|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
2-387 |
0e+00 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 701.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK05790 4 VVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPALT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC-AHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 160
Cdd:PRK05790 84 INKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPHVlPGSRWGQKMGDVELVDTMIHDGLTDAFNGYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGTVT 239
Cdd:PRK05790 164 LAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDpVVVDTDEHPRPDTTAESLAKLRPAFDKDGTVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 240 AGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQ 319
Cdd:PRK05790 244 AGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEINEAFAAQ 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 320 ACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK05790 324 ALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVE 391
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
2-389 |
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: 607.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:COG0183 4 VVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPAVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA-HLRGGVKMgDFKMIDTMIKDGLTDAFYGYHMGTTAEN 160
Cdd:COG0183 84 VNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLpKARWGYRM-NAKLVDPMINPGLTDPYTGLSMGETAEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTA 240
Cdd:COG0183 163 VAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 241 GNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQA 320
Cdd:COG0183 243 GNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINEAFAAQV 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 321 CAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:COG0183 323 LAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
3-387 |
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: 605.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGM 82
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 83 NQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVA 162
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLDDGLTDPFTGLSMGITAENVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 163 KQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGN 242
Cdd:cd00751 161 EKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDGTVTAGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 243 ASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACA 322
Cdd:cd00751 241 ASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFAAQALA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1DLV_A 323 VNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:cd00751 321 CLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIE 385
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
4-387 |
2.47e-179 |
|
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: 503.68 E-value: 2.47e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMN 83
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 84 QLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAP--HCAHLRGGVKMGDFKMIDTMIKDgLTDAFYGYHMGTTAENV 161
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPygVPRSLRWGVKPGNAELEDARLKD-LTDANTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 162 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAG 241
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDGTVTAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 242 NASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQAC 321
Cdd:TIGR01930 240 NSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFAAQVL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DLV_A 322 AVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:TIGR01930 320 ACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
5-388 |
1.37e-173 |
|
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: 489.31 E-value: 1.37e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 5 ASAARTAVGSF---NGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:cd00826 1 AGAAMTAFGKFggeNGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSmaphcahlrggvkmgdfkmidtmikdgltdafygyhmgTTAENV 161
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKME--------------------------------------TSAENN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 162 AKQWQL--------SRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHG--ATLDSMAKLRPA 231
Cdd:cd00826 123 AKEKHIdvlinkygMRACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVKGRKGDIHSDADEYIQFGdeASLDEIAKLRPA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 232 FDKEGTVTAGNASGLNDGAAAALLMSEAEAS-------RRGIQPLGRIVSWATVGVDPK----VMGTGPIPASRKALERA 300
Cdd:cd00826 203 FDKEDFLTAGNACGLNDGAAAAILMSEAEAQkhglqskAREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 301 GWKIGDLDLVEANEAFAAQACAVNKDLGWDP------------------SIVNVNGGAIAIGHPIGASGARILNTLLFEM 362
Cdd:cd00826 283 GLGIGDLDLIEAHDAFAANACATNEALGLCPegqggalvdrgdntyggkSIINPNGGAIAIGHPIGASGAAICAELCFEL 362
|
410 420 430
....*....|....*....|....*....|.
1DLV_A 363 KRR-----GARKGLATLCIGGGMGVAMCIES 388
Cdd:cd00826 363 KGEagkrqGAGAGLALLCIGGGGGAAMCIES 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
2-389 |
6.21e-170 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 480.23 E-value: 6.21e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAgEGQNP--ARQAAMKAGVPQEATA 79
Cdd:PRK09051 5 VVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPT-EPRDMylSRVAAINAGVPQETPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 80 WGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA-HLRGGVKMGDFKMIDTMIKdGLTDAFYGYHMGTTA 158
Cdd:PRK09051 84 FNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLpAARWGARMGDAKLVDMMVG-ALHDPFGTIHMGVTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 159 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKE-GT 237
Cdd:PRK09051 163 ENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVFDTDEHVRADTTLEDLAKLKPVFKKEnGT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 238 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFA 317
Cdd:PRK09051 243 VTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEANEAFA 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1DLV_A 318 AQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK09051 323 AQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
2-387 |
4.57e-167 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 472.84 E-value: 4.57e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK05656 4 VVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC-AHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 160
Cdd:PRK05656 84 LNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVlPGARTGLRMGHAQLVDSMITDGLWDAFNDYHMGITAEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGTVT 239
Cdd:PRK05656 164 LVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEpLAFATDEQPRAGTTAESLAKLKPAFKKDGSVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 240 AGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQ 319
Cdd:PRK05656 244 AGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEANEAFAAQ 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 320 ACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK05656 324 SLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
2-389 |
2.05e-164 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 466.04 E-value: 2.05e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK06633 5 VYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPGYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENV 161
Cdd:PRK06633 85 INKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKFGDIKMVDLMQYDGLTDVFSGVFMGITAENI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 162 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAG 241
Cdd:PRK06633 165 SKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGVVTAG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 242 NASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQAC 321
Cdd:PRK06633 245 NASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSI 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 322 AVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK06633 325 YVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
3-387 |
5.00e-150 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 429.52 E-value: 5.00e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGM 82
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 83 NQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENV 161
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYiLPGARWGYRMGDNEVIDLMVADGLTCAFSGVHMGVYGGEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 162 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRPAFDKEGTVTA 240
Cdd:PRK08235 165 AKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDpIVVAKDEAPRKDTTIEKLAKLKPVFDKTGTITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 241 GNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQA 320
Cdd:PRK08235 245 GNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEAFAAVA 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1DLV_A 321 CAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK08235 325 LASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
2-387 |
1.46e-144 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 415.93 E-value: 1.46e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK06205 4 AVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPGMQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAH-LRGGVKMGDFKMIDTMIKDGLTD--AFYGY--HMGT 156
Cdd:PRK06205 84 LDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFYTTdMRWGVRGGGVQLHDRLARGRETAggRRFPVpgGMIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 157 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAKLRP---AF 232
Cdd:PRK06205 164 TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDpTVVDRDEHPRADTTLESLAKLRPimgKQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 233 DKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEA 312
Cdd:PRK06205 244 DPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLDDIDLIEL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 313 NEAFAAQACAVNKDLGW---DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK06205 324 NEAFAAQVLAVLKEWGFgadDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFE 401
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
2-259 |
4.36e-133 |
|
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: 381.65 E-value: 4.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCA--HLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAE 159
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALptDARSGLKHGDEKKHDLLIPDGLTDAFNGYHMGLTAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 160 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVT 239
Cdd:pfam00108 161 NVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTVDKDEGIRPPTTAEPLAKLKPAFDKEGTVT 240
|
250 260
....*....|....*....|
1DLV_A 240 AGNASGLNDGAAAALLMSEA 259
Cdd:pfam00108 241 AGNASPINDGAAAVLLMSES 260
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
4-387 |
1.55e-130 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 380.45 E-value: 1.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK09050 6 ICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARnPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVSVPGTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCahlrggvkMG--------DFKMIDTMIK----DGLTDAF 149
Cdd:PRK09050 86 INRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFV--------MGkadsafsrQAEIFDTTIGwrfvNPLMKAQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 150 YGYH-MGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD-ITVDADEYIRHGATLDSMAK 227
Cdd:PRK09050 158 YGVDsMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDpVVVDRDEHPRPETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 228 LRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDL 307
Cdd:PRK09050 238 LKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 308 DLVEANEAFAAQACAVNKDLGW--DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMC 385
Cdd:PRK09050 318 DVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIALA 397
|
..
1DLV_A 386 IE 387
Cdd:PRK09050 398 IE 399
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-389 |
1.35e-125 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 367.50 E-value: 1.35e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PLN02644 3 VCIVGVARTPIGGFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTICTT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 160
Cdd:PLN02644 83 VNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKyLPEARKGSRLGHDTVVDGMLKDGLWDVYNDFGMGVCAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD--ITVDADEYIRHgATLDSMAKLRPAFDKE-GT 237
Cdd:PLN02644 163 CADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRpsVIVDKDEGLGK-FDPAKLRKLRPSFKEDgGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 238 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFA 317
Cdd:PLN02644 242 VTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEINEAFS 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1DLV_A 318 AQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PLN02644 322 VVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
2-387 |
7.31e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 355.74 E-value: 7.31e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPH-CAHLRGGVKMGDFKMIDTMIKDGLTDAF-YGYHMGTTAE 159
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPYlLPKARGGMRMGHGQVLDHMFLDGLEDAYdKGRLMGTFAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 160 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHgATLDSMAKLRPAFDKEGTVT 239
Cdd:PRK06954 169 ECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDTVIDRDEQPFK-ANPEKIPTLKPAFSKTGTVT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 240 AGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQ 319
Cdd:PRK06954 248 AANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINEAFAVV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 320 ACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK06954 328 TMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
3-389 |
3.83e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 350.97 E-value: 3.83e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVGSFN-GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 80
Cdd:PRK07661 5 VIVAGARTPVGKAKkGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEqGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 81 GMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHlrggVKMGDFKMIDTMIKdgltdafYGYHMGTTAEN 160
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMGH----VVRPNPRLVEAAPE-------YYMGMGHTAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD---------ITVDADEYIRHGATLDSMAKLRPA 231
Cdd:PRK07661 154 VAVKYGISREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRTVGennklqeetITFSQDEGVRADTTLEILGKLRPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 232 FDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVE 311
Cdd:PRK07661 234 FNVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 312 ANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK07661 314 LNEAFASQSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
2-387 |
6.98e-118 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 347.72 E-value: 6.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVG-SFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEAT 78
Cdd:PRK08947 4 VVIVDAIRTPMGrSKGGAFRNVRAEDLSAHLMRSLLARnPALDPAEIDDIIWGCVQQTLEqGFNIARNAALLAGIPHSVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 79 AWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMsmaphcahlrGGVKMGdfKMIDTMIKDGLTDAFYGYHMGTTA 158
Cdd:PRK08947 84 AVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHM----------GHVPMN--HGVDFHPGLSKNVAKAAGMMGLTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 159 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGD---ITVDADEYIRHGATLDSMAKLRPAFD-K 234
Cdd:PRK08947 152 EMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIP--TEGHDADgvlKLFDYDEVIRPETTVEALAALRPAFDpV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 314
Cdd:PRK08947 230 NGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DLV_A 315 AFAAQACAVNKDLGWDPSI---VNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK08947 310 AFAAQSLPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
4-389 |
9.36e-118 |
|
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: 347.93 E-value: 9.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 81
Cdd:TIGR02430 5 ICDAIRTPIGRYGGSLSSVRADDLAAVPIKALLARnPQLDWAAIDDVIYGCANQAGEdNRNVARMAALLAGLPVSVPGTT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIK----DGLTDAFYGYH-MGT 156
Cdd:TIGR02430 85 VNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADSAFSRSAKIEDTTIGwrfiNPLMKALYGVDsMPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 157 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDIT-VDADEYIRHGATLDSMAKLRPAFDKE 235
Cdd:TIGR02430 165 TAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTvVDQDEHPRPETTLEGLAKLKPVVRPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 236 GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEA 315
Cdd:TIGR02430 245 GTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQFDVIELNEA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DLV_A 316 FAAQACAVNKDLGW--DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:TIGR02430 325 FAAQALAVLRELGLadDDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIALAIERV 400
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
4-389 |
6.05e-116 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 343.14 E-value: 6.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVG-SFNGAFANTPAHELGATVISAVLERA-GVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 80
Cdd:PRK09052 10 IVAATRTPVGkAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEqGLNVARIGALLAGLPNSVGGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 81 GMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahlrggvKMGDFKMIDTMIKDGLTDAFYGYHMGTTAEN 160
Cdd:PRK09052 90 TVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVP---------MMGNKPSMSPAIFARDENVGIAYGMGLTAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDI----------TVDADEYIRHGATLDSMAKLRP 230
Cdd:PRK09052 161 VAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITERFPDLatgevdvktrTVDLDEGPRADTSLEGLAKLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 231 AFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 310
Cdd:PRK09052 241 VFANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 311 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK09052 321 ELNEAFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
2-387 |
6.22e-116 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 342.86 E-value: 6.22e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFN------GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQN-PARQAAMKAGVP 74
Cdd:PRK06445 4 VYLVDFARTAFSRFRpkdpqkDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLyGGRHPIFLARLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 75 QEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahlrggvkMGDFKMIDTMIKdGLTDAFY---- 150
Cdd:PRK06445 84 YNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTP----------MGDNPHIEPNPK-LLTDPKYieyd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 151 ---GYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAK 227
Cdd:PRK06445 153 lttGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEVEGKKKVVDVDQSVRPDTSLEKLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 228 LRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDL 307
Cdd:PRK06445 233 LPPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 308 DLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK06445 313 DLWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLE 392
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
2-387 |
1.32e-115 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 344.06 E-value: 1.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAV-GSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVL-PAGEGQNPARQAAMKAGVPQEATA 79
Cdd:PLN02287 48 VVIVAAYRTPIcKAKRGGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLaPGSQRANECRMAAFYAGFPETVPV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 80 WGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcAHLRGGV--KMGDFKMI-DTMIKdgltdafygyhMGT 156
Cdd:PLN02287 128 RTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNP--MAWEGGVnpRVESFSQAqDCLLP-----------MGI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 157 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPF---IVKGRKGD---ITVDADEYIRHGATLDSMAKLRP 230
Cdd:PLN02287 195 TSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkIVDPKTGEekpIVISVDDGIRPNTTLADLAKLKP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 231 AFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 310
Cdd:PLN02287 275 VFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLF 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 311 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRG--ARKGLATLCIGGGMGVAMCIE 387
Cdd:PLN02287 355 EINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFE 433
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
2-387 |
1.25e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 334.29 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK06366 4 VYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTKYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHC--AHLRGGVKM---GDFKMIDTMIKDGLTDAFYGYHMGT 156
Cdd:PRK06366 84 VNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLlpSDLRWGPKHllhKNYKIDDAMLVDGLIDAFYFEHMGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 157 TAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIvkgrkgdiTVDADEYIRHgATLDSMAKLRPAFDKEG 236
Cdd:PRK06366 164 SAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFN--------DLDRDEGIRK-TTMEDLAKLPPAFDKNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 237 TVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAF 316
Cdd:PRK06366 235 ILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDLVEHNEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1DLV_A 317 AAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK06366 315 SIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
4-387 |
7.93e-106 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 317.21 E-value: 7.93e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAART--AVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 80
Cdd:PRK08242 6 IYDAVRTprGKGKKDGSLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDqGADIARTAVLAAGLPETVPGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 81 GMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHcahlrgGVKMGDFKMiDTMIkdgltdAFYGYHM--GTTA 158
Cdd:PRK08242 86 QINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPM------GSDGGAWAM-DPST------NFPTYFVpqGISA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 159 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTV 238
Cdd:PRK08242 153 DLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVP--VKDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 239 ---------------------TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKAL 297
Cdd:PRK08242 231 ggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 298 ERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIG 377
Cdd:PRK08242 311 AKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVG 390
|
410
....*....|
1DLV_A 378 GGMGVAMCIE 387
Cdd:PRK08242 391 GGMGIATIIE 400
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
3-389 |
1.26e-103 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 311.32 E-value: 1.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVG-SFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAW 80
Cdd:PRK07108 5 VIVSTARTPLAkSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTVPGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 81 GMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHcahlrggvKMGDFKMIDTMIKDGLTDAFYgyHMGTTAEN 160
Cdd:PRK07108 85 TVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQN--------EMNRHMLREGWLVEHKPEIYW--SMLQTAEN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 161 VAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGD----------ITVDADEYIRHGATLDSMAKLRP 230
Cdd:PRK07108 155 VAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAGVADkatgrlftkeVTVSADEGIRPDTTLEGVSKIRS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 231 AFDKeGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLV 310
Cdd:PRK07108 235 ALPG-GVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLW 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 311 EANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK07108 314 ELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFEVL 392
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
4-387 |
5.80e-103 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 310.17 E-value: 5.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWGM 82
Cdd:PRK08131 6 IYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEdSRNVARNALLLAGLPVTVPGQTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 83 NQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMI-----KDGLTDAFYGYHMGTT 157
Cdd:PRK08131 86 NRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTTIgarfpNPKIVAQYGNDSMPET 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 158 AENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVK--GRKGDITVDADEYIRHGATLDSMAKLRPAFDkE 235
Cdd:PRK08131 166 GDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPqgRKLPPKLVAEDEHPRPSSTVEALTKLKPLFE-G 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 236 GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEA 315
Cdd:PRK08131 245 GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDDMDIIEINEA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1DLV_A 316 FAAQACAVNKDLG--WDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK08131 325 FASQVLGCLKGLGvdFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
3-389 |
2.81e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 303.46 E-value: 2.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVG-SFNGAFANTPAHELGATVISAVLERA-GVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATA 79
Cdd:PRK07851 5 VIVSTARSPIGrAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEqGFNMARVVAVLLGYDFLPGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 80 wGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMS---------------------MAPHCAHLRGGVKMGDfkmiD 138
Cdd:PRK07851 85 -TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnsdslpdtknplfaeaQARTAARAEGGAEAWH----D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 139 TMIKDGLTDAFYGyhMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGdITVDADEYIRH 218
Cdd:PRK07851 160 PREDGLLPDVYIA--MGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITP--VTLPDG-TVVSTDDGPRA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 219 GATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALE 298
Cdd:PRK07851 235 GTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 299 RAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGG 378
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCVGG 394
|
410
....*....|.
1DLV_A 379 GMGVAMCIESL 389
Cdd:PRK07851 395 GQGMAMVLERL 405
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
2-387 |
8.86e-100 |
|
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: 301.48 E-value: 8.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVG-SFNGAFANTPAHELGATVISAVLER-AGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEAT 78
Cdd:TIGR02445 2 VVIVDFGRTPMGrSKGGAFRNTRAEDLSAHLMSKLLARnPKVDPAEVEDIYWGCVQQTLEqGFNIARNAALLAQIPHTSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 79 AWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPhcahLRGGVKMGDFKMIDTMIKDGLtdafygyhMGTTA 158
Cdd:TIGR02445 82 AVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVP----MMHGVDFHPGMSLHVAKAAGM--------MGLTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 159 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGD---ITVDADEYIRHGATLDSMAKLRPAFD-K 234
Cdd:TIGR02445 150 EMLGKMHGISREQQDAFAARSHARAHAATQEGKFKNEIIP--TQGHDADgflKQFDYDEVIRPETTVESLAALRPAFDpK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 314
Cdd:TIGR02445 228 NGTVTAGTSSALSDGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DLV_A 315 AFAAQACAVNKDLGWDPSI---VNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:TIGR02445 308 AFAAQALPCLKDLGLLDKMdekVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFE 383
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
8-389 |
1.62e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 291.92 E-value: 1.62e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 8 ARTAVGSFNGAfantpahELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCG 87
Cdd:PRK08170 18 ARGGPGPFSAS-------DLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPAWTVQRNCA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 88 SGLRAVALGMQQIATGDASIIVAGGMESMSMAP----------------------HCAHLrGGVKMGDFKMIDTMIKdGL 145
Cdd:PRK08170 91 SGMQALDSAAANIALGRADLVLAGGVEAMSHAPllfsekmvrwlagwyaaksigqKLAAL-GKLRPSYLAPVIGLLR-GL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 146 TDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKdEIVPFIvkGRKGDItVDADEYIRHGATLDSM 225
Cdd:PRK08170 169 TDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPLF--DRDGKF-YDHDDGVRPDSSMEKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 226 AKLRPAFDKE-GTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKI 304
Cdd:PRK08170 245 AKLKPFFDRPyGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHAATPLLQRHGLTL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 305 GDLDLVEANEAFAAQ--AC--AVNKD------LGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGA 367
Cdd:PRK08170 325 EDLDLWEINEAFAAQvlAClaAWADEeycreqLGLdgalgelDRERLNVDGGAIALGHPVGASGARIVLHLLHALKRRGT 404
|
410 420
....*....|....*....|..
1DLV_A 368 RKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK08170 405 KRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
4-389 |
2.27e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 284.68 E-value: 2.27e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAG-EGQNPARQAAMKAGVPQEATAWGM 82
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGpQAGNIARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 83 NQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMG------DFKMIDTMIKDGLTDAFYGyhmgt 156
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISSAMTAGEQLGftspfaESKGWLHRYGDQEVSQFRG----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 157 tAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrkGDITVDadEYIRHgATLDSMAKLRPAFDkEG 236
Cdd:PRK07801 161 -AELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV------GGVTVD--EGPRE-TSLEKMAGLKPLVE-GG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 237 TVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAF 316
Cdd:PRK07801 230 RLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVEINEAF 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DLV_A 317 AAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK07801 310 APVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTIIERL 382
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
3-389 |
3.43e-90 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 276.99 E-value: 3.43e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK07850 5 VIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGATT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLrgGVKMGDFKMIDTMIKDGltDAFygyhmgTTAENV 161
Cdd:PRK07850 85 IDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANA--GPGRGLPRPDSWDIDMP--NQF------EAAERI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 162 AKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFI--VKGRKGDIT-----VDADEYIRHgATLDSMAKLRPAFDk 234
Cdd:PRK07850 155 AKRRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQapVLDEEGQPTgetrlVTRDQGLRD-TTMEGLAGLKPVLE- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANE 314
Cdd:PRK07850 233 GGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINE 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1DLV_A 315 AFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK07850 313 AFASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
2-387 |
2.42e-89 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 276.09 E-value: 2.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 2 IVIASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWG 81
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 82 MNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAP-----HCAH----LRGGVKMGD-FKMIDTM-IKD------G 144
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPigvskKLARalvdLNKARTLGQrLKLFSRLrLRDllpvppA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 145 LTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGdiTVDADEYIRHGATLDS 224
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVMTAHVPPYKQ--PLEEDNNIRGDSTLED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 225 MAKLRPAFD-KEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDP-KVMGTGPIPASRKALERAGW 302
Cdd:PRK08963 245 YAKLRPAFDrKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLALERAGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 303 KIGDLDLVEANEAFAAQACA----------VNKDLGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRR 365
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLAnlqmfaserfAREKLGRsqaigevDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
|
410 420
....*....|....*....|..
1DLV_A 366 GARKGLATLCIGGGMGVAMCIE 387
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
4-389 |
2.55e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 269.68 E-value: 2.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGE-GQNPARQAAMKAGVPQEATAWGM 82
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEqATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 83 NQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKDGLTDAFYGYHMGttAENVA 162
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGMEERYPGIQFSQFTG--AEMMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 163 KQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITV-DADEYIRHGATLDSMAKLRPaFDKEGTVTAG 241
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMhTVDEGIRFDATLEGIAGVKL-IAEGGRLTAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 242 NASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQAC 321
Cdd:PRK06504 243 TASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFASVPL 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 322 AVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK06504 323 AWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
4-389 |
1.03e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 248.15 E-value: 1.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 4 IASAARTAVG---SFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAG-EGQNPARQAAMKAGVPQEATA 79
Cdd:PRK06025 6 IIDAVRTPRGigkVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGkQGGDLGRMAALDAGYDIKASG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 80 WGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMIKdgLTDAFYGYHMGTTAE 159
Cdd:PRK06025 86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPLGMGSGNLR--LRALHPQSHQGVCGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 160 NVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPfiVKGRKGDITVDADEYIRHGATLDSMAKLRPAF------- 232
Cdd:PRK06025 164 AIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVP--VYRDDGSVALDHEEFPRPQTTAEGLAALKPAFtaiadyp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 233 -DKEGTV------------------TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPAS 293
Cdd:PRK06025 242 lDDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNAPVPAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 294 RKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLAT 373
Cdd:PRK06025 322 KKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERRGLKRGLVT 401
|
410
....*....|....*.
1DLV_A 374 LCIGGGMGVAMCIESL 389
Cdd:PRK06025 402 MCAAGGMAPAIIIERV 417
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
3-389 |
4.44e-76 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 239.67 E-value: 4.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 3 VIASAARTAVGSFNGAFANTPAHELGATVI---SAVLERagvaagEVNEVILGQVLpaGEGQNPARQAAMKAGVPQEATA 79
Cdd:PRK06690 4 VIVEAKRTPIGKKNGMLKDYEVQQLAAPLLtflSKGMER------EIDDVILGNVV--GPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 80 WGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLR-GGVKMGDfkmidtmikdgltdafygYHMGTTA 158
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARfSPETIGD------------------PDMGVAA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 159 ENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrkGDITVDADEYIRHGATLDSMAKlrPAFDKEGTV 238
Cdd:PRK06690 138 EYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF------NGLLDESIKKEMNYERIIKRTK--PAFLHNGTV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 239 TAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAA 318
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFAS 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1DLV_A 319 QACAVNKDLGWDPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIESL 389
Cdd:PRK06690 290 KVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
267-387 |
8.92e-65 |
|
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: 202.49 E-value: 8.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 267 QPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIVNVNGGAIAIGHP 346
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGHP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
1DLV_A 347 IGASGARILNTLLFEMKRRGARKGLATLCIGGGMGVAMCIE 387
Cdd:pfam02803 82 LGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIE 122
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
16-388 |
1.51e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 193.58 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 16 NGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVAL 95
Cdd:PRK09268 23 NGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSALSPYTPAYDLQQACGTGLEAAIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 96 GMQQIATGDASIIVAGGMESMSMAPHCAH--LR-------------------GGVKMGDFKMIDTMIKDGLTdafyGYHM 154
Cdd:PRK09268 103 VANKIALGQIDSGIAGGVDTTSDAPIAVNegLRkillelnrakttgdrlkalGKLRPKHLAPEIPRNGEPRT----GLSM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 155 GTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFivkgrKGditVDADEYIRHGATLDSMAKLRPAFDK 234
Cdd:PRK09268 179 GEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-----LG---LTRDNNLRPDSSLEKLAKLKPVFGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 --EGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDpKVMG-----TGPIPASRKALERAGWKIGDL 307
Cdd:PRK09268 251 ggRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVD-FVHGkegllMAPAYAVPRLLARNGLTLQDF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 308 DLVEANEAFAAQACAVNK----------DLGW-------DPSIVNVNGGAIAIGHPIGASGARILNTLLFEMKRRGARKG 370
Cdd:PRK09268 330 DFYEIHEAFASQVLATLKawedeeycreRLGLdaplgsiDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSGRG 409
|
410
....*....|....*...
1DLV_A 371 LATLCIGGGMGVAMCIES 388
Cdd:PRK09268 410 LISICAAGGQGVTAILER 427
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
24-386 |
2.04e-52 |
|
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: 174.94 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 24 AHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPqEATAWGMNQLCGSGLRAVALGMQQIATG 103
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 104 DASIIVAGGMESmsmaphcahlrggvkmgdfkmidtmikdgltdafygyhmgttaenvakqwqlsrdeqdafavasqnka 183
Cdd:cd00327 86 KADIVLAGGSEE-------------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 184 eaaqkdgrfkdeivpfivkgrkgditvdadeyirhgatldsmaklrpafdkegtvtagnaSGLNDGAAAALLMSEAEASR 263
Cdd:cd00327 98 ------------------------------------------------------------FVFGDGAAAAVVESEEHALR 117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 264 RGIQPLGRIVSWATVGVD----PKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACAVNKDLGWDPSIV---NV 336
Cdd:cd00327 118 RGAHPQAEIVSTAATFDGasmvPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELALGLDPDGVrspAV 197
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
1DLV_A 337 NGGAIAIGHPIGASGARILNTLLFEMK-------RRGARKGLATLCIGGGMGVAMCI 386
Cdd:cd00327 198 SATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGFGLGGTNAAVVL 254
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
17-358 |
2.20e-10 |
|
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: 61.51 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 17 GAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPqEATAWGMNQLCGSGLRAVALG 96
Cdd:cd00829 9 GRRSDRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLL-GKPATRVEAAGASGSAAVRAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 97 MQQIATGDASIIVAGGMESMSMAPHCAHLRGGVkmGDFKMIDTMIKDGLT--DAF------YGYHMGTTAENVAKqwqls 168
Cdd:cd00829 88 AAAIASGLADVVLVVGAEKMSDVPTGDEAGGRA--SDLEWEGPEPPGGLTppALYalaarrYMHRYGTTREDLAK----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 169 rdeqdafaVASQNKAEA-----AQkdgrfkdeivpfivkgRKGDITVDadeyirhgatlDSMAKlRPAFDKegtVTAGNA 243
Cdd:cd00829 161 --------VAVKNHRNAarnpyAQ----------------FRKPITVE-----------DVLNS-RMIADP---LRLLDC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 244 SGLNDGAAAALLMSEAEASRRGIQPLgRIVSWAtVGVDPKVMG--------TGPIPASRKALERAGWKIGDLDLVEANEA 315
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDRPV-WILGVG-AASDTPSLSerddflslDAARLAARRAYKMAGITPDDIDVAELYDC 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
1DLV_A 316 FAA---------------QACAVNKD----LGWDPSiVNVNGGAIAIGHPIGASGARILNTL 358
Cdd:cd00829 280 FTIaellaledlgfcekgEGGKLVREgdtaIGGDLP-VNTSGGLLSKGHPLGATGLAQAVEA 340
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
235-378 |
9.98e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 50.46 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 EGTVTAGNASGLNDGAAAALLMSEAEASR-RGIQPLGRIVSW----ATVGVDPKVMGT--GP--IPASRK----ALERAG 301
Cdd:PRK06289 211 EGRLRRQDCSQVTDGGAGVVLASDAYLRDyADARPIPRIKGWghrtAPLGLEQKLDRSagDPyvLPHVRQavldAYRRAG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 302 WKIGDLDLVEANEAFAAQACAVNKDLG-------W----DPSI-------VNVNGGAIAIGHPIGASGARILNTLLFEMK 363
Cdd:PRK06289 291 VGLDDLDGFEVHDCFTPSEYLAIDHIGltgpgesWkaieNGEIaiggrlpINPSGGLIGGGHPVGASGVRMLLDAAKQVT 370
|
170 180
....*....|....*....|..
1DLV_A 364 RR-------GARKGLaTLCIGG 378
Cdd:PRK06289 371 GTagdyqveGAKTFG-TLNIGG 391
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
232-352 |
1.48e-06 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 49.67 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 232 FDK--EGTVtagnasgLNDGAAAALLMSEAEASRRGIQPLGRIVSW-----ATVGVDPKVMGTGPIPASRKALERAGWKI 304
Cdd:PRK05952 199 FDRqrEGLV-------LGEGGAILVLESAELAQKRGAKIYGQILGFgltcdAYHMSAPEPDGKSAIAAIQQCLARSGLTP 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
1DLV_A 305 GDLDLVEA-------NEAFAAQACAVnkdlgWDPSIVNVNGGAIAIGHPIGASGA 352
Cdd:PRK05952 272 EDIDYIHAhgtatrlNDQREANLIQA-----LFPHRVAVSSTKGATGHTLGASGA 321
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
229-352 |
7.67e-06 |
|
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: 47.53 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 229 RPaFDKE--GTVtagnasgLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVG-----VDPKVMGTGPIPASRKALERAG 301
Cdd:cd00834 218 RP-FDKDrdGFV-------LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAG 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 302 WKIGDLDLV-------EANEAFAAQAC-AVNKDLGWDPSIVNVNGgaiAIGHPIGASGA 352
Cdd:cd00834 290 LSPEDIDYInahgtstPLNDAAESKAIkRVFGEHAKKVPVSSTKS---MTGHLLGAAGA 345
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
86-353 |
1.16e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 46.81 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 86 CGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLRGGVKMGDFKMIDTMikdGLTdaFYGY-------HM---G 155
Cdd:PRK06064 85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEAIARAGDYEWEEFF---GAT--FPGLyaliarrYMhkyG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 156 TTAENVAKqwqlsrdeqdafaVASQNKAEAAQ-KDGRFKDEIvpfivkgrkgditvdadeyirhgaTLDSMAKLRPAFDK 234
Cdd:PRK06064 160 TTEEDLAL-------------VAVKNHYNGSKnPYAQFQKEI------------------------TVEQVLNSPPVADP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 235 egtVTAGNASGLNDGAAAALLMSEAEASRRGIQPLgRIVSWAtvgvdpkvMGTGPIP---------------ASRKALER 299
Cdd:PRK06064 203 ---LKLLDCSPITDGAAAVILASEEKAKEYTDTPV-WIKASG--------QASDTIAlhdrkdfttldaavvAAEKAYKM 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1DLV_A 300 AGWKIGDLDLVEANEAFA-AQACAVnKDLGW-----------------DPSI-VNVNGGAIAIGHPIGASGAR 353
Cdd:PRK06064 271 AGIEPKDIDVAEVHDCFTiAEILAY-EDLGFakkgeggklaregqtyiGGDIpVNPSGGLKAKGHPVGATGVS 342
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
223-352 |
3.86e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 45.49 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 223 DSMAKLRPaFDKegtvtagNASGLNDGAAAALLMSEAE--ASRRGIQPLGRIVSWATVG-----VDPKVMGTGPIPASRK 295
Cdd:PRK07910 223 DPAGACRP-FDK-------DRDGFVFGEGGALMVIETEehAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTR 294
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1DLV_A 296 ALERAGWKIGDLDLVEANEAFA-----AQACAVNKDLGWDPSIVNVNGGAIaiGHPIGASGA 352
Cdd:PRK07910 295 AIELAGLTPGDIDHVNAHATGTsvgdvAEGKAINNALGGHRPAVYAPKSAL--GHSVGAVGA 354
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
244-363 |
1.62e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 43.34 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 244 SGLNDGAAAALLMSEAEASRRGIQPL-GRIVSWATVGV----------DPKVMGTGpIPASRKALERAGWKIGDLDLVEA 312
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdSRLVEIKSLACasgnlyedppDATRMFTS-RAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 313 NEAFAAQACAVNKDLGW-DPS-----------------IVNVNGGAIAIGHPIGASGARILNTLLFEMK 363
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaEYGhakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
248-383 |
3.75e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 42.24 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 248 DGAAAALLMSEAEASRrgiqpLGRIVSW-ATVGV---------DPKVMgTGPIPASRKALERAGWKIGDLDLVEANEAF- 316
Cdd:PRK07516 217 DGAAALVLADAETARA-----LQRAVRFrARAHVndflplsrrDPLAF-EGPRRAWQRALAQAGVTLDDLSFVETHDCFt 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 317 -----------------AAQACA---VNKDlGWDPsiVNVNGGAIAIGHPIGASG-------ARILNTLLFEMKRRGARk 369
Cdd:PRK07516 291 iaelieyeamglappgqGARAIRegwTAKD-GKLP--VNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAK- 366
|
170
....*....|....
1DLV_A 370 gLATLCIGGGMGVA 383
Cdd:PRK07516 367 -LAGVFNMGGAAVA 379
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
229-352 |
5.58e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 41.62 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 229 RPaFDKegtvtagNASGLN--DGAAAALLMSEAEASRRGIQPLGRIVSWAT-------VGVDPKvmGTGPIPASRKALER 299
Cdd:COG0304 218 RP-FDK-------DRDGFVlgEGAGVLVLEELEHAKARGAKIYAEVVGYGAssdayhiTAPAPD--GEGAARAMRAALKD 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1DLV_A 300 AGWKIGDLDLV-------EANEafAAQACAVNKDLGWDPSIVNVNggAI--AIGHPIGASGA 352
Cdd:COG0304 288 AGLSPEDIDYInahgtstPLGD--AAETKAIKRVFGDHAYKVPVS--STksMTGHLLGAAGA 345
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
248-363 |
9.49e-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: 40.70 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 248 DGAAAALLMSEAEASRRGIQPLGRIVSWA-----TVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFAAQACA 322
Cdd:cd00825 161 DGAGALVVEELEHALARGAHIYAEIVGTAatidgAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDV 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1DLV_A 323 VNKDLGWD---PSIVNVNGGAIAIGHPIGASGARILNTLLFEMK 363
Cdd:cd00825 241 KELKLLRSefgDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLE 284
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
238-351 |
1.45e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 40.66 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 238 VTAGNASGLNDGAAAALLMSEAEASRRGIQPLgrIVSWATVGVD---PKVMGTGPIP----------------------- 291
Cdd:PRK06365 217 LTRLDVCAMSDGAACAILASEDKAFEITDKPV--LIKAIGTGSDtlrLADRPFGEVPllpnespddykdlrypgvhsfra 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DLV_A 292 ---ASRKALERAGWK--IGDLDLVEANEAFAAQACAVNKDLGW-------------DPSI-----VNVNGGAIAIGHPIG 348
Cdd:PRK06365 295 grmAAKEAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgKPELpgklpVNPSGGLLAAGHAVG 374
|
...
1DLV_A 349 ASG 351
Cdd:PRK06365 375 ATG 377
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
249-312 |
1.67e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 40.40 E-value: 1.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1DLV_A 249 GAAAALLMSEAEASRRGIQPLGRIVSW-----ATVGVDPKVmgTGPIPASRKALERAGWKIGDLDLVEA 312
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWsmrldANRGPDPSL--EGEMRVIRAALRRAGLGPEDIDYVNP 306
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
249-312 |
4.41e-03 |
|
"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: 38.96 E-value: 4.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1DLV_A 249 GAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERA----GWKIGDLDLVEA 312
Cdd:cd00828 232 GAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRTAlakaGLSLDDLDVISA 299
|
|
| |
