|
Name |
Accession |
Description |
Interval |
E-value |
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
5-391 |
0e+00 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 808.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 5 PRDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPH 84
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 85 TSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSLYAAKASGMMGLTAEMLGKMHGI 164
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 165 SREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAFNPKGGTVTAGTSSQ 244
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 245 ITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLK 324
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598209 325 DLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK08947 321 DLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
7-391 |
0e+00 |
|
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: 717.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTS 86
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 87 AAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSLYAAKASGMMGLTAEMLGKMHGISR 166
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAKAAGMMGLTAEMLGKMHGISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 167 EAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAFNPKGGTVTAGTSSQIT 246
Cdd:TIGR02445 161 EQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKNGTVTAGTSSALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 247 DGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLKDL 326
Cdd:TIGR02445 241 DGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 327 KLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:TIGR02445 321 GLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
6-391 |
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: 524.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMHrNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPHT 85
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALA-DVRADDLGAAVIKALLERA-GLDPEAVDDVILGCVLQA-GQGQNPARQAALLAGLPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGM------------MHGVDPNPHLSLYAAKASGMMGL 153
Cdd:COG0183 79 VPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMllpkarwgyrmnAKLVDPMINPGLTDPYTGLSMGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 154 TAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGfLKVFDFDETIRPETTVETLAELKPAFNpK 233
Cdd:COG0183 159 TAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKG-EVVVDRDEGPRPDTTLEKLAKLKPAFK-K 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 234 GGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNE 313
Cdd:COG0183 237 DGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEINE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598209 314 AFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:COG0183 317 AFAAQVLAVLRELGL---DPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIERV 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
9-390 |
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: 513.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 9 VIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLERNPkVDPAEVEDVIWGCVNQTLEqGWNIARMASLMTQIPHTSAA 88
Cdd:cd00751 1 VIVSAVRTPIGRFGGAL-KDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 89 QTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPN------------PHLSLYAAKASGMMGLTAE 156
Cdd:cd00751 78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRggrlglntldgmLDDGLTDPFTGLSMGITAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 157 MLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEgYDENGFLKVFDFDETIRPETTVETLAELKPAFnPKGGT 236
Cdd:cd00751 158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVE-VPGRKGPVVVDRDEGPRPDTTLEKLAKLKPAF-KKDGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 237 VTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFA 316
Cdd:cd00751 236 VTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598209 317 AQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFER 390
Cdd:cd00751 316 AQALACLKELGL---DPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
10-389 |
5.97e-167 |
|
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: 472.10 E-value: 5.97e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 10 IVDFGRTPMGRSKGGMHrNTRAETMSAHLISKLLERNPkVDPAEVEDVIWGCVNQTLEQGwNIARMASLMTQIPHTSAAQ 89
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLK-DVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQQ-NIARQAALLAGLPESVPAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 90 TVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLS-------------LYAAKASGMMGLTAE 156
Cdd:TIGR01930 78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRWGVKpgnaeledarlkdLTDANTGLPMGVTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 157 MLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGfLKVFDFDETIRPETTVETLAELKPAFNPKGgT 236
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKG-PVTVSSDEGIRPNTTLEKLAKLKPAFDPDG-T 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 237 VTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFA 316
Cdd:TIGR01930 236 VTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598209 317 AQALPVLKDLKLLdkmDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFE 389
Cdd:TIGR01930 316 AQVLACIKELGLD---LEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
5-391 |
6.49e-148 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 424.18 E-value: 6.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 5 PRDVVIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPH 84
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGAL-KDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQA-GAGQNPARQAALKAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 85 TSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMG---HV------GMMHG----VDPNPHLSLYAAKASGMM 151
Cdd:PRK05790 78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSqapHVlpgsrwGQKMGdvelVDTMIHDGLTDAFNGYHM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 152 GLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAFN 231
Cdd:PRK05790 158 GITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 232 pKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVEL 311
Cdd:PRK05790 238 -KDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 312 NEAFAAQALPVLKDLKlLDkmDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK05790 317 NEAFAAQALAVEKELG-LD--PEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
6-391 |
9.14e-134 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 388.31 E-value: 9.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGG-----MHRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMT 80
Cdd:PRK06445 2 EDVYLVDFARTAFSRFRPKdpqkdVFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 81 QIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHG--VDPNPHLSL------YAAKASGMMG 152
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphIEPNPKLLTdpkyieYDLTTGYVMG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 153 LTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEgYDENGFLKVFDFDETIRPETTVETLAELKPAFNP 232
Cdd:PRK06445 161 LTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIE-VEVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 233 kGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELN 312
Cdd:PRK06445 240 -DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEIN 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598209 313 EAFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK06445 319 EAFAVVVLYAIKELGL---DPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
6-391 |
1.09e-128 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 375.83 E-value: 1.09e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSkGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK09050 2 TEAFICDAIRTPIGRY-GGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGH----------------------VG-------M--MHGV 134
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRapfvmgkadsafsrqaeifdttIGwrfvnplMkaQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 135 DPnphlslyaakasgmMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETI 214
Cdd:PRK09050 161 DS--------------MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 215 RPETTVETLAELKPAFNPkGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNK 294
Cdd:PRK09050 227 RPETTLEALAKLKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 295 ALKRAGLTIADIDFVELNEAFAAQALPVLKDLKLLDKmDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVS 374
Cdd:PRK09050 306 LLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLADD-DARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALC 384
|
410
....*....|....*..
gi 15598209 375 TMCVGLGQGITTVFERI 391
Cdd:PRK09050 385 TMCIGVGQGIALAIERV 401
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-391 |
6.67e-127 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 371.26 E-value: 6.67e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 1 MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMT 80
Cdd:PRK09052 1 MSKQLQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 81 QIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMM-HGVDPNPHL---SLYAAKASGMmGLTAE 156
Cdd:PRK09052 81 GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgNKPSMSPAIfarDENVGIAYGM-GLTAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 157 MLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYD-----ENGFL----KVFDFDETIRPETTVETLAELK 227
Cdd:PRK09052 160 KVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDEITPYEITErfpdlATGEVdvktRTVDLDEGPRADTSLEGLAKLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 228 PAFNPKGgTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADID 307
Cdd:PRK09052 240 PVFANKG-SVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 308 FVELNEAFAAQALPVLKDLKlLDKmdEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTV 387
Cdd:PRK09052 319 WIELNEAFAAQSLAVIRDLG-LDP--SKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGI 395
|
....
gi 15598209 388 FERI 391
Cdd:PRK09052 396 FERL 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
6-391 |
3.46e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 364.07 E-value: 3.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDpAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK07661 2 REAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYE-GPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMM-HGVDPNPHLSLYAAKASGMMGLTAEMLGKMHGI 164
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMMgHVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 165 SREAQDKFGARSHQLAWKATQEGKFKDEIIPME----GYDENGFLK----VFDFDETIRPETTVETLAELKPAFNPKGgT 236
Cdd:PRK07661 161 SREDQDAFAVRSHQRAAKALAEGKFADEIVPVDvtlrTVGENNKLQeetiTFSQDEGVRADTTLEILGKLRPAFNVKG-S 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 237 VTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFA 316
Cdd:PRK07661 240 VTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 317 AQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK07661 320 SQSIQVIRELGL---DEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
6-391 |
1.05e-121 |
|
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: 357.94 E-value: 1.05e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMHRnTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHT 85
Cdd:TIGR02430 1 REAYICDAIRTPIGRYGGSLSS-VRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDP-------------------NPHL-SLYAA 145
Cdd:TIGR02430 80 VPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKADsafsrsakiedttigwrfiNPLMkALYGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 146 KAsgmMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAE 225
Cdd:TIGR02430 160 DS---MPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 226 LKPAFNPkGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIAD 305
Cdd:TIGR02430 237 LKPVVRP-DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 306 IDFVELNEAFAAQALPVLKDLKLLDKmDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGIT 385
Cdd:TIGR02430 316 FDVIELNEAFAAQALAVLRELGLADD-DARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIA 394
|
....*.
gi 15598209 386 TVFERI 391
Cdd:TIGR02430 395 LAIERV 400
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
5-391 |
5.13e-119 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 351.21 E-value: 5.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 5 PRDVVIVDFGRTPMGRSkGGMHRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGcvnqtleQGWN------IARMASL 78
Cdd:PRK06205 1 MRDAVICEPVRTPVGRF-GGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFG-------QGYPngeapaIGRVAAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 79 MTQIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHV-----GMMHGVdPNPHLSLYAA-------- 145
Cdd:PRK06205 72 DAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVefyttDMRWGV-RGGGVQLHDRlargreta 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 146 ------KASGMMGlTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETT 219
Cdd:PRK06205 151 ggrrfpVPGGMIE-TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 220 VETLAELKP--AFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALK 297
Cdd:PRK06205 230 LESLAKLRPimGKQDPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 298 RAGLTIADIDFVELNEAFAAQALPVLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMC 377
Cdd:PRK06205 310 RAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMC 389
|
410
....*....|....
gi 15598209 378 VGLGQGITTVFERI 391
Cdd:PRK06205 390 IGGGQGLAAVFERV 403
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
7-391 |
7.36e-118 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 348.15 E-value: 7.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTS 86
Cdd:PRK07851 3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYDFLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 87 AAqTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGM-MHGVDPNPHLSLY-------AAKASG--------- 149
Cdd:PRK07851 83 GT-TVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKgNSDSLPDTKNPLFaeaqartAARAEGgaeawhdpr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 150 ----------MMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDEngflKVFDFDETIRPETT 219
Cdd:PRK07851 162 edgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDG----TVVSTDDGPRAGTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 220 VETLAELKPAFNPkGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRA 299
Cdd:PRK07851 238 YEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALARA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 300 GLTIADIDFVELNEAFAAQALPVLKDLklldKMDE-KVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCV 378
Cdd:PRK07851 317 GMSIDDIDLVEINEAFAAQVLPSAREL----GIDEdKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMCV 392
|
410
....*....|...
gi 15598209 379 GLGQGITTVFERI 391
Cdd:PRK07851 393 GGGQGMAMVLERL 405
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
6-391 |
1.32e-112 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 334.62 E-value: 1.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGrSKGGMHRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK09051 3 REVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGH-------------------VGMMHGVDPNPHlslyaak 146
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRapyllpaarwgarmgdaklVDMMVGALHDPF------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 147 ASGMMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGfLKVFDFDETIRPETTVETLAEL 226
Cdd:PRK09051 154 GTIHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKG-EVVFDTDEHVRADTTLEDLAKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 227 KPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADI 306
Cdd:PRK09051 233 KPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 307 DFVELNEAFAAQALPVLKDLKLldkmD-EKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGIT 385
Cdd:PRK09051 313 DVIEANEAFAAQACAVTRELGL----DpAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIA 388
|
....*.
gi 15598209 386 TVFERI 391
Cdd:PRK09051 389 AIFERL 394
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-390 |
2.15e-110 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 330.96 E-value: 2.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 1 MSLNPRDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMT 80
Cdd:PLN02287 41 TTAFGDDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKT-GLNPSEVGDIVVGTVLAPGSQRANECRMAAFYA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 81 QIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSLYAAKASGM--MGLTAEML 158
Cdd:PLN02287 120 GFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLlpMGITSENV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 159 GKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPM-----EGYDENGFLKVFDFDETIRPETTVETLAELKPAFNpK 233
Cdd:PLN02287 200 AERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkivDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFK-K 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 234 GGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNE 313
Cdd:PLN02287 279 NGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINE 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598209 314 AFAAQALPVLKDLKlLDKmdEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGT--LGVSTMCVGLGQGITTVFER 390
Cdd:PLN02287 359 AFASQFVYCCKKLG-LDP--EKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGKDcrFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
7-391 |
3.74e-107 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 320.68 E-value: 3.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSK--GGMHrNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPH 84
Cdd:PRK08242 3 EAYIYDAVRTPRGKGKkdGSLH-EVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 85 TSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGM-MHG----VDPNphlslyAAKASGMM--GLTAEM 157
Cdd:PRK08242 81 TVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMgSDGgawaMDPS------TNFPTYFVpqGISADL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 158 LGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEgyDENGfLKVFDFDETIRPETTVETLAELKPAFNPKGGTV 237
Cdd:PRK08242 155 IATKYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNG-LTILDHDEHMRPGTTMESLAKLKPSFAMMGEMG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 238 --------------------TAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALK 297
Cdd:PRK08242 232 gfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 298 RAGLTIADIDFVELNEAFAAQalpVLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMC 377
Cdd:PRK08242 312 KAGLTVDDIDLFELNEAFASV---VLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLC 388
|
410
....*....|....
gi 15598209 378 VGLGQGITTVFERI 391
Cdd:PRK08242 389 VGGGMGIATIIERV 402
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
10-391 |
2.54e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 312.80 E-value: 2.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 10 IVDFGRTPMGRSKGGMHRnTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQ 89
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAG-VHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 90 TVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHgvdpnphlSLYAAKASGMMGLT--------------- 154
Cdd:PRK07801 84 TVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISS--------AMTAGEQLGFTSPFaeskgwlhrygdqev 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 155 -----AEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGydengflkvFDFDETIRpETTVETLAELKPA 229
Cdd:PRK07801 156 sqfrgAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMAGLKPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 230 FnpKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFV 309
Cdd:PRK07801 226 V--EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 310 ELNEAFAAQALPVLKDLklldKMD-EKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVF 388
Cdd:PRK07801 304 EINEAFAPVVLAWLKET----GADpAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTANVTII 379
|
...
gi 15598209 389 ERI 391
Cdd:PRK07801 380 ERL 382
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
10-391 |
1.12e-103 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 311.66 E-value: 1.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 10 IVDFGRTPMGRsKGGMHRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTSAAQ 89
Cdd:PRK06504 6 IVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDRS-GADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 90 TVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHV------------GMMHGVDPNPHLSLYAAKASGMMGltAEM 157
Cdd:PRK06504 84 SIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVpmgspstlpaknGLGHYKSPGMEERYPGIQFSQFTG--AEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 158 LGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAfnPKGGTV 237
Cdd:PRK06504 162 MAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLI--AEGGRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 238 TAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFAa 317
Cdd:PRK06504 240 TAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAFA- 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 318 qalPV-LKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK06504 319 ---SVpLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
8-258 |
9.90e-102 |
|
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: 301.91 E-value: 9.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 8 VVIVDFGRTPMGrSKGGMHRNTRAETMSAHLISKLLERNPkVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPHTSA 87
Cdd:pfam00108 1 VVIVSAARTPFG-SFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQA-GEGQNPARQAALKAGIPDSAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 88 AQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSLYAAKASGM--------------MGL 153
Cdd:pfam00108 78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLlipdgltdafngyhMGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 154 TAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLkVFDFDETIRPETTVETLAELKPAFNpK 233
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-TVDKDEGIRPPTTAEPLAKLKPAFD-K 235
|
250 260
....*....|....*....|....*
gi 15598209 234 GGTVTAGTSSQITDGASCMIVMSAQ 258
Cdd:pfam00108 236 EGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
7-391 |
2.01e-101 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 306.32 E-value: 2.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLERNPkVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTS 86
Cdd:PRK08131 3 DAYIYDGLRSPFGRHAGAL-ASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 87 AAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVD-------------------PNPhlSLYAAKA 147
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAesafsrdakvfdttigarfPNP--KIVAQYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 148 SGMMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPME--GYDENGFLKVFDfDETIRPETTVETLAE 225
Cdd:PRK08131 159 NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEvpQGRKLPPKLVAE-DEHPRPSSTVEALTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 226 LKPAFNpkGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIAD 305
Cdd:PRK08131 238 LKPLFE--GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLDD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 306 IDFVELNEAFAAQALPVLKDLKlLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGIT 385
Cdd:PRK08131 316 MDIIEINEAFASQVLGCLKGLG-VDFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGLA 394
|
....*.
gi 15598209 386 TVFERI 391
Cdd:PRK08131 395 MVIERV 400
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
6-390 |
2.39e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 305.66 E-value: 2.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVnQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK05656 2 QDVVIVAATRTAIGSFQGSL-ANIPAVELGAAVIRRLLEQT-GLDPAQVDEVILGQV-LTAGAGQNPARQAAIKAGLPHS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHM----------------GHVGMmhgVDPNPHLSLYAAKASG 149
Cdd:PRK05656 79 VPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMslapyvlpgartglrmGHAQL---VDSMITDGLWDAFNDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 150 MMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPA 229
Cdd:PRK05656 156 HMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 230 FNpKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFV 309
Cdd:PRK05656 236 FK-KDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 310 ELNEAFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFE 389
Cdd:PRK05656 315 EANEAFAAQSLAVGKELGW---DAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
.
gi 15598209 390 R 390
Cdd:PRK05656 392 R 392
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
7-389 |
5.23e-98 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 297.07 E-value: 5.23e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLISKLLERnPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHTS 86
Cdd:PRK07108 3 EAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 87 AAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVG--MMHGVDPNPHLSLYAAKASGMMGLTAEMLGKMHGI 164
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQneMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRYGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 165 SREAQDKFGARSHQLAWKATQEGKFKDEIIPME-----GYDENGFLKVFDF----DETIRPETTVETLAELKPAFnpKGG 235
Cdd:PRK07108 162 SKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITvtagvADKATGRLFTKEVtvsaDEGIRPDTTLEGVSKIRSAL--PGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 236 TVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAF 315
Cdd:PRK07108 240 VITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598209 316 AAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFE 389
Cdd:PRK07108 320 AVQVLYCRDTLGI---PMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
4-391 |
1.25e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 292.31 E-value: 1.25e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 4 NPRDVVIVDFGRTPMGRSKGGMHRNTrAETMSAHLISKLLERNPkVDPAEVEDVIWGCVNQTLEQGwNIARMASLMTQIP 83
Cdd:PRK08170 1 MARPVYIVDGARTPFLKARGGPGPFS-ASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMPSPDEA-NIARVVALRLGCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 84 HTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMmhgVDPNPHLS----LYAAKASG---------- 149
Cdd:PRK08170 78 EKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPL---LFSEKMVRwlagWYAAKSIGqklaalgklr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 150 ---------------------MMGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKdEIIPMegYDENGflKVF 208
Cdd:PRK08170 155 psylapvigllrgltdpvvglNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVPL--FDRDG--KFY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 209 DFDETIRPETTVETLAELKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGP 288
Cdd:PRK08170 230 DHDDGVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 289 VPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLKDLK-------------LLDKMD-EKVNLHGGAIALGHPFGCSGA 354
Cdd:PRK08170 310 VHAATPLLQRHGLTLEDLDLWEINEAFAAQVLACLAAWAdeeycreqlgldgALGELDrERLNVDGGAIALGHPVGASGA 389
|
410 420 430
....*....|....*....|....*....|....*..
gi 15598209 355 RISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK08170 390 RIVLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
6-391 |
2.31e-93 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 285.39 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLErNPKVDPAEVEDVIWGCVnQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK06633 3 KPVYITHAKRTAFGSFMGSL-STTPAPMLAAHLIKDILQ-NSKIDPALVNEVILGQV-ITGGSGQNPARQTLIHAGIPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHvgMMHG--------------VDPNPHLSLYAAKASGMM 151
Cdd:PRK06633 80 VPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSL--GMHGsyiragakfgdikmVDLMQYDGLTDVFSGVFM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 152 GLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGfLKVFDFDETIRPETTVETLAELKPAFN 231
Cdd:PRK06633 158 GITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKT-TSLFDHDETVRPDTSLEILSKLRPAFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 232 pKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVEL 311
Cdd:PRK06633 237 -KNGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 312 NEAFAAQALPVLKDLKLldKMdEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK06633 316 NEAFAAQSIYVNREMKW--DM-EKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEAV 392
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
9-391 |
3.25e-90 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 276.99 E-value: 3.25e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 9 VIVDFGRTPMGRSKG---GMHRntrAETMSAhLISKLLERnPKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMTQIPHT 85
Cdd:PRK07850 5 VIVEAVRTPIGKRNGwlsGLHA---AELLGA-VQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNPHLSlYAAKASGMMG---LTAEMLGKMH 162
Cdd:PRK07850 80 VGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLP-RPDSWDIDMPnqfEAAERIAKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 163 GISREAQDKFGARSHQLAWKATQEGKFKDEIIPM------EGYDENGFLKVFDFDETIRpETTVETLAELKPAFnpKGGT 236
Cdd:PRK07850 159 GITREDVDAFGLRSQRRAAQAWAEGRFDREISPVqapvldEEGQPTGETRLVTRDQGLR-DTTMEGLAGLKPVL--EGGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 237 VTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFA 316
Cdd:PRK07850 236 HTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 317 AQalpVLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK07850 316 SV---VLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
6-391 |
3.59e-88 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 271.97 E-value: 3.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMhRNTRAETMSAHLISKLLERnPKVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPHT 85
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLGSL-SSLSATELGSIAIQAALER-AGVDPALVQEVFFGNVLSA-NLGQAPARQAALGAGLPPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHV---------GMMHG----VDPNPHLSLYAAKASGMMG 152
Cdd:PLN02644 78 TICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNApkylpearkGSRLGhdtvVDGMLKDGLWDVYNDFGMG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 153 LTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVF-DFDETIRpETTVETLAELKPAFN 231
Cdd:PLN02644 158 VCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSVIvDKDEGLG-KFDPAKLRKLRPSFK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 232 PKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVEL 311
Cdd:PLN02644 237 EDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 312 NEAFAAQAlpvLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PLN02644 317 NEAFSVVA---LANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELM 393
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
6-383 |
7.53e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 268.50 E-value: 7.53e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSkGGMHRNTRAETMSAHLISKLLERnPKVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPHT 85
Cdd:PRK08235 2 SKTVIVSAARTPFGKF-GGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQG-GQGQIPSRQAARAAGIPWE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGH-----------VGMMHG--VDPNPHLSLYAAKASGMMG 152
Cdd:PRK08235 79 VQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNapyilpgarwgYRMGDNevIDLMVADGLTCAFSGVHMG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 153 LTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLKVFDFDETIRPETTVETLAELKPAFNP 232
Cdd:PRK08235 159 VYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPVFDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 233 KGgTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELN 312
Cdd:PRK08235 239 TG-TITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEIN 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598209 313 EAFAAQAlpvLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQG 383
Cdd:PRK08235 318 EAFAAVA---LASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQG 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-390 |
1.56e-83 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 261.07 E-value: 1.56e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 4 NPRDVVIVDFGRTPMGRSKGGMHrNTRAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGwNIARMASLMTQIP 83
Cdd:PRK08963 3 QGDRIAIVSGLRTPFAKQATAFH-GIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPEAP-NIAREIVLGTGMN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 84 HTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMmhGVD-PNPHLSLYAAKA--------------- 147
Cdd:PRK08963 80 VHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPI--GVSkKLARALVDLNKArtlgqrlklfsrlrl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 148 --------------SGM-MGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIipMEGYDENgFLKVFDFDE 212
Cdd:PRK08963 158 rdllpvppavaeysTGLrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPP-YKQPLEEDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 213 TIRPETTVETLAELKPAFNPKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDP-AIMGYGPVPS 291
Cdd:PRK08963 235 NIRGDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 292 TNKALKRAGLTIADIDFVELNEAFAAQALPVLKDL-------------KLLDKMD-EKVNLHGGAIALGHPFGCSGARIS 357
Cdd:PRK08963 315 TPLALERAGLTLADLTLIDMHEAFAAQTLANLQMFaserfareklgrsQAIGEVDmSKFNVLGGSIAYGHPFAATGARMI 394
|
410 420 430
....*....|....*....|....*....|...
gi 15598209 358 GTLLNVMKQNGGTLGVSTMCVGLGQGITTVFER 390
Cdd:PRK08963 395 TQTLHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
7-391 |
6.08e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 251.62 E-value: 6.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKGG------MHrntrAETMSAHLISKLLERNpKVDPAEVEDVIWGCVNQTLEQGWNIARMASLMT 80
Cdd:PRK06025 3 EAYIIDAVRTPRGIGKVGkgalahLH----PQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 81 QIPHTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDPNP----------HLSLYAAKASGM 150
Cdd:PRK06025 78 GYDIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAgkpplgmgsgNLRLRALHPQSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 151 MGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMegYDENGFLkVFDFDETIRPETTVETLAELKPAF 230
Cdd:PRK06025 158 QGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--YRDDGSV-ALDHEEFPRPQTTAEGLAALKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 231 --------NPKGGTVT-----------------AGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMG 285
Cdd:PRK06025 235 taiadyplDDKGTTYRglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 286 YGPVPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLKDLKlLDKmdEKVNLHGGAIALGHPFGCSGARISGTLLNVMK 365
Cdd:PRK06025 315 NAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLD-LDR--DKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
|
410 420
....*....|....*....|....*.
gi 15598209 366 QNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK06025 392 RRGLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
9-391 |
1.26e-68 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 220.41 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 9 VIVDFGRTPMGRsKGGMHRNTRAETMSAHLI---SKLLERnpkvdpaEVEDVIWGCVnqtLEQGWNIARMASLMTQIPHT 85
Cdd:PRK06690 4 VIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLtflSKGMER-------EIDDVILGNV---VGPGGNVARLSALEAGLGLH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMG-------------HVGmmhgvDPNphlslyaakasgmMG 152
Cdd:PRK06690 73 IPGVTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTStspfqnrarfspeTIG-----DPD-------------MG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 153 LTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMegydeNGFLkvfdfDETIRPETTVETL-AELKPAFN 231
Cdd:PRK06690 135 VAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEEILSF-----NGLL-----DESIKKEMNYERIiKRTKPAFL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 232 pKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVEL 311
Cdd:PRK06690 205 -HNGTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 312 NEAFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFERI 391
Cdd:PRK06690 284 NEAFASKVVACAKELQI---PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
6-391 |
2.62e-68 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 220.65 E-value: 2.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 6 RDVVIVDFGRTPMGRSKGGMHRnTRAETMSAHLISKLLErNPKVDPAEVEDVIWGCVNQTlEQGWNIARMASLMTQIPHT 85
Cdd:PRK06366 2 KDVYIVSAKRTAIGKFGRSFSK-IKAPQLGGAAIKAVID-DAKLDPALVQEVIMGNVIQA-GVGQNPAGQAAYHAGLPFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 86 SAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVDP--NPHLSLY-------AAKASGM------ 150
Cdd:PRK06366 79 VTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLrwGPKHLLHknykiddAMLVDGLidafyf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 151 --MGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDEngflkvfdfDETIRpETTVETLAELKP 228
Cdd:PRK06366 159 ehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFNDLDR---------DEGIR-KTTMEDLAKLPP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 229 AFNpKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDF 308
Cdd:PRK06366 229 AFD-KNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 309 VELNEAFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVF 388
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKI---DNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLTL 384
|
...
gi 15598209 389 ERI 391
Cdd:PRK06366 385 EMV 387
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
8-382 |
7.82e-65 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 212.06 E-value: 7.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 8 VVIVDFGRTPMGRSKGGMHRNTrAETMSAHLISKLLERnPKVDPAEVEDVIWGCVnQTLEQGWNIARMASLMTQIPHTSA 87
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLT-APQLGAAAIAAAVER-AGLKPEQIDEVVMGCV-LPAGQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 88 AQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHM-----------GHVGMMHG--VDPNPHLSLYAAKASG-MMGL 153
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMtnapyllpkarGGMRMGHGqvLDHMFLDGLEDAYDKGrLMGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 154 TAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDENGFLkVFDFDETIRpETTVETLAELKPAFNpK 233
Cdd:PRK06954 166 FAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT-VIDRDEQPF-KANPEKIPTLKPAFS-K 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 234 GGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNE 313
Cdd:PRK06954 243 TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEINE 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598209 314 AFAAQALPVLKDLKLldkMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQ 382
Cdd:PRK06954 323 AFAVVTMAAMKEHGL---PHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGE 388
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
266-390 |
3.08e-62 |
|
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: 195.94 E-value: 3.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 266 QPMAVIRSMAVAGVDPAIMGYGPVPSTNKALKRAGLTIADIDFVELNEAFAAQALPVLKDLKLLDkmdEKVNLHGGAIAL 345
Cdd:pfam02803 2 KPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP---EKVNVNGGAIAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15598209 346 GHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFER 390
Cdd:pfam02803 79 GHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
4-390 |
1.52e-52 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 180.48 E-value: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 4 NPRDVVIVDFGRTPMGRSKGGMHRNTRAETMSAHLiSKLLERNpKVDPAEVEDVIWGCVnQTLEQGWNIARMASLMTQIP 83
Cdd:PRK09268 5 TVRRVAILGGNRIPFARSNGAYADASNQDMLTAAL-DGLVDRF-GLQGERLGEVVAGAV-LKHSRDFNLTRECVLGSALS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 84 HTSAAQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGV-----------EHMGHVGM--------------MHGVDPN- 137
Cdd:PRK09268 82 PYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVdttsdapiavnEGLRKILLelnrakttgdrlkaLGKLRPKh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 138 --PHLSLYAAKASGM-MGLTAEMLGKMHGISREAQDKFGARSHQLAWKATQEGKFKDEIIPMEGYDEngflkvfdfDETI 214
Cdd:PRK09268 162 laPEIPRNGEPRTGLsMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLGLTR---------DNNL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 215 RPETTVETLAELKPAFN-PKGGTVTAGTSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVD-----------PA 282
Cdd:PRK09268 233 RPDSSLEKLAKLKPVFGkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgkegllmaPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 283 ImgygPVPstnKALKRAGLTIADIDFVELNEAFAAQALPVLK----------DLKL---LDKMD-EKVNLHGGAIALGHP 348
Cdd:PRK09268 313 Y----AVP---RLLARNGLTLQDFDFYEIHEAFASQVLATLKawedeeycreRLGLdapLGSIDrSKLNVNGSSLAAGHP 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15598209 349 FGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGITTVFER 390
Cdd:PRK09268 386 FAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
11-389 |
3.35e-52 |
|
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: 178.84 E-value: 3.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 11 VDFGRTPMGRSKGGMHR--NTRAETMSAHLISKLLERnPKVDPAEVEDVIWGCVNQTLEqGWNIARMASLMTQIPHTSAA 88
Cdd:cd00826 1 AGAAMTAFGKFGGENGAdaNDLAHEAGAKAIAAALEP-AGVAAGAVEEACLGQVLGAGE-GQNCAQQAAMHAGGLQEAPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 89 QTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGmmHGVDPNPHLSLYAAKASgmmgltaemlgkmhgiSREA 168
Cdd:cd00826 79 IGMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETSA--ENNAKEKHIDVLINKYG----------------MRAC 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 169 QDKFGARSHQLAWKATQEGKFKDEIIPMeGYDENGFLKVFDFDETIR--PETTVETLAELKPAFNpKGGTVTAGTSSQIT 246
Cdd:cd00826 141 PDAFALAGQAGAEAAEKDGRFKDEFAKF-GVKGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFD-KEDFLTAGNACGLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 247 DGASCMIVMSAQRAQD-------LGIQPMAVIRSMAVAGVDPA----IMGYGPVPSTNKALKRAGLTIADIDFVELNEAF 315
Cdd:cd00826 219 DGAAAAILMSEAEAQKhglqskaREIQALEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 316 AAQALPVLKDL---------KLLDKMDEK------VNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTL-----GVST 375
Cdd:cd00826 299 AANACATNEALglcpegqggALVDRGDNTyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqgagaGLAL 378
|
410
....*....|....
gi 15598209 376 MCVGLGQGITTVFE 389
Cdd:cd00826 379 LCIGGGGGAAMCIE 392
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
49-384 |
1.15e-18 |
|
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: 86.55 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 49 VDPAEVEDVIWGCVNQTLEQGWNIARMAS--LMTQIP--HTSAAqtvsrlCGSSMSALHTAAQAIQTGNGDVFVIGGVEH 124
Cdd:cd00829 33 LEPADIDAVVVGNAAGGRFQSFPGALIAEylGLLGKPatRVEAA------GASGSAAVRAAAAAIASGLADVVLVVGAEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 125 MGHVG-----MMHGVDP--NPHLSLYAAKASGMMGLTAEMLGKMHGISREAQDKFGARSHQ------LAWkatqegkFKD 191
Cdd:cd00829 107 MSDVPtgdeaGGRASDLewEGPEPPGGLTPPALYALAARRYMHRYGTTREDLAKVAVKNHRnaarnpYAQ-------FRK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 192 EIIpMEGYDEN----GFLKVFDFdetirpettvetlaelkpafnpkggtvtagtsSQITDGASCMIVMSAQRAQDLGIQP 267
Cdd:cd00829 180 PIT-VEDVLNSrmiaDPLRLLDC--------------------------------CPVSDGAAAVVLASEERARELTDRP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 268 MAvIRSMAVAgVDPAIMGYGPVPSTN--------KALKRAGLTIADIDFVELNEAFAAQALPVLKDLKLLDK------MD 333
Cdd:cd00829 227 VW-ILGVGAA-SDTPSLSERDDFLSLdaarlaarRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFCEKgeggklVR 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 334 E---------KVNLHGGAIALGHPFGCSGARISGTLLNVMKQNGGTLGVSTMCVGLGQGI 384
Cdd:cd00829 305 EgdtaiggdlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQVPGARVGLAHNI 364
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
231-387 |
1.75e-18 |
|
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: 84.03 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 231 NPKGGTVTAGTSSQI--TDGASCMIVMSAQRAQDLGIQPMAVIRSMAV----AGVDPAIMGYGPVPSTNKALKRAGLTIA 304
Cdd:cd00327 84 NGKADIVLAGGSEEFvfGDGAAAAVVESEEHALRRGAHPQAEIVSTAAtfdgASMVPAVSGEGLARAARKALEGAGLTPS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 305 DIDFVELNEAFAAQALPVLKDLKLLDKMDEKVNLHGGAIALGHPFGCSGARISGTLLNVMK-------QNGGTLGVSTMC 377
Cdd:cd00327 164 DIDYVEAHGTGTPIGDAVELALGLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEhefipptPREPRTVLLLGF 243
|
170
....*....|
gi 15598209 378 VGLGQGITTV 387
Cdd:cd00327 244 GLGGTNAAVV 253
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
95-355 |
2.31e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 73.78 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 95 CGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVgmmhgvdPNPHLSLYAAKAS-----GMMGLTAEMLGKMhgISREAQ 169
Cdd:PRK06064 85 CASGGAALRQAYLAVASGEADVVLAAGVEKMTDV-------PTPDATEAIARAGdyeweEFFGATFPGLYAL--IARRYM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 170 DKFGARSHQLAWKATqegkfKDEiipmegydENGflkVFDFDETIRPETTVETLAELKPAFNPkggtVTAGTSSQITDGA 249
Cdd:PRK06064 156 HKYGTTEEDLALVAV-----KNH--------YNG---SKNPYAQFQKEITVEQVLNSPPVADP----LKLLDCSPITDGA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 250 SCMIVMSAQRAQDLGIQPMaVIRSMAVA-------------GVDPAIMgygpvpSTNKALKRAGLTIADIDFVELNEAFA 316
Cdd:PRK06064 216 AAVILASEEKAKEYTDTPV-WIKASGQAsdtialhdrkdftTLDAAVV------AAEKAYKMAGIEPKDIDVAEVHDCFT 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15598209 317 AQALPVLKDLKLLDK-------------MDEK--VNLHGGAIALGHPFGCSGAR 355
Cdd:PRK06064 289 IAEILAYEDLGFAKKgeggklaregqtyIGGDipVNPSGGLKAKGHPVGATGVS 342
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
93-346 |
6.26e-09 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 57.35 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 93 RLCGSS-MSALHTAAQAIQTGNGDVFVI--GGVEHMGHVGMMHGVDPNPH---------LSLYAAKASGMM---GLTAEM 157
Cdd:PRK06158 82 MIGGSSfLAHLLPAALALEAGLCDVALIcyGSNQRSAGGKLRSMLDPQPYeapykpvnpVSAYALAAARHMhqyGTTREQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 158 LgkmhgisreAQDKFGARshqlAWKATQEGKFKDEiipmegydengflkvfdfdetirPETTVETLAElKPAFNPkggtV 237
Cdd:PRK06158 162 L---------AEVAVAAR----QWAQLNPEAFMRD-----------------------PLTIDDVLAA-RMVSDP----L 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 238 TAGTSSQITDGASCMIVMSAQRAQDLGIQPMAV-----------IRSMAVAGVDPAIMgygpvpSTNKALKRAGLTIADI 306
Cdd:PRK06158 201 SVRDCCLVTDGAGAVVMVRADRARDLPRPPVYVlgaaaatwhrqISSMPDLTVTAAAE------SGPRAFAMAGLTPADI 274
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15598209 307 DFVELNEAFAAQALPVLKDLKLLDKMDEKVNLHGGAIALG 346
Cdd:PRK06158 275 DVVELYDAFTINTILFLEDLGFCAKGEGGAFVEGGRIAPG 314
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
95-372 |
3.90e-07 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 51.61 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 95 CGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGmmhgvdpnphlslyAAKAsgmmgltAEMLGKMHGISREAQDKfga 174
Cdd:PRK06289 90 CASGSVATLAAMADLRAGRYDVALVVGVELMKTVP--------------GDVA-------AEHLGAAAWTGHEGQDA--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 175 rshQLAWKATQeGKFKDEIIPMEGYDEnGFLKVF---DFDETIR-PETTVETLAELKPAFNPKGGT--VTAG-----TSS 243
Cdd:PRK06289 146 ---RFPWPSMF-ARVADEYDRRYGLDE-EHLRAIaeiNFANARRnPNAQTRGWAFPDEATNDDDATnpVVEGrlrrqDCS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 244 QITDGASCMIVMSAQRAQDLG--------------IQPMAVIRSMAVAGVDPAIMgygpvPSTNK----ALKRAGLTIAD 305
Cdd:PRK06289 221 QVTDGGAGVVLASDAYLRDYAdarpiprikgwghrTAPLGLEQKLDRSAGDPYVL-----PHVRQavldAYRRAGVGLDD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 306 IDFVELNEAFAAQALPVLKDLKLLD-------------KMDEK--VNLHGGAIALGHPFGCSGARIsgtLLNVMKQNGGT 370
Cdd:PRK06289 296 LDGFEVHDCFTPSEYLAIDHIGLTGpgeswkaiengeiAIGGRlpINPSGGLIGGGHPVGASGVRM---LLDAAKQVTGT 372
|
..
gi 15598209 371 LG 372
Cdd:PRK06289 373 AG 374
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
245-356 |
6.57e-07 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 50.84 E-value: 6.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 245 ITDGASCMIVMSAQRAQDLGIQPmAVIRSMAvAGVDPAIMG---YGPVPSTNKALKRA-GLTIADIDFVELNEAFAAQAL 320
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELRERP-AWITGIE-HRIESPSLGardLTRSPSTALAAEAAtGGDAGGVDVAELHAPFTHQEL 281
|
90 100 110
....*....|....*....|....*....|....*.
gi 15598209 321 PVLKDLKLLDKMdeKVNLHGGAIALGHPFGCSGARI 356
Cdd:PRK07937 282 ILREALGLGDKT--KVNPSGGALAANPMFAAGLERI 315
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
91-366 |
1.03e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 50.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 91 VSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGM------------------MHGVDPNPHLSLYAAKASGMMG 152
Cdd:PRK12578 78 VEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVDTstslaiggrggnyqweyhFYGTTFPTYYALYATRHMAVYG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 153 LTAEMLGKmhgISREAQdKFGARSH--QLAWKATQEGKFKDEIIPMEgydengfLKVFDfdetirpettvetlaelkpaf 230
Cdd:PRK12578 158 TTEEQMAL---VSVKAH-KYGAMNPkaHFQKPVTVEEVLKSRAISWP-------IKLLD--------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 231 npkggtvtagtSSQITDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYG-------PVPSTNKALKRAGLTI 303
Cdd:PRK12578 206 -----------SCPISDGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVARRGewvgfkaTQLAARQAYNMAKVTP 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598209 304 ADIDFVELNEAFAAQALPVLKDL---------KLLDKMD-EK-----VNLHGGAIALGHPFGCSGArisGTLLNVMKQ 366
Cdd:PRK12578 275 NDIEVATVHDAFTIAEIMGYEDLgftekgkggKFIEEGQsEKggkvgVNLFGGLKAKGHPLGATGL---SMIYEITKQ 349
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
7-353 |
1.58e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 49.56 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 7 DVVIVDFGRTPMGRSKggmhrntrAETMSAHLISKLLE--RNPKVDPAEVEDVIWGCVNQTL-EQGWNIARMASLMTQIP 83
Cdd:PRK07516 3 TASIVGWAHTPFGKLD--------AETLESLIVRVAREalAHAGIAAGDVDGIFLGHFNAGFsPQDFPASLVLQADPALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 84 HTSAAQtVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVgmmhgvdPNPHLSLYAAKASGMM---GLTAEMLGK 160
Cdd:PRK07516 75 FKPATR-VENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTAT-------PTAEVGDILLGASYLKeegDTPGGFAGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 161 MHGISREAQDKFGARSHQLAWKATQEGKfkdeiipmegydeNG-------FLKVFDFD--ETIRPEttvetlaelkpafN 231
Cdd:PRK07516 147 FGRIAQAYFQRYGDQSDALAMIAAKNHA-------------NGvanpyaqMRKDLGFEfcRTVSEK-------------N 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 232 PkggtVTAG-----TSSQITDGASCMIVMSAQRAQDLgiqPMAV-IRSMAVAG-------VDPAIMGyGPVPSTNKALKR 298
Cdd:PRK07516 201 P----LVAGplrrtDCSLVSDGAAALVLADAETARAL---QRAVrFRARAHVNdflplsrRDPLAFE-GPRRAWQRALAQ 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598209 299 AGLTIADIDFVELNEAF------------------AAQALP---VLKDLKLldkmdeKVNLHGGAIALGHPFGCSG 353
Cdd:PRK07516 273 AGVTLDDLSFVETHDCFtiaelieyeamglappgqGARAIRegwTAKDGKL------PVNPSGGLKAKGHPIGATG 342
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
91-355 |
3.48e-05 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 45.40 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 91 VSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHM---GHVGM--------MHGVDPNphlslyaAKASGMMGLTAEMLG 159
Cdd:PRK06157 84 VENFCATGSEAFRGAVYAVASGAYDIALALGVEKLkdtGYGGLpvanpgtlADMTMPN-------VTAPGNFAQLASAYA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 160 KMHGISREaqDKFGARSHqLAWKAtqegkfkdeiipmegyDENGFLKVfdfDETIRPETTVETLAELKPAFNPKGGTVTA 239
Cdd:PRK06157 157 AKYGVSRE--DLKRAMAH-VSVKS----------------HANGARNP---KAHLRKAVTEEQVLKAPMIAGPLGLFDCC 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 240 GTSsqitDGASCMIVMSAQRAQDLGIQPMAVIRSMAVAGVDPAIMGYGP-----VPSTNKALKR----AGLT--IADIDF 308
Cdd:PRK06157 215 GVS----DGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQYNGwdgsyFPTTRIAARKayreAGITdpREELSM 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598209 309 VELNEAFAAQALPVLKDLKLL-------DKMDEK--------VNLHGGAIALGHPFGCSGAR 355
Cdd:PRK06157 291 AEVHDCFSITELVTMEDLGLSergqawrDVLDGFfdadgglpCQIDGGLKCFGHPIGASGLR 352
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
243-385 |
1.88e-04 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 43.34 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 243 SQITDGASCMIVMSAQRAQDLGIQP----MAVIRSMAVAG----VDP--AIMGYGPVPSTNKALKRAGLTIADIDFVELN 312
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPndsrLVEIKSLACASgnlyEDPpdATRMFTSRAAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 313 EAFAAQALPVLKDLKLLDKMDEK---------------VNLHGGAIALGHPFGCSGARisgTLLNVMKQNGGTLGVSTMC 377
Cdd:PTZ00455 336 DCFTIAELLMYEALGIAEYGHAKdlirngatalegripVNTGGGLLSFGHPVGATGVK---QIMEVYRQMKGQCGEYQMK 412
|
....*...
gi 15598209 378 VGLGQGIT 385
Cdd:PTZ00455 413 NIPALGAT 420
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
88-152 |
5.46e-04 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 41.08 E-value: 5.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 88 AQTVSRLCGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHvgmmhgvdPNPHLSLYAAKASGMMG 152
Cdd:pfam00109 166 SVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLT--------PLGFAGFSAAGMLSPDG 222
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
245-353 |
6.41e-04 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 41.82 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 245 ITDGASCMIVMSAQRAQDLGIQPMAVirSMAVAGVD---PAIMGYGPVP--------------------------STNKA 295
Cdd:PRK06365 225 MSDGAACAILASEDKAFEITDKPVLI--KAIGTGSDtlrLADRPFGEVPllpnespddykdlrypgvhsfragrmAAKEA 302
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598209 296 LKRAGLT--IADIDFVELNEAFAAQALPVLKDLKLL------DKMDE---------KVNLHGGAIALGHPFGCSG 353
Cdd:PRK06365 303 YEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLCkygeggQFIESgkpelpgklPVNPSGGLLAAGHAVGATG 377
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
95-150 |
8.32e-04 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 41.39 E-value: 8.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598209 95 CGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHGVD------PNPHLSLYAAKASGM 150
Cdd:cd00833 170 CSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSkagmlsPDGRCRPFDADADGY 231
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
244-346 |
8.44e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 41.12 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598209 244 QITDGASCMIVMSAQRAQDLGiQPMAVIRSMAV-AGVDPAIMG--YGPVPSTNKAL--------KRAGLTIADIDFVELN 312
Cdd:PRK07855 214 QESDGAVALVVTSAERARDLK-QRPAVIKAAAQgSGADQYMMTsyYRDDITGLPEMglvarqlwAQSGLGPADIDTAILY 292
|
90 100 110
....*....|....*....|....*....|....
gi 15598209 313 EAFAAQALPVLKDLKLLDKMDEKVNLHGGAIALG 346
Cdd:PRK07855 293 DHFTPFVLMQLEELGFCGRGEAKDFIADGALELG 326
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
95-133 |
7.09e-03 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 38.08 E-value: 7.09e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15598209 95 CGSSMSALHTAAQAIQTGNGDVFVIGGVEHMGHVGMMHG 133
Cdd:smart00825 97 CSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVG 135
|
|
| |
