|
Name |
Accession |
Description |
Interval |
E-value |
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
1-387 |
0e+00 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 846.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGMMGLTAEMLGKLHGI 160
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHGVDFHPGLSKNVAKAAGMMGLTAEMLGKMHGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 161 SRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFDPVNGTVTAGTSSA 240
Cdd:PRK08947 161 SREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLKLFDYDEVIRPETTVEALAALRPAFDPVNGTVTAGTSSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 241 LSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVK 320
Cdd:PRK08947 241 LSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQSLPCLK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752540570 321 DLGLQDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK08947 321 DLGLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQFGLATMCIGLGQGIATVFERV 387
|
|
| fadA |
TIGR02445 |
fatty oxidation complex, beta subunit FadA; This subunit of the FadBA complex has acetyl-CoA ... |
3-387 |
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: 700.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 3 DVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPKQV 82
Cdd:TIGR02445 1 DVVIVDFGRTPMGRSKGGAFRNTRAEDLSAHLMSKLLARNPKVDPAEVEDIYWGCVQQTLEQGFNIARNAALLAQIPHTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 83 GAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGMMGLTAEMLGKLHGISR 162
Cdd:TIGR02445 81 AAVTVNRLCGSSMQALHDAARAIMTGDADVCLVGGVEHMGHVPMMHGVDFHPGMSLHVAKAAGMMGLTAEMLGKMHGISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 163 SQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFDPVNGTVTAGTSSALS 242
Cdd:TIGR02445 161 EQQDAFAARSHARAHAATQEGKFKNEIIPTQGHDADGFLKQFDYDEVIRPETTVESLAALRPAFDPKNGTVTAGTSSALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 243 DGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDL 322
Cdd:TIGR02445 241 DGASAMLVMSEQRANELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEAFAAQALPCLKDL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752540570 323 GLQDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:TIGR02445 321 GLLDKMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMEQKDATFGLATMCIGLGQGIATVFERV 385
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
1-387 |
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: 540.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPK 80
Cdd:COG0183 1 MREVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERA-GLDPEAVDDVILGCVLQA-GQGQNPARQAALLAGLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM------------SHGVD--FHPGMAKSVAKASgm 146
Cdd:COG0183 78 SVPAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMllpkarwgyrmnAKLVDpmINPGLTDPYTGLS-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 147 MGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVF 226
Cdd:COG0183 156 MGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVPDRKGEVVV-DRDEGPRPDTTLEKLAKLKPAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 227 DPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFE 306
Cdd:COG0183 235 KK-DGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 307 LNEAFAAQSLPCVKDLGLqDlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:COG0183 314 INEAFAAQVLAVLRELGL-D--PDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGRYGLATMCIGGGQGIALIIER 390
|
.
gi 752540570 387 V 387
Cdd:COG0183 391 V 391
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
5-386 |
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: 519.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 5 VIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNPnLDPNEIEDIYWGCVQQTLEqGFNIARNAALLAGIPKQVGA 84
Cdd:cd00751 1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAG-LDPEEVDDVIMGNVLQAGE-GQNPARQAALLAGLPESVPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 85 VTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGM------------MGLTAE 152
Cdd:cd00751 78 TTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGMLddgltdpftglsMGITAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 153 MLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVFDPvNGT 232
Cdd:cd00751 158 NVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVPGRKGPVVV-DRDEGPRPDTTLEKLAKLKPAFKK-DGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 233 VTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFA 312
Cdd:cd00751 236 VTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752540570 313 AQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:cd00751 316 AQALACLKELGLD---PEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
6-385 |
1.15e-176 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 496.75 E-value: 1.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 6 IVDCIRTPMGrSKGGAFRNVRAEDLSAHLMKSILLRNPnLDPNEIEDIYWGCVQQTLEQgFNIARNAALLAGIPKQVGAV 85
Cdd:TIGR01930 1 IVAAARTPIG-KFGGSLKDVSAEDLGAAVIKELLERNP-LDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 86 TVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM----SHGVDFHPGMAK---------SVAKASGMMGLTAE 152
Cdd:TIGR01930 78 TVNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYgvprSLRWGVKPGNAEledarlkdlTDANTGLPMGVTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 153 MLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVFDPvNGT 232
Cdd:TIGR01930 158 NLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVKGRKGPVTV-SSDEGIRPNTTLEKLAKLKPAFDP-DGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 233 VTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFA 312
Cdd:TIGR01930 236 VTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752540570 313 AQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFE 385
Cdd:TIGR01930 316 AQVLACIKELGLD---LEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGRYGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
1-387 |
3.84e-154 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 439.97 E-value: 3.84e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPK 80
Cdd:PRK05790 1 MKDVVIVSAARTPIGKF-GGALKDVSAVELGAIVIKAALERA-GVPPEQVDEVIMGQVLQA-GAGQNPARQAALKAGLPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMG---HVPMSHGVDFHPG-------MAKSV---AKASGMM 147
Cdd:PRK05790 78 EVPALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSqapHVLPGSRWGQKMGdvelvdtMIHDGltdAFNGYHM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 148 GLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFD 227
Cdd:PRK05790 158 GITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIKQRKGDPVVVDTDEHPRPDTTAESLAKLRPAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 228 PvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:PRK05790 238 K-DGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDLIEI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 308 NEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK05790 317 NEAFAAQALAVEKELGLD---PEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAKKGLATLCIGGGQGVALIVERP 393
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
1-387 |
7.34e-142 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 408.96 E-value: 7.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK09050 1 MTEAFICDAIRTPIGRY-GGALSSVRADDLGAVPLKALMARNPGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM---------SHGVDFH----------PGMAKSVA 141
Cdd:PRK09050 80 SVPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFvmgkadsafSRQAEIFdttigwrfvnPLMKAQYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 142 KASgmMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQ 221
Cdd:PRK09050 160 VDS--MPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTIPQKKGDPVVVDRDEHPRPETTLEALAK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 222 LRPVFDPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGD 301
Cdd:PRK09050 238 LKPVFRP-DGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPRIMGIGPAPATRKLLARLGLTIDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 302 IDLFELNEAFAAQSLPCVKDLGLQDlVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIA 381
Cdd:PRK09050 317 FDVIELNEAFAAQGLAVLRQLGLAD-DDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGRYALCTMCIGVGQGIA 395
|
....*.
gi 752540570 382 TVFERV 387
Cdd:PRK09050 396 LAIERV 401
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
1-386 |
2.87e-135 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 392.44 E-value: 2.87e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPk 80
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVPALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGYD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHM--------GHVPMSHGVDFHPGMAKSVAKASG------- 145
Cdd:PRK07851 80 FLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVsrfakgnsDSLPDTKNPLFAEAQARTAARAEGgaeawhd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 146 ------------MMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASgarfFYDYDEVIRPE 213
Cdd:PRK07851 160 predgllpdvyiAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLPDGT----VVSTDDGPRAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 214 TTVETLSQLRPVFDPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALK 293
Cdd:PRK07851 236 TTYEKVSQLKPVFRP-DGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQALA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 294 RAGLTVGDIDLFELNEAFAAQSLPCVKDLGLqDLvdEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMC 373
Cdd:PRK07851 315 RAGMSIDDIDLVEINEAFAAQVLPSARELGI-DE--DKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKTFGLETMC 391
|
410
....*....|...
gi 752540570 374 IGLGQGIATVFER 386
Cdd:PRK07851 392 VGGGQGMAMVLER 404
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
1-387 |
1.99e-132 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 385.13 E-value: 1.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK09052 5 LQDAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMS-HGVDFHPGMAKS---VAKASGmMGLTAEMLGK 156
Cdd:PRK09052 85 SVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPMMgNKPSMSPAIFARdenVGIAYG-MGLTAEKVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 157 LHGISRSQQDEFAARSHRRAHAATVEGRFAKEIV---------GLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFD 227
Cdd:PRK09052 164 QWKVSREDQDAFALESHQKAIAAQQAGEFKDEITpyeiterfpDLATGEVDVKTRTVDLDEGPRADTSLEGLAKLKPVFA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 228 PvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:PRK09052 244 N-KGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 308 NEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK09052 323 NEAFAAQSLAVIRDLGLD---PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFERL 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
1-387 |
5.29e-131 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 381.02 E-value: 5.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNPNLDPNeIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGP-IDDLIIGCAMPEAEQGLNMARNIGALAGLPY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM-SHGVDFHPGMAKSVAKASGMMGLTAEMLGKLHG 159
Cdd:PRK07661 80 TVPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMmGHVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 160 ISRSQQDEFAARSHRRAHAATVEGRFAKEIVGL--------EGHDASGARFFYDYDEVIRPETTVETLSQLRPVFDpVNG 231
Cdd:PRK07661 160 ISREDQDAFAVRSHQRAAKALAEGKFADEIVPVdvtlrtvgENNKLQEETITFSQDEGVRADTTLEILGKLRPAFN-VKG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 232 TVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAF 311
Cdd:PRK07661 239 SVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752540570 312 AAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK07661 319 ASQSIQVIRELGLD---EEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFELL 391
|
|
| pcaF |
TIGR02430 |
3-oxoadipyl-CoA thiolase; Members of this family are designated beta-ketoadipyl CoA thiolase, ... |
2-387 |
1.18e-130 |
|
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: 380.67 E-value: 1.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 2 KDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPKQ 81
Cdd:TIGR02430 1 REAYICDAIRTPIGRY-GGSLSSVRADDLAAVPIKALLARNPQLDWAAIDDVIYGCANQAGEDNRNVARMAALLAGLPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 82 VGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVD-------------------FHPGMAKSVAK 142
Cdd:TIGR02430 80 VPGTTVNRLCGSGLDAIGMAARAIKAGEADLLIAGGVESMSRAPFVMGKAdsafsrsakiedttigwrfINPLMKALYGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 143 ASgmMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQL 222
Cdd:TIGR02430 160 DS--MPETAENVAEEFGISREDQDAFALRSQQRTAAAQASGFFAEEIVPVVIPQKKGEPTVVDQDEHPRPETTLEGLAKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 223 RPVFDPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDI 302
Cdd:TIGR02430 238 KPVVRP-DGTVTAGNASGVNDGAAALLLASEEAVQRHGLTPRARILAAATAGVEPRIMGIGPVPATQKLLARAGLSIDQF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 303 DLFELNEAFAAQSLPCVKDLGLQDlVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIAT 382
Cdd:TIGR02430 317 DVIELNEAFAAQALAVLRELGLAD-DDARVNPNGGAIALGHPLGASGARLVLTALRQLERSGGRYALCTMCIGVGQGIAL 395
|
....*
gi 752540570 383 VFERV 387
Cdd:TIGR02430 396 AIERV 400
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
1-387 |
1.50e-125 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 367.78 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGcvqqtleQGFN------IARNAAL 74
Cdd:PRK06205 1 MRDAVICEPVRTPVGRF-GGAFKDVPAEELAATVIRALVERT-GIDPARIDDVIFG-------QGYPngeapaIGRVAAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 75 LAGIPKQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM----------SHGVDFHPGMA------- 137
Cdd:PRK06205 72 DAGLPVTVPGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEFyttdmrwgvrGGGVQLHDRLArgretag 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 138 -KSVAKASGMMGlTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTV 216
Cdd:PRK06205 152 gRRFPVPGGMIE-TAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTVPQRKGDPTVVDRDEHPRADTTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 217 ETLSQLRPVFDPV--NGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKR 294
Cdd:PRK06205 231 ESLAKLRPIMGKQdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALAR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 295 AGLTVGDIDLFELNEAFAAQSLPCVKDLGLQDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCI 374
Cdd:PRK06205 311 AGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRRQARYGLETMCI 390
|
410
....*....|...
gi 752540570 375 GLGQGIATVFERV 387
Cdd:PRK06205 391 GGGQGLAAVFERV 403
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
1-387 |
7.52e-125 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 365.58 E-value: 7.52e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGG-----AFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALL 75
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdVFNNIRPEELAAMLINRLIEKT-GIKPEEIDDIITGCALQVGENWLYGGRHPIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 76 AGIPKQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHG--VDFHPG-MAKSVAKASGM-----M 147
Cdd:PRK06445 80 ARLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphIEPNPKlLTDPKYIEYDLttgyvM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 148 GLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGhDASGARFFYDYDEVIRPETTVETLSQLRPVFD 227
Cdd:PRK06445 160 GLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-EVEGKKKVVDVDQSVRPDTSLEKLAKLPPAFK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 228 PvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:PRK06445 239 P-DGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 308 NEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK06445 318 NEAFAVVVLYAIKELGLD---PETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
1-387 |
2.27e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 364.59 E-value: 2.27e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSK-GGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIP 79
Cdd:PRK08242 1 MTEAYIYDAVRTPRGKGKkDGSLHEVKPVRLAAGLLEALRDRN-GLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 80 KQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM-SHGVDFhpGMAKSVAKASGMM--GLTAEMLGK 156
Cdd:PRK08242 80 ETVPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMgSDGGAW--AMDPSTNFPTYFVpqGISADLIAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 157 LHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEghDASGARFFyDYDEVIRPETTVETLSQLRPVFDP-------- 228
Cdd:PRK08242 158 KYGFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVK--DQNGLTIL-DHDEHMRPGTTMESLAKLKPSFAMmgemggfd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 229 ------------VNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAG 296
Cdd:PRK08242 235 avalqkypeverINHVHHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALAKAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 297 LTVGDIDLFELNEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGL 376
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDIP---HDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKRTALITLCVGG 391
|
410
....*....|.
gi 752540570 377 GQGIATVFERV 387
Cdd:PRK08242 392 GMGIATIIERV 402
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
1-387 |
9.92e-120 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 352.34 E-value: 9.92e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGrSKGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK09051 2 MREVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARA-GVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVP-MSHGVDFHPGMAKSVAK-----------ASGMMG 148
Cdd:PRK09051 80 ETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPyLLPAARWGARMGDAKLVdmmvgalhdpfGTIHMG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 149 LTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVFDP 228
Cdd:PRK09051 160 VTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEIKTRKGEVVF-DTDEHVRADTTLEDLAKLKPVFKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 229 VNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELN 308
Cdd:PRK09051 239 ENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLDVIEAN 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 309 EAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK09051 319 EAFAAQACAVTRELGLD---PAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGRYALVTMCIGGGQGIAAIFERL 394
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
3-386 |
1.66e-118 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 351.37 E-value: 1.66e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 3 DVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPKQV 82
Cdd:PLN02287 47 DVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVEKT-GLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 83 GAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGM--MGLTAEMLGKLHGI 160
Cdd:PLN02287 126 PVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVNPRVESFSQAQDCLlpMGITSENVAERFGV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 161 SRSQQDEFAARSHRRAHAATVEGRFAKEIVGL-----EGHDASGARFFYDYDEVIRPETTVETLSQLRPVFDPvNGTVTA 235
Cdd:PLN02287 206 TREEQDQAAVESHRKAAAATASGKFKDEIVPVhtkivDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKK-NGTTTA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 236 GTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQS 315
Cdd:PLN02287 285 GNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQF 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752540570 316 LPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEE--KDATLGVATMCIGLGQGIATVFER 386
Cdd:PLN02287 365 VYCCKKLGLD---PEKVNVNGGAIALGHPLGATGARCVATLLHEMKRrgKDCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
1-387 |
2.08e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 330.90 E-value: 2.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK07801 1 MAEAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRT-GIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHgvdfhpgmAKSVAKASGMMGLTAEMLGKLH-- 158
Cdd:PRK07801 79 EVPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPISS--------AMTAGEQLGFTSPFAESKGWLHry 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 159 ------------------GISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGhdasgarffYDYDEVIRpETTVETLS 220
Cdd:PRK07801 151 gdqevsqfrgaeliaekwGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG---------VTVDEGPR-ETSLEKMA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 221 QLRPVFDpvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVG 300
Cdd:PRK07801 221 GLKPLVE--GGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 301 DIDLFELNEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGI 380
Cdd:PRK07801 299 DIDVVEINEAFAPVVLAWLKETGAD---PAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRYGLQTMCEGGGTAN 375
|
....*..
gi 752540570 381 ATVFERV 387
Cdd:PRK07801 376 VTIIERL 382
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
1-387 |
8.41e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 327.07 E-value: 8.41e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK06504 1 MAEAYIVAAARTAGGR-KGGRLAGWHPADLAAQVLDALVDRS-GADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGM------------MG 148
Cdd:PRK06504 79 SVPGTSIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPSTLPAKNGLGHYKSPGMeerypgiqfsqfTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 149 ltAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFDp 228
Cdd:PRK06504 159 --AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTVDEGIRFDATLEGIAGVKLIAE- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 229 vNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELN 308
Cdd:PRK06504 236 -GGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVN 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 309 EAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK06504 315 EAFASVPLAWLKATGAD---PERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMANVTIVERL 390
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
1-386 |
1.68e-104 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 313.75 E-value: 1.68e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGrSKGGAFRNVRAEDLSAHLMKSiLLRNPNLDPNEIEDIYWGCVQqTLEQGFNIARNAALLAGIPK 80
Cdd:PRK05656 1 MQDVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRR-LLEQTGLDPAQVDEVILGQVL-TAGAGQNPARQAAIKAGLPH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVP-----------MSHGVDFHPGMAKSVAKASG--MM 147
Cdd:PRK05656 78 SVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPyvlpgartglrMGHAQLVDSMITDGLWDAFNdyHM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 148 GLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPVFD 227
Cdd:PRK05656 158 GITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPILIPQRKGEPLAFATDEQPRAGTTAESLAKLKPAFK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 228 PvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:PRK05656 238 K-DGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 308 NEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:PRK05656 317 NEAFAAQSLAVGKELGWD---AAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIGGGQGVALAIER 392
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
1-387 |
1.19e-103 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 311.71 E-value: 1.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSILLRNPnLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK08131 1 MLDAYIYDGLRSPFGR-HAGALASVRPDDLAATVIRRLLEKSG-FPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM------------------SHGVDF-HPGMAKSVA 141
Cdd:PRK08131 79 TVPGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFvmgkaesafsrdakvfdtTIGARFpNPKIVAQYG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 142 KASgmMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDAS-GARFFYDYDEVIRPETTVETLS 220
Cdd:PRK08131 159 NDS--MPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEVPQGRkLPPKLVAEDEHPRPSSTVEALT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 221 QLRPVFDpvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVG 300
Cdd:PRK08131 237 KLKPLFE--GGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 301 DIDLFELNEAFAAQSLPCVKDLGLqDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGI 380
Cdd:PRK08131 315 DMDIIEINEAFASQVLGCLKGLGV-DFDDPRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKRYAVVSLCIGVGQGL 393
|
....*..
gi 752540570 381 ATVFERV 387
Cdd:PRK08131 394 AMVIERV 400
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
1-387 |
2.04e-103 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 310.50 E-value: 2.04e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK07850 1 MGNPVIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDR-AGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGMMG--LTAEMLGKLH 158
Cdd:PRK07850 79 HVGATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGANAGPGRGLPRPDSWDIDMPNqfEAAERIAKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 159 GISRSQQDEFAARSHRRAHAATVEGRFAKEIVGL------EGHDASGARFFYDYDEVIRpETTVETLSQLRPVFDpvNGT 232
Cdd:PRK07850 159 GITREDVDAFGLRSQRRAAQAWAEGRFDREISPVqapvldEEGQPTGETRLVTRDQGLR-DTTMEGLAGLKPVLE--GGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 233 VTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFA 312
Cdd:PRK07850 236 HTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752540570 313 AQSLPCVKDLGlQDLvdEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK07850 316 SVVLSWAQVHE-PDM--DKVNVNGGAIALGHPVGSTGARLITTALHELERTDKSTALITMCAGGALSTGTIIERI 387
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
1-387 |
4.52e-97 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 295.77 E-value: 4.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPM--GRSKGGAFRnvrAEDLSAHLMKSILLRNPnLDPNEIEDIYWGCVQQTLEQgFNIARNAALLAGI 78
Cdd:PRK08170 2 ARPVYIVDGARTPFlkARGGPGPFS---ASDLAVAAGRALLNRQP-FAPDDLDEVILGCAMPSPDE-ANIARVVALRLGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 79 PKQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPM---SHGVDFHPGM--AKSV-AKASGM------ 146
Cdd:PRK08170 77 GEKVPAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLlfsEKMVRWLAGWyaAKSIgQKLAALgklrps 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 147 --------------------MGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFaKEIVGLegHDASGArfFYDY 206
Cdd:PRK08170 157 ylapvigllrgltdpvvglnMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRL-KEVVPL--FDRDGK--FYDH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 207 DEVIRPETTVETLSQLRPVFDPVNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVP 286
Cdd:PRK08170 232 DDGVRPDSSMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 287 ATQKALKRAGLTVGDIDLFELNEAFAAQSLPCV----------KDLGLQ----DLVDEKVNLNGGAIALGHPLGCSGARI 352
Cdd:PRK08170 312 AATPLLQRHGLTLEDLDLWEINEAFAAQVLACLaawadeeycrEQLGLDgalgELDRERLNVDGGAIALGHPVGASGARI 391
|
410 420 430
....*....|....*....|....*....|....*
gi 752540570 353 STTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK08170 392 VLHLLHALKRRGTKRGIAAICIGGGQGGAMLLERV 426
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
1-385 |
1.24e-96 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 293.60 E-value: 1.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGIPK 80
Cdd:PRK07108 1 MTEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVER-AKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHV--PMSHGVDFHPGMAKSVAKASGMMGLTAEMLGKLH 158
Cdd:PRK07108 80 TVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVqnEMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 159 GISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEG----HDASGARFF-----YDYDEVIRPETTVETLSQLRPVFDpv 229
Cdd:PRK07108 160 GISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVtagvADKATGRLFtkevtVSADEGIRPDTTLEGVSKIRSALP-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 230 NGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNE 309
Cdd:PRK07108 238 GGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752540570 310 AFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFE 385
Cdd:PRK07108 318 AFAVQVLYCRDTLGIP---MDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
1-385 |
2.19e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 292.77 E-value: 2.19e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPK 80
Cdd:PRK08235 1 MSKTVIVSAARTPFGKF-GGSLKDVKATELGGIAIKEALER-ANVSAEDVEEVIMGTVLQG-GQGQIPSRQAARAAGIPW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVP-----------MSHG--VDF--HPGMAKSVAKASg 145
Cdd:PRK08235 78 EVQTETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyilpgarwgyrMGDNevIDLmvADGLTCAFSGVH- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 146 mMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFYDYDEVIRPETTVETLSQLRPV 225
Cdd:PRK08235 157 -MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTIPQRKGDPIVVAKDEAPRKDTTIEKLAKLKPV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 226 FDPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLF 305
Cdd:PRK08235 236 FDK-TGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 306 ELNEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFE 385
Cdd:PRK08235 315 EINEAFAAVALASTEIAGID---PEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGGIGIAAICSGGGQGDAVLIE 391
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
1-387 |
6.84e-95 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 289.24 E-value: 6.84e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGrSKGGAFRNVRAEDLSAHLMKSILlRNPNLDPNEIEDIYWGCVQqTLEQGFNIARNAALLAGIPK 80
Cdd:PRK06633 2 TKPVYITHAKRTAFG-SFMGSLSTTPAPMLAAHLIKDIL-QNSKIDPALVNEVILGQVI-TGGSGQNPARQTLIHAGIPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGhVPMsHGVDFHPGMAKSVAKA-------------SGM- 146
Cdd:PRK06633 79 EVPGYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS-LGM-HGSYIRAGAKFGDIKMvdlmqydgltdvfSGVf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 147 MGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVF 226
Cdd:PRK06633 157 MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTIKKTTSLF-DHDETVRPDTSLEILSKLRPAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 227 DPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFE 306
Cdd:PRK06633 236 DK-NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 307 LNEAFAAQSLPCVKDLGLqDLvdEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:PRK06633 315 VNEAFAAQSIYVNREMKW-DM--EKVNINGGAIAIGHPIGASGGRVLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
.
gi 752540570 387 V 387
Cdd:PRK06633 392 V 392
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
4-254 |
2.96e-93 |
|
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: 279.96 E-value: 2.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 4 VVIVDCIRTPMGrSKGGAFRNVRAEDLSAHLMKSILLRNPnLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPKQVG 83
Cdd:pfam00108 1 VVIVSAARTPFG-SFGGSLKDVSAVELGAEAIKAALERAG-VDPEDVDEVIVGNVLQA-GEGQNPARQAALKAGIPDSAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 84 AVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGM--------------MGL 149
Cdd:pfam00108 78 AVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDARSGLKHGDEKKHDLlipdgltdafngyhMGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 150 TAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARFFyDYDEVIRPETTVETLSQLRPVFDPV 229
Cdd:pfam00108 158 TAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKPTV-DKDEGIRPPTTAEPLAKLKPAFDKE 236
|
250 260
....*....|....*....|....*
gi 752540570 230 nGTVTAGTSSALSDGAAAMLVMSAD 254
Cdd:pfam00108 237 -GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
2-387 |
1.63e-87 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 270.04 E-value: 1.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 2 KDVVIVDCIRTPMGRSKGgAFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIYWGCVQQT-LEQGfnIARNAALLAGIPK 80
Cdd:PLN02644 1 RDVCIVGVARTPIGGFLG-SLSSLSATELGSIAIQAALER-AGVDPALVQEVFFGNVLSAnLGQA--PARQAALGAGLPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVP-----------MSHG--VDfhpGMAKS----VAKA 143
Cdd:PLN02644 77 STICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPkylpearkgsrLGHDtvVD---GMLKDglwdVYND 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 144 SGMmGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGARF-FYDYDEVIRpETTVETLSQL 222
Cdd:PLN02644 154 FGM-GVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEVPGGRGRPSvIVDKDEGLG-KFDPAKLRKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 223 RPVFDPVNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDI 302
Cdd:PLN02644 232 RPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 303 DLFELNEAFAAQSLPCVKDLGLQDlvdEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIAT 382
Cdd:PLN02644 312 DYYEINEAFSVVALANQKLLGLDP---EKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGKYGVAGICNGGGGASAI 388
|
....*
gi 752540570 383 VFERV 387
Cdd:PLN02644 389 VVELM 393
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
4-386 |
1.11e-85 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 266.46 E-value: 1.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 4 VVIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGfNIARNAALLAGIPKQVG 83
Cdd:PRK08963 7 IAIVSGLRTPFAK-QATAFHGIPAVDLGKMVVGELLARS-EIDPELIEQLVFGQVVQMPEAP-NIAREIVLGTGMNVHTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 84 AVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMshGV------------------------------DFH 133
Cdd:PRK08963 84 AYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPI--GVskklaralvdlnkartlgqrlklfsrlrlrDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 134 PgMAKSVAKAS-GM-MGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIvgLEGHDASGARFFyDYDEVIR 211
Cdd:PRK08963 162 P-VPPAVAEYStGLrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEV--MTAHVPPYKQPL-EEDNNIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 212 PETTVETLSQLRPVFDPVNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDA-AIMGYGPVPATQK 290
Cdd:PRK08963 238 GDSTLEDYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 291 ALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLGLQDL-------------VD-EKVNLNGGAIALGHPLGCSGARISTTL 356
Cdd:PRK08963 318 ALERAGLTLADLTLIDMHEAFAAQTLANLQMFASERFareklgrsqaigeVDmSKFNVLGGSIAYGHPFAATGARMITQT 397
|
410 420 430
....*....|....*....|....*....|
gi 752540570 357 INLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:PRK08963 398 LHELRRRGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
1-387 |
2.34e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 262.79 E-value: 2.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSK--GGAFRNVRAEDLSAHLMKSILLRNpNLDPNEIEDIYWGCVQQTLEQGFNIARNAALLAGI 78
Cdd:PRK06025 1 MAEAYIIDAVRTPRGIGKvgKGALAHLHPQHLAATVLKALAERN-GLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 79 PKQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAKASGM----------MG 148
Cdd:PRK06025 80 DIKASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAGKPPLGMGSGNLrlralhpqshQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 149 LTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGHDASGArffYDYDEVIRPETTVETLSQLRPVFD- 227
Cdd:PRK06025 160 VCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPVYRDDGSVA---LDHEEFPRPQTTAEGLAALKPAFTa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 228 ----PVNGTVT--------------------AGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYG 283
Cdd:PRK06025 237 iadyPLDDKGTtyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLMLNA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 284 PVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLglqDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEK 363
Cdd:PRK06025 317 PVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDL---DLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELERR 393
|
410 420
....*....|....*....|....
gi 752540570 364 DATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK06025 394 GLKRGLVTMCAAGGMAPAIIIERV 417
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
5-387 |
6.98e-78 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 244.29 E-value: 6.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 5 VIVDCIRTPMGRsKGGAFRNVRAEDLSAHLMKSIllrNPNLDPnEIEDIYWGCVqqtLEQGFNIARNAALLAGIPKQVGA 84
Cdd:PRK06690 4 VIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLTFL---SKGMER-EIDDVILGNV---VGPGGNVARLSALEAGLGLHIPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 85 VTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPGMAKSVAkasgmMGLTAEMLGKLHGISRSQ 164
Cdd:PRK06690 76 VTIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSPETIGDPD-----MGVAAEYVAERYNITREM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 165 QDEFAARSHRRAHAATVEGRFAKEIVGLEGHDasgarffydyDEVIRPETTVETL-SQLRPVFDPvNGTVTAGTSSALSD 243
Cdd:PRK06690 151 QDEYACLSYKRTLQALEKGYIHEEILSFNGLL----------DESIKKEMNYERIiKRTKPAFLH-NGTVTAGNSCGVND 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 244 GAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLG 323
Cdd:PRK06690 220 GACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAKELQ 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752540570 324 LQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFERV 387
Cdd:PRK06690 300 IP---YEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMKYGIATLGIGGGIGLALLFEKV 360
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
1-387 |
6.42e-74 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 234.90 E-value: 6.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSkGGAFRNVRAEDLSAHLMKSILlRNPNLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPK 80
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKF-GRSFSKIKAPQLGGAAIKAVI-DDAKLDPALVQEVIMGNVIQA-GVGQNPAGQAAYHAGLPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 81 QVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPG----MAKSVAKASGM---------- 146
Cdd:PRK06366 78 GVTKYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRWGpkhlLHKNYKIDDAMlvdglidafy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 147 ---MGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGhdasgarffYDYDEVIRpETTVETLSQLR 223
Cdd:PRK06366 158 fehMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND---------LDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 224 PVFDPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDID 303
Cdd:PRK06366 228 PAFDK-NGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 304 LFELNEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATV 383
Cdd:PRK06366 307 LVEHNEAFSIASIIVRDQLKID---NERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKTGLATLCHGGGGAHTLT 383
|
....
gi 752540570 384 FERV 387
Cdd:PRK06366 384 LEMV 387
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
4-385 |
2.27e-71 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 228.62 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 4 VVIVDCIRTPMGRSKGGaFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIYWGCVQQTlEQGFNIARNAALLAGIPKQVG 83
Cdd:PRK06954 9 IVIASAARTPMAAFQGE-FASLTAPQLGAAAIAAAVER-AGLKPEQIDEVVMGCVLPA-GQGQAPARQAALGAGLPLSVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 84 AVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVP-----------MSHG--VD--FHPGMAKSVAKASgMMG 148
Cdd:PRK06954 86 CTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGqvLDhmFLDGLEDAYDKGR-LMG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 149 LTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEI--VGLEGhdaSGARFFYDYDEVIRpETTVETLSQLRPVF 226
Cdd:PRK06954 165 TFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIapVTVAG---KKGDTVIDRDEQPF-KANPEKIPTLKPAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 227 DPvNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFE 306
Cdd:PRK06954 241 SK-TGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 307 LNEAFAAQSLPCVKDLGLQDlvdEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFE 385
Cdd:PRK06954 320 INEAFAVVTMAAMKEHGLPH---EKVNVNGGACALGHPIGASGARILVTLIGALRARGGKRGVASLCIGGGEATAMGIE 395
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
261-386 |
5.76e-63 |
|
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: 197.48 E-value: 5.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 261 LTPRARVRAMAIAGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLGLQdlvDEKVNLNGGAIA 340
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGID---PEKVNVNGGAIA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 752540570 341 LGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:pfam02803 78 LGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
11-385 |
3.28e-55 |
|
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: 186.55 E-value: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 11 RTPMGRSKG--GAFRNVRAEDLSAHLMKSILLRnPNLDPNEIEDIywgCVQQTLEQGF--NIARNAALLAGIPKQVGAVT 86
Cdd:cd00826 5 MTAFGKFGGenGADANDLAHEAGAKAIAAALEP-AGVAAGAVEEA---CLGQVLGAGEgqNCAQQAAMHAGGLQEAPAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 87 VNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVpmshgvdfhpgmAKSVAKASGMMGLTAEMLgklhgiSRSQQD 166
Cdd:cd00826 81 MNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS------------AENNAKEKHIDVLINKYG------MRACPD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 167 EFAARSHRRAHAATVEGRFAKEIV-----GLEGHDASgarffyDYDEVIR--PETTVETLSQLRPVFDPvNGTVTAGTSS 239
Cdd:cd00826 143 AFALAGQAGAEAAEKDGRFKDEFAkfgvkGRKGDIHS------DADEYIQfgDEASLDEIAKLRPAFDK-EDFLTAGNAC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 240 ALSDGAAAMLVMSADRA-------KALGLTPRARVRAMAIAGCD----AAIMGYGPVPATQKALKRAGLTVGDIDLFELN 308
Cdd:cd00826 216 GLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDkkviKMVGGDGPIEAARKALEKAGLGIGDLDLIEAH 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 309 EAFAAQSLPCVKDLGL------QDLVDEK---------VNLNGGAIALGHPLGCSGARISTTLINLMEEKD-----ATLG 368
Cdd:cd00826 296 DAFAANACATNEALGLcpegqgGALVDRGdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAgkrqgAGAG 375
|
410
....*....|....*..
gi 752540570 369 VATMCIGLGQGIATVFE 385
Cdd:cd00826 376 LALLCIGGGGGAAMCIE 392
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
66-386 |
1.77e-49 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 172.39 E-value: 1.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 66 FNIARNAALLAGIPKQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDF-HPGMAKSVAKAS 144
Cdd:PRK09268 68 FNLTRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLrKILLELNRAKTT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 145 G----------------------------MMGLTAEMLGKLHGISRSQQDEFAARSHRRAHAATVEGRFAKEIVGLEGhd 196
Cdd:PRK09268 148 GdrlkalgklrpkhlapeiprngeprtglSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 197 asgarffYDYDEVIRPETTVETLSQLRPVFD-PVNGTVTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIA-- 273
Cdd:PRK09268 226 -------LTRDNNLRPDSSLEKLAKLKPVFGkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAav 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 274 ----GCDAAIMGygPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLP----------CVKDLGLQDL---VD-EKVNLN 335
Cdd:PRK09268 299 dfvhGKEGLLMA--PAYAVPRLLARNGLTLQDFDFYEIHEAFASQVLAtlkawedeeyCRERLGLDAPlgsIDrSKLNVN 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 752540570 336 GGAIALGHPLGCSGARISTTLINLMEEKDATLGVATMCIGLGQGIATVFER 386
Cdd:PRK09268 377 GSSLAAGHPFAATGGRIVATLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
1-351 |
1.24e-21 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 95.35 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKGGAFRNVRAEDLSAhlmksiLLRNPNLDPNEIEDIYWGCVQQTLEQG-FNIARNAALLAGIP 79
Cdd:PRK06064 1 MRDVAIIGVGQTKFGELWDVSLRDLAVEAGLE------ALEDAGIDGKDIDAMYVGNMSAGLFVSqEHIAALIADYAGLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 80 kQVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFhpgmaksVAKAS-----GMMGLT---- 150
Cdd:PRK06064 75 -PIPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDATEA-------IARAGdyeweEFFGATfpgl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 151 AEMLGKLH----GISRSQQDEFAARSHRRAhAATVEGRFAKEIvgleghdasgarffydydevirpetTVETLSQLRPVF 226
Cdd:PRK06064 147 YALIARRYmhkyGTTEEDLALVAVKNHYNG-SKNPYAQFQKEI-------------------------TVEQVLNSPPVA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 227 DPVngtvTAGTSSALSDGAAAMLVMSADRAKALGLTPrARVRAMAIA-------------GCDAAIMgygpvpATQKALK 293
Cdd:PRK06064 201 DPL----KLLDCSPITDGAAAVILASEEKAKEYTDTP-VWIKASGQAsdtialhdrkdftTLDAAVV------AAEKAYK 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 752540570 294 RAGLTVGDIDLFELNEAFAAQSLPCVKDLGL------QDLVDEK---------VNLNGGAIALGHPLGCSGAR 351
Cdd:PRK06064 270 MAGIEPKDIDVAEVHDCFTIAEILAYEDLGFakkgegGKLAREGqtyiggdipVNPSGGLKAKGHPVGATGVS 342
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
44-351 |
2.48e-21 |
|
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: 94.25 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 44 NLDPNEIEDIYWGCVQQTLEQGFnIARNAALLAGIPKqVGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGH 123
Cdd:cd00829 32 GLEPADIDAVVVGNAAGGRFQSF-PGALIAEYLGLLG-KPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 124 VPMSHGVDFHPG-------MAKSVAKASGMMGLTAEMLGKLHGISRSQQDEFAARSHRRA----HAatvegrfakeivgl 192
Cdd:cd00829 110 VPTGDEAGGRASdlewegpEPPGGLTPPALYALAARRYMHRYGTTREDLAKVAVKNHRNAarnpYA-------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 193 eghdasgarffydydeVIRPETTVETLSQLRPVFDPVngtvTAGTSSALSDGAAAMLVMSADRAKALGLTPrARVRAMAI 272
Cdd:cd00829 176 ----------------QFRKPITVEDVLNSRMIADPL----RLLDCCPVSDGAAAVVLASEERARELTDRP-VWILGVGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 273 A-------GCDAAIMGYGPVPATQKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLGL------QDLVDE--------- 330
Cdd:cd00829 235 AsdtpslsERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAELLALEDLGFcekgegGKLVREgdtaiggdl 314
|
330 340
....*....|....*....|.
gi 752540570 331 KVNLNGGAIALGHPLGCSGAR 351
Cdd:cd00829 315 PVNTSGGLLSKGHPLGATGLA 335
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
235-383 |
1.47e-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: 84.42 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 235 AGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDA----AIMGYGPVPATQKALKRAGLTVGDIDLFELNEA 310
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGAsmvpAVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 311 FAAQSLPCVKDLGLQDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLMEEKD-------ATLGVATMCIGLGQGIATV 383
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFipptprePRTVLLLGFGLGGTNAAVV 253
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
14-351 |
5.76e-11 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 63.51 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 14 MGRSKGGAFRNVRAEDLsahLMKSIL--LRNPNLDPNEIEDIYWGCVQQTLEQGFN-IARNAAL-LAGIPkqvgaVT-VN 88
Cdd:PRK06157 14 MGCTKFGERWDAGAEDL---MVEAFLeaLADAGIEPKDIDAAWFGTHYDEIGSGKSgTPLSRALrLPNIP-----VTrVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 89 RLCGSSMQALHDASRAIQVGDGDIFIIGGVEHM-----GHVPMSHGVDFHPGMAKSVAkASGMMGLTAEMLGKLHGISRs 163
Cdd:PRK06157 86 NFCATGSEAFRGAVYAVASGAYDIALALGVEKLkdtgyGGLPVANPGTLADMTMPNVT-APGNFAQLASAYAAKYGVSR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 164 qQDEFAARSHrrahaatvegrfakeiVGLEGHdASGARffyDYDEVIRPETTVET------LSQLRPVFDpvngtvtagt 237
Cdd:PRK06157 164 -EDLKRAMAH----------------VSVKSH-ANGAR---NPKAHLRKAVTEEQvlkapmIAGPLGLFD---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 238 SSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYG---------PVPATQKALKRAGLT--VGDIDLFE 306
Cdd:PRK06157 213 CCGVSDGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQYNgwdgsyfptTRIAARKAYREAGITdpREELSMAE 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 307 LNEAFAAQSLPCVKDLGL-------QDLVDEK--------VNLNGGAIALGHPLGCSGAR 351
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLsergqawRDVLDGFfdadgglpCQIDGGLKCFGHPIGASGLR 352
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
75-349 |
6.10e-10 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 60.30 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 75 LAGIPkqvgAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGVDFHPG-MAKSVAKASGMMG----- 148
Cdd:PRK08256 68 MTGIP----IVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQPGALGSVWDDRPSpLERFDKALAELQGfdpap 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 149 LTAEMLGKlhgisrsqqdefAARSHRRAHAATVEgRFAKEIVGLEGHDASGARffydydEVIRPETTVETLSQLRPVFDP 228
Cdd:PRK08256 144 PALRMFGG------------AGREHMEKYGTTAE-TFAKIGVKARRHAANNPY------AQFRDEYTLEDVLASPMIWGP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 229 VngtvTAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAI--------AGCDAA-IMGYG-PVPATQKALKRAGLT 298
Cdd:PRK08256 205 L----TRLQCCPPTCGAAAAIVCSEEFARKHGLDRAVEIVAQAMttdtpstfDGRSMIdLVGYDmTRAAAQQVYEQAGIG 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 752540570 299 VGDIDLFELNEAFAAQSLPCVKDLGL------QDLVDEK---------VNLNGGAIALGHPLGCSG 349
Cdd:PRK08256 281 PEDIDVVELHDCFSANELLTYEALGLcpegeaEKFIDDGdntyggrwvVNPSGGLLSKGHPLGATG 346
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
1-349 |
5.86e-09 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 57.26 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 1 MKDVVIVDCIRTPMGRSKggafrnvrAEDLSAhLMKSIL---LRNPNLDPNEIEDIYWGCVQQTL-EQGFNiarnAALLA 76
Cdd:PRK07516 1 MMTASIVGWAHTPFGKLD--------AETLES-LIVRVAreaLAHAGIAAGDVDGIFLGHFNAGFsPQDFP----ASLVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 77 GIPKQ---VGAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSH------GVDFHPGMAKSVAKASGMM 147
Cdd:PRK07516 68 QADPAlrfKPATRVENACATGSAAVYAALDAIEAGRARIVLVVGAEKMTATPTAEvgdillGASYLKEEGDTPGGFAGVF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 148 GLTAEMLGKLHGisrSQQDEF---AARSHRRAhaatVEGRFAKeivgleghdasgarffydydevIRPETTVE---TLSQ 221
Cdd:PRK07516 148 GRIAQAYFQRYG---DQSDALamiAAKNHANG----VANPYAQ----------------------MRKDLGFEfcrTVSE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 222 LRP-VFDPVNGTvtagTSSALSDGAAAMLVMSADRAKALgltPRA-RVRAMAIAGcDAAIMGY-------GPVPATQKAL 292
Cdd:PRK07516 199 KNPlVAGPLRRT----DCSLVSDGAAALVLADAETARAL---QRAvRFRARAHVN-DFLPLSRrdplafeGPRRAWQRAL 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 752540570 293 KRAGLTVGDIDLFELNEAFAAQSLPCVKDLGL------QDLVDE---------KVNLNGGAIALGHPLGCSG 349
Cdd:PRK07516 271 AQAGVTLDDLSFVETHDCFTIAELIEYEAMGLappgqgARAIREgwtakdgklPVNPSGGLKAKGHPIGATG 342
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
83-349 |
7.65e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 53.70 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 83 GAVTVNRLCGSSMQALHDASRAIQVGDGDIFIIGGVEHMGHVPMSHGV-----------DFHpgMAKSVAKASGMMGLTA 151
Cdd:PRK12578 74 VPLRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKMTEVDTSTSLaiggrggnyqwEYH--FYGTTFPTYYALYATR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 152 EMlgKLHGISRSQQDEFAARSHRRAhAATVEGRFAKEIvgleghdasgarffydydevirpetTVETLSQLRPVFDPVNg 231
Cdd:PRK12578 152 HM--AVYGTTEEQMALVSVKAHKYG-AMNPKAHFQKPV-------------------------TVEEVLKSRAISWPIK- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 232 tvtAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAIAGCDAAIMGYG-------PVPATQKALKRAGLTVGDIDL 304
Cdd:PRK12578 203 ---LLDSCPISDGSATAIFASEEKVKELKIDSPVWITGIGYANDYAYVARRGewvgfkaTQLAARQAYNMAKVTPNDIEV 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 305 FELNEAFAAQSLPCVKDLGLQD------LVDE---------KVNLNGGAIALGHPLGCSG 349
Cdd:PRK12578 280 ATVHDAFTIAEIMGYEDLGFTEkgkggkFIEEgqsekggkvGVNLFGGLKAKGHPLGATG 339
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
239-352 |
1.12e-06 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 50.07 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 239 SALSDGAAAMLVMSADRAKAL-GLTPRARVRAMaiaGCDAAIMGYGP-----------VP----ATQKALKRAGLTVGDI 302
Cdd:PRK06289 220 SQVTDGGAGVVLASDAYLRDYaDARPIPRIKGW---GHRTAPLGLEQkldrsagdpyvLPhvrqAVLDAYRRAGVGLDDL 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 752540570 303 DLFELNEAFAAQSLPCVKDLGLQ------DLVDE---------KVNLNGGAIALGHPLGCSGARI 352
Cdd:PRK06289 297 DGFEVHDCFTPSEYLAIDHIGLTgpgeswKAIENgeiaiggrlPINPSGGLIGGGHPVGASGVRM 361
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
235-385 |
2.43e-06 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 48.92 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 235 AGTSSALSDGAAAMLVMSADRAKALgltpraRVRAMAIAGCDAAIMGYGP-------VPATQKALKRA-GLTVGDIDLFE 306
Cdd:PRK07937 198 RHDIAPITDGAAAVVLAAGDRAREL------RERPAWITGIEHRIESPSLgardltrSPSTALAAEAAtGGDAGGVDVAE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 307 LNEAFAAQSLPCVKDLGLQDLVdeKVNLNGGAIAlGHPLGCSG-ARISTTLINLME-EKDATLGVATMCIGLGQGIATVF 384
Cdd:PRK07937 272 LHAPFTHQELILREALGLGDKT--KVNPSGGALA-ANPMFAAGlERIGEAARHIWDgSARRALAHATSGPALQQNLVAVL 348
|
.
gi 752540570 385 E 385
Cdd:PRK07937 349 E 349
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
239-351 |
6.71e-06 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 47.97 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 239 SALSDGAAAMLVMSADRAKALGLTPR----ARVRAMAIAGC-------DAAIMgYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLSPNdsrlVEIKSLACASGnlyedppDATRM-FTSRAAAQKALSMAGVKPSDLQVAEV 334
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 308 NEAFAAQSLPCVKDLGL------QDLVDE---------KVNLNGGAIALGHPLGCSGAR 351
Cdd:PTZ00455 335 HDCFTIAELLMYEALGIaeyghaKDLIRNgatalegriPVNTGGGLLSFGHPVGATGVK 393
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
240-349 |
1.25e-05 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 46.83 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 240 ALSDGAAAMLVMSADRAKALGLTPrarVRAMAI-AGCDA---AIMGYGPVP--------------------------ATQ 289
Cdd:PRK06365 224 AMSDGAACAILASEDKAFEITDKP---VLIKAIgTGSDTlrlADRPFGEVPllpnespddykdlrypgvhsfragrmAAK 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752540570 290 KALKRAGLT--VGDIDLFELNEAFAAQSLPCVKDLGL------QDLVDE---------KVNLNGGAIALGHPLGCSG 349
Cdd:PRK06365 301 EAYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygegGQFIESgkpelpgklPVNPSGGLLAAGHAVGATG 377
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
241-350 |
6.67e-05 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 44.66 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 241 LSDGAAAMLVMSADRAKALGLTPRARVRAMAIAgCDAAIM------GYGPVPATQKALKRAGLTVGDIDLF-------EL 307
Cdd:PRK05952 208 LGEGGAILVLESAELAQKRGAKIYGQILGFGLT-CDAYHMsapepdGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRL 286
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 752540570 308 NEAFAAQSlpcvkdlgLQDLVDEKVNLNGGAIALGHPLGCSGA 350
Cdd:PRK05952 287 NDQREANL--------IQALFPHRVAVSSTKGATGHTLGASGA 321
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
215-323 |
1.01e-04 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 43.87 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 215 TVETLSQLRPVFDPVngtvTAGTSSALSDGAAAMLVMSADRAKALgltPRARV----RAMAIAGCDAAIMGYGPVPAT-- 288
Cdd:PRK06158 186 TIDDVLAARMVSDPL----SVRDCCLVTDGAGAVVMVRADRARDL---PRPPVyvlgAAAATWHRQISSMPDLTVTAAae 258
|
90 100 110
....*....|....*....|....*....|....*..
gi 752540570 289 --QKALKRAGLTVGDIDLFELNEAFAAQSLPCVKDLG 323
Cdd:PRK06158 259 sgPRAFAMAGLTPADIDVVELYDAFTINTILFLEDLG 295
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
241-303 |
1.04e-04 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 44.07 E-value: 1.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 241 LSDGAAAMLVMSADRAKALGLTPRARVRAMAIAgCDAAIM------GYGPVPATQKALKRAGLTVGDID 303
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGAS-SDAYHItapdpdGEGAARAMRAALADAGLSPEDID 296
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
235-373 |
7.41e-04 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 41.08 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 235 AGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAiAGCDAAIMGY------GPVPATQKALKRAGLTVGDIDLFELN 308
Cdd:cd00825 153 AADGFVFGDGAGALVVEELEHALARGAHIYAEIVGTA-ATIDGAGMGAfapsaeGLARAAKEALAVAGLTVWDIDYLVAH 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 752540570 309 EAFAAQSLPCVKDLGLQDLVDEKVNLNGGAIALGHPLGCSGARISTTLINLME--EKDATLGVATMC 373
Cdd:cd00825 232 GTGTPIGDVKELKLLRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEhgFIPPSIHIEELD 298
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
234-307 |
1.22e-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: 40.50 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 752540570 234 TAGTSSALSDGAAAMLVMSADRAKALGLTPRARVRAMAI----AGCDAAIMGYGPVPATQKALKRAGLTVGDIDLFEL 307
Cdd:cd00828 222 ETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASttdgAGRSVPAGGKGIARAIRTALAKAGLSLDDLDVISA 299
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
241-303 |
1.71e-03 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 40.08 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 752540570 241 LSDGAAAMLVMSADRAKALGLTPRARVRAMAIAgCDAAIM------GYGPVPATQKALKRAGLTVGDID 303
Cdd:COG0304 229 LGEGAGVLVLEELEHAKARGAKIYAEVVGYGAS-SDAYHItapapdGEGAARAMRAALKDAGLSPEDID 296
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
168-342 |
3.02e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 39.36 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 168 FAARSHRR--AHAATVEGrFAKEIVGLEGHDASG--ARFfydydeviRPETTVETLSQLRPVFDPVNGTVTAGTSsalsD 243
Cdd:PRK06059 147 FALLARRRmdLYGATVED-FAQVKVKNARHGLLNpnARY--------RKEVTVEDVLASPVVSDPLRLLDICATS----D 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 244 GAAAMLVMSADRAKALGLTPRARVRAMAIAGC------------DAAIMGYGPVPAT---------QKALKRAGLTVGDI 302
Cdd:PRK06059 214 GAAALIVASKSFARRHLGSVAGVPSVRAISTVtprypqhlpelpDIATDSTAAVPAPervfkdqilDAAYAEAGIGPEDL 293
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 752540570 303 DLFELNEAFAAQSLPCVKDLGLQDLVDEKVNLNGGAIALG 342
Cdd:PRK06059 294 SLAEVYDLSTALELDWYEHLGLCPKGEAEALLRSGATTLG 333
|
|
| PRK07855 |
PRK07855 |
lipid-transfer protein; Provisional |
242-342 |
3.64e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181147 [Multi-domain] Cd Length: 386 Bit Score: 39.19 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752540570 242 SDGAAAMLVMSADRAKALGLTPrARVRAMAI-AGCDAAIMG--YGPVPAT--------QKALKRAGLTVGDIDLFELNEA 310
Cdd:PRK07855 216 SDGAVALVVTSAERARDLKQRP-AVIKAAAQgSGADQYMMTsyYRDDITGlpemglvaRQLWAQSGLGPADIDTAILYDH 294
|
90 100 110
....*....|....*....|....*....|..
gi 752540570 311 FAAQSLPCVKDLGLQDLVDEKVNLNGGAIALG 342
Cdd:PRK07855 295 FTPFVLMQLEELGFCGRGEAKDFIADGALELG 326
|
|
| |
