|
Name |
Accession |
Description |
Interval |
E-value |
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
6-393 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 538.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMgHNEVKDHMFLDGLEDADTGKLMGQFAQE 165
Cdd:COG0183 84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETAEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 166 MADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKEGSITA 244
Cdd:COG0183 163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPrPDTTLEKLAKLKPAFKKDGTVTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 245 ANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVT 324
Cdd:COG0183 243 GNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494637755 325 MAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIELP 393
Cdd:COG0183 323 LAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
7-391 |
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: 525.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVTI 86
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVkDHMFLDGLEDADTGKLMGQFAQEM 166
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 167 ADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKEGSITAA 245
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPrPDTTLEKLAKLKPAFKKDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 246 NASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTM 325
Cdd:cd00751 240 NASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494637755 326 AAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:cd00751 320 ACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-392 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 525.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 1 MSSDSVVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDS 80
Cdd:PRK06954 4 VDQDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 81 TGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMFLDGLEDA-DTGKLM 159
Cdd:PRK06954 84 VGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAyDKGRLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 160 GQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQPAKANAERIPLLRPAFAKE 239
Cdd:PRK06954 164 GTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFKANPEKIPTLKPAFSKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 240 GSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEA 319
Cdd:PRK06954 244 GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494637755 320 FAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIEL 392
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIEL 396
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
4-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 508.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 4 DSVVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGA 83
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMFLDGLEDADTGKLMGQFA 163
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 164 QEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQP-AKANAERIPLLRPAFAKEGS 241
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPrPDTTAESLAKLRPAFDKDGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 242 ITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFA 321
Cdd:PRK05790 242 VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494637755 322 MVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIELP 393
Cdd:PRK05790 322 AQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
6-392 |
5.95e-160 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 454.94 E-value: 5.95e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMFLDGLEDADTGKLMGQFAQE 165
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 166 MADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD--VVVESDEQPAKANAERIPLLRPAFAKE-GSI 242
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGKFDPAKLRKLRPSFKEDgGSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 243 TAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAM 322
Cdd:PLN02644 243 TAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFSV 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 323 VTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIEL 392
Cdd:PLN02644 323 VALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
8-391 |
3.70e-152 |
|
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: 434.73 E-value: 3.70e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVTIN 87
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 88 KLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQA-RNGYRMGHNEVKDHMFLDgLEDADTGKLMGQFAQEM 166
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSlRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 167 ADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKEGSITAA 245
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIrPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 246 NASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTM 325
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494637755 326 AAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
7-393 |
2.58e-145 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 417.96 E-value: 2.58e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVTI 86
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMFLDGLEDADTGKLMGQFAQEM 166
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 167 ADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQPAK-ANAERIPLLRPAFAKEGSITA 244
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDpIVVAKDEAPRKdTTIEKLAKLKPVFDKTGTITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 245 ANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVT 324
Cdd:PRK08235 245 GNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVA 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494637755 325 MAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIELP 393
Cdd:PRK08235 325 LASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
6-393 |
2.25e-129 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 377.31 E-value: 2.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMFLDGLEDADTGKLMGQFAQE 165
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 166 MADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQP-AKANAERIPLLRPAFAKEGSIT 243
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEpLAFATDEQPrAGTTAESLAKLKPAFKKDGSVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 244 AANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMV 323
Cdd:PRK05656 244 AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQ 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 324 TMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIELP 393
Cdd:PRK05656 324 SLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIERD 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
2-391 |
9.07e-119 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 350.41 E-value: 9.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 2 SSDSVVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMG-CILTAGVKQGPARQAMRNAGIPDS 80
Cdd:PRK09051 1 MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGhVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 81 TGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMfLDGLEDADTGKLMG 160
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMM-VGALHDPFGTIHMG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 161 QFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKE 239
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVrADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 240 -GSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINE 318
Cdd:PRK09051 240 nGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494637755 319 AFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
6-392 |
3.25e-105 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 315.41 E-value: 3.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPqarNGYRMG-------HNEVKDHMFLDGLEDADTGKL 158
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLP---SDLRWGpkhllhkNYKIDDAMLVDGLIDAFYFEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 159 MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVktrkgdvvVESDEQPAKANAERIPLLRPAFAK 238
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------LDRDEGIRKTTMEDLAKLPPAFDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 239 EGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINE 318
Cdd:PRK06366 233 NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494637755 319 AFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIEL 392
Cdd:PRK06366 313 AFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLEM 386
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
6-391 |
2.38e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 313.51 E-value: 2.38e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMT---NAPYIlpqaRNGYRMGHNEVKDHMFLDGLEDADTGKLMGQF 162
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmHGSYI----RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 163 AQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQ-PAKANAERIPLLRPAFAKEGS 241
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETvRPDTSLEILSKLRPAFDKNGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 242 ITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFA 321
Cdd:PRK06633 241 VTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 322 MVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK06633 321 AQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
6-391 |
9.05e-103 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 309.58 E-value: 9.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVER-AGVNPAEIDEVIMGCILTAGV-KQGPARQAMRNAGIPDSTGA 83
Cdd:PRK09050 4 AFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMgHNEVKDHM----FLDGLEDADTG-KL 158
Cdd:PRK09050 84 TTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAFSR-QAEIFDTTigwrFVNPLMKAQYGvDS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 159 MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQP-AKANAERIPLLRPAF 236
Cdd:PRK09050 163 MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPrPETTLEALAKLKPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 237 AKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEI 316
Cdd:PRK09050 243 RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQFDVIEL 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494637755 317 NEAFAMVTMAAMDELNIPH--EKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK09050 323 NEAFAAQGLAVLRQLGLADddARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-262 |
3.34e-95 |
|
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: 285.35 E-value: 3.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQ-ARNGYRMGHNEVKDHMFLDGLEDADTGKLMGQFAQ 164
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTdARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 165 EMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKEGSIT 243
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIrPPTTAEPLAKLKPAFDKEGTVT 240
|
250
....*....|....*....
gi 494637755 244 AANASSISDGAAAVVVTSE 262
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSE 259
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
8-391 |
2.27e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 287.37 E-value: 2.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGP-ARQAMRNAGIPDSTGAVTI 86
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNiARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPY---ILPQARNGYRMGHNEVKdhMFLDGLEDADTGKLMGqfA 163
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPIssaMTAGEQLGFTSPFAESK--GWLHRYGDQEVSQFRG--A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 164 QEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVtvktrkGDVVVesDEQPAKANAERIPLLRPaFAKEGSIT 243
Cdd:PRK07801 162 ELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GGVTV--DEGPRETSLEKMAGLKP-LVEGGRLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 244 AANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMV 323
Cdd:PRK07801 233 AAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAFAPV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494637755 324 TMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK07801 313 VLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
6-391 |
1.84e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 286.11 E-value: 1.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGvkQGPA--RQAMRNAGIPDSTGA 83
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNG--EAPAigRVAALDAGLPVTVPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHMfldgledaDTGKLMGQ-- 161
Cdd:PRK06205 82 MQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDRL--------ARGRETAGgr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 162 ----------FAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQP-AKANAERI 229
Cdd:PRK06205 154 rfpvpggmieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPrADTTLESL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 230 PLLRPAFAK---EGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGW 306
Cdd:PRK06205 234 AKLRPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 307 SVEDVDLWEINEAFAMVTMAAMDELNIP---HEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGG 383
Cdd:PRK06205 314 TLDDIDLIELNEAFAAQVLAVLKEWGFGaddEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGG 393
|
....*...
gi 494637755 384 EAVAVAIE 391
Cdd:PRK06205 394 QGLAAVFE 401
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
6-391 |
2.58e-93 |
|
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, an enzyme that acts at the end of pathways for the degradation of protocatechuate (from benzoate and related compounds) and of phenylacetic acid.
Pssm-ID: 131483 Cd Length: 400 Bit Score: 285.52 E-value: 2.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVER-AGVNPAEIDEVIMGCILTAGV-KQGPARQAMRNAGIPDSTGA 83
Cdd:TIGR02430 3 AYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYRMGHNEVKDHM---FLDGLEDADTG-KLM 159
Cdd:TIGR02430 83 TTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIgwrFINPLMKALYGvDSM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 160 GQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDEQP-AKANAERIPLLRPAFA 237
Cdd:TIGR02430 163 PETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEpTVVDQDEHPrPETTLEGLAKLKPVVR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 238 KEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEIN 317
Cdd:TIGR02430 243 PDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELN 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494637755 318 EAFAMVTMAAMDELNIPH--EKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:TIGR02430 323 EAFAAQALAVLRELGLADddARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
4-391 |
8.48e-90 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 276.22 E-value: 8.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 4 DSVVIVSGARTPMGGF------QGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGvKQGP--ARQAMRNA 75
Cdd:PRK06445 2 EDVYLVDFARTAFSRFrpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVG-ENWLygGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 76 GIPDSTGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHN-EVKDHM-FLDGLE-- 151
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP-----------MGDNpHIEPNPkLLTDPKyi 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 152 --DADTGKLMGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDeQPAKANA--E 227
Cdd:PRK06445 150 eyDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVD-QSVRPDTslE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 228 RIPLLRPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWS 307
Cdd:PRK06445 229 KLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 308 VEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVA 387
Cdd:PRK06445 309 VKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGA 388
|
....
gi 494637755 388 VAIE 391
Cdd:PRK06445 389 VVLE 392
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
7-391 |
1.09e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 271.11 E-value: 1.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMG-GFQGDLSGATAPQLGAAAIKAAVERA-GVNPAEIDEVIMGCILTAGvKQGP--ARQAMRNAGIpDSTG 82
Cdd:PRK07851 5 VIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGG-EQGFnmARVVAVLLGY-DFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 83 AVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMT--------------NAPYILPQARNGYRMGHNEVKDHmflD 148
Cdd:PRK07851 83 GTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtkNPLFAEAQARTAARAEGGAEAWH---D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 149 GLEDA---DTGKLMGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTvkTRKGDVVVESDEQPAKAN 225
Cdd:PRK07851 160 PREDGllpDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVT--LPDGTVVSTDDGPRAGTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 226 AERIPLLRPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAG 305
Cdd:PRK07851 238 YEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARAG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 306 WSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEA 385
Cdd:PRK07851 318 MSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGGGQG 397
|
....*.
gi 494637755 386 VAVAIE 391
Cdd:PRK07851 398 MAMVLE 403
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
6-391 |
6.40e-87 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 268.76 E-value: 6.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGdlsGA----TAPQLGAAAIKAAVER-AGVNPAEIDEVIMGCILTAgVKQG--PARQAMRNAGIP 78
Cdd:PRK08947 4 VVIVDAIRTPMGRSKG---GAfrnvRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQT-LEQGfnIARNAALLAGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 79 DSTGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHNeVKDHMFLdGLEDADTGKL 158
Cdd:PRK08947 80 HSVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG-VDFHPGL-SKNVAKAAGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 159 MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD-VVVESDE--QPaKANAERIPLLRPA 235
Cdd:PRK08947 147 MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVlKLFDYDEviRP-ETTVEALAALRPA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 236 F-AKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLW 314
Cdd:PRK08947 226 FdPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 315 EINEAFAMVTMAAMDELNI---PHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK08947 306 ELNEAFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
8-391 |
1.11e-85 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 265.71 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMGGFQGDLSGATAP-QLGAAAIKAAVERA-GVNPAEIDEVIMGCILTAGvKQG--PARQAMRNAGIPDSTGA 83
Cdd:PRK09052 10 IVAATRTPVGKAPRGMFKNTRPdDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEA-EQGlnVARIGALLAGLPNSVGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHNEV--KDHMFlDGLEDADTGKLMGQ 161
Cdd:PRK09052 89 VTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP-----------MMGNKPsmSPAIF-ARDENVGIAYGMGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 162 FAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDV----------VVESDEQP-AKANAERIP 230
Cdd:PRK09052 157 TAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktrTVDLDEGPrADTSLEGLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 231 LLRPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVED 310
Cdd:PRK09052 237 KLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 311 VDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAI 390
Cdd:PRK09052 317 LDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIF 396
|
.
gi 494637755 391 E 391
Cdd:PRK09052 397 E 397
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
7-392 |
1.31e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 265.46 E-value: 1.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMG-GFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCIlTAGVKQG--PARQAMRNAGIPDSTGA 83
Cdd:PRK07661 5 VIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCA-MPEAEQGlnMARNIGALAGLPYTVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHNEVKDHMFLdgLEDADTGKL-MGQF 162
Cdd:PRK07661 84 ITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP-----------MMGHVVRPNPRL--VEAAPEYYMgMGHT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 163 AQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD---------VVVESDEQ-PAKANAERIPLL 232
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGennklqeetITFSQDEGvRADTTLEILGKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 233 RPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVD 312
Cdd:PRK07661 231 RPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 313 LWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIEL 392
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFEL 390
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
13-391 |
3.26e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 264.82 E-value: 3.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 13 RTPMGGFQ--GDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGvKQGP--ARQAMRNAGIPDSTGAVTINK 88
Cdd:PRK08242 11 RTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVG-DQGAdiARTAVLAAGLPETVPGVQINR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 89 LCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHNevKDHMFLDGLEDADTGkLMGQ--FAQEM 166
Cdd:PRK08242 90 FCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP-----------MGSD--GGAWAMDPSTNFPTY-FVPQgiSADLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 167 ADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVtvKTRKGDVVVESDEQP-AKANAERIPLLRPAFAKEGSI--- 242
Cdd:PRK08242 156 ATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--KDQNGLTILDHDEHMrPGTTMESLAKLKPSFAMMGEMggf 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 243 ------------------TAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKA 304
Cdd:PRK08242 234 davalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 305 GWSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGE 384
Cdd:PRK08242 314 GLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGM 393
|
....*..
gi 494637755 385 AVAVAIE 391
Cdd:PRK08242 394 GIATIIE 400
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
6-391 |
1.24e-83 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 261.49 E-value: 1.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PRK08170 5 VYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQ-----------ARN-GYRMGH-NEVKDHMF------ 146
Cdd:PRK08170 85 VQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEkmvrwlagwyaAKSiGQKLAAlGKLRPSYLapvigl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 147 LDGLEDADTGKLMGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKdEVTPVTvkTRKGDVVVESDEQPAKANA 226
Cdd:PRK08170 165 LRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF--DRDGKFYDHDDGVRPDSSM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 227 ERIPLLRPAFAKE-GSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAG 305
Cdd:PRK08170 242 EKLAKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 306 WSVEDVDLWEINEAFAMVTMAAM----------DELNIPH-------EKVNIEGGACALGHPVGCSGARILVTLINSLKR 368
Cdd:PRK08170 322 LTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGLDGalgeldrERLNVDGGAIALGHPVGASGARIVLHLLHALKR 401
|
410 420
....*....|....*....|...
gi 494637755 369 TGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK08170 402 RGTKRGIAAICIGGGQGGAMLLE 424
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
8-391 |
8.20e-82 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 255.42 E-value: 8.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGP-ARQAMRNAGIPDSTGAVTI 86
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNvARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQ---ARNGYrmghnevkDHMFLDGLEDADTGKLMGQF- 162
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPStlpAKNGL--------GHYKSPGMEERYPGIQFSQFt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 163 -AQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDEQPAKANA--ERIPLLRPaFAKE 239
Cdd:PRK06504 158 gAEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDAtlEGIAGVKL-IAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 240 GSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEA 319
Cdd:PRK06504 237 GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494637755 320 FAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK06504 317 FASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVE 388
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
5-387 |
6.00e-81 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 253.54 E-value: 6.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 5 SVVIVSGARTPMG----GFQGDLSGATapqLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGP-ARQAMRNAGIPD 79
Cdd:PRK07108 3 EAVIVSTARTPLAkswrGAFNMTHGAT---LGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANiARQIALRAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 80 STGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNApyilpqarngyrmgHNEVKDHMFLDGLEDADTGKL- 158
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV--------------QNEMNRHMLREGWLVEHKPEIy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 159 --MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGD----------VVVESDE-QPAKAN 225
Cdd:PRK07108 146 wsMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADkatgrlftkeVTVSADEgIRPDTT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 226 AERIPLLRPAFAKeGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAG 305
Cdd:PRK07108 226 LEGVSKIRSALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 306 WSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEA 385
Cdd:PRK07108 305 LKVDDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQG 384
|
..
gi 494637755 386 VA 387
Cdd:PRK07108 385 AA 386
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
8-391 |
1.02e-80 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 253.16 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGV-KQGPARQAMRNAGIPDSTGAVTI 86
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGY----RMGHNEVKDHMFLDGLEDADTGKLMGQF 162
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFsrdaKVFDTTIGARFPNPKIVAQYGNDSMPET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 163 AQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKT--RKGDVVVESDEQP-AKANAERIPLLRPAFAkE 239
Cdd:PRK08131 166 GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEHPrPSSTVEALTKLKPLFE-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 240 GSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEA 319
Cdd:PRK08131 245 GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494637755 320 FAMVTMAAMDELNIPHE--KVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK08131 325 FASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
7-391 |
1.35e-78 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 247.33 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQG-PARQAMRNAGIPDSTGAVT 85
Cdd:PRK07850 5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNnITRTAWLHAGLPYHVGATT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYilpqarnGYRMGHNEvkdhmfldGLEDADTGKL-MG-QF- 162
Cdd:PRK07850 85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL-------GANAGPGR--------GLPRPDSWDIdMPnQFe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 163 -AQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRK-------GDVVVESDEQPAKANAERIPLLRP 234
Cdd:PRK07850 150 aAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRDTTMEGLAGLKP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 235 AFakEGSI-TAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDL 313
Cdd:PRK07850 230 VL--EGGIhTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494637755 314 WEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-391 |
1.80e-78 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 248.91 E-value: 1.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 3 SDSVVIVSGARTPM-----GGFQGDLsgatAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQG-PARQAMRNAG 76
Cdd:PLN02287 45 GDDVVIVAAYRTPIckakrGGFKDTY----PDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRAnECRMAAFYAG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 77 IPDSTGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNgyrmghNEVKDhmfldgLEDADTG 156
Cdd:PLN02287 121 FPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVN------PRVES------FSQAQDC 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 157 KL-MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTR-------KGDVVVESDEQPAKANAER 228
Cdd:PLN02287 189 LLpMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVdpktgeeKPIVISVDDGIRPNTTLAD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 229 IPLLRPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSV 308
Cdd:PLN02287 269 LAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLEL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 309 EDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTG--GKKGVGSLCIGGGEAV 386
Cdd:PLN02287 349 DDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGA 428
|
....*
gi 494637755 387 AVAIE 391
Cdd:PLN02287 429 AAVFE 433
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
6-393 |
3.89e-76 |
|
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]
Pssm-ID: 131498 Cd Length: 385 Bit Score: 241.00 E-value: 3.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGAT-APQLGAAAIKAAVER-AGVNPAEIDEVIMGCIlTAGVKQG--PARQAMRNAGIPDST 81
Cdd:TIGR02445 2 VVIVDFGRTPMGRSKGGAFRNTrAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCV-QQTLEQGfnIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 82 GAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyilpqarngyrMGHN-EVKDHMfldGLEDADTGKLMG 160
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-----------MMHGvDFHPGM---SLHVAKAAGMMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 161 QFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPV-------TVKTRKGDVVVESDeqpakANAERIPLLR 233
Cdd:TIGR02445 147 LTAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTqghdadgFLKQFDYDEVIRPE-----TTVESLAALR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 234 PAF-AKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVD 312
Cdd:TIGR02445 222 PAFdPKNGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDID 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 313 LWEINEAFAMVTMAAMDELNI---PHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVA 389
Cdd:TIGR02445 302 VFELNEAFAAQALPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATV 381
|
....
gi 494637755 390 IELP 393
Cdd:TIGR02445 382 FERV 385
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
8-391 |
1.13e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 230.43 E-value: 1.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 8 IVSGARTPMG---GFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGvKQGP--ARQAMRNAGIPDSTG 82
Cdd:PRK06025 6 IIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRG-KQGGdlGRMAALDAGYDIKAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 83 AVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMT-NAPYILPQARNG---YRMGHNevkdHMFLDGLEDADTgkl 158
Cdd:PRK06025 85 GVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSyTAAMAAEDMAAGkppLGMGSG----NLRLRALHPQSH--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 159 MGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVtvKTRKGDVVVESDEQP-AKANAERIPLLRPAFA 237
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSVALDHEEFPrPQTTAEGLAALKPAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 238 K-------EGSIT-------------------AANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTI 291
Cdd:PRK06025 236 AiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 292 APIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGG 371
Cdd:PRK06025 316 APVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGL 395
|
410 420
....*....|....*....|
gi 494637755 372 KKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK06025 396 KRGLVTMCAAGGMAPAIIIE 415
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
7-391 |
1.87e-63 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 207.31 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 7 VIVSGARTPMGGFQGDLSGATAPQLGAAAIK---AAVERagvnpaEIDEVIMGCILTAGvkQGPARQAMRNAGIPDSTGA 83
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTflsKGMER------EIDDVILGNVVGPG--GNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 84 VTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYilpqarngyrmghnEVKDHMFLDGLEDADtgklMGQFA 163
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF--------------QNRARFSPETIGDPD----MGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 164 QEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVtvktrkGDVVVESDEQpaKANAER-IPLLRPAFAKEGSI 242
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF------NGLLDESIKK--EMNYERiIKRTKPAFLHNGTV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 243 TAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAM 322
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFAS 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494637755 323 VTMAAMDELNIPHEKVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK06690 290 KVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
9-391 |
2.39e-61 |
|
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: 202.72 E-value: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 9 VSGARTPMGGFQGDlSGATAP----QLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAV 84
Cdd:cd00826 1 AGAAMTAFGKFGGE-NGADANdlahEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 85 TINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNApyilpqARNGYRMGHNEVkdhmfldgledadtgklmgqfaq 164
Cdd:cd00826 80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------AENNAKEKHIDV----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 165 emADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRKGDVVVESDE---QPAKANAERIPLLRPAFAKEGS 241
Cdd:cd00826 131 --LINKYGMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEyiqFGDEASLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 242 ITAANASSISDGAAAVVVTSEKVAQEKGFNIEA-------RIVATASNSRHPSEFTIA----PIGAMEKVLAKAGWSVED 310
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAQKHGLQSKAreiqaleMITDMASTFEDKKVIKMVggdgPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 311 VDLWEINEAFAMVTMAAMDELNIPHEK------------------VNIEGGACALGHPVGCSGARILVTLINSLKRTGGK 372
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
410 420
....*....|....*....|....
gi 494637755 373 -----KGVGSLCIGGGEAVAVAIE 391
Cdd:cd00826 369 rqgagAGLALLCIGGGGGAAMCIE 392
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-391 |
1.15e-52 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 180.95 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 2 SSDSVVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGciltaGVKQGP-----ARQAMRNAG 76
Cdd:PRK08963 3 QGDRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFG-----QVVQMPeapniAREIVLGTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 77 IPDSTGAVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPyiLPQARNGYRMGHNEVKDHMFLDGLE----- 151
Cdd:PRK08963 78 MNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLP--IGVSKKLARALVDLNKARTLGQRLKlfsrl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 152 -------------DADTGKLMGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTV----KTRKGDVV 214
Cdd:PRK08963 156 rlrdllpvppavaEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVppykQPLEEDNN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 215 VESD---EQPAKanaeriplLRPAF-AKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSE-F 289
Cdd:PRK08963 236 IRGDstlEDYAK--------LRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQdM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 290 TIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMA----------AMDELN-------IPHEKVNIEGGACALGHPVG 352
Cdd:PRK08963 308 LLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFA 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 494637755 353 CSGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK08963 388 ATGARMITQTLHELRRRGGGLGLTTACAAGGLGAAMVLE 426
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
274-391 |
1.80e-46 |
|
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: 155.11 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 274 ARIVATASNSRHPSEFTIAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALGHPVGC 353
Cdd:pfam02803 5 ARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHPLGA 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 494637755 354 SGARILVTLINSLKRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:pfam02803 85 SGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
6-391 |
4.39e-44 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 158.14 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 6 VVIVSGARTPMGGFQGDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTGAVT 85
Cdd:PRK09268 9 VAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 86 INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAP--------YILPQARNGYRMGHN-----EVKDHMF---LDG 149
Cdd:PRK09268 89 LQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPiavneglrKILLELNRAKTTGDRlkalgKLRPKHLapeIPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 150 LEDADTGKLMGQFAQEMADEKGYTREQMDNFAIESLNRALTAINEGHFKDEVTPVTVKTRkgDVVVESDeqpakANAERI 229
Cdd:PRK09268 169 NGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--DNNLRPD-----SSLEKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 230 PLLRPAFAK--EGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIV---ATASNSRHPSE-FTIAPIGAMEKVLAK 303
Cdd:PRK09268 242 AKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVdaeTAAVDFVHGKEgLLMAPAYAVPRLLAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 304 AGWSVEDVDLWEINEAFA---MVTMAAMDELN--------------IPHEKVNIEGGACALGHPVGCSGARILVTLINSL 366
Cdd:PRK09268 322 NGLTLQDFDFYEIHEAFAsqvLATLKAWEDEEycrerlgldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLL 401
|
410 420
....*....|....*....|....*
gi 494637755 367 KRTGGKKGVGSLCIGGGEAVAVAIE 391
Cdd:PRK09268 402 AEKGSGRGLISICAAGGQGVTAILE 426
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
21-390 |
2.58e-29 |
|
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: 116.98 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 21 GDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDsTGAVTINKLCGSGMKAVMQA 100
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 101 HDTIKAGSADIVVAGGMESMTNAPY---ILPQARNGYRMGHNEVKDHMFLDgledadtgkLMGQFAQEMADEKGYTREQM 177
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTgdeAGGRASDLEWEGPEPPGGLTPPA---------LYALAARRYMHRYGTTREDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 178 DNFAIesLNRALTAINEG-HFKDEVTPVTVKtrkgdvvvesdeqpakaNAERI--PLlrpafakegsiTAANASSISDGA 254
Cdd:cd00829 159 AKVAV--KNHRNAARNPYaQFRKPITVEDVL-----------------NSRMIadPL-----------RLLDCCPVSDGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 255 AAVVVTSEKVAQEKGFNIeARIVATASNSRHPS-----EFTIAPIGAM--EKVLAKAGWSVEDVDLWEINEAFAMVTMAA 327
Cdd:cd00829 209 AAVVLASEERARELTDRP-VWILGVGAASDTPSlserdDFLSLDAARLaaRRAYKMAGITPDDIDVAELYDCFTIAELLA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 328 MDEL---------------------NIPhekVNIEGGACALGHPVGCSGARILVTLINSLKRTGGKKGV------GSLCI 380
Cdd:cd00829 288 LEDLgfcekgeggklvregdtaiggDLP---VNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVpgarvgLAHNI 364
|
410
....*....|
gi 494637755 381 GGGEAVAVAI 390
Cdd:cd00829 365 GGTGSAAVVT 374
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
35-367 |
8.37e-17 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 81.10 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 35 AIKAAVERAGVNPAEIDEVIMGCiLTAGVKQGparQAMRNAGIPDSTG-----AVTINKLCGSGMKAVMQAHDTIKAGSA 109
Cdd:PRK06064 29 AGLEALEDAGIDGKDIDAMYVGN-MSAGLFVS---QEHIAALIADYAGlapipATRVEAACASGGAALRQAYLAVASGEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 110 DIVVAGGMESMTNAPYILP---QARNGYRmghnevkdhmFLDGLEDADTGKLMGQFAQEMADEKGYTREQMDNFAIEslN 186
Cdd:PRK06064 105 DVVLAAGVEKMTDVPTPDAteaIARAGDY----------EWEEFFGATFPGLYALIARRYMHKYGTTEEDLALVAVK--N 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 187 RALTAIN-EGHFKDEVTPVTVKtrKGDVVvesdeqpakanAERIPLLrpafakegsitaaNASSISDGAAAVVVTSEKVA 265
Cdd:PRK06064 173 HYNGSKNpYAQFQKEITVEQVL--NSPPV-----------ADPLKLL-------------DCSPITDGAAAVILASEEKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 266 QE---KGFNIEARIVA--TASNSRHPSEFTI-APIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDEL-------- 331
Cdd:PRK06064 227 KEytdTPVWIKASGQAsdTIALHDRKDFTTLdAAVVAAEKAYKMAGIEPKDIDVAEVHDCFTIAEILAYEDLgfakkgeg 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 494637755 332 -------------NIPhekVNIEGGACALGHPVGCSGARILVTLINSLK 367
Cdd:PRK06064 307 gklaregqtyiggDIP---VNPSGGLKAKGHPVGATGVSQAVEIVWQLR 352
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
24-390 |
1.31e-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: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 24 SGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPDSTgAVTINKLCGSGMKAVMQAHDT 103
Cdd:cd00327 3 LGITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGISGGP-AYSVNQACATGLTALALAVQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 104 IKAGSADIVVAGGMESmtnapyilpqarngyrmghnevkdhmfldgledadtgklmgqfaqemadekgytreqmdnfaie 183
Cdd:cd00327 82 VQNGKADIVLAGGSEE---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 184 slnraltaineghfkdevtpvtvktrkgdvvvesdeqpakanaeripllrpafakegsitaanaSSISDGAAAVVVTSEK 263
Cdd:cd00327 98 ----------------------------------------------------------------FVFGDGAAAAVVESEE 113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 264 VAQEKGFNIEARIVATASNSRHPSEFTI----APIGAMEKVLAKAGWSVEDVDLWEINEAFA----MVTMAAMDELNIPH 335
Cdd:cd00327 114 HALRRGAHPQAEIVSTAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHGTGTpigdAVELALGLDPDGVR 193
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494637755 336 EkVNIEGGACALGHPVGCSGARILVTLINSLKRTGGK-------KGVGSLCIGGGEAVAVAI 390
Cdd:cd00327 194 S-PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPptpreprTVLLLGFGLGGTNAAVVL 254
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
4-355 |
7.75e-15 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 75.37 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 4 DSVVIVSGARTPMGgfqgDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQG-PARQAMRNAGIPDSTG 82
Cdd:PRK07516 2 MTASIVGWAHTPFG----KLDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDfPASLVLQADPALRFKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 83 AVTINKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPY-----ILpqARNGYRMghnevkdhmfldglEDADTGk 157
Cdd:PRK07516 78 ATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTaevgdIL--LGASYLK--------------EEGDTP- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 158 lmGQFAQEMAD-EKGYTREQMDnfaiesLNRALTAINEGHFKDEVTPVTVKTRKgDVVVE-----SDEQPAKANaeriPL 231
Cdd:PRK07516 141 --GGFAGVFGRiAQAYFQRYGD------QSDALAMIAAKNHANGVANPYAQMRK-DLGFEfcrtvSEKNPLVAG----PL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 232 LRpafakegsitaANASSISDGAAAVVVTSEKVAQEkgFNIEARIVATAS-------NSRHPSEFTiAPIGAMEKVLAKA 304
Cdd:PRK07516 208 RR-----------TDCSLVSDGAAALVLADAETARA--LQRAVRFRARAHvndflplSRRDPLAFE-GPRRAWQRALAQA 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494637755 305 GWSVEDVDLWEINEAFamvTMAAMDELNI----PHEK-----------------VNIEGGACALGHPVGCSG 355
Cdd:PRK07516 274 GVTLDDLSFVETHDCF---TIAELIEYEAmglaPPGQgarairegwtakdgklpVNPSGGLKAKGHPIGATG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
26-372 |
3.02e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 73.34 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 26 ATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIPdSTGAVTINKLCGSGMKAVMQAHDTIK 105
Cdd:PRK12578 19 VSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLT-GKVPLRVEAMCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 106 AGSADIVVAGGMESMTNAPYILPQARNGyRMGHNEVKDHMF---LDGLEDADTGKLMGQFaqemadekGYTREQMDNFAI 182
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVDTSTSLAIGG-RGGNYQWEYHFYgttFPTYYALYATRHMAVY--------GTTEEQMALVSV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 183 ESLNRAltAINE-GHFKDEVTpvtvktrkgdvvVEsDEQPAKANAERIPLLrpafakegsitaaNASSISDGAAAVVVTS 261
Cdd:PRK12578 169 KAHKYG--AMNPkAHFQKPVT------------VE-EVLKSRAISWPIKLL-------------DSCPISDGSATAIFAS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 262 EKVAQEKGFNIEARI--VATASNSRHPS---EFT--IAPIGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDELNIP 334
Cdd:PRK12578 221 EEKVKELKIDSPVWItgIGYANDYAYVArrgEWVgfKATQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYEDLGFT 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 494637755 335 H-------------EK-----VNIEGGACALGHPVGCSGARILVTLINSLKRTGGK 372
Cdd:PRK12578 301 EkgkggkfieegqsEKggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGK 356
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
4-359 |
4.43e-10 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 60.81 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 4 DSVVIVSGARTPMGgfqgDLSGATAPQLGAAAIKAAVERAGVNPAEIDEVIMG---CILTAGVKQGPARQAMRNAGIPds 80
Cdd:PRK06157 7 DKVAILGMGCTKFG----ERWDAGAEDLMVEAFLEALADAGIEPKDIDAAWFGthyDEIGSGKSGTPLSRALRLPNIP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 81 tgaVT-INKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNApyilpqarnGYRmghnevkdhmfldGLEDADTGKLM 159
Cdd:PRK06157 81 ---VTrVENFCATGSEAFRGAVYAVASGAYDIALALGVEKLKDT---------GYG-------------GLPVANPGTLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 160 ----------GQFAQ---EMADEKGYTREQMDNfAIESL---NRALTAINE-GHFKDEVTPvtvktrkgdvvvesdEQPA 222
Cdd:PRK06157 136 dmtmpnvtapGNFAQlasAYAAKYGVSREDLKR-AMAHVsvkSHANGARNPkAHLRKAVTE---------------EQVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 223 KAnaeripllrPAFAkeGSITAANASSISDGAAAVVVTSEKVAQEKGFN----IEAR--IVATASNSRHPSE-FTIAP-- 293
Cdd:PRK06157 200 KA---------PMIA--GPLGLFDCCGVSDGAAAAIVTTPEIARALGKKdpvyVKALqlAVSNGWELQYNGWdGSYFPtt 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 294 IGAMEKVLAKAGWS--VEDVDLWEINEAFAMVTMAAMDELNIPHE------------------KVNIEGGACALGHPVGC 353
Cdd:PRK06157 269 RIAARKAYREAGITdpREELSMAEVHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGA 348
|
....*.
gi 494637755 354 SGARIL 359
Cdd:PRK06157 349 SGLRML 354
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
27-367 |
5.85e-10 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 60.68 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 27 TAPQLGAAAIKAAVERAGVNPAE--IDEVIMGCILTAGVKQ----GPArqAMRNAGIPDSTG------AVTINKLCGSGM 94
Cdd:PTZ00455 47 TLEELLATAIQGTLENTGLDGKAalVDKVVVGNFLGELFSSqghlGPA--AVGSLGQSGASNallykpAMRVEGACASGG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 95 KAVMQAHDTIKAGSADIVVAGGMESMTNApyilpQARNGyrmghnevkdhmfldgledadtgklmGQFAQEMADekgYTR 174
Cdd:PTZ00455 125 LAVQSAWEALLAGTSDIALVVGVEVQTTV-----SARVG--------------------------GDYLARAAD---YRR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 175 E-QMDNFAIESL-NRALTAINE-GHF-KDEVTPVTVK--------------TRKGDVVVESDEQPAK----ANAERIPLL 232
Cdd:PTZ00455 171 QrKLDDFTFPCLfAKRMKYIQEhGHFtMEDTARVAAKayangnknplahmhTRKLSLEFCTGASDKNpkflGNETYKPFL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 233 RpafakegsitAANASSISDGAAAVVVTSEKVAQEKGFN------IEARIVATASNSRH--PSEFT--IAPIGAMEKVLA 302
Cdd:PTZ00455 251 R----------MTDCSQVSDGGAGLVLASEEGLQKMGLSpndsrlVEIKSLACASGNLYedPPDATrmFTSRAAAQKALS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 303 KAGWSVEDVDLWEINEAFAMVTMAAMDELNIP---HEK---------------VNIEGGACALGHPVGCSGARILVTLIN 364
Cdd:PTZ00455 321 MAGVKPSDLQVAEVHDCFTIAELLMYEALGIAeygHAKdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYR 400
|
...
gi 494637755 365 SLK 367
Cdd:PTZ00455 401 QMK 403
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
16-389 |
3.05e-08 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 55.08 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 16 MGGFQGDLS------GATAPQLGAAAIKAAVERAGVNPAEIDEVIMGCI---LTAGVKQGPARQAMRNAGIpDSTGAVTI 86
Cdd:PRK06289 8 LGGYQSDFArnwtkeGRDFADLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 87 NKLCGSGMKAVMQAHDTIKAGSADIVVAGGMESMTNAPYILPQARNGYR--MGHnEVKDHMFLdgledadTGKLMGQFAQ 164
Cdd:PRK06289 87 EAACASGSVATLAAMADLRAGRYDVALVVGVELMKTVPGDVAAEHLGAAawTGH-EGQDARFP-------WPSMFARVAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 165 EMADEKGYTREQMD-----NFAIESLN-RALT---AINEGHFK--DEVTPVTvktrkgdvvvesdeqpakanaeripllr 233
Cdd:PRK06289 159 EYDRRYGLDEEHLRaiaeiNFANARRNpNAQTrgwAFPDEATNddDATNPVV---------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 234 pafakEGSITAANASSISDGAAAVVVTSEKVAQEKGfniEARIVATASNSRHPSeftiAPIG------------------ 295
Cdd:PRK06289 211 -----EGRLRRQDCSQVTDGGAGVVLASDAYLRDYA---DARPIPRIKGWGHRT----APLGleqkldrsagdpyvlphv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 296 --AMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDELNI--PHEK----------------VNIEGGACALGHPVGCSG 355
Cdd:PRK06289 279 rqAVLDAYRRAGVGLDDLDGFEVHDCFTPSEYLAIDHIGLtgPGESwkaiengeiaiggrlpINPSGGLIGGGHPVGASG 358
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 494637755 356 ARILVTLINSLKRT------GGKKGVGSLCIGGGEAVAVA 389
Cdd:PRK06289 359 VRMLLDAAKQVTGTagdyqvEGAKTFGTLNIGGSTTTTVS 398
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
29-321 |
9.99e-08 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 53.36 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 29 PQLGAAAIKAAVERAGVNPAEIDEVIMGCIL---TAGVKqgpARQAMRNAGIPdstgAVTINKLCGSGMKAVMQAHDTIK 105
Cdd:PRK08256 23 PDMAAEAGRAALADAGIDYDAVQQAYVGYVYgdsTSGQR---ALYEVGMTGIP----IVNVNNNCSTGSTALFLARQAVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 106 AGSADIVVAGGMESMTnaPYILPQA---RNGYRMGHNEVkdhmfLDGLEDADTG----KLMGQFAQEMADEKGYTREQmd 178
Cdd:PRK08256 96 SGAADCALALGFEQMQ--PGALGSVwddRPSPLERFDKA-----LAELQGFDPAppalRMFGGAGREHMEKYGTTAET-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 179 nFA-IESLNRALTAINE-GHFKDEVTPvtvktrkgDVVVESdeqpakanaeripllRPAFakeGSITAANASSISDGAAA 256
Cdd:PRK08256 167 -FAkIGVKARRHAANNPyAQFRDEYTL--------EDVLAS---------------PMIW---GPLTRLQCCPPTCGAAA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494637755 257 VVVTSEKVAQEKGFNIEARIVATASNSRHPSEF----TIAPIG------AMEKVLAKAGWSVEDVDLWEINEAFA 321
Cdd:PRK08256 220 AIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFdgrsMIDLVGydmtraAAQQVYEQAGIGPEDIDVVELHDCFS 294
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
30-122 |
1.29e-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: 43.68 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 30 QLGAAAIKAAVERAGVNPAEIDEVIMGCIL---TAGVKQGPARQAMRNAGIPDSTGAVTINKL----------------- 89
Cdd:cd00834 73 QFALAAAEEALADAGLDPEELDPERIGVVIgsgIGGLATIEEAYRALLEKGPRRVSPFFVPMAlpnmaagqvairlglrg 152
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 494637755 90 --------CGSGMKAVMQAHDTIKAGSADIVVAGGMESMTN 122
Cdd:cd00834 153 pnytvstaCASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
|
| PRK08257 |
PRK08257 |
acetyl-CoA acetyltransferase; Validated |
246-334 |
8.77e-04 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 236204 [Multi-domain] Cd Length: 498 Bit Score: 41.44 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 246 NASSISDGAAAVVVTSEKVAQEKGFNiEARIV-----ATASNSRHPSE---FTIAPigAME----KVLAKAGWSVEDVDL 313
Cdd:PRK08257 238 NANDMVDQGAAVLLTSVAKARRLGVP-EDRWVylhggADAHDPYDILErpdLHRSP--AIRaagrRALALAGLGIDDIDA 314
|
90 100
....*....|....*....|.
gi 494637755 314 WEINEAFAMVTMAAMDELNIP 334
Cdd:PRK08257 315 FDLYSCFPSAVQVAARELGLD 335
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
229-315 |
8.98e-04 |
|
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: 41.08 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 229 IPLLRPAFAKEGSITAANASSISDGAAAVVVTSEKVAQEKGFNIEARIVATASNSRHPSEFTIAPIG-----AMEKVLAK 303
Cdd:cd00825 138 GALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAeglarAAKEALAV 217
|
90
....*....|..
gi 494637755 304 AGWSVEDVDLWE 315
Cdd:cd00825 218 AGLTVWDIDYLV 229
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
30-122 |
1.75e-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: 40.08 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 30 QLGAAAIKAAVERAGVNPAEIDEVIMGCILTAGV--------------KQGPAR-------QAMRNAgipdSTGAVTIN- 87
Cdd:COG0304 73 QYALAAAREALADAGLDLDEVDPDRTGVIIGSGIggldtleeayrallEKGPRRvspffvpMMMPNM----AAGHVSIRf 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 494637755 88 KL----------CGSGMKAVMQAHDTIKAGSADIVVAGGMESMTN 122
Cdd:COG0304 149 GLkgpnytvstaCASGAHAIGEAYRLIRRGRADVMIAGGAEAAIT 193
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
249-312 |
2.50e-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: 39.83 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494637755 249 SISDGAAAVVVTSEKVAQEKGFNIEARIV--ATASNSRH---PSEFTIAPIGAMEKVLAKAGWSVEDVD 312
Cdd:cd00834 228 VLGEGAGVLVLESLEHAKARGAKIYAEILgyGASSDAYHitaPDPDGEGAARAMRAALADAGLSPEDID 296
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
250-317 |
3.23e-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: 39.31 E-value: 3.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494637755 250 ISDGAAAVVVTSEKVAQEKGFNIEARIVATASNS--RH---PSEFTIAPIGAMEKVLAKAGWSVEDVDLweIN 317
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSdaYHitaPAPDGEGAARAMRAALKDAGLSPEDIDY--IN 299
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
24-348 |
4.90e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 38.81 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 24 SGATAPQLGAAAIKAAVERAGVNPAEIDEVImgcilTAGVKQGPARQAMRNAGIPDSTGAVTINKLCGSGMKAVMQAHDT 103
Cdd:PRK07855 20 SGRSELRLACEAVLAALDDAGLAPSDVDGLV-----TFTMDTNPEIAVARALGIGELKFFSRIHYGGGAACATVQQAAMA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 104 IKAGSADIVVAggmesmtnapYILPQARNGYRMGHNEVKDHMFLDGlEDADTGKLM-----------GQFAQEMADEKGY 172
Cdd:PRK07855 95 VATGVADVVVC----------YRAFNERSGMRFGQGQTGLAENPTS-TGVDYGWSYphglltpaawvAMLARRYMHEYGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 173 TREQMDNFAIESLNRALTAINeGHFKDEvtPVTVKtrkgdvvvesDEQPAKANAERIPLLrpafakegsitaaNASSISD 252
Cdd:PRK07855 164 TSEDFGRVAVADRKHAATNPK-AWFYGR--PITLE----------DHQNSRWIAEPLRLL-------------DCCQESD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 253 GAAAVVVTSEKVAQEKGfNIEARIVATASNSRHPSEFT-------IAPIGAMEKV----LAKAGWSVEDVDLWEINEAFA 321
Cdd:PRK07855 218 GAVALVVTSAERARDLK-QRPAVIKAAAQGSGADQYMMtsyyrddITGLPEMGLVarqlWAQSGLGPADIDTAILYDHFT 296
|
330 340 350
....*....|....*....|....*....|
gi 494637755 322 MVTMAAMDELNI--PHE-KVNIEGGACALG 348
Cdd:PRK07855 297 PFVLMQLEELGFcgRGEaKDFIADGALELG 326
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
294-348 |
5.45e-03 |
|
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) and similar proteins; DDRA, also called DDR large subunit, diol dehydratase-reactivase large subunit, diol dehydratase-reactivating factor alpha subunit, or DDR alpha subunit, is the large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one. DDR has weak ATPase activity which is required for DD reactivation. DDRA contains the adenosine nucleotide binding site. DDRA has four domains, the ATPase domain, the swiveling domain, the linker domain, and the insert domain. The model corresponds to the ATPase domain. DDRA belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation.
Pssm-ID: 466880 Cd Length: 260 Bit Score: 38.34 E-value: 5.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 494637755 294 IGAMEKVLAKAGWSVEDVDLWEINEAFAMVTMAAMDELNIPHEKVNIEGGACALG 348
Cdd:cd24030 49 IKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELGIPVEIGGVEAEMAILG 103
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
30-121 |
6.89e-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: 38.17 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 30 QLGAAAIKAAVERAGVNPAEIDEVIMGCIL-------TAGVKQgparqamRNAGIPDsTGAVTINKLCGSGMKAVMQAHD 102
Cdd:COG0332 53 DLAVEAARKALEAAGIDPEDIDLIIVATVTpdylfpsTACLVQ-------HKLGAKN-AAAFDINAACSGFVYALSVAAA 124
|
90 100
....*....|....*....|
gi 494637755 103 TIKAGSAD-IVVAGGmESMT 121
Cdd:COG0332 125 LIRSGQAKnVLVVGA-ETLS 143
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
39-122 |
9.50e-03 |
|
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: 37.61 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494637755 39 AVERAGVNPAEIDEVIMGCILTAGVKQGPARQAMRNAGIP-----------------------DSTG-AVTINKLCGSGM 94
Cdd:pfam00109 98 ALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPrrgspfavgtmpsviagrisyflGLRGpSVTVDTACSSSL 177
|
90 100
....*....|....*....|....*...
gi 494637755 95 KAVMQAHDTIKAGSADIVVAGGMESMTN 122
Cdd:pfam00109 178 VAIHAAVQSIRSGEADVALAGGVNLLLT 205
|
|
| |
