|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
4-393 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 694.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 4 PSIVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATA 83
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 84 WGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHA-AHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITA 162
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVlPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 163 ENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRPAFDKDGT 241
Cdd:PRK05790 162 ENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDGT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 242 VTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFA 321
Cdd:PRK05790 242 VTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516620718 322 AQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK05790 322 AQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| 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: 593.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAA-HLRGGVKMgDMKMIDTMIKDGLTDAFHGYHMGITAEN 164
Cdd:COG0183 84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLpKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETAEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 165 VARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVTA 244
Cdd:COG0183 163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 245 ANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQA 324
Cdd:COG0183 243 GNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 325 CAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:COG0183 323 LAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
7-392 |
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: 588.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 7 VIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWGV 86
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 87 NQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITAENVA 166
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 167 RQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVTAAN 246
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 247 ASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACA 326
Cdd:cd00751 241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516620718 327 VTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEA 392
Cdd:cd00751 321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
8-391 |
8.34e-176 |
|
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: 494.82 E-value: 8.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWGVN 87
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 88 QLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHA--AHLRGGVKMGDMKMIDTMIKDgLTDAFHGYHMGITAENV 165
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGvpRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 166 ARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVTAA 245
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 246 NASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQAC 325
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516620718 326 AVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
6-393 |
7.15e-169 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 477.60 E-value: 7.15e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITAENV 165
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAENI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 166 ARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVTAA 245
Cdd:PRK06633 165 SKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGVVTAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 246 NASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQAC 325
Cdd:PRK06633 245 NASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSI 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 326 AVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK06633 325 YVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
2-393 |
6.53e-168 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 475.22 E-value: 6.53e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 2 SNPSIVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAgEGQNP--ARQAAMKAGIPQ 79
Cdd:PRK09051 1 MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPT-EPRDMylSRVAAINAGVPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 80 EATAWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAA-HLRGGVKMGDMKMIDTMIKdGLTDAFHGYHM 158
Cdd:PRK09051 80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVDMMVG-ALHDPFGTIHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 159 GITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDK 238
Cdd:PRK09051 159 GVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 239 D-GTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEAN 317
Cdd:PRK09051 239 EnGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEAN 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516620718 318 EAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK09051 319 EAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
6-391 |
1.07e-166 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 472.07 E-value: 1.07e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHA-AHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITAEN 164
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVlPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 165 VARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRPAFDKDGTVT 243
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEpLAFATDEQPRAGTTAESLAKLKPAFKKDGSVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 244 AANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQ 323
Cdd:PRK05656 244 AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQ 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 324 ACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK05656 324 SLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
7-391 |
4.71e-146 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 419.50 E-value: 4.71e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 7 VIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWGV 86
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 87 NQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHA-AHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITAENV 165
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYIlPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 166 ARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRPAFDKDGTVTA 244
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDpIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 245 ANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQA 324
Cdd:PRK08235 245 GNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVA 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516620718 325 CAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK08235 325 LASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
9-391 |
6.82e-146 |
|
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: 419.21 E-value: 6.82e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 9 ASAGRTAVGAFNG---AFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:cd00826 1 AGAAMTAFGKFGGengADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMaphaahlrggvkmgdmkmidtmikdgltdafhgyhmgiTAENV 165
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMET--------------------------------------SAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 166 ARQWQL--------SRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHG--ATIEAMGKLRPA 235
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGdeASLDEIAKLRPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 236 FDKDGTVTAANASGLNDGAAVAVLMSEAEA-------VRRGIQPLARIVSWATAGVDPQ----IMGTGPIPASRKALEKA 304
Cdd:cd00826 203 FDKEDFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 305 GWSVNDLDLVEANEAFAAQACAVTKDLGWDP------------------SIVNVNGGAIAIGHPIGASGARVLNTLLFEM 366
Cdd:cd00826 283 GLGIGDLDLIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFEL 362
|
410 420 430
....*....|....*....|....*....|
gi 516620718 367 KRR-----GAKKGLATLCIGGGMGVAMCFE 391
Cdd:cd00826 363 KGEagkrqGAGAGLALLCIGGGGGAAMCIE 392
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
6-392 |
2.12e-142 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 410.92 E-value: 2.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAH-LRGGVKMGDMKMIDTMIKDGLTD--AFHGYHMGI-- 160
Cdd:PRK06205 84 LDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDRLARGRETAggRRFPVPGGMie 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 161 TAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRP---AF 236
Cdd:PRK06205 164 TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPRADTTLESLAKLRPimgKQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 237 DKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEA 316
Cdd:PRK06205 244 DPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIEL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 317 NEAFAAQACAVTKDLGW---DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEA 392
Cdd:PRK06205 324 NEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFER 402
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
8-391 |
2.53e-129 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 377.37 E-value: 2.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVGAFNGAFATVLAHELGAAVIKGALER-AGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK09050 6 ICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPGTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAahlrggvkMG--------DMKMIDTMIK----DGLTDAF 153
Cdd:PRK09050 86 INRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFV--------MGkadsafsrQAEIFDTTIGwrfvNPLMKAQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 154 HGYH-MGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGK 231
Cdd:PRK09050 158 YGVDsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPRPETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 232 LRPAFDKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDL 311
Cdd:PRK09050 238 LKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 312 DLVEANEAFAAQACAVTKDLGW--DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMC 389
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397
|
..
gi 516620718 390 FE 391
Cdd:PRK09050 398 IE 399
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
6-263 |
5.32e-126 |
|
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: 363.55 E-value: 5.32e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAA--HLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITAE 163
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALptDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 164 NVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVT 243
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
gi 516620718 244 AANASGLNDGAAVAVLMSEA 263
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
4-393 |
3.81e-125 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 366.73 E-value: 3.81e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 4 PSIVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATA 83
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 84 WGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPH-AAHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGITA 162
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 163 ENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD--VTVDADEYIRHgATIEAMGKLRPAFDKD- 239
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGK-FDPAKLRKLRPSFKEDg 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 240 GTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEA 319
Cdd:PLN02644 240 GSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516620718 320 FAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PLN02644 320 FSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
7-393 |
1.37e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 349.82 E-value: 1.37e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 7 VIASAGRTAVG-AFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAW 84
Cdd:PRK07661 5 VIVAGARTPVGkAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 85 GVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAH-LRGGVKmgdmkmidtmikdgLTDAFHGYHMGI--T 161
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGHvVRPNPR--------------LVEAAPEYYMGMghT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 162 AENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD---------VTVDADEYIRHGATIEAMGKL 232
Cdd:PRK07661 151 AEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGennklqeetITFSQDEGVRADTTLEILGKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPAFDKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLD 312
Cdd:PRK07661 231 RPAFNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 313 LVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEA 392
Cdd:PRK07661 311 LFELNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFEL 390
|
.
gi 516620718 393 L 393
Cdd:PRK07661 391 L 391
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
8-393 |
6.79e-118 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 348.15 E-value: 6.79e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVG-AFNGAFATVLAHELGAAVIKGALERA-GVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAW 84
Cdd:PRK09052 10 IVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 85 GVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPhaahlrggvKMGDMKMIDTMIKDGLTDAFHGYHMGITAEN 164
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP---------MMGNKPSMSPAIFARDENVGIAYGMGLTAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 165 VARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDV----------TVDADEYIRHGATIEAMGKLRP 234
Cdd:PRK09052 161 VAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktrTVDLDEGPRADTSLEGLAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 235 AFDKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLV 314
Cdd:PRK09052 241 VFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 315 EANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK09052 321 ELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
6-391 |
3.93e-117 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 345.80 E-value: 3.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVG-AFNGAFATVLAHELGAAVIKGALER-AGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEAT 82
Cdd:PRK08947 4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 83 AWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMsmaphaahlrGGVKMgdMKMIDTMIKDGLTDAFHGYHMGITA 162
Cdd:PRK08947 84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM----------GHVPM--NHGVDFHPGLSKNVAKAAGMMGLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 163 ENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRPAFD-KDG 240
Cdd:PRK08947 152 EMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVlKLFDYDEVIRPETTVEALAALRPAFDpVNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 241 TVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAF 320
Cdd:PRK08947 232 TVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAF 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516620718 321 AAQACAVTKDLGWDPSI---VNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK08947 312 AAQSLPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
8-391 |
1.58e-116 |
|
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: 344.84 E-value: 1.58e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVGAFNGAFATVLAHELGAAVIKGALER-AGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAWG 85
Cdd:TIGR02430 5 ICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSVPGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMIK----DGLTDAFHGYH-MGI 160
Cdd:TIGR02430 85 VNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGwrfiNPLMKALYGVDsMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 161 TAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVT-VDADEYIRHGATIEAMGKLRPAFDKD 239
Cdd:TIGR02430 165 TAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLKPVVRPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 240 GTVTAANASGLNDGAAvAVLMSEAEAVRR-GIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANE 318
Cdd:TIGR02430 245 GTVTAGNASGVNDGAA-ALLLASEEAVQRhGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNE 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516620718 319 AFAAQACAVTKDLGW--DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:TIGR02430 324 AFAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIE 398
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
6-391 |
4.11e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 343.80 E-value: 4.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPH-AAHLRGGVKMGDMKMIDTMIKDGLTDAF-HGYHMGITAE 163
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYlLPKARGGMRMGHGQVLDHMFLDGLEDAYdKGRLMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 164 NVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHgATIEAMGKLRPAFDKDGTVT 243
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGTVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 244 AANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQ 323
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 324 ACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
6-391 |
5.11e-113 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 335.44 E-value: 5.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPH--AAHLRGGVKM---GDMKMIDTMIKDGLTDAFHGYHMGI 160
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFllPSDLRWGPKHllhKNYKIDDAMLVDGLIDAFYFEHMGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 161 TAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYiiktrkgdVTVDADEYIRHgATIEAMGKLRPAFDKDG 240
Cdd:PRK06366 164 SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPF--------NDLDRDEGIRK-TTMEDLAKLPPAFDKNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 241 TVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAF 320
Cdd:PRK06366 235 ILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516620718 321 AAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK06366 315 SIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
6-392 |
1.74e-111 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 333.65 E-value: 1.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAV-GAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQ-NPARQAAMKAGIPQEATA 83
Cdd:PLN02287 48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRaNECRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 84 WGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHA--AHLRGGVKMGDMKMiDTMIKdgltdafhgyhMGIT 161
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAweGGVNPRVESFSQAQ-DCLLP-----------MGIT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 162 AENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPyiIKTRKGD--------VTVDADEYIRHGATIEAMGKLR 233
Cdd:PLN02287 196 SENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVP--VHTKIVDpktgeekpIVISVDDGIRPNTTLADLAKLK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 234 PAFDKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDL 313
Cdd:PLN02287 274 PVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 314 VEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRG--AKKGLATLCIGGGMGVAMCFE 391
Cdd:PLN02287 354 FEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFE 433
|
.
gi 516620718 392 A 392
Cdd:PLN02287 434 R 434
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
23-391 |
5.30e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 330.53 E-value: 5.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 23 FATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQN-PARQAAMKAGIPQEATAWGVNQLCGSGLRAVALGM 101
Cdd:PRK06445 27 FNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLARLPYNIPAMAVDRQCASSLTTVSIGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 102 QQIATGDAKIIVAGGQESMSMAPhaahlrggvkMGDMKMIDTMIKdGLTDAFH-------GYHMGITAENVARQWQLSRD 174
Cdd:PRK06445 107 MEIATGMADIVIAGGVEHMTRTP----------MGDNPHIEPNPK-LLTDPKYieydlttGYVMGLTAEKLAEEAGIKRE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 175 DQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTVTAANASGLNDGA 254
Cdd:PRK06445 176 EMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKPDGVITAGNSSPLNSGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 255 AVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWD 334
Cdd:PRK06445 256 SYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 516620718 335 PSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK06445 336 PETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
4-393 |
2.99e-102 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 308.47 E-value: 2.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 4 PSIVIASAGRTAVG-AFNGAFATVLAHELGAAVIKGALERA-GVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQE 80
Cdd:PRK07851 2 PEAVIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 81 ATAwGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMS---------------------MAPHAAHLRGGVKMGDmk 139
Cdd:PRK07851 82 PGT-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtknplfaeaQARTAARAEGGAEAWH-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 140 miDTMIKDGLTDAFHGyhMGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYiikTRKGDVTVDADEY 219
Cdd:PRK07851 159 --DPREDGLLPDVYIA--MGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPV---TLPDGTVVSTDDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 220 IRHGATIEAMGKLRPAFDKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRK 299
Cdd:PRK07851 232 PRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 300 ALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLC 379
Cdd:PRK07851 312 ALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
|
410
....*....|....
gi 516620718 380 IGGGMGVAMCFEAL 393
Cdd:PRK07851 392 VGGGQGMAMVLERL 405
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
4-393 |
7.30e-101 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 304.38 E-value: 7.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 4 PSIVIASAGRTAVG-AFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEA 81
Cdd:PRK07108 2 TEAVIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 82 TAWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHaahlrggvkmgdmKMIDTMIKDGLTDAFHG---YHM 158
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN-------------EMNRHMLREGWLVEHKPeiyWSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 159 GITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD----------VTVDADEYIRHGATIEA 228
Cdd:PRK07108 149 LQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADkatgrlftkeVTVSADEGIRPDTTLEG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 229 MGKLRPAFdKDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSV 308
Cdd:PRK07108 229 VSKIRSAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 309 NDLDLVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAM 388
Cdd:PRK07108 308 DDIDLWELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAG 387
|
....*
gi 516620718 389 CFEAL 393
Cdd:PRK07108 388 LFEVL 392
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
20-387 |
1.30e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 304.11 E-value: 1.30e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 20 NGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAWGVNQLCGSGLRAVA 98
Cdd:PRK08242 20 DGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETVPGVQINRFCASGLEAVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 99 LGMQQIATGDAKIIVAGGQESMSMAPHaahlrgGVKMGDMKMiDTMIkdgltdAFHGYHM--GITAENVARQWQLSRDDQ 176
Cdd:PRK08242 100 LAAAKVRSGWDDLVIAGGVESMSRVPM------GSDGGAWAM-DPST------NFPTYFVpqGISADLIATKYGFSREDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 177 DQFAVSSQNKAEAAQKAGRFTDEIIPyiIKTRKGDVTVDADEYIRHGATIEAMGKLRPAFDKDGTV-------------- 242
Cdd:PRK08242 167 DAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMggfdavalqkypev 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 243 -------TAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVE 315
Cdd:PRK08242 245 erinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAGLTVDDIDLFE 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516620718 316 ANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVA 387
Cdd:PRK08242 325 LNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIA 396
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
13-391 |
9.15e-100 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 302.08 E-value: 9.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 13 RTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAWGVNQLCG 91
Cdd:PRK08131 11 RSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTVNRLCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 92 SGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMI-----KDGLTDAFHGYHMGITAENVA 166
Cdd:PRK08131 91 SGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIgarfpNPKIVAQYGNDSMPETGDNVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 167 RQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKT--RKGDVTVDADEYIRHGATIEAMGKLRPAFDkDGTVTA 244
Cdd:PRK08131 171 AEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQgrKLPPKLVAEDEHPRPSSTVEALTKLKPLFE-GGVVTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 245 ANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQA 324
Cdd:PRK08131 250 GNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEAFASQV 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 325 CAVTKDLG--WDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK08131 330 LGCLKGLGvdFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
6-391 |
2.46e-99 |
|
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: 300.32 E-value: 2.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVG-AFNGAFATVLAHELGAAVIKGALER-AGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEAT 82
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTLEqGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 83 AWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMsmaphaahlrGGVKMgdMKMIDTMIKDGLTDAFHGYHMGITA 162
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHM----------GHVPM--MHGVDFHPGMSLHVAKAAGMMGLTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 163 ENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGDV-TVDADEYIRHGATIEAMGKLRPAFD-KDG 240
Cdd:TIGR02445 150 EMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLkQFDYDEVIRPETTVESLAALRPAFDpKNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 241 TVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAF 320
Cdd:TIGR02445 230 TVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516620718 321 AAQACAVTKDLGWDPSI---VNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:TIGR02445 310 AAQALPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
8-383 |
1.68e-98 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 298.16 E-value: 1.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAG-EGQNPARQAAMKAGIPQEATAWGV 86
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 87 NQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMG------DMKMIDTMIKDGLTDAFHGyhmgi 160
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGftspfaESKGWLHRYGDQEVSQFRG----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 161 tAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYiiktrkGDVTVDadEYIRHgATIEAMGKLRPAFDkDG 240
Cdd:PRK07801 161 -AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GGVTVD--EGPRE-TSLEKMAGLKPLVE-GG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 241 TVTAANASGLNDGAAvAVLMSEAEAVRR-GIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEA 319
Cdd:PRK07801 230 RLTAAVASQISDGAS-AVLLASERAVKRhGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516620718 320 FAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGG 383
Cdd:PRK07801 309 FAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGG 372
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
12-393 |
2.99e-89 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 275.74 E-value: 2.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 12 GRTAVGAFNgafATVLAHELGAAVikgaLERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWGVNQLCG 91
Cdd:PRK08170 18 ARGGPGPFS---ASDLAVAAGRAL----LNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 92 SGLRAVALGMQQIATGDAKIIVAGGQESMSMAP----------------------HAAHLrGGVKMGDMKMIDTMIKdGL 149
Cdd:PRK08170 91 SGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvrwlagwyaaksigqKLAAL-GKLRPSYLAPVIGLLR-GL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 150 TDAFHGYHMGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTdEIIPYIikTRKGDVtVDADEYIRHGATIEAM 229
Cdd:PRK08170 169 TDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF--DRDGKF-YDHDDGVRPDSSMEKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 230 GKLRPAFDKD-GTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSV 308
Cdd:PRK08170 245 AKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 309 NDLDLVEANEAFAAQ--AC-AVTKDLGW--------------DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGA 371
Cdd:PRK08170 325 EDLDLWEINEAFAAQvlAClAAWADEEYcreqlgldgalgelDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGT 404
|
410 420
....*....|....*....|..
gi 516620718 372 KKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK08170 405 KRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
8-393 |
6.97e-85 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 263.51 E-value: 6.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 8 IASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQEATAWGV 86
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEqATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 87 NQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMIKDGLTDAFHGYHMGitAENVA 166
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGMEERYPGIQFSQFTG--AEMMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 167 RQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGD-VTVDADEYIRHGATIEAMGKLRPaFDKDGTVTAA 245
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSgEMHTVDEGIRFDATLEGIAGVKL-IAEGGRLTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 246 NASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQAC 325
Cdd:PRK06504 243 TASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 326 AVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK06504 323 AWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-391 |
1.03e-84 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 263.12 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 1 MSNPsiVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGE-GQNPARQAAMKAGIPQ 79
Cdd:PRK07850 1 MGNP--VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 80 EATAWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLrgGVKMGDMKMIDTMIKDGltDAFHGyhmg 159
Cdd:PRK07850 79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANA--GPGRGLPRPDSWDIDMP--NQFEA---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 160 itAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRK-------GDVTVDADEYIRHgATIEAMGKL 232
Cdd:PRK07850 151 --AERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDeegqptgETRLVTRDQGLRD-TTMEGLAGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPAFDkDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLD 312
Cdd:PRK07850 228 KPVLE-GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDID 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 313 LVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK07850 307 LVEINEAFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
6-392 |
4.63e-83 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 259.92 E-value: 4.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 6 IVIASAGRTAVGAFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWG 85
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 86 VNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAP--------HAAH-LRGGVKMGD-MKMIDTM-IKD------G 148
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskklaRALVdLNKARTLGQrLKLFSRLrLRDllpvppA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 149 LTDAFHGYHMGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRKGdvTVDADEYIRHGATIEA 228
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--PLEEDNNIRGDSTLED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 229 MGKLRPAFD-KDGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDP-QIMGTGPIPASRKALEKAGW 306
Cdd:PRK08963 245 YAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 307 SVNDLDLVEANEAFAAQACAVTK----------DLGW-------DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRR 369
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLANLQmfaserfareKLGRsqaigevDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
|
410 420
....*....|....*....|...
gi 516620718 370 GAKKGLATLCIGGGMGVAMCFEA 392
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
7-393 |
1.14e-76 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 241.59 E-value: 1.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 7 VIASAGRTAVGAFNGAFATVLAHELGAAVIK---GALERagvdagEVDEVILGQVLaaGEGQNPARQAAMKAGIPQEATA 83
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTflsKGMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 84 WGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSMAPHAAHLR-GGVKMGDMKmidtmikdgltdafhgyhMGITA 162
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGDPD------------------MGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 163 ENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYiiktrkGDVtvdADEYIRHGATIEAM-GKLRPAFDKDGT 241
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF------NGL---LDESIKKEMNYERIiKRTKPAFLHNGT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 242 VTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFA 321
Cdd:PRK06690 209 VTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516620718 322 AQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEAL 393
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
4-391 |
2.11e-75 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 240.06 E-value: 2.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 4 PSIVIASAGRTAVG---AFNGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAG-EGQNPARQAAMKAGIPQ 79
Cdd:PRK06025 2 AEAYIIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 80 EATAWGVNQLCGSGLRAVALGMQQIATGDAKIIVAGGQESMSM--APHAAHLRGGVKMGDMKMIDTMIkdgltDAFH-GY 156
Cdd:PRK06025 82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYtaAMAAEDMAAGKPPLGMGSGNLRL-----RALHpQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 157 HMGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPyiIKTRKGDVTVDADEYIRHGATIEAMGKLRPAF 236
Cdd:PRK06025 157 HQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 237 --------DKDGTVT------------------AANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMG 290
Cdd:PRK06025 235 taiadyplDDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 291 TGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRG 370
Cdd:PRK06025 315 NAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRG 394
|
410 420
....*....|....*....|.
gi 516620718 371 AKKGLATLCIGGGMGVAMCFE 391
Cdd:PRK06025 395 LKRGLVTMCAAGGMAPAIIIE 415
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
271-392 |
3.43e-66 |
|
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: 205.95 E-value: 3.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 271 QPLARIVSWATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWDPSIVNVNGGAIAIGHP 350
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 516620718 351 IGASGARVLNTLLFEMKRRGAKKGLATLCIGGGMGVAMCFEA 392
Cdd:pfam02803 82 LGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
20-392 |
5.75e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 194.73 E-value: 5.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 20 NGAFATVLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEATAWGVNQLCGSGLRAVAL 99
Cdd:PRK09268 23 NGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 100 GMQQIATGDAKIIVAGGQESMSMAPHAAH--LR-------------------GGVKMGDMKMIDTMIKDGLTdafhGYHM 158
Cdd:PRK09268 103 VANKIALGQIDSGIAGGVDTTSDAPIAVNegLRkillelnrakttgdrlkalGKLRPKHLAPEIPRNGEPRT----GLSM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 159 GITAENVARQWQLSRDDQDQFAVSSQNKAEAAQKAGRFTDEIIPYIIKTRkgdvtvdaDEYIRHGATIEAMGKLRPAFDK 238
Cdd:PRK09268 179 GEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR--------DNNLRPDSSLEKLAKLKPVFGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 239 --DGTVTAANASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVD----PQIMGTGPIPASRKALEKAGWSVNDLD 312
Cdd:PRK09268 251 ggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGLLMAPAYAVPRLLARNGLTLQDFD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 313 LVEANEAFAAQACAVTK----------DLGW-------DPSIVNVNGGAIAIGHPIGASGARVLNTLLFEMKRRGAKKGL 375
Cdd:PRK09268 331 FYEIHEAFASQVLATLKawedeeycreRLGLdaplgsiDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGL 410
|
410
....*....|....*..
gi 516620718 376 ATLCIGGGMGVAMCFEA 392
Cdd:PRK09268 411 ISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
26-389 |
1.95e-45 |
|
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: 156.84 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 26 VLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPqEATAWGVNQLCGSGLRAVALGMQQIA 105
Cdd:cd00327 5 ITASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 106 TGDAKIIVAGGQESmsmaphaahlrggvkmgdmkmidtmikdgltdafhgyhmgitaenvarqwqlsrddqdqfavssqn 185
Cdd:cd00327 84 NGKADIVLAGGSEE------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 186 kaeaaqkagrftdeiipyiiktrkgdvtvdadeyirhgatieamgklrpafdkdgtvtaanaSGLNDGAAVAVLMSEAEA 265
Cdd:cd00327 98 --------------------------------------------------------------FVFGDGAAAAVVESEEHA 115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 266 VRRGIQPLARIVSWAT----AGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWDPSIV--- 338
Cdd:cd00327 116 LRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrsp 195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 339 NVNGGAIAIGHPIGASGARVLNTLLFEMK-------RRGAKKGLATLCIGGGMGVAMC 389
Cdd:cd00327 196 AVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVV 253
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
29-362 |
3.00e-16 |
|
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: 79.61 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 29 HELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPqEATAWGVNQLCGSGLRAVALGMQQIATGD 108
Cdd:cd00829 17 LELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAAAAAIASGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 109 AKIIVAGGQESMSMAPHAAHLRGGVkmGDMKMIDTMIKDGLTdaFHGYHmGITAENVARQWQLSRDDQDQFAVSSQNKAE 188
Cdd:cd00829 96 ADVVLVVGAEKMSDVPTGDEAGGRA--SDLEWEGPEPPGGLT--PPALY-ALAARRYMHRYGTTREDLAKVAVKNHRNAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 189 AAQKAgrftdeiipyiikTRKGDVTVdaDEYIRHGATIEAMGKLrpafdkdgtvtaaNASGLNDGAAVAVLMSEaEAVRR 268
Cdd:cd00829 171 RNPYA-------------QFRKPITV--EDVLNSRMIADPLRLL-------------DCCPVSDGAAAVVLASE-ERARE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 269 GIQPLARIVSWATA-------GVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLGWDP------ 335
Cdd:cd00829 222 LTDRPVWILGVGAAsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEkgeggk 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 516620718 336 -------SI-----VNVNGGAIAIGHPIGASGARVLNTL 362
Cdd:cd00829 302 lvregdtAIggdlpVNTSGGLLSKGHPLGATGLAQAVEA 340
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
233-356 |
5.46e-08 |
|
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: 54.47 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPaFDK--DGTVtaanasgLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAG-----VDPQIMGTGPIPASRKALEKAG 305
Cdd:cd00834 218 RP-FDKdrDGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAG 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 306 WSVNDLDLV-------EANEAFAAQAC-AVTKDLGWDPSIVNVNGgaiAIGHPIGASGA 356
Cdd:cd00834 290 LSPEDIDYInahgtstPLNDAAESKAIkRVFGEHAKKVPVSSTKS---MTGHLLGAAGA 345
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
26-355 |
1.35e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 52.93 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 26 VLAHELGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQNPARQAAMKAGIPQEaTAWGVNQLCGSGLRAVALGMQQIA 105
Cdd:PRK12578 19 VSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGK-VPLRVEAMCATGLAASLTAYTAVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 106 TGDAKIIVAGGQESMSMAPHAAHL----RGGVKMGDMKMIDTmikdgltdAFHGYHMGITAENVARqwqlsrddqdqFAV 181
Cdd:PRK12578 98 SGLVDMAIAVGVDKMTEVDTSTSLaiggRGGNYQWEYHFYGT--------TFPTYYALYATRHMAV-----------YGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 182 SSQNKAEAAQKAGRFTdeiipyiiktrkgdvTVDADEYIRHGATIEAMGKLR----PafdkdgtVTAANASGLNDGAAVA 257
Cdd:PRK12578 159 TEEQMALVSVKAHKYG---------------AMNPKAHFQKPVTVEEVLKSRaiswP-------IKLLDSCPISDGSATA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 258 VLMSEAEAVRRGIQPLARI--VSWA--TAGVDPQIMGTG---PIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKD 330
Cdd:PRK12578 217 IFASEEKVKELKIDSPVWItgIGYAndYAYVARRGEWVGfkaTQLAARQAYNMAKVTPNDIEVATVHDAFTIAEIMGYED 296
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 516620718 331 LGWDPS------------------IVNVNGGAIAIGHPIGASG 355
Cdd:PRK12578 297 LGFTEKgkggkfieegqsekggkvGVNLFGGLKAKGHPLGATG 339
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
36-357 |
4.64e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 51.44 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 36 IKGALERAGVDAGEVDEVILGQVLAAG--EGQNPARQAAMKAGI-PQEATAwgVNQLCGSGLRAVALGMQQIATGDAKII 112
Cdd:PRK06064 30 GLEALEDAGIDGKDIDAMYVGNMSAGLfvSQEHIAALIADYAGLaPIPATR--VEAACASGGAALRQAYLAVASGEADVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 113 VAGGQESMSMAPHAAHLRGGVKMGDMKMIDTMikdGLTdaFHGYHmGITAENVARQWQLSRDDQDQFAVSSQNKAEAAQK 192
Cdd:PRK06064 108 LAAGVEKMTDVPTPDATEAIARAGDYEWEEFF---GAT--FPGLY-ALIARRYMHKYGTTEEDLALVAVKNHYNGSKNPY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 193 AgRFTDEIipyiiktrkgdvtvdadeyirhgaTIEAMGKLRPAFDKdgtVTAANASGLNDGAAVAVLMSEaEAVRRGIQP 272
Cdd:PRK06064 182 A-QFQKEI------------------------TVEQVLNSPPVADP---LKLLDCSPITDGAAAVILASE-EKAKEYTDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 273 LARIVSWATA-------------GVDPQIMgtgpipASRKALEKAGWSVNDLDLVEANEAFA-AQACAVtKDLGW----- 333
Cdd:PRK06064 233 PVWIKASGQAsdtialhdrkdftTLDAAVV------AAEKAYKMAGIEPKDIDVAEVHDCFTiAEILAY-EDLGFakkge 305
|
330 340 350
....*....|....*....|....*....|....*..
gi 516620718 334 ------------DPSI-VNVNGGAIAIGHPIGASGAR 357
Cdd:PRK06064 306 ggklaregqtyiGGDIpVNPSGGLKAKGHPVGATGVS 342
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
233-356 |
1.51e-06 |
|
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: 49.71 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPaFDK--DGTVTAanasglnDGAAVAVLMSEAEAVRRGIQPLARIVSWATAG-----VDPQIMGTGPIPASRKALEKAG 305
Cdd:COG0304 218 RP-FDKdrDGFVLG-------EGAGVLVLEELEHAKARGAKIYAEVVGYGASSdayhiTAPAPDGEGAARAMRAALKDAG 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 306 WSVNDLDLV-------EANEafAAQACAVTKDLGWDPSIVNVNggAI--AIGHPIGASGA 356
Cdd:COG0304 290 LSPEDIDYInahgtstPLGD--AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
249-356 |
3.76e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 48.51 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 249 GLNDGAAVAVLMSEAEAVRRGIQPLARIVSW-----ATAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEA------- 316
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAhgtatrl 286
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 516620718 317 NEAFAAQACAVtkdlgWDPSIVNVNGGAIAIGHPIGASGA 356
Cdd:PRK05952 287 NDQREANLIQA-----LFPHRVAVSSTKGATGHTLGASGA 321
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
248-382 |
2.45e-05 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 46.22 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 248 SGLNDGAAVAVLMSEAEAVR-RGIQPLARIVSWA--TAGV-----------DPQIMgtgpiPASRK----ALEKAGWSVN 309
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDyADARPIPRIKGWGhrTAPLgleqkldrsagDPYVL-----PHVRQavldAYRRAGVGLD 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 310 DLDLVEANEAFAAQACAVTKDLG-------W----DPSI-------VNVNGGAIAIGHPIGASGARVLNTLLFEMKRR-- 369
Cdd:PRK06289 295 DLDGFEVHDCFTPSEYLAIDHIGltgpgesWkaieNGEIaiggrlpINPSGGLIGGGHPVGASGVRMLLDAAKQVTGTag 374
|
170
....*....|....*...
gi 516620718 370 -----GAKKGLaTLCIGG 382
Cdd:PRK06289 375 dyqveGAKTFG-TLNIGG 391
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
242-376 |
3.29e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 45.67 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 242 VTAANASGLNDGAAVAVLMSEAEAVRRGIQPLarIVSWATAGVD---PQIMGTGPIP----------------------- 295
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPV--LIKAIGTGSDtlrLADRPFGEVPllpnespddykdlrypgvhsfra 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 296 ---ASRKALEKAGWS--VNDLDLVEANEAFAAQACAVTKDLGW-------------DPSI-----VNVNGGAIAIGHPIG 352
Cdd:PRK06365 295 grmAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgKPELpgklpVNPSGGLLAAGHAVG 374
|
170 180 190
....*....|....*....|....*....|....*..
gi 516620718 353 ASGARVLNTLLFEMKRR-------------GAKKGLA 376
Cdd:PRK06365 375 ATGIMQAVFMFWQLQGRikkhfhddylqvkNAKRGLI 411
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
31-387 |
5.44e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 44.94 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 31 LGAAVIKGALERAGVDAGEVDEVILGQVLAAGEGQN-PARQAAMKAGIPQEATAWGVNQLCGSGLRAVALGMQQIATGDA 109
Cdd:PRK07516 25 LIVRVAREALAHAGIAAGDVDGIFLGHFNAGFSPQDfPASLVLQADPALRFKPATRVENACATGSAAVYAALDAIEAGRA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 110 KIIVAGGQESMSMAPhaahlrgGVKMGDMKMIDTMIKDGlTDAFHGYhMGITAENVARQWQLSRDDQDQFA-VSSQNKAE 188
Cdd:PRK07516 105 RIVLVVGAEKMTATP-------TAEVGDILLGASYLKEE-GDTPGGF-AGVFGRIAQAYFQRYGDQSDALAmIAAKNHAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 189 AAQKagrftdeiiPYiiktrkgdvtvdadeyirhgatieamGKLRPAFDKD--GTVTAAN-----------ASGLNDGAA 255
Cdd:PRK07516 176 GVAN---------PY--------------------------AQMRKDLGFEfcRTVSEKNplvagplrrtdCSLVSDGAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 256 VAVLMSEAEAVRrgiqpLARIVSW-ATAGV---------DPQIMgTGPIPASRKALEKAGWSVNDLDLVEANEAF----- 320
Cdd:PRK07516 221 ALVLADAETARA-----LQRAVRFrARAHVndflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDCFtiael 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 321 ----------AAQACAVTKDlGW---DPSI-VNVNGGAIAIGHPIGASG-------ARVLNTLLFEMKRRGAKkgLATLC 379
Cdd:PRK07516 295 ieyeamglapPGQGARAIRE-GWtakDGKLpVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAK--LAGVF 371
|
....*...
gi 516620718 380 IGGGMGVA 387
Cdd:PRK07516 372 NMGGAAVA 379
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
233-356 |
6.13e-05 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 44.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPaFDKD--GTVtaanasgLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAG-----VDPQIMGTGPIPASRKAL-EKA 304
Cdd:PTZ00050 226 RP-FDKDraGFV-------MGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSdahhiTAPHPDGRGARRCMENALkDGA 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516620718 305 GWSVNDLDLVEAN----------EAFAAQAcaVTKDLGWDPSIVNVNGGAIaiGHPIGASGA 356
Cdd:PTZ00050 298 NININDVDYVNAHatstpigdkiELKAIKK--VFGDSGAPKLYVSSTKGGL--GHLLGAAGA 355
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
233-356 |
7.44e-05 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 44.39 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 233 RPaFDK--DGTVtaanasgLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAG-----VDPQIMGTGPIPASRKALEKAG 305
Cdd:PRK07314 219 RP-FDKdrDGFV-------MGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAG 290
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 306 WSVNDLDLVEA-------NEAFAAQacAVTKDLGWDPSIVNVNGGAIAIGHPIGASGA 356
Cdd:PRK07314 291 INPEDIDYINAhgtstpaGDKAETQ--AIKRVFGEHAYKVAVSSTKSMTGHLLGAAGA 346
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
29-355 |
1.56e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 43.35 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 29 HELGAAVIKGALERAGVDAGEVDEVILGQVLAAG-EGQNPARQAAMkAGIPqeatAWGVNQLCGSGLRAVALGMQQIATG 107
Cdd:PRK08256 23 PDMAAEAGRAALADAGIDYDAVQQAYVGYVYGDStSGQRALYEVGM-TGIP----IVNVNNNCSTGSTALFLARQAVRSG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 108 DAKIIVAGGQESMS--------------MAPHAAHLRGGVKMGDMKMIDTMikdgltdaFHG---YHM---GITAENVAR 167
Cdd:PRK08256 98 AADCALALGFEQMQpgalgsvwddrpspLERFDKALAELQGFDPAPPALRM--------FGGagrEHMekyGTTAETFAK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 168 qwqlsrddqdqfaVSSQNKAEAAQKA-GRFTDEiipyiiktrkgdVTVDadeyirhgatiEAMGKlRPAFDKdgtVTAAN 246
Cdd:PRK08256 170 -------------IGVKARRHAANNPyAQFRDE------------YTLE-----------DVLAS-PMIWGP---LTRLQ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 247 ASGLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIP----------ASRKALEKAGWSVNDLDLVEA 316
Cdd:PRK08256 210 CCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMTTDTPSTFDGRSMIdlvgydmtraAAQQVYEQAGIGPEDIDVVEL 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 516620718 317 NEAFAAQACAVTKDLGWDPS------------------IVNVNGGAIAIGHPIGASG 355
Cdd:PRK08256 290 HDCFSANELLTYEALGLCPEgeaekfiddgdntyggrwVVNPSGGLLSKGHPLGATG 346
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
252-367 |
1.57e-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: 43.39 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 252 DGAAVAVLMSEAEAVRRGIQPLARIVSWA-----TAGVDPQIMGTGPIPASRKALEKAGWSVNDLDLVEANEAFAAQACA 326
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 516620718 327 VTKDLGWD---PSIVNVNGGAIAIGHPIGASGARVLNTLLFEMK 367
Cdd:cd00825 241 KELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
230-356 |
1.75e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 43.57 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 230 GKLRPaFDKD--GTVtaanasgLNDGAAVAVLMSEAEAVRRGIQPLARIVSWATAG-----VDPQIMGTGPIPASRKALE 302
Cdd:PRK07910 226 GACRP-FDKDrdGFV-------FGEGGALMVIETEEHAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTRAIE 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 303 KAGWSVNDLDLVEANEAFA-----AQACAVTKDLGWDPSIVNVNGGAIaiGHPIGASGA 356
Cdd:PRK07910 298 LAGLTPGDIDHVNAHATGTsvgdvAEGKAINNALGGHRPAVYAPKSAL--GHSVGAVGA 354
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
248-367 |
2.97e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 42.57 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516620718 248 SGLNDGAAVAVLMSEAEAVRRGIQP----LARIVSWATAG-------VDPQIMGTGpIPASRKALEKAGWSVNDLDLVEA 316
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASgnlyedpPDATRMFTS-RAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 317 NEAFAAQACAVTKDLGW-DPS-----------------IVNVNGGAIAIGHPIGASGARVLNTLLFEMK 367
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaEYGhakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
253-316 |
5.97e-04 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 41.56 E-value: 5.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516620718 253 GAAVAVLMSEAEAVRRGIQPLARIVSW-----ATAGVDPQImgTGPIPASRKALEKAGWSVNDLDLVEA 316
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWsmrldANRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYVNP 306
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
253-316 |
6.67e-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: 41.66 E-value: 6.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516620718 253 GAAVAVLMSEAEAVRRGIQPLARIVSWATAGVDPQIMGTGPIPAS----RKALEKAGWSVNDLDLVEA 316
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIaraiRTALAKAGLSLDDLDVISA 299
|
|
| ASKHA_NBD_HSP70_DDRA |
cd24030 |
nucleotide-binding domain (NBD) of diol dehydratase-reactivating factor large subunit (DDRA) ... |
292-332 |
6.70e-03 |
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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: 37.96 E-value: 6.70e-03
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....*....|....*....|....*....|....*....|.
gi 516620718 292 GPIPASRKALEKAGWSVNDLDLVEANEAFAAQACAVTKDLG 332
Cdd:cd24030 47 GIIKALELALEKAGINLSDIDLIRLNEAMQQIARELEEELG 87
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