|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-392 |
0e+00 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 739.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYHMGIT 160
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 161 AENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPAFKKDG 240
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFKKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PRK05656 241 SVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK05656 321 AAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-392 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 712.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYHMGIT 160
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVLPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 161 AENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPAFKKDG 240
Cdd:PRK05790 161 AENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFDKDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PRK05790 241 TVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK05790 321 AAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-392 |
0e+00 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 645.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMgHGQLVDSMITDGLWDAFNDYHMGIT 160
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGET 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 161 AENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDpKVFDRDEQPRPDTTADSLAKLRPAFKKDG 240
Cdd:COG0183 160 AENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGE-VVVDRDEGPRPDTTLEKLAKLKPAFKKDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:COG0183 239 TVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:COG0183 319 AAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-392 |
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: 616.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 5 VIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALTL 84
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 85 NKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLvDSMITDGLWDAFNDYHMGITAENL 164
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTL-DGMLDDGLTDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 165 VEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGdPKVFDRDEQPRPDTTADSLAKLRPAFKKDGSVTA 244
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKG-PVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 245 GNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQA 324
Cdd:cd00751 239 GNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872863 325 LAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:cd00751 319 LACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-391 |
0e+00 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 525.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 6 IVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALTLN 85
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 86 KVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMP-SARTGQRMGHGQLVDSMITDgLWDAFNDYHMGITAENL 164
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPrSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 165 VEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGdPKVFDRDEQPRPDTTADSLAKLRPAFKKDGSVTA 244
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 245 GNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQA 324
Cdd:TIGR01930 239 GNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872863 325 LAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:TIGR01930 319 LACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-392 |
1.28e-177 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 499.87 E-value: 1.28e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPYSV 79
Cdd:PRK09051 2 MREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIpTEPRDMYLSRVAAINAGVPQET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITdGLWDAFNDYHMGI 159
Cdd:PRK09051 82 PAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVG-ALHDPFGTIHMGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDpKVFDRDEQPRPDTTADSLAKLRPAFKKD 239
Cdd:PRK09051 161 TAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGE-VVFDTDEHVRADTTLEDLAKLKPVFKKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 240 -GSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANE 318
Cdd:PRK09051 240 nGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872863 319 AFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK09051 320 AFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFER 393
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-391 |
4.47e-165 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 468.04 E-value: 4.47e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYHMGIT 160
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 161 AENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPAFKKDG 240
Cdd:PRK08235 161 GGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDKTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PRK08235 241 TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:PRK08235 321 AAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
3-392 |
4.72e-159 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 452.63 E-value: 4.72e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 3 DVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPAL 82
Cdd:PLN02644 2 DVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 83 TLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYHMGITAE 162
Cdd:PLN02644 82 TVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 163 NLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVF-DRDEQPRpDTTADSLAKLRPAFKKD-G 240
Cdd:PLN02644 162 LCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIvDKDEGLG-KFDPAKLRKLRPSFKEDgG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PLN02644 241 SVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAF 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PLN02644 321 SVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVEL 392
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
4-391 |
8.92e-158 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 449.48 E-value: 8.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 4 VVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALT 83
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 84 LNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLA---PYVmpsaRTGQRMGHGQLVDSMITDGLWDAFNDYHMGIT 160
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGmhgSYI----RAGAKFGDIKMVDLMQYDGLTDVFSGVFMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 161 AENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKgDPKVFDRDEQPRPDTTADSLAKLRPAFKKDG 240
Cdd:PRK06633 161 AENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKK-TTSLFDHDETVRPDTSLEILSKLRPAFDKNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 241 SVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PRK06633 240 VVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:PRK06633 320 AAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-392 |
4.18e-156 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 445.59 E-value: 4.18e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQvlTAGAGQNPA--RQAAIKAGLPYS 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQ--GYPNGEAPAigRVAALDAGLPVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSmITDGLWDAFNDYH-- 156
Cdd:PRK06205 79 VPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTDMRWGVRGGGVQLHDR-LARGRETAGGRRFpv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 157 ---MGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLR 233
Cdd:PRK06205 158 pggMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTLESLAKLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 234 P---AFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGE 310
Cdd:PRK06205 238 PimgKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 311 LDLIEANEAFAAQALAVGKALEWDAA---RVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVA 387
Cdd:PRK06205 318 IDLIELNEAFAAQVLAVLKEWGFGADdeeRLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLA 397
|
....*
gi 820872863 388 LAIER 392
Cdd:PRK06205 398 AVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-392 |
5.48e-153 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 437.46 E-value: 5.48e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLE-QTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPYS 78
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTG-QRmgHGQLVDSMITdglWDAFNDY-- 155
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFVMGKADSAfSR--QAEIFDTTIG---WRFVNPLmk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 156 ------HMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSL 229
Cdd:PRK09050 156 aqygvdSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 230 AKLRPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLG 309
Cdd:PRK09050 236 AKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 310 ELDLIEANEAFAAQALAVGKALEW--DAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVA 387
Cdd:PRK09050 316 QFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIA 395
|
....*
gi 820872863 388 LAIER 392
Cdd:PRK09050 396 LAIER 400
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-392 |
7.97e-137 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 395.87 E-value: 7.97e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQT-GLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPY 77
Cdd:PRK08947 1 MEDVVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQqTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 78 SVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvmpsartgqrMGHGqlVDSMITDGLWDAFNDYHM 157
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVP-----------MNHG--VDFHPGLSKNVAKAAGMM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 158 GITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPAFK 237
Cdd:PRK08947 148 GLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 238 -KDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEA 316
Cdd:PRK08947 228 pVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872863 317 NEAFAAQALAVGKALEW-DAA--RVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK08947 308 NEAFAAQSLPCLKDLGLlDKMdeKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFER 386
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-392 |
1.96e-136 |
|
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: 395.31 E-value: 1.96e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 2 NDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLE-QTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPYSV 79
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLArNPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSART----GQRMGHGQLVDSMITDGLWDAFNDY 155
Cdd:TIGR02430 81 PGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSafsrSAKIEDTTIGWRFINPLMKALYGVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 156 HMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPA 235
Cdd:TIGR02430 161 SMPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKLKPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 236 FKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIE 315
Cdd:TIGR02430 241 VRPDGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872863 316 ANEAFAAQALAVGKALEW--DAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:TIGR02430 321 LNEAFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIER 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-262 |
3.18e-132 |
|
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: 379.34 E-value: 3.18e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 4 VVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALT 83
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 84 LNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPS-ARTGQRMGHGQLVDSMITDGLWDAFNDYHMGITAE 162
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTdARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 163 NLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPkVFDRDEQPRPDTTADSLAKLRPAFKKDGSV 242
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFDKEGTV 239
|
250 260
....*....|....*....|
gi 820872863 243 TAGNASSLNDGAAAVLLMSA 262
Cdd:pfam00108 240 TAGNASPINDGAAAVLLMSE 259
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
1-391 |
1.18e-126 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 370.38 E-value: 1.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK06954 6 QDPIVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYH-MGI 159
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYLLPKARGGMRMGHGQVLDHMFLDGLEDAYDKGRlMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDpKVFDRDEQPRpDTTADSLAKLRPAFKKD 239
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGD-TVIDRDEQPF-KANPEKIPTLKPAFSKT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 240 GSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEA 319
Cdd:PRK06954 244 GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEA 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 320 FAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:PRK06954 324 FAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-392 |
3.16e-125 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 367.02 E-value: 3.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQT-GLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPY 77
Cdd:PRK09052 5 LQDAYIVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 78 SVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYvmpsartgqrMGHGQLVDSMITDGLWDAFNDYHM 157
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM----------MGNKPSMSPAIFARDENVGIAYGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 158 GITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDP---------KVFDRDEQPRPDTTADS 228
Cdd:PRK09052 155 GLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktRTVDLDEGPRADTSLEG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 229 LAKLRPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQL 308
Cdd:PRK09052 235 LAKLKPVFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 309 GELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVAL 388
Cdd:PRK09052 315 DDLDWIELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAG 394
|
....
gi 820872863 389 AIER 392
Cdd:PRK09052 395 IFER 398
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.42e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 364.46 E-value: 2.42e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPYS 78
Cdd:PRK07661 1 MREAVIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYvmpsartgqrMGHgqLVDSMITdgLWDAFNDYHMG 158
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM----------MGH--VVRPNPR--LVEAAPEYYMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 159 I--TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDP--------KVFDRDEQPRPDTTADS 228
Cdd:PRK07661 147 MghTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGEnnklqeetITFSQDEGVRADTTLEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 229 LAKLRPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQL 308
Cdd:PRK07661 227 LGKLRPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 309 GELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVAL 388
Cdd:PRK07661 307 SDIGLFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAG 386
|
....
gi 820872863 389 AIER 392
Cdd:PRK07661 387 VFEL 390
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-392 |
8.14e-124 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 365.24 E-value: 8.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 2 NDVVIVAATRTAI-GSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQ-NPARQAAIKAGLPYSV 79
Cdd:PLN02287 46 DDVVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARTGQRMGHGQLVDSMITdglwdafndyhMGI 159
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmPQKKGDPK-------VFDRDEQPRPDTTADSLAKL 232
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPV--HTKIVDPKtgeekpiVISVDDGIRPNTTLADLAKL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 233 RPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELD 312
Cdd:PLN02287 273 KPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDID 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 313 LIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKR--DAKKGLATLCIGGGQGVALAI 390
Cdd:PLN02287 353 LFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRgkDCRFGVVSMCIGTGMGAAAVF 432
|
..
gi 820872863 391 ER 392
Cdd:PLN02287 433 ER 434
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-391 |
2.47e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 356.63 E-value: 2.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSARtgqRMGHGQLV-------DSMITDGLWDAFN 153
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDL---RWGPKHLLhknykidDAMLVDGLIDAFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 154 DYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmpqkkgdpKVFDRDEQPRpDTTADSLAKLR 233
Cdd:PRK06366 158 FEHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF---------NDLDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 234 PAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDL 313
Cdd:PRK06366 228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872863 314 IEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-392 |
9.25e-117 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 345.17 E-value: 9.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAigsFQGALANVPAVD---------LGAAVIKRLLEQTGLDPAQVDEVILGQVLtaGAGQN---PARQ 68
Cdd:PRK06445 1 LEDVYLVDFARTA---FSRFRPKDPQKDvfnnirpeeLAAMLINRLIEKTGIKPEEIDDIITGCAL--QVGENwlyGGRH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 69 AAIKAGLPYSVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvmpsartgqrMGHGQLVD---SMIT 145
Cdd:PRK06445 76 PIFLARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP-----------MGDNPHIEpnpKLLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 146 DG---LWDAFNDYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMpQKKGDPKVFDRDEQPRP 222
Cdd:PRK06445 145 DPkyiEYDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 223 DTTADSLAKLRPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLD 302
Cdd:PRK06445 224 DTSLEKLAKLPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 303 KAGWQLGELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGG 382
Cdd:PRK06445 304 KAGLSVKDIDLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGG 383
|
410
....*....|
gi 820872863 383 GQGVALAIER 392
Cdd:PRK06445 384 GQGGAVVLER 393
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-392 |
1.34e-114 |
|
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC 2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (TIGR02437). The FadBA complex is the major complex active for beta-oxidation of fatty acids in E. coli. [Fatty acid and phospholipid metabolism, Degradation]
Pssm-ID: 131498 Cd Length: 385 Bit Score: 339.23 E-value: 1.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 3 DVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQ-TGLDPAQVDEVILGQV-LTAGAGQNPARQAAIKAGLPYSV 79
Cdd:TIGR02445 1 DVVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVqQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvmpsartgqrMGHGqlVDSMITDGLWDAFNDYHMGI 159
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP-----------MMHG--VDFHPGMSLHVAKAAGMMGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPAFK-K 238
Cdd:TIGR02445 148 TAEMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDpK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 239 DGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANE 318
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872863 319 AFAAQALAVGK---ALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:TIGR02445 308 AFAAQALPCLKdlgLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFER 384
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-392 |
1.73e-114 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 339.67 E-value: 1.73e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQT-GLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPy 77
Cdd:PRK07851 1 MPEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 78 SVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPY----VMPS----------ARTGQRMGHGQLV--D 141
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgnsdSLPDtknplfaeaqARTAARAEGGAEAwhD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 142 SMITDGLWDAFndYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPqkkgDPKVFDRDEQPR 221
Cdd:PRK07851 160 PREDGLLPDVY--IAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP----DGTVVSTDDGPR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 222 PDTTADSLAKLRPAFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCL 301
Cdd:PRK07851 234 AGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 302 DKAGWQLGELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIG 381
Cdd:PRK07851 314 ARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVG 393
|
410
....*....|.
gi 820872863 382 GGQGVALAIER 392
Cdd:PRK07851 394 GGQGMAMVLER 404
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-392 |
1.28e-111 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 332.13 E-value: 1.28e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPYSV 79
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSART-------------GQRMGHGQLVDSmitd 146
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESafsrdakvfdttiGARFPNPKIVAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 147 glwdaFNDYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQ-KKGDPKVFDRDEQPRPDTT 225
Cdd:PRK08131 157 -----YGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgRKLPPKLVAEDEHPRPSST 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 226 ADSLAKLRPAFKkDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAG 305
Cdd:PRK08131 232 VEALTKLKPLFE-GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 306 WQLGELDLIEANEAFAAQALAVGKAL--EWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGG 383
Cdd:PRK08131 311 LTLDDMDIIEINEAFASQVLGCLKGLgvDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVG 390
|
....*....
gi 820872863 384 QGVALAIER 392
Cdd:PRK08131 391 QGLAMVIER 399
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.49e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 326.46 E-value: 2.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQ--GALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPY 77
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkdGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 78 SVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvMPSArtgqrmGHGQLVDSMItdglwdAFNDYHM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP--MGSD------GGAWAMDPST------NFPTYFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 158 --GITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmpQKKGDPKVFDRDEQPRPDTTADSLAKLRPA 235
Cdd:PRK08242 147 pqGISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV---KDQNGLTILDHDEHMRPGTTMESLAKLKPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 236 FKKDGSV---------------------TAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPV 294
Cdd:PRK08242 224 FAMMGEMggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 295 SATQRCLDKAGWQLGELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKG 374
Cdd:PRK08242 304 PATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTA 383
|
410
....*....|....*...
gi 820872863 375 LATLCIGGGQGVALAIER 392
Cdd:PRK08242 384 LITLCVGGGMGIATIIER 401
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.30e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 310.49 E-value: 2.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAG--AGqNPARQAAIKAGLPYS 78
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpqAG-NIARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvMPSART-GQRMGhgqLVDSMITDGLWDA-FNDYH 156
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIP--ISSAMTaGEQLG---FTSPFAESKGWLHrYGDQE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 157 MG--ITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmpqkkGDpkvFDRDEQPRpDTTADSLAKLRP 234
Cdd:PRK07801 155 VSqfRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GG---VTVDEGPR-ETSLEKMAGLKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 235 aFKKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLI 314
Cdd:PRK07801 225 -LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872863 315 EANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK07801 304 EINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIER 381
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-392 |
4.11e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 311.57 E-value: 4.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK08170 2 ARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMP-----------SART-GQRMGH-GQLVDSM---- 143
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSekmvrwlagwyAAKSiGQKLAAlGKLRPSYlapv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 144 --ITDGLWDAFNDYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKdEITPIVMPqkkgDPKVFDRDEQPR 221
Cdd:PRK08170 162 igLLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLFDR----DGKFYDHDDGVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 222 PDTTADSLAKLRPAF-KKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRC 300
Cdd:PRK08170 237 PDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 301 LDKAGWQLGELDLIEANEAFAAQALAVGKAL-----------------EWDAARVNVNGGAIALGHPIGASGCRVLVTLL 363
Cdd:PRK08170 317 LQRHGLTLEDLDLWEINEAFAAQVLACLAAWadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASGARIVLHLL 396
|
410 420
....*....|....*....|....*....
gi 820872863 364 HEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK08170 397 HALKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-392 |
1.60e-102 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 308.57 E-value: 1.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPYSV 79
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYvmpsartGQRMGHGqLVDSMITDGLWDAFNDYHmgi 159
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPL-------GANAGPG-RGLPRPDSWDIDMPNQFE--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 TAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMP------QKKGDPKVFDRDEQPRpDTTADSLAKLR 233
Cdd:PRK07850 150 AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPvldeegQPTGETRLVTRDQGLR-DTTMEGLAGLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 234 PAFKkDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDL 313
Cdd:PRK07850 229 PVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872863 314 IEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK07850 308 VEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIER 386
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-392 |
7.94e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 304.34 E-value: 7.94e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAG-AGQNPARQAAIKAGLPYSV 79
Cdd:PRK06504 1 MAEAYIVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGeQATNVARNAVLASKLPESV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSArTGQRMGHGQLVDSMITDGLWDAFNDYHMGi 159
Cdd:PRK06504 81 PGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPST-LPAKNGLGHYKSPGMEERYPGIQFSQFTG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 tAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKVFDRDEQPRPDTTADSLAKLRPaFKKD 239
Cdd:PRK06504 159 -AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKL-IAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 240 GSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEA 319
Cdd:PRK06504 237 GRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872863 320 FAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK06504 317 FASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-387 |
1.23e-99 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 301.30 E-value: 1.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIG-SFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLPYS 78
Cdd:PRK07108 1 MTEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLapyvmpsarTGQRMGHGQLVDSMITDGLWDAFndYHMG 158
Cdd:PRK07108 81 VPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISC---------VQNEMNRHMLREGWLVEHKPEIY--WSML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 159 ITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDPKV---------FDRDEQPRPDTTADSL 229
Cdd:PRK07108 150 QTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADKATgrlftkevtVSADEGIRPDTTLEGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 230 AKLRPAFKkDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLG 309
Cdd:PRK07108 230 SKIRSALP-GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872863 310 ELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVA 387
Cdd:PRK07108 309 DIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAA 386
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-392 |
2.58e-94 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 288.81 E-value: 2.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 4 VVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALT 83
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 84 LNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVM--PSARTgqrmghgqLVDSMITDGLWD----------- 150
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVskKLARA--------LVDLNKARTLGQrlklfsrlrlr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 151 -------AFNDY----HMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKgdpKVFDRDEQ 219
Cdd:PRK08963 159 dllpvppAVAEYstglRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYK---QPLEEDNN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 220 PRPDTTADSLAKLRPAF-KKDGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDP-AIMGIGPVSAT 297
Cdd:PRK08963 236 IRGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 298 QRCLDKAGWQLGELDLIEANEAFAAQALAVGKAL-----------------EWDAARVNVNGGAIALGHPIGASGCRVLV 360
Cdd:PRK08963 316 PLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsqaigEVDMSKFNVLGGSIAYGHPFAATGARMIT 395
|
410 420 430
....*....|....*....|....*....|..
gi 820872863 361 TLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK08963 396 QTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
7-391 |
3.36e-89 |
|
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: 274.76 E-value: 3.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 7 VAATRTAIGSF---QGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVPALT 83
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 84 LNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLapyvmpSARTGQRMGHgqlvdsmitdglwdafndyhmgitAEN 163
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMET------SAENNAKEKH------------------------IDV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 164 LVEKYSiSREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKGDpKVFDRDE--QPRPDTTADSLAKLRPAFKKDGS 241
Cdd:cd00826 131 LINKYG-MRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGD-IHSDADEyiQFGDEASLDEIAKLRPAFDKEDF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 242 VTAGNASSLNDGAAAVLLMSAGKA-------KALGLPVLAKIAGYASAGVDPA----IMGIGPVSATQRCLDKAGWQLGE 310
Cdd:cd00826 209 LTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGD 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 311 LDLIEANEAFAAQALAVGKALEWDAAR------------------VNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAK 372
Cdd:cd00826 289 LDLIEAHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGK 368
|
410 420
....*....|....*....|....
gi 820872863 373 -----KGLATLCIGGGQGVALAIE 391
Cdd:cd00826 369 rqgagAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
2-391 |
9.59e-81 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 251.99 E-value: 9.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 2 NDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLleQTGLDPaQVDEVILGQVLtaGAGQNPARQAAIKAGLPYSVPA 81
Cdd:PRK06690 1 NRAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMER-EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 82 LTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYvMPSARTGQrmghgqlvdsmitdglwDAFNDYHMGITA 161
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF-QNRARFSP-----------------ETIGDPDMGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 162 ENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmpqkkgdPKVFDRDEQPRPDTTAdSLAKLRPAFKKDGS 241
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF--------NGLLDESIKKEMNYER-IIKRTKPAFLHNGT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 242 VTAGNASSLNDGAAAVLLMSAGKAKALGL-PVLaKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAF 320
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYkPVL-RFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAF 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872863 321 AAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIE 391
Cdd:PRK06690 288 ASKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-392 |
3.15e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 252.39 E-value: 3.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRT--AIGSF-QGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGA-GQNPARQAAIKAGLP 76
Cdd:PRK06025 1 MAEAYIIDAVRTprGIGKVgKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 77 YSVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSL----APYVMPSARTGQRMGHGQLvdsmitdGLWDAF 152
Cdd:PRK06025 81 IKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYtaamAAEDMAAGKPPLGMGSGNL-------RLRALH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 153 NDYHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIVMPQKKgdpKVFDRDEQPRPDTTADSLAKL 232
Cdd:PRK06025 154 PQSHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGS---VALDHEEFPRPQTTAEGLAAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 233 RPAFKK-------DGSVT-------------------AGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDP 286
Cdd:PRK06025 231 KPAFTAiadypldDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 287 AIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGHPIGASGCRVLVTLLHEM 366
Cdd:PRK06025 311 TLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDEL 390
|
410 420
....*....|....*....|....*.
gi 820872863 367 IKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK06025 391 ERRGLKRGLVTMCAAGGMAPAIIIER 416
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
270-392 |
4.46e-64 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 200.56 E-value: 4.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 270 LPVLAKIAGYASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQALAVGKALEWDAARVNVNGGAIALGH 349
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 820872863 350 PIGASGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
1-392 |
2.67e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 206.29 E-value: 2.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYSVP 80
Cdd:PRK09268 6 VRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 81 ALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMP-----------SART-GQRMGH-GQLVDSMIT-- 145
Cdd:PRK09268 86 AYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNeglrkillelnRAKTtGDRLKAlGKLRPKHLApe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 146 --------DGLwdafndyHMGITAENLVEKYSISREQQDAFAAQSQRKAVAAIDTGRFKDEITPIvmpqkKGdpkvFDRD 217
Cdd:PRK09268 166 iprngeprTGL-------SMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG----LTRD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 218 EQPRPDTTADSLAKLRPAFKK--DGSVTAGNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAGVDpAIMG----- 290
Cdd:PRK09268 230 NNLRPDSSLEKLAKLKPVFGKggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD-FVHGkegll 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 291 IGPVSATQRCLDKAGWQLGELDLIEANEAFAAQALAVGKALE----------WDAA-------RVNVNGGAIALGHPIGA 353
Cdd:PRK09268 309 MAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEdeeycrerlgLDAPlgsidrsKLNVNGSSLAAGHPFAA 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 820872863 354 SGCRVLVTLLHEMIKRDAKKGLATLCIGGGQGVALAIER 392
Cdd:PRK09268 389 TGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
29-390 |
7.54e-22 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 93.66 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 29 LGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPySVPALTLNKVCGSGLKALHLAAQAIRCGDAE 108
Cdd:cd00327 10 LGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGKAD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 109 VVIAGGqenmslapyvmpsartgqrmghgqlvdsmitdglwdafndyhmgitaenlvekysisreqqdafaaqsqrkava 188
Cdd:cd00327 89 IVLAGG-------------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 189 aidtgrfkdeitpivmpqkkgdpkvfdrdeqprpdttadslaklrpafkkdgsvtaGNASSLNDGAAAVLLMSAGKAKAL 268
Cdd:cd00327 95 --------------------------------------------------------SEEFVFGDGAAAAVVESEEHALRR 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 269 GLPVLAKIAGYAS----AGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQALAVGKALEWDA---ARVNVN 341
Cdd:cd00327 119 GAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPdgvRSPAVS 198
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872863 342 GGAIALGHPIGASGCRVLVTLLHEM-------IKRDAKKGLATLCIGGGQGVALAI 390
Cdd:cd00327 199 ATLIMTGHPLGAAGLAILDELLLMLehefippTPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
19-362 |
1.65e-17 |
|
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: 83.08 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 19 GALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPYsVPALTLNKVCGSGLKALHLA 98
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG-KPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 99 AQAIRCGDAEVVIAGGQENMSLAPYV-MPSARTGQRMGHGQLVDSMITDGLWDAFN-DYHMgitaenlvEKYSISREQQD 176
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGdEAGGRASDLEWEGPEPPGGLTPPALYALAaRRYM--------HRYGTTREDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 177 AFAAQSQRKAVA---AIdtgrFKDEITpivMPQKKGDPKVFDRdeqprpdttadslaklrpafkkdgsVTAGNASSLNDG 253
Cdd:cd00829 160 KVAVKNHRNAARnpyAQ----FRKPIT---VEDVLNSRMIADP-------------------------LRLLDCCPVSDG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 254 AAAVLLMSAGKAKALGLPvLAKIAGYASAGVDPAIMGIGP-------VSATQRCLDKAGWQLGELDLIE------ANEAF 320
Cdd:cd00829 208 AAAVVLASEERARELTDR-PVWILGVGAASDTPSLSERDDflsldaaRLAARRAYKMAGITPDDIDVAElydcftIAELL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 820872863 321 AAQAL---AVGKALEWDAAR---------VNVNGGAIALGHPIGASGCRVLVTL 362
Cdd:cd00829 287 ALEDLgfcEKGEGGKLVREGdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEA 340
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-374 |
8.60e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 72.24 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSfqgaLANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAG-AGQ-NPARQAAIKAGLPyS 78
Cdd:PRK06064 1 MRDVAIIGVGQTKFGE----LWDVSLRDLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLfVSQeHIAALIADYAGLA-P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPYVMPSArtgqrmghgqlVDSMITDGLWDAFndyhMG 158
Cdd:PRK06064 76 IPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATE-----------AIARAGDYEWEEF----FG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 159 IT--------AENLVEKYSISREQQDAFAAQSQRKAVAAIDtGRFKDEITpivMPQKKGDPKVfdrdeqprpdttADSLA 230
Cdd:PRK06064 141 ATfpglyaliARRYMHKYGTTEEDLALVAVKNHYNGSKNPY-AQFQKEIT---VEQVLNSPPV------------ADPLK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 231 KLrpafkkdgsvtagNASSLNDGAAAVLLMSAGKAKALGL-PVLAKIAGYASAGVD----PAIMGIGP-VSATQRCLDKA 304
Cdd:PRK06064 205 LL-------------DCSPITDGAAAVILASEEKAKEYTDtPVWIKASGQASDTIAlhdrKDFTTLDAaVVAAEKAYKMA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 305 GWQLGELDLIEANEAFA-AQALAV--------GKAleWDAAR-----------VNVNGGAIALGHPIGASGCRVLVTLLH 364
Cdd:PRK06064 272 GIEPKDIDVAEVHDCFTiAEILAYedlgfakkGEG--GKLARegqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVW 349
|
410
....*....|
gi 820872863 365 EmIKRDAKKG 374
Cdd:PRK06064 350 Q-LRGEAEKG 358
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-355 |
2.61e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 64.58 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 1 MNDVVIVAATRTAIGSfqgaLANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQN-PARQAA-IKAGLPYs 78
Cdd:PRK07516 1 MMTASIVGWAHTPFGK----LDAETLESLIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDfPASLVLqADPALRF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 79 VPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMSLAPyvmpSARTGQRMGHG--QLVDSMITDGLWDAFndyh 156
Cdd:PRK07516 76 KPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATP----TAEVGDILLGAsyLKEEGDTPGGFAGVF---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 157 mGITAENLVEKYSISREQQDAFAAQSQRKAVAaidtgrfkdeiTPIVMPQKKGDPKvFDRDEQPRPDTTADSLAKLrpaf 236
Cdd:PRK07516 148 -GRIAQAYFQRYGDQSDALAMIAAKNHANGVA-----------NPYAQMRKDLGFE-FCRTVSEKNPLVAGPLRRT---- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 237 kkdgsvtagNASSLNDGAAAVLLMSAGKAKALGLPVLAKIAGYAS-----AGVDPAIMGiGPVSATQRCLDKAGWQLGEL 311
Cdd:PRK07516 211 ---------DCSLVSDGAAALVLADAETARALQRAVRFRARAHVNdflplSRRDPLAFE-GPRRAWQRALAQAGVTLDDL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872863 312 DLIEANEAFAAQAL----AVGKALEWDAAR--------------VNVNGGAIALGHPIGASG 355
Cdd:PRK07516 281 SFVETHDCFTIAELieyeAMGLAPPGQGARairegwtakdgklpVNPSGGLKAKGHPIGATG 342
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
28-355 |
7.90e-09 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 56.83 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 28 DLGAAVIKRLLEQTGLDPAQVDEVILGQVltagAGQNPARQAAI-KAGLPySVPALTLNKVCGSGLKALHLAAQAIRCGD 106
Cdd:PRK08256 24 DMAAEAGRAALADAGIDYDAVQQAYVGYV----YGDSTSGQRALyEVGMT-GIPIVNVNNNCSTGSTALFLARQAVRSGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 107 AEVVIAGGQENMSlaPYVMPSARTGQRMGHGQLVDSMITDGLWDAFNDYHM--GITAENLVEKYSISREQQDAFAAQSQR 184
Cdd:PRK08256 99 ADCALALGFEQMQ--PGALGSVWDDRPSPLERFDKALAELQGFDPAPPALRmfGGAGREHMEKYGTTAETFAKIGVKARR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 185 KAVA---AIdtgrFKDEITP-IVMpqkkGDPKVFDRdeqprpdttadsLAKLRpafkkdgsvtagnASSLNDGAAAVLLM 260
Cdd:PRK08256 177 HAANnpyAQ----FRDEYTLeDVL----ASPMIWGP------------LTRLQ-------------CCPPTCGAAAAIVC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 261 SAGKAKALGLPVLAKIAGYA-----SAGVDP--AIMGIG---PVSATQRCLDKAGWQLGELDLIEANEAFAAQAL----A 326
Cdd:PRK08256 224 SEEFARKHGLDRAVEIVAQAmttdtPSTFDGrsMIDLVGydmTRAAAQQVYEQAGIGPEDIDVVELHDCFSANELltyeA 303
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 820872863 327 VGKALEWDAAR--------------VNVNGGAIALGHPIGASG 355
Cdd:PRK08256 304 LGLCPEGEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
28-382 |
1.13e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 53.54 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 28 DLGAAVIKRLLEQTGLDPAQVDEVILGQV---LTAGAGQNPARQAAIKAGLpYSVPALTLNKVCGSGLKALHLAAQAIRC 104
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNFfgeLFAGQGHLGAMPATVHPAL-WGVPASRHEAACASGSVATLAAMADLRA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 105 GDAEVVIAGGQENMSlapyVMPSARTGQRMGHGQLVDSMITDG--LW-DAFNDyhmgiTAENLVEKYSISREQQDAFA-- 179
Cdd:PRK06289 107 GRYDVALVVGVELMK----TVPGDVAAEHLGAAAWTGHEGQDArfPWpSMFAR-----VADEYDRRYGLDEEHLRAIAei 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 180 --AQSQRKAVAAIDTGRFKDEItpivmpqkkgdpkvFDRDEQPRPDTtadslaklrpafkkDGSVTAGNASSLNDGAAAV 257
Cdd:PRK06289 178 nfANARRNPNAQTRGWAFPDEA--------------TNDDDATNPVV--------------EGRLRRQDCSQVTDGGAGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 258 LLMSAGKAKAL-GLPVLAKIAGY--------------ASAGvDPAIMGiGPVSATQRCLDKAGWQLGELDLIEANEAFAA 322
Cdd:PRK06289 230 VLASDAYLRDYaDARPIPRIKGWghrtaplgleqkldRSAG-DPYVLP-HVRQAVLDAYRRAGVGLDDLDGFEVHDCFTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 323 QALAVGKAL-------EWDAAR-----------VNVNGGAIALGHPIGASGCRVLVTLLHEMIKR------DAKKGLATL 378
Cdd:PRK06289 308 SEYLAIDHIgltgpgeSWKAIEngeiaiggrlpINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTagdyqvEGAKTFGTL 387
|
....
gi 820872863 379 CIGG 382
Cdd:PRK06289 388 NIGG 391
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
65-355 |
3.36e-07 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 51.77 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 65 PARQAAIKAGLpySVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGqenmslapyvmpsartgqrmghgqlVDSMI 144
Cdd:cd00834 140 AAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGG-------------------------AEALI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 145 TDGLWDAFNdyhmgitaeNLvekYSISREQQDAFAAqsqrkavaaidtgrfkdeitpivmpqkkgdPKVFDRDeqprpdt 224
Cdd:cd00834 193 TPLTLAGFA---------AL---RALSTRNDDPEKA------------------------------SRPFDKD------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 225 tadslaklrpafkKDGSVtagnassLNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAG-----VDPAIMGIGPVSATQR 299
Cdd:cd00834 224 -------------RDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRA 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872863 300 CLDKAGWQLGELDLI-------EANEafAAQALAVGKALEWDAARVNVNGGAIALGHPIGASG 355
Cdd:cd00834 284 ALADAGLSPEDIDYInahgtstPLND--AAESKAIKRVFGEHAKKVPVSSTKSMTGHLLGAAG 344
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
16-114 |
2.22e-06 |
|
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: 48.40 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 16 SFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLP-----------YSV----- 79
Cdd:pfam00109 77 SPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPrrgspfavgtmPSViagri 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 820872863 80 --------PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGG 114
Cdd:pfam00109 157 syflglrgPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGG 199
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
20-119 |
9.43e-06 |
|
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: 47.03 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 20 ALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILgqvltagAGQNPARQ----AAI---KAGLPySVPALTLNKVCGSGL 92
Cdd:COG0332 45 AAPDETTSDLAVEAARKALEAAGIDPEDIDLIIV-------ATVTPDYLfpstACLvqhKLGAK-NAAAFDINAACSGFV 116
|
90 100
....*....|....*....|....*...
gi 820872863 93 KALHLAAQAIRCGDAE-VVIAGGqENMS 119
Cdd:COG0332 117 YALSVAAALIRSGQAKnVLVVGA-ETLS 143
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
80-114 |
1.92e-05 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 46.40 E-value: 1.92e-05
10 20 30
....*....|....*....|....*....|....*
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGG 114
Cdd:cd00833 162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGG 196
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
253-355 |
3.09e-05 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 45.86 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 253 GAAAVLLMSAGKAKALGLPVLAKIAGYASAG-----VDPAIMGIGPVSATQRCLDKAGWQLGELDLI-------EANEaf 320
Cdd:COG0304 232 GAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAGLSPEDIDYInahgtstPLGD-- 309
|
90 100 110
....*....|....*....|....*....|....*..
gi 820872863 321 AAQALAVGKALEWDAARVNVNggAI--ALGHPIGASG 355
Cdd:COG0304 310 AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAG 344
|
|
| PRK09352 |
PRK09352 |
beta-ketoacyl-ACP synthase 3; |
10-119 |
4.76e-05 |
|
beta-ketoacyl-ACP synthase 3;
Pssm-ID: 236475 [Multi-domain] Cd Length: 319 Bit Score: 44.68 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 10 TRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILGQV----LTAGAGqnPARQAAIKAGlpySVPALTLN 85
Cdd:PRK09352 36 TRTGIKERRIAAPDETTSDLATEAAKKALEAAGIDPEDIDLIIVATTtpdyAFPSTA--CLVQARLGAK---NAAAFDLS 110
|
90 100 110
....*....|....*....|....*....|....*
gi 820872863 86 KVCgSG-LKALHLAAQAIRCGDAEVVIAGGQENMS 119
Cdd:PRK09352 111 AAC-SGfVYALSTADQFIRSGAYKNVLVIGAEKLS 144
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
31-366 |
8.00e-05 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 44.50 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 31 AAVIKRLLEQTGLDPAQ--VDEVILGQVLTA---------GAGQNPARQAAIKAGLPYSvPALTLNKVCGSGLKALHLAA 99
Cdd:PTZ00455 53 ATAIQGTLENTGLDGKAalVDKVVVGNFLGElfssqghlgPAAVGSLGQSGASNALLYK-PAMRVEGACASGGLAVQSAW 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 100 QAIRCGDAEVVIAGGQENMSLApyvmpSARTG----QRMGHGQLvDSMITDGLWDAFNDYHMgitaENLVEKYSISREQQ 175
Cdd:PTZ00455 132 EALLAGTSDIALVVGVEVQTTV-----SARVGgdylARAADYRR-QRKLDDFTFPCLFAKRM----KYIQEHGHFTMEDT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 176 DAFAAqsqrKAVAAIDTgrfkdeiTPIV-MPQKKGDPKVFDRDEQPRPDTTADslaklrPAFKKDGSVTagNASSLNDGA 254
Cdd:PTZ00455 202 ARVAA----KAYANGNK-------NPLAhMHTRKLSLEFCTGASDKNPKFLGN------ETYKPFLRMT--DCSQVSDGG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 255 AAVLLMSAGKAKALGLP----VLAKIAGYASAG------VDPAIMGIGPVSATQRCLDKAGWQLGELDLIEANEAFAAQA 324
Cdd:PTZ00455 263 AGLVLASEEGLQKMGLSpndsRLVEIKSLACASgnlyedPPDATRMFTSRAAAQKALSMAGVKPSDLQVAEVHDCFTIAE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 325 LAVGKAL---EWDAAR---------------VNVNGGAIALGHPIGASGCRVLVTLLHEM 366
Cdd:PTZ00455 343 LLMYEALgiaEYGHAKdlirngatalegripVNTGGGLLSFGHPVGATGVKQIMEVYRQM 402
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
61-114 |
1.02e-04 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 43.86 E-value: 1.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 820872863 61 AGQNPARQAAIK----AGLPYSVPALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGG 114
Cdd:smart00825 66 AGIDPESLRGSRtgvfVGVSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGG 123
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
9-119 |
1.54e-04 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 43.30 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 9 ATRTAIGSFQGALANVPAVDLGAAVIKRLLEQTGLDPAQVDEVILgqvltagAGQNPARQ----AAI---KAGLPySVPA 81
Cdd:cd00830 33 RTRTGIRERRIADPGETTSDLAVEAAKKALEDAGIDADDIDLIIV-------ATSTPDYLfpatACLvqaRLGAK-NAAA 104
|
90 100 110
....*....|....*....|....*....|....*...
gi 820872863 82 LTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGQENMS 119
Cdd:cd00830 105 FDINAACSGFLYGLSTAAGLIRSGGAKNVLVVGAETLS 142
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
80-114 |
2.87e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 43.32 E-value: 2.87e-04
10 20 30
....*....|....*....|....*....|....*
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGG 114
Cdd:COG3321 166 PSVTVDTACSSSLVAVHLACQSLRSGECDLALAGG 200
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
250-355 |
3.52e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 42.35 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 250 LNDGAAAVLLMSAGKAKALGLPVLAKIAGY-----ASAGVDPAIMGIGPVSATQRCLDKAGWQLGELDLIEA-------N 317
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrlN 287
|
90 100 110
....*....|....*....|....*....|....*...
gi 820872863 318 EAFAAQALAvgkalEWDAARVNVNGGAIALGHPIGASG 355
Cdd:PRK05952 288 DQREANLIQ-----ALFPHRVAVSSTKGATGHTLGASG 320
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
80-371 |
7.72e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 41.27 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 80 PALTLNKVCGSGLKALHLAAQAIRCGDAEVVIAGGqenmslapyvmpsartgqrmghgqlVDSMITDGLwdafndyhmgi 159
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGG-------------------------VEDPLEEGL----------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 160 taenlvekysisreqqDAFAAQSqrkavaAIDTGRFKDEitpivmpqkkgdpkvfdrdEQPRPDTTAdslaklrpafkKD 239
Cdd:cd00828 198 ----------------SGFANMG------ALSTAEEEPE-------------------EMSRPFDET-----------RD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 240 GSVTAGnasslndGAAAVLLMSAGKAKALGLPVLAKIAGYASAgVDPAIMGI-----GPVSATQRCLDKAGWQLGELDLI 314
Cdd:cd00828 226 GFVEAE-------GAGVLVLERAELALARGAPIYGRVAGTAST-TDGAGRSVpaggkGIARAIRTALAKAGLSLDDLDVI 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872863 315 EA----------NEAFAAQALA--VGKALEWDAARVNVnggaialGHPIGASGcRVLVTLLHEMIKRDA 371
Cdd:cd00828 298 SAhgtstpandvAESRAIAEVAgaLGAPLPVTAQKALF-------GHSKGAAG-ALQLIGALQSLEHGL 358
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
250-355 |
1.67e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 40.16 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872863 250 LNDGAAAVLLMSAGKAKALGLPVLAKIAGYASAG-----VDPAIMGIGPVSATQRCLDKAGWQLGELDLIEA-------N 317
Cdd:PRK07314 230 MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYINAhgtstpaG 309
|
90 100 110
....*....|....*....|....*....|....*...
gi 820872863 318 EAFAAQalAVGKALEWDAARVNVNGGAIALGHPIGASG 355
Cdd:PRK07314 310 DKAETQ--AIKRVFGEHAYKVAVSSTKSMTGHLLGAAG 345
|
|
| |
