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAP-FVMGKAESAFSrDAKVFDTTIgarfpNPKIVAQYGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 154 FHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINH--KTGETIVNNDEDifkviP------EK 225
Cdd:PRK08131 160 DSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEH-----PrpsstvEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 226 VSKLNPVFvKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSL 305
Cdd:PRK08131 235 LTKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 306 NDIDYFEINEAYAAVVLANQKILDL--DSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGAS 383
Cdd:PRK08131 314 DDMDIIEINEAFASQVLGCLKGLGVdfDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGL 393
|
....*..
gi 500641576 384 AIIIENI 390
Cdd:PRK08131 394 AMVIERV 400
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-391 |
8.28e-76 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 240.68 E-value: 8.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG-GFLGNLAEFSATQLGAIAIKEAYQSV-GIDPNAICSVYMGNVLSA-NLGQSPARQASIFAGIsE 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGgEQGFNMARVVAVLLGY-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 78 NTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNL-----LRKPVkFGDANC-------------I 139
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSdslpdTKNPL-FAEAQArtaaraeggaeawH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 140 DGLLNDGLTDVYnnFHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKInhKTGETIVNNDEDIF 219
Cdd:PRK07851 159 DPREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTL--PDGTVVSTDDGPRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 220 KVIPEKVSKLNPVFVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALK 299
Cdd:PRK07851 235 GTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 300 QAKLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGG 379
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|..
gi 500641576 380 GGASAIIIENIN 391
Cdd:PRK07851 395 GQGMAMVLERLS 406
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-390 |
1.73e-73 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 233.85 E-value: 1.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANlGQS--PARQASIFAGISEN 78
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAG-EQSnnITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 79 TDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPhynlLRKPVKFGdancidglLNDGLTDVYNnFHMGN 158
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP----LGANAGPG--------RGLPRPDSWD-IDMPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 159 ---AAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPI------KINHKTGET-IVNNDEDIFKVIPEKVSK 228
Cdd:PRK07850 147 qfeAAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVqapvldEEGQPTGETrLVTRDQGLRDTTMEGLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 229 LNPVfVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDI 308
Cdd:PRK07850 227 LKPV-LEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 309 DYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK07850 306 DLVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
..
gi 500641576 389 NI 390
Cdd:PRK07850 386 RI 387
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
2-390 |
4.03e-72 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 229.65 E-value: 4.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 2 NEVYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKeaYQSVGIDPnAICSVYMGNVLSAnlGQSPARQASIFAGISENTDC 81
Cdd:PRK06690 1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLT--FLSKGMER-EIDDVILGNVVGP--GGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 82 TTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLR-KPVKFGDANcidgllndgltdvynnfhMGNAA 160
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGDPD------------------MGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 161 EMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIkinhktgetivNN--DEDIFKVIP-EK-VSKLNPVFVKN 236
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-----------NGllDESIKKEMNyERiIKRTKPAFLHN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 237 GTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEA 316
Cdd:PRK06690 207 GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEA 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500641576 317 YAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK06690 287 FASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-388 |
4.65e-65 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 212.32 E-value: 4.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG-GFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGnvlSAN----LGQSPARQASIFAGI 75
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMG---CANpegaTGANIARQIALRAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 76 SENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMS---NVPHYNLLRkpvkfgdanciDGLLNDGLTDVYN 152
Cdd:PRK07108 78 PVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESIScvqNEMNRHMLR-----------EGWLVEHKPEIYW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 153 NfhMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKI-----NHKTG-----ETIVNNDEDIFK-V 221
Cdd:PRK07108 147 S--MLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVtagvaDKATGrlftkEVTVSADEGIRPdT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 222 IPEKVSKLNPVfVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEWFTTAPSIAITKALKQA 301
Cdd:PRK07108 225 TLEGVSKIRSA-LPGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 302 KLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGG 381
Cdd:PRK07108 304 GLKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQ 383
|
....*..
gi 500641576 382 ASAIIIE 388
Cdd:PRK07108 384 GAAGLFE 390
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-388 |
1.46e-64 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 212.15 E-value: 1.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 4 VYIIAAKRTPIGGFLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLsanlgQSP-----ARQASIFAGISEN 78
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVV-----QMPeapniAREIVLGTGMNVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 79 TDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVP---HYNLLRKPVKFGDA-------NCIDGL-LND-- 145
Cdd:PRK08963 82 TDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvSKKLARALVDLNKArtlgqrlKLFSRLrLRDll 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 146 -----------GLTdvynnfhMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINhKTGETIVNN 214
Cdd:PRK08963 162 pvppavaeystGLR-------MGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVP-PYKQPLEED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 215 DEDIFKVIPEKVSKLNPVF-VKNGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAPEW-FTTAPSI 292
Cdd:PRK08963 234 NNIRGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdMLLGPAY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 293 AITKALKQAKLSLNDIDYFEINEAYAAVVLANQKIL-----------------DLDSKKINIYGGAVAMGHPLGASGARI 355
Cdd:PRK08963 314 ATPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARM 393
|
410 420 430
....*....|....*....|....*....|...
gi 500641576 356 ICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK08963 394 ITQTLHELRRRGGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-390 |
1.95e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 211.56 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIG-GFLGN--LAEFSATQLGAIAIKEAYQSVGIDPNAI------CSVYMGNvLSANLGqspaRQASI 71
Cdd:PRK06025 1 MAEAYIIDAVRTPRGiGKVGKgaLAHLHPQHLAATVLKALAERNGLNTADVddiiwsTSSQRGK-QGGDLG----RMAAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 72 FAGISENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMS-----NVPHYNLLRKPVKFGDANcidgllnDG 146
Cdd:PRK06025 76 DAGYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytaamAAEDMAAGKPPLGMGSGN-------LR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 147 LTDVYNNFHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKinHKTGETIVNNDEdiF---KVIP 223
Cdd:PRK06025 149 LRALHPQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVY--RDDGSVALDHEE--FprpQTTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 224 EKVSKLNPVF-------VKNGTIT-------------------AANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYA 277
Cdd:PRK06025 225 EGLAALKPAFtaiadypLDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 278 DAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGHPLGASGARIIC 357
Cdd:PRK06025 305 NMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIG 384
|
410 420 430
....*....|....*....|....*....|...
gi 500641576 358 TLISVLKQEGGKYGVASICNGGGGASAIIIENI 390
Cdd:PRK06025 385 TVLDELERRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-388 |
4.28e-58 |
|
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: 194.25 E-value: 4.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 7 IAAKRTPIGGFLGNLAEFS---ATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDCTT 83
Cdd:cd00826 1 AGAAMTAFGKFGGENGADAndlAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 84 VNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPvkfgdancIDGLLNdgltdvynnfhmgnaaemc 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNAKEKH--------IDVLIN------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 164 veKYNLtREQQDEYALSSYAKAVKATNEGKFTNEIIPIKINHKTGETIVNNDEDI---FKVIPEKVSKLNPVFVKNGTIT 240
Cdd:cd00826 134 --KYGM-RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIqfgDEASLDEIAKLRPAFDKEDFLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 241 AANASNLNDSAAALLLASKEAVEKYNLK-------PLAKIISYADAAQAPEWFT----TAPSIAITKALKQAKLSLNDID 309
Cdd:cd00826 211 AGNACGLNDGAAAAILMSEAEAQKHGLQskareiqALEMITDMASTFEDKKVIKmvggDGPIEAARKALEKAGLGIGDLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 310 YFEINEAYAAVVLANQKILDLDSKK------------------INIYGGAVAMGHPLGASGARIICTLISVLKQEGGKY- 370
Cdd:cd00826 291 LIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRq 370
|
410 420
....*....|....*....|..
gi 500641576 371 ----GVASICNGGGGASAIIIE 388
Cdd:cd00826 371 gagaGLALLCIGGGGGAAMCIE 392
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
267-388 |
4.46e-57 |
|
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: 182.46 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 267 LKPLAKIISYADAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVLANQKILDLDSKKINIYGGAVAMGH 346
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 500641576 347 PLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
66-388 |
2.57e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 169.31 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 66 ARQASIFAGISENTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVP---HYNLLRKPVKFGDANCIDGL 142
Cdd:PRK09268 71 TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavNEGLRKILLELNRAKTTGDR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 143 L--------NDGLTDVYNN------FHMGNAAEMCVEKYNLTREQQDEYALSSYAKAVKATNEGKFTNEIIPIKinhktG 208
Cdd:PRK09268 151 LkalgklrpKHLAPEIPRNgeprtgLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFL-----G 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 209 ETIVNN---DEDifkviPEKVSKLNPVFVK--NGTITAANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAA--- 280
Cdd:PRK09268 226 LTRDNNlrpDSS-----LEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAvdf 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 281 -QAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVLANQKI------------LD-----LDSKKINIYGGAV 342
Cdd:PRK09268 301 vHGKEGLLMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAwedeeycrerlgLDaplgsIDRSKLNVNGSSL 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 500641576 343 AMGHPLGASGARIICTLISVLKQEGGKYGVASICNGGGGASAIIIE 388
Cdd:PRK09268 381 AAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILE 426
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
28-387 |
2.22e-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: 105.81 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 28 QLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISeNTDCTTVNKVCAAGMKATILGAQQIQLGLE 107
Cdd:cd00829 18 ELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAAAAAIASGLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 108 DLVITGGMESMSNVPHYNLLRKpvKFGDANCIDGLLNDGLT--DVYNNF---HMgnaaemcvEKYNLTREQqdeyalssY 182
Cdd:cd00829 97 DVVLVVGAEKMSDVPTGDEAGG--RASDLEWEGPEPPGGLTppALYALAarrYM--------HRYGTTRED--------L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 183 AK-AVKatnegkftneiipikiNHKTGetiVNNDEDIFK--VIPEKVSKLNPVfvkNGTITAANASNLNDSAAALLLASK 259
Cdd:cd00829 159 AKvAVK----------------NHRNA---ARNPYAQFRkpITVEDVLNSRMI---ADPLRLLDCCPVSDGAAAVVLASE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 260 EAVEKYNLKPlAKIISYADAA-----QAPEWFTTAPSI--AITKALKQAKLSLNDIDYFEINEAYAAVVL---------- 322
Cdd:cd00829 217 ERARELTDRP-VWILGVGAASdtpslSERDDFLSLDAArlAARRAYKMAGITPDDIDVAELYDCFTIAELlaledlgfce 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500641576 323 ---ANQKILDLDSKK-----INIYGGAVAMGHPLGASGARIICTLISVLKQEGGKYGVAS-----ICNGGGGASAIII 387
Cdd:cd00829 296 kgeGGKLVREGDTAIggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGarvglAHNIGGTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-386 |
1.56e-19 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 89.19 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPIGgflgNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVLSANL-GQS-PARQASIFAGISeN 78
Cdd:PRK06064 1 MRDVAIIGVGQTKFG----ELWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLFvSQEhIAALIADYAGLA-P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 79 TDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHYNLLRKPVKFGDA--NCIDGLLNDGLTDVYNNFHM 156
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAGDYewEEFFGATFPGLYALIARRYM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 157 gnaaemcvEKYNLTREQQDEYALSSYAKAVKATNeGKFTNEIipikinhkTGETIVNND--EDIFKVIpekvsklnpvfv 234
Cdd:PRK06064 156 --------HKYGTTEEDLALVAVKNHYNGSKNPY-AQFQKEI--------TVEQVLNSPpvADPLKLL------------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 235 kngtitaaNASNLNDSAAALLLASKEAVEKYNLKPLaKIISYADAAQAP-----EWFTT--APSIAITKALKQAKLSLND 307
Cdd:PRK06064 207 --------DCSPITDGAAAVILASEEKAKEYTDTPV-WIKASGQASDTIalhdrKDFTTldAAVVAAEKAYKMAGIEPKD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 308 IDYFEINEAYA-----------------AVVLANQKILDLDSK-KINIYGGAVAMGHPLGASGARIICTLISVLKQEGGK 369
Cdd:PRK06064 278 IDVAEVHDCFTiaeilayedlgfakkgeGGKLAREGQTYIGGDiPVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEK 357
|
410 420
....*....|....*....|....*
gi 500641576 370 YGVASICN--------GGGGASAII 386
Cdd:PRK06064 358 GRQQVIGAgyglthnvGGTGHTAVV 382
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
241-387 |
1.24e-15 |
|
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: 75.94 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 241 AANASNLNDSAAALLLASKEAVEKYNLKPLAKIISYADAAQAP-EWFT---TAPSIAITKALKQAKLSLNDIDYFEINEA 316
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGAsMVPAvsgEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 317 YAAVVLANQKILDLDS---KKINIYGGAVAMGHPLGASGARIICTLISVLKQEGGKY-------GVASICNGGGGASAII 386
Cdd:cd00327 174 GTPIGDAVELALGLDPdgvRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtpreprtVLLLGFGLGGTNAAVV 253
|
.
gi 500641576 387 I 387
Cdd:cd00327 254 L 254
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
33-369 |
1.26e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 65.64 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 33 AIKEAYQSVGIDPNAICSVYMGNVLSANLGQSPARQASIFAGISENTDcTTVNKVCAAGMKATILGAQQIQLGLEDLVIT 112
Cdd:PRK12578 28 SIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 113 GGMESMSNVPHYNLLRKPVKFGDancidgllndgltdVYNNFHMgnaaemcvekYNLTREQQdeYALSSYAK-AVKATNE 191
Cdd:PRK12578 107 VGVDKMTEVDTSTSLAIGGRGGN--------------YQWEYHF----------YGTTFPTY--YALYATRHmAVYGTTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 192 GKFTneIIPIKiNHKTGETivnNDEDIF--KVIPEKVSKLNpvfVKNGTITAANASNLNDSAAALLLASKEAVEKYNLKP 269
Cdd:PRK12578 161 EQMA--LVSVK-AHKYGAM---NPKAHFqkPVTVEEVLKSR---AISWPIKLLDSCPISDGSATAIFASEEKVKELKIDS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 270 LAKIIS------YADAAQAPEWFT-TAPSIAITKALKQAKLSLNDIDYFEINEAYA-AVVLANQK------------ILD 329
Cdd:PRK12578 232 PVWITGigyandYAYVARRGEWVGfKATQLAARQAYNMAKVTPNDIEVATVHDAFTiAEIMGYEDlgftekgkggkfIEE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 500641576 330 LDSKK-----INIYGGAVAMGHPLGASGARIICTLISVLKQEGGK 369
Cdd:PRK12578 312 GQSEKggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGK 356
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-352 |
1.21e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 56.49 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 1 MNEVYIIAAKRTPiggfLGNLAEFSATQLGAIAIKEAYQSVGIDPNAICSVYMGNVlsaNLGQSP-ARQASIFAGISE-- 77
Cdd:PRK07516 1 MMTASIVGWAHTP----FGKLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHF---NAGFSPqDFPASLVLQADPal 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 78 -NTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSNVPHY----NLLRKPVKFGDANcIDGllndGLTDVYn 152
Cdd:PRK07516 74 rFKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTAevgdILLGASYLKEEGD-TPG----GFAGVF- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 153 nfhmGNAAEMCVEKYnltREQQDEYAlssyAKAVKatnegkftneiipikiNHKTGetiVNN---------DEDIFKVIP 223
Cdd:PRK07516 148 ----GRIAQAYFQRY---GDQSDALA----MIAAK----------------NHANG---VANpyaqmrkdlGFEFCRTVS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 224 EKvsklNPVFVknGTITAANASNLNDSAAALLLASKEAVEKynlkpLAKIISYADAAQAPEWFT---------TAPSIAI 294
Cdd:PRK07516 198 EK----NPLVA--GPLRRTDCSLVSDGAAALVLADAETARA-----LQRAVRFRARAHVNDFLPlsrrdplafEGPRRAW 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641576 295 TKALKQAKLSLNDIDY------FEINE--AYAAVVLA-----NQKILDLDSKK-----INIYGGAVAMGHPLGASG 352
Cdd:PRK07516 267 QRALAQAGVTLDDLSFvethdcFTIAEliEYEAMGLAppgqgARAIREGWTAKdgklpVNPSGGLKAKGHPIGATG 342
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
230-390 |
3.93e-07 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 51.82 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 230 NPVFVKNGTIT----AANASNLNDSAAALLLASKEAVEKYNLKP----LAKIIS--------YADAAQAPEWFTTapSIA 293
Cdd:PTZ00455 237 NPKFLGNETYKpflrMTDCSQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSlacasgnlYEDPPDATRMFTS--RAA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 294 ITKALKQAKLSLNDIDYFEINEAYA-AVVLANQKI----------------LDLDSK-KINIYGGAVAMGHPLGASGARI 355
Cdd:PTZ00455 315 AQKALSMAGVKPSDLQVAEVHDCFTiAELLMYEALgiaeyghakdlirngaTALEGRiPVNTGGGLLSFGHPVGATGVKQ 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500641576 356 ICTLISVLKQEGGKY------GVASICNGGGG---ASAIIIENI 390
Cdd:PTZ00455 395 IMEVYRQMKGQCGEYqmknipALGATLNMGGDdktAVSTVLQNI 438
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
229-371 |
1.87e-06 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 49.69 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 229 LNPVFvkNGTITAANASNLNDSAAALLLASKEAVEKY-NLKPLAKI---------ISYAD----AAQAPEWFttaPSI-- 292
Cdd:PRK06289 206 TNPVV--EGRLRRQDCSQVTDGGAGVVLASDAYLRDYaDARPIPRIkgwghrtapLGLEQkldrSAGDPYVL---PHVrq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 293 AITKALKQAKLSLNDIDYFEINEA-----YAAV------------VLANQKILDLDSKK-INIYGGAVAMGHPLGASGAR 354
Cdd:PRK06289 281 AVLDAYRRAGVGLDDLDGFEVHDCftpseYLAIdhigltgpgeswKAIENGEIAIGGRLpINPSGGLIGGGHPVGASGVR 360
|
170
....*....|....*..
gi 500641576 355 IictLISVLKQEGGKYG 371
Cdd:PRK06289 361 M---LLDAAKQVTGTAG 374
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
247-353 |
9.00e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 47.35 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 247 LNDSAAALLLASKEAVEKYNLKPLAKIISY---ADA--AQAPEWFTTAPSIAITKALKQAKLSLNDIDYF-------EIN 314
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFgltCDAyhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLN 287
|
90 100 110
....*....|....*....|....*....|....*....
gi 500641576 315 EAYAAVVLANqkildLDSKKINIYGGAVAMGHPLGASGA 353
Cdd:PRK05952 288 DQREANLIQA-----LFPHRVAVSSTKGATGHTLGASGA 321
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
246-353 |
3.25e-05 |
|
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: 45.61 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 246 NLNDSAAALLLASKEAVEKYNLKPLAKIISYA---DAAQApewftTAPSI-------AITKALKQAKLSLNDIDYfeIN- 314
Cdd:cd00834 228 VLGEGAGVLVLESLEHAKARGAKIYAEILGYGassDAYHI-----TAPDPdgegaarAMRAALADAGLSPEDIDY--INa 300
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 500641576 315 -------------EAYAAVVLANQKILDLDSKKiniyggavAM-GHPLGASGA 353
Cdd:cd00834 301 hgtstplndaaesKAIKRVFGEHAKKVPVSSTK--------SMtGHLLGAAGA 345
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
245-356 |
7.33e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 44.63 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 245 SNLNDSAAALLLASKEAVEKYNLKPLAKI------ISYADAAQAPEW-FTTAP--SIAITKALKQA-------KLSLNDI 308
Cdd:PRK06157 214 CGVSDGAAAAIVTTPEIARALGKKDPVYVkalqlaVSNGWELQYNGWdGSYFPttRIAARKAYREAgitdpreELSMAEV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500641576 309 -DYFEINEayaaVVL-----------ANQKIL----DLDSK-KINIYGGAVAMGHPLGASGARII 356
Cdd:PRK06157 294 hDCFSITE----LVTmedlglsergqAWRDVLdgffDADGGlPCQIDGGLKCFGHPIGASGLRML 354
|
|
| PRK06066 |
PRK06066 |
thiolase domain-containing protein; |
249-369 |
1.02e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 180380 [Multi-domain] Cd Length: 385 Bit Score: 43.97 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 249 DSAAALLLASKEAVEKYNLKPL-AKIISYADAAQAPEW--FTTAPS--IAITKALKQAKLS--LNDIDYFEINEAYA--- 318
Cdd:PRK06066 212 DGAIVVVLASEEVAKKLTDDPVwIKGIGWSTESSNLETaeLGKANYmrIAADMAYKMAGIEspRKEVDAAEVDDRYSyke 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500641576 319 -----AVVLANQKI---------LDLDSKK-INIYGGAVAMGHPLGASGARIICTLISVLKQEGGK 369
Cdd:PRK06066 292 lqhieALRLSEEPEkdsllregnFDPQGELpVNPSGGHLAKGVPLEASGLSLLLDAVEYLRGEAGA 357
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
251-353 |
3.11e-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: 42.39 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 251 AAALLLASKEAVEKYNLKPLAKIISYA---DA----AQAPEwfTTAPSIAITKALKQAKLSLNDIDYfeIN--------- 314
Cdd:COG0304 233 AGVLVLEELEHAKARGAKIYAEVVGYGassDAyhitAPAPD--GEGAARAMRAALKDAGLSPEDIDY--INahgtstplg 308
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 500641576 315 ---EAyAAVvlanQKILDLDSKKINIYGGAVAMGHPLGASGA 353
Cdd:COG0304 309 daaET-KAI----KRVFGDHAYKVPVSSTKSMTGHLLGAAGA 345
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
26-120 |
1.31e-03 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 40.60 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 26 ATQLGAIAIKEAYQSVGIDPNAI----CSVYMG-------------NVLSANLGQ-------------SPARQASIFAGI 75
Cdd:cd00834 71 FAQFALAAAEEALADAGLDPEELdperIGVVIGsgigglatieeayRALLEKGPRrvspffvpmalpnMAAGQVAIRLGL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500641576 76 SenTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSN 120
Cdd:cd00834 151 R--GPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
26-120 |
2.47e-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: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 26 ATQLGAIAIKEAYQSVGIDPNAI----CSVYMGN-------------VLSAN-------------LGQSPARQASIFAGI 75
Cdd:COG0304 71 FTQYALAAAREALADAGLDLDEVdpdrTGVIIGSgiggldtleeayrALLEKgprrvspffvpmmMPNMAAGHVSIRFGL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500641576 76 seNTDCTTVNKVCAAGMKATILGAQQIQLGLEDLVITGGMESMSN 120
Cdd:COG0304 151 --KGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
288-364 |
3.14e-03 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 39.46 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 288 TAPS-----IAITKALKQAKLSLNDIDYFE----------------INEAYAAVVLANQKILdLDSKKINIyggavamGH 346
Cdd:cd00833 274 TAPSgeaqaALIRRAYARAGVDPSDIDYVEahgtgtplgdpieveaLAKVFGGSRSADQPLL-IGSVKSNI-------GH 345
|
90
....*....|....*...
gi 500641576 347 PLGASGariictLISVLK 364
Cdd:cd00833 346 LEAAAG------LAGLIK 357
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
249-367 |
3.29e-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: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 249 DSAAALLLASKEAVEKYNLKPLAKIISYA-----DAAQAPEWFTTAPSIAITKALKQAKLSLNDIDYFEINEAYAAVVLA 323
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 500641576 324 NQKILDLDS---KKINIYGGAVAMGHPLGASGARIICTLISVLKQEG 367
Cdd:cd00825 241 KELKLLRSEfgdKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGF 287
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
270-365 |
6.81e-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: 36.39 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 270 LAKIISYADAAQAPEWFTTAPSI-----AITKALKQAKLSLNDIDYFE-----INEAYAAVVLANQKILDLDSKKINIYG 339
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGegqarAIRRALADAGVDPEDVDYVEahgtgTPLGDPIEAEALKRVFGSGARKQPLAI 80
|
90 100
....*....|....*....|....*...
gi 500641576 340 GAV--AMGHPLGASGariICTLISVLKQ 365
Cdd:pfam02801 81 GSVksNIGHLEGAAG---AAGLIKVVLA 105
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
247-353 |
8.15e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 38.23 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500641576 247 LNDSAAALLLASKEAVEKYNLKPLAKIISYA---DAaqapeWFTTAPS-------IAITKALKQAKLSLNDIDYfeINeA 316
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGmtgDA-----YHMTAPApdgegaaRAMKLALKDAGINPEDIDY--IN-A 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500641576 317 YAAVVLANQKI--------LDLDSKKINIYGGAVAMGHPLGASGA 353
Cdd:PRK07314 302 HGTSTPAGDKAetqaikrvFGEHAYKVAVSSTKSMTGHLLGAAGA 346
|
|
| |
