|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
1-420 |
0e+00 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 611.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 1 MHRLQVVLGHLAGRPESSSALQAAPCSARFPQASAS------DVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQ 74
Cdd:PLN02287 5 INRQRVLLRHLRPSSSEPSSLSASACAAGDSAAYHRttafgdDVVIVAAYRTPICKAKRGGFKDTYPDDLLAPVLKAVVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 75 DVRLKPEQLGDISVGNVLEPGAG-AVMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESM 153
Cdd:PLN02287 85 KTGLNPSEVGDIVVGTVLAPGSQrANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 154 SLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDD 233
Cdd:PLN02287 165 TTNPMAWEGGVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDEIVPVHTKIVDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 234 K-GDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGV 312
Cdd:PLN02287 245 KtGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 313 PPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLN 392
Cdd:PLN02287 325 DPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPLGATGARCVATLLH 404
|
410 420
....*....|....*....|....*....
gi 18700004 393 ELKRRGRRA-YGVVSMCIGTGMGAAAVFE 420
Cdd:PLN02287 405 EMKRRGKDCrFGVVSMCIGTGMGAAAVFE 433
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
39-421 |
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: 545.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 39 VVVHGRRTPIGRAsRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLST 118
Cdd:cd00751 1 VIVSAVRTPIGRF-GGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEK----------ARDCLTPMGMTSENV 188
Cdd:cd00751 80 VNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTldgmlddgltDPFTGLSMGITAENV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 189 AERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGG 268
Cdd:cd00751 160 AEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEV-----PGRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKKDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAF 348
Cdd:cd00751 235 TVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18700004 349 ASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFEY 421
Cdd:cd00751 315 AAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGGR-YGLATMCIGGGQGAAMVIER 386
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
36-420 |
1.13e-180 |
|
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: 508.45 E-value: 1.13e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRAsRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVP 115
Cdd:COG0183 2 REVVIVDAVRTPFGRF-GGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESE----KARDCLT------PMGMTS 185
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKlvdpMINPGLTdpytglSMGETA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 186 ENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFK 265
Cdd:COG0183 161 ENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEV-----PDRKGEVVVDRDEGPRPDTTLEKLAKLKPAFK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEIN 345
Cdd:COG0183 236 KDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDIDLIEIN 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18700004 346 EAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:COG0183 316 EAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGGR-YGLATMCIGGGQGIALIIE 389
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
40-420 |
2.49e-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: 474.79 E-value: 2.49e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 40 VVHGRRTPIGRAsRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSTV 119
Cdd:TIGR01930 1 IVAAARTPIGKF-GGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 120 NRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNI----SSRLLESEKAR-------DCLTPMGMTSENV 188
Cdd:TIGR01930 80 NRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLrwgvKPGNAELEDARlkdltdaNTGLPMGVTAENL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 189 AERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttvldDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGG 268
Cdd:TIGR01930 160 AKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVT-----VKGRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDPDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAF 348
Cdd:TIGR01930 235 TVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 349 ASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:TIGR01930 315 AAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGGR-YGLATMCIGGGQGAAVILE 385
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
36-422 |
4.20e-155 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 443.82 E-value: 4.20e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVP 115
Cdd:PRK05790 2 KDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLS-----------GMGNPGnissrlLESEKARDCLT----- 179
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAphvlpgsrwgqKMGDVE------LVDTMIHDGLTdafng 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 180 -PMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGLA 258
Cdd:PRK05790 155 yHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVT--IKQRKGD--PVVVDTDEHPRPDTTAESLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 259 KLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVND 338
Cdd:PRK05790 231 KLRPAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 339 IDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAV 418
Cdd:PRK05790 311 LDLIEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGAK-KGLATLCIGGGQGVALI 389
|
....
gi 18700004 419 FEYP 422
Cdd:PRK05790 390 VERP 393
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
37-420 |
3.48e-145 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 419.02 E-value: 3.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVR-LKPEQLGDISVGNVL-EPGAGAVMARIAQFLSGIPETV 114
Cdd:PRK09052 7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVPgLDPKLIEDAIVGCAMpEAEQGLNVARIGALLAGLPNSV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 115 PLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSG-MGNPGNISSRLLESEKARDCLTPMGMTSENVAERFG 193
Cdd:PRK09052 87 GGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPmMGNKPSMSPAIFARDENVGIAYGMGLTAEKVAEQWK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 194 ISRQKQDDFALASQQKAASAQSRGCFRAEIVP--VTTTVLDDKG---DKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGG 268
Cdd:PRK09052 167 VSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERFPDLATgevDVKTRTVDLDEGPRADTSLEGLAKLKPVFANKG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAF 348
Cdd:PRK09052 247 SVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAF 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 349 ASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK09052 327 AAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNLK-YGMVTMCVGTGMGAAGIFE 397
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
39-420 |
1.95e-139 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 404.13 E-value: 1.95e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 39 VVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVL-EPGAGAVMARIAQFLSGIPETVPLS 117
Cdd:PRK07661 5 VIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMpEAEQGLNMARNIGALAGLPYTVPAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGnpGNI---SSRLLESekARDCLTPMGMTSENVAERFGI 194
Cdd:PRK07661 85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPMM--GHVvrpNPRLVEA--APEYYMGMGHTAEQVAVKYGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 195 SRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVL----DDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGST 270
Cdd:PRK07661 161 SREDQDAFAVRSHQRAAKALAEGKFADEIVPVDVTLRtvgeNNKLQEETITFSQDEGVRADTTLEILGKLRPAFNVKGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 271 TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFAS 350
Cdd:PRK07661 241 TAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFAS 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 351 QAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK07661 321 QSIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNEQ-FGIVTMCIGGGMGAAGVFE 389
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
34-420 |
7.64e-120 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 354.27 E-value: 7.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 34 SASDVVVVHGRRTPIGrASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVL--EPgAGAVMARIAQFLSGIP 111
Cdd:PRK09051 1 MMREVVVVSGVRTAIG-TFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIptEP-RDMYLSRVAAINAGVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 112 ETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLT----------PM 181
Cdd:PRK09051 79 QETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPYLLPAARWGARMGDAKLVDMMVgalhdpfgtiHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 182 GMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVRPSTTMQGLAKLK 261
Cdd:PRK09051 159 GVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPVEI-----KTRKGEVVFDTDEHVRADTTLEDLAKLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 262 PAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDID 340
Cdd:PRK09051 234 PVFkKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLTVADLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 341 IFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK09051 314 VIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGGR-YALVTMCIGGGQGIAAIFE 392
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
37-420 |
5.43e-113 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 336.55 E-value: 5.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVL-QDVRLKPEQLGDISVGNV---LEPGAGavMARIAQFLSGIPE 112
Cdd:PRK08947 3 DVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLaRNPALDPAEIDDIIWGCVqqtLEQGFN--IARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 113 TVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMG-----NPGNISSrlleSEKARDCltpMGMTSEN 187
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNhgvdfHPGLSKN----VAKAAGM---MGLTAEM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 188 VAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTvlDDKGDKKTITVsqDEGVRPSTTMQGLAKLKPAFKD- 266
Cdd:PRK08947 154 LGKMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGH--DADGVLKLFDY--DEVIRPETTVEALAALRPAFDPv 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 267 GGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINE 346
Cdd:PRK08947 230 NGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18700004 347 AFASQAVYCVEKLGI---PAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK08947 310 AFAAQSLPCLKDLGLldkMDEKVNLNGGAIALGHPLGCSGARISTTLLNLMERKDAQ-FGLATMCIGLGQGIATVFE 385
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
36-420 |
1.93e-112 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 335.20 E-value: 1.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGA-GAVMARIAQFLSGIPETV 114
Cdd:PRK07108 2 TEAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGAtGANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 115 PLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGI 194
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCVQNEMNRHMLREGWLVEHKPEIYWSMLQTAENVAKRYGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 195 SRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTV-LDDKGD----KKTITVSQDEGVRPSTTMQGLAKLKPAFKdGGS 269
Cdd:PRK07108 162 SKERQDEYGVQSQQRAAAAQAAGRFDDEIVPITVTAgVADKATgrlfTKEVTVSADEGIRPDTTLEGVSKIRSALP-GGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 270 TTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFA 349
Cdd:PRK07108 241 ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18700004 350 SQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK07108 321 VQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRGAK-YVVVTMCIGGGQGAAGLFE 390
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
36-420 |
4.88e-112 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 334.61 E-value: 4.88e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQ-DVRLKPEQLGDISVGNVLEPGA-GAVMARIAQFLSGIPET 113
Cdd:PRK09050 2 TEAFICDAIRTPIGRYG-GALSSVRADDLGAVPLKALMArNPGVDWEAVDDVIYGCANQAGEdNRNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSG--MGNPGNISSRLLESE-------------KARDCL 178
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPfvMGKADSAFSRQAEIFdttigwrfvnplmKAQYGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 179 TPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVttTVLDDKGDkkTITVSQDEGVRPSTTMQGLA 258
Cdd:PRK09050 161 DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPV--TIPQKKGD--PVVVDRDEHPRPETTLEALA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 259 KLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGL-PILGVLrSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVN 337
Cdd:PRK09050 237 KLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLtPRARIL-GMATAGVEPRIMGIGPAPATRKLLARLGLTID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 338 DIDIFEINEAFASQAVYCVEKLGIP--AEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGA 415
Cdd:PRK09050 316 QFDVIELNEAFAAQGLAVLRQLGLAddDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGGR-YALCTMCIGVGQGI 394
|
....*
gi 18700004 416 AAVFE 420
Cdd:PRK09050 395 ALAIE 399
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
36-420 |
3.58e-111 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 332.34 E-value: 3.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVP 115
Cdd:PRK06205 2 RDAVICEPVRTPVGRFG-GAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMS-----LSGM---GNPGNIS-----SRLLESEKARDCLTPMG 182
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSnvefyTTDMrwgVRGGGVQlhdrlARGRETAGGRRFPVPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 183 M--TSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGLAKL 260
Cdd:PRK06205 161 MieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVT--VPQRKGD--PTVVDRDEHPRADTTLESLAKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 261 KP--AFKDGGST-TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVN 337
Cdd:PRK06205 237 RPimGKQDPEATvTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 338 DIDIFEINEAFASQAVYCVEKLGIPA---EKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMG 414
Cdd:PRK06205 317 DIDLIELNEAFAAQVLAVLKEWGFGAddeERLNVNGSGISLGHPVGATGGRILATLLRELQRRQAR-YGLETMCIGGGQG 395
|
....*.
gi 18700004 415 AAAVFE 420
Cdd:PRK06205 396 LAAVFE 401
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
37-420 |
3.75e-109 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 327.06 E-value: 3.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRAS-----RGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAG-AVMARIAQFLSGI 110
Cdd:PRK06445 3 DVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLARL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 111 PETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMG-NPG-NISSRLLESEKARDCLTP----MGMT 184
Cdd:PRK06445 83 PYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdNPHiEPNPKLLTDPKYIEYDLTtgyvMGLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 185 SENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVlddkgDKKTITVSQDEGVRPSTTMQGLAKLKPAF 264
Cdd:PRK06445 163 AEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEVEV-----EGKKKVVDVDQSVRPDTSLEKLAKLPPAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 265 KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEI 344
Cdd:PRK06445 238 KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDIDLWEI 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18700004 345 NEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06445 318 NEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKD-YGVATLCVGGGQGGAVVLE 392
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
37-420 |
4.00e-101 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 306.93 E-value: 4.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDV-RLKPEQLGDISVGNVLEPG-AGAVMARIAQFLSGIPeTV 114
Cdd:PRK07851 3 EAVIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGeQGFNMARVVAVLLGYD-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 115 PLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGN----PGNISSRLLESEkAR--------------- 175
Cdd:PRK07851 82 PGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNsdslPDTKNPLFAEAQ-ARtaaraeggaeawhdp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 176 -------DCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTT---TVlddkgdkktitVSQD 245
Cdd:PRK07851 161 redgllpDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLpdgTV-----------VSTD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 246 EGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAI 325
Cdd:PRK07851 230 DGPRAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 326 PAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVV 405
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDKT-FGLE 388
|
410
....*....|....*
gi 18700004 406 SMCIGTGMGAAAVFE 420
Cdd:PRK07851 389 TMCVGGGQGMAMVLE 403
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
45-420 |
4.38e-100 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 304.11 E-value: 4.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 45 RTPIGRASRGG-FKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPG-AGAVMARIAQFLSGIPETVPLSTVNRQ 122
Cdd:PRK08242 11 RTPRGKGKKDGsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGdQGADIARTAVLAAGLPETVPGVQINRF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPG---------NISSRLlesekardclTPMGMTSENVAERFG 193
Cdd:PRK08242 91 CASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVPMGSDGgawamdpstNFPTYF----------VPQGISADLIATKYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 194 ISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTT----TVLDdkgdkktitvsQDEGVRPSTTMQGLAKLKPAFKDGGS 269
Cdd:PRK08242 161 FSREDVDAYAVESQQRAAAAWAEGYFAKSVVPVKDqnglTILD-----------HDEHMRPGTTMESLAKLKPSFAMMGE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 270 T---------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAA 328
Cdd:PRK08242 230 MggfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 329 LQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMC 408
Cdd:PRK08242 310 LAKAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGKR-TALITLC 388
|
410
....*....|..
gi 18700004 409 IGTGMGAAAVFE 420
Cdd:PRK08242 389 VGGGMGIATIIE 400
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
38-291 |
1.99e-98 |
|
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: 294.60 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 38 VVVVHGRRTPIGRaSRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLS 117
Cdd:pfam00108 1 VVIVSAARTPFGS-FGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGN-ISSRLLESEKARDCLTP-----------MGMTS 185
Cdd:pfam00108 80 TINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDaRSGLKHGDEKKHDLLIPdgltdafngyhMGLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 186 ENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGdkktiTVSQDEGVRPSTTMQGLAKLKPAFK 265
Cdd:pfam00108 160 ENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP-----TVDKDEGIRPPTTAEPLAKLKPAFD 234
|
250 260
....*....|....*....|....*.
gi 18700004 266 DGGSTTAGNSSQVSDGAAAVLLARRS 291
Cdd:pfam00108 235 KEGTVTAGNASPINDGAAAVLLMSES 260
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
37-420 |
1.93e-96 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 294.31 E-value: 1.93e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGrASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPL 116
Cdd:PLN02644 2 DVCIVGVARTPIG-GFLGSLSSLSATELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQAPARQAALGAGLPPSTIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCL-----------TPMGMTS 185
Cdd:PLN02644 81 TTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAPKYLPEARKGSRLGHDTVVDGMlkdglwdvyndFGMGVCA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 186 ENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDKKTItVSQDEGVRpSTTMQGLAKLKPAFK 265
Cdd:PLN02644 161 ELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVE--VPGGRGRPSVI-VDKDEGLG-KFDPAKLRKLRPSFK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 266 -DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEI 344
Cdd:PLN02644 237 eDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGLEASQVDYYEI 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18700004 345 NEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PLN02644 317 NEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNGK-YGVAGICNGGGGASAIVVE 391
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
39-422 |
4.37e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 293.54 E-value: 4.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 39 VVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLST 118
Cdd:PRK08235 5 VIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPG-NISSRLLESE----KARDCLT------PMGMTSEN 187
Cdd:PRK08235 84 VNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYILPGaRWGYRMGDNEvidlMVADGLTcafsgvHMGVYGGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 188 VAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDkkTITVSQDEGVRPSTTMQGLAKLKPAFKDG 267
Cdd:PRK08235 164 VAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVT--IPQRKGD--PIVVAKDEAPRKDTTIEKLAKLKPVFDKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 268 GSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEA 347
Cdd:PRK08235 240 GTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEINEA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18700004 348 FASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGrRAYGVVSMCIGTGMGAAAVFEYP 422
Cdd:PRK08235 320 FAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRG-GGIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
37-422 |
5.24e-96 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 293.33 E-value: 5.24e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGrASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPL 116
Cdd:PRK05656 3 DVVIVAATRTAIG-SFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLTP-----------MGMTS 185
Cdd:PRK05656 82 MTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYVLPGARTGLRMGHAQLVDSMITdglwdafndyhMGITA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 186 ENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttVLDDKGDKktITVSQDEGVRPSTTMQGLAKLKPAFK 265
Cdd:PRK05656 162 ENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITPIL--IPQRKGEP--LAFATDEQPRAGTTAESLAKLKPAFK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEIN 345
Cdd:PRK05656 238 KDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAELDLIEAN 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18700004 346 EAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGTGMGAAAVFEYP 422
Cdd:PRK05656 318 EAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKK-GLATLCIGGGQGVALAIERD 393
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
37-420 |
2.08e-95 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 292.07 E-value: 2.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAV-MARIAQFLSGIPETVP 115
Cdd:PRK08131 3 DAYIYDGLRSPFGRHA-GALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRnVARNALLLAGLPVTVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSG--MGNPGNISSR----------------LLESEKARDc 177
Cdd:PRK08131 82 GQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPfvMGKAESAFSRdakvfdttigarfpnpKIVAQYGND- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 178 ltPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTttvLDDKGDKKTITVSQDEGVRPSTTMQGL 257
Cdd:PRK08131 161 --SMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIE---VPQGRKLPPKLVAEDEHPRPSSTVEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 258 AKLKPAFkDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVN 337
Cdd:PRK08131 236 TKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARAGLTLD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 338 DIDIFEINEAFASQAVYCVEKLGIPAE--KVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGA 415
Cdd:PRK08131 315 DMDIIEINEAFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGKR-YAVVSLCIGVGQGL 393
|
....*
gi 18700004 416 AAVFE 420
Cdd:PRK08131 394 AMVIE 398
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
38-420 |
1.06e-94 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 290.01 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 38 VVVVHGRRTPIGraSRGGFKNTTPDELLSAVLTA-VLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPL 116
Cdd:PRK06633 5 VYITHAKRTAFG--SFMGSLSTTPAPMLAAHLIKdILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSR--------LLESEKARDCLTP--MGMTSE 186
Cdd:PRK06633 83 YTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSLGMHGSYIRAGAKfgdikmvdLMQYDGLTDVFSGvfMGITAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 187 NVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVlddkgDKKTITVSQDEGVRPSTTMQGLAKLKPAFKD 266
Cdd:PRK06633 163 NISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDEILPIEVTI-----KKTTSLFDHDETVRPDTSLEILSKLRPAFDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 267 GGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINE 346
Cdd:PRK06633 238 NGVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18700004 347 AFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELkRRGRRAYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06633 318 AFAAQSIYVNREMKWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGL-RRAKAKKGLVTLCIGGGMGMAMCVE 390
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
39-420 |
2.00e-91 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 281.23 E-value: 2.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 39 VVVHGRRTPIGRasRGG-FKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGA-GAVMARIAQFLSGIPETVPL 116
Cdd:PRK07850 5 VIVEAVRTPIGK--RNGwLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEqSNNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMG-----NPGNISSrlleseKARDCLTPMGMTS-ENVAE 190
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGanagpGRGLPRP------DSWDIDMPNQFEAaERIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 191 RFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDK--KTITVSQDEGVRpSTTMQGLAKLKPAFkDGG 268
Cdd:PRK07850 157 RRGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPtgETRLVTRDQGLR-DTTMEGLAGLKPVL-EGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAF 348
Cdd:PRK07850 235 IHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAF 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 349 ASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK07850 315 ASVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDKS-TALITMCAGGALSTGTIIE 385
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
37-420 |
3.42e-87 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 271.51 E-value: 3.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRAsRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLePGAGAV-MARIAQFLSGIPETVP 115
Cdd:PRK08170 4 PVYIVDGARTPFLKA-RGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAM-PSPDEAnIARVVALRLGCGEKVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 116 LSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMS-------------LSGMGNPGNISSRLLESEKAR-DCLTP- 180
Cdd:PRK08170 82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMShapllfsekmvrwLAGWYAAKSIGQKLAALGKLRpSYLAPv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 181 ---------------MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGcFRAEIVPVtttvLDDKGDkktiTVSQD 245
Cdd:PRK08170 162 igllrgltdpvvglnMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEG-RLKEVVPL----FDRDGK----FYDHD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 246 EGVRPSTTMQGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYA 324
Cdd:PRK08170 233 DGVRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGPVHA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 325 IPAALQKAGLTVNDIDIFEINEAFASQAV----------YCVEKLGIPA-------EKVNPLGGAIALGHPLGCTGARQV 387
Cdd:PRK08170 313 ATPLLQRHGLTLEDLDLWEINEAFAAQVLaclaawadeeYCREQLGLDGalgeldrERLNVDGGAIALGHPVGASGARIV 392
|
410 420 430
....*....|....*....|....*....|...
gi 18700004 388 VTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK08170 393 LHLLHALKRRGTK-RGIAAICIGGGQGGAMLLE 424
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
38-420 |
2.13e-84 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 264.54 E-value: 2.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 38 VVVVHGRRTPIGRASRGgFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLS 117
Cdd:PRK08963 7 IAIVSGLRTPFAKQATA-FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDC--------------LTP--- 180
Cdd:PRK08963 86 SVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLgqrlklfsrlrlrdLLPvpp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 181 ----------MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEivpVTTTVLDDKGDkktiTVSQDEGVRP 250
Cdd:PRK08963 166 avaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE---VMTAHVPPYKQ----PLEEDNNIRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 251 STTMQGLAKLKPAF-KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPP-DVMGIGPAYAIPAA 328
Cdd:PRK08963 239 DSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVwQDMLLGPAYATPLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 329 LQKAGLTVNDIDIFEINEAFASQAV----------YCVEKLG-------IPAEKVNPLGGAIALGHPLGCTGARQVVTLL 391
Cdd:PRK08963 319 LERAGLTLADLTLIDMHEAFAAQTLanlqmfaserFAREKLGrsqaigeVDMSKFNVLGGSIAYGHPFAATGARMITQTL 398
|
410 420
....*....|....*....|....*....
gi 18700004 392 NELKRRGrRAYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK08963 399 HELRRRG-GGLGLTTACAAGGLGAAMVLE 426
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
39-420 |
4.97e-80 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 251.22 E-value: 4.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 39 VVVHGRRTPIGRASrGGFKNTTPDELLSAVLTAVLQDVrlkPEQLGDISVGNVLEPGAGavMARIAQFLSGIPETVPLST 118
Cdd:PRK06690 4 VIVEAKRTPIGKKN-GMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVVGPGGN--VARLSALEAGLGLHIPGVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 119 VNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSrllesEKARDclTPMGMTSENVAERFGISRQK 198
Cdd:PRK06690 78 IDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQNRARFSP-----ETIGD--PDMGVAAEYVAERYNITREM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 199 QDDFALASQQKAASAQSRGCFRAEIVPVTTtvLDDKGDKKTitvsqdegvRPSTTMqgLAKLKPAFKDGGSTTAGNSSQV 278
Cdd:PRK06690 151 QDEYACLSYKRTLQALEKGYIHEEILSFNG--LLDESIKKE---------MNYERI--IKRTKPAFLHNGTVTAGNSCGV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 279 SDGAAAVLLARRSKAEELGL-PILGVLRSyAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVE 357
Cdd:PRK06690 218 NDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFASKVVACAK 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18700004 358 KLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06690 297 ELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDMK-YGIATLGIGGGIGLALLFE 358
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
36-420 |
7.06e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 251.55 E-value: 7.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRaSRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNV--LEPGAGAVmARIAQFLSGIPET 113
Cdd:PRK07801 2 AEAYIVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVdtIGPQAGNI-ARTSWLAAGLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 114 VPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSL----SGM--GNPGNISSRLLESE--KARDCLTPMGM-- 183
Cdd:PRK07801 80 VPGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQipisSAMtaGEQLGFTSPFAESKgwLHRYGDQEVSQfr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 184 TSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvlddkGDkktitVSQDEGVRpSTTMQGLAKLKPa 263
Cdd:PRK07801 160 GAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPV--------GG-----VTVDEGPR-ETSLEKMAGLKP- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 264 FKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFE 343
Cdd:PRK07801 225 LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKTGLSIDDIDVVE 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18700004 344 INEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK07801 305 INEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGR-YGLQTMCEGGGTANVTIIE 380
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
40-420 |
7.51e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 243.87 E-value: 7.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 40 VVHGRRTPIGRasRGG-FKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAV-MARIAQFLSGIPETVPLS 117
Cdd:PRK06504 6 IVAAARTAGGR--KGGrLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATnVARNAVLASKLPESVPGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNP---------GNISSRLLEsEKARDCLTPMGMTSENV 188
Cdd:PRK06504 84 SIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVPMGSPstlpaknglGHYKSPGME-ERYPGIQFSQFTGAEMM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 189 AERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDKKTItvsqDEGVRPSTTMQGLAKLKPaFKDGG 268
Cdd:PRK06504 163 AKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHTV----DEGIRFDATLEGIAGVKL-IAEGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 269 STTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAF 348
Cdd:PRK06504 238 RLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDIDLYEVNEAF 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 349 ASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06504 318 ASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKR-YGLQTMCEGGGMANVTIVE 388
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
38-420 |
1.66e-72 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 232.86 E-value: 1.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 38 VVVVHGRRTPIGrASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLS 117
Cdd:PRK06954 9 IVIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 118 TVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSG-----------MGNPGNISSRLLES-EKARDCLTPMGMTS 185
Cdd:PRK06954 88 TVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDGlEDAYDKGRLMGTFA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 186 ENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTvlddkGDKKTITVSQDEGVRpSTTMQGLAKLKPAFK 265
Cdd:PRK06954 168 EECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVA-----GKKGDTVIDRDEQPF-KANPEKIPTLKPAFS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 266 DGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEIN 345
Cdd:PRK06954 242 KTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRAAEVDLFEIN 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18700004 346 EAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06954 322 EAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGGKR-GVASLCIGGGEATAMGIE 395
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
36-420 |
6.20e-70 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 226.97 E-value: 6.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTP--IGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGA-GAVMARIAQFLSGIPE 112
Cdd:PRK06025 2 AEAYIIDAVRTPrgIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKqGGDLGRMAALDAGYDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 113 TVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMgnpgnissrlLESEKARDCLTPMGMTSEN----- 187
Cdd:PRK06025 82 KASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAA----------MAAEDMAAGKPPLGMGSGNlrlra 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 188 -------------VAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvLDDKGdkkTITVSQDEGVRPSTTM 254
Cdd:PRK06025 152 lhpqshqgvcgdaIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV----YRDDG---SVALDHEEFPRPQTTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 255 QGLAKLKPAFK--------DGGST------------------TAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYA 308
Cdd:PRK06025 225 EGLAALKPAFTaiadypldDKGTTyrglinqkypdleikhvhHAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 309 VVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVV 388
Cdd:PRK06025 305 NMGDDPTLMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIG 384
|
410 420 430
....*....|....*....|....*....|..
gi 18700004 389 TLLNELKRRGRRaYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06025 385 TVLDELERRGLK-RGLVTMCAAGGMAPAIIIE 415
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
37-420 |
4.62e-69 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 223.73 E-value: 4.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 37 DVVVVHGRRTPIGRASRGgFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPL 116
Cdd:PRK06366 3 DVYIVSAKRTAIGKFGRS-FSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 117 STVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNI----SSRLLESEKARDCL-----------TPM 181
Cdd:PRK06366 82 YTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLrwgpKHLLHKNYKIDDAMlvdglidafyfEHM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 182 GMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTtvlddkgdkktitVSQDEGVRpSTTMQGLAKLK 261
Cdd:PRK06366 162 GVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND-------------LDRDEGIR-KTTMEDLAKLP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 262 PAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDI 341
Cdd:PRK06366 228 PAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAPIPATRKLLEKQNKSIDYYDL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18700004 342 FEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAyGVVSMCIGTGMGAAAVFE 420
Cdd:PRK06366 308 VEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTRHMKT-GLATLCHGGGGAHTLTLE 385
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
31-420 |
1.15e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 221.31 E-value: 1.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 31 PQASASDVVVVHGRRTPIGRaSRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGI 110
Cdd:PRK09268 2 TMPTVRRVAILGGNRIPFAR-SNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 111 PETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDC------------- 177
Cdd:PRK09268 81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTgdrlkalgklrpk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 178 -LTP-------------MGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVtttvlddKGdkktitVS 243
Cdd:PRK09268 161 hLAPeiprngeprtglsMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDLITPF-------LG------LT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 244 QDEGVRPSTTMQGLAKLKPAF--KDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVP----PDVM 317
Cdd:PRK09268 228 RDNNLRPDSSLEKLAKLKPVFgkGGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhgKEGL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 318 GIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQ----------AVYCVEKLGIPA-------EKVNPLGGAIALGHPLG 380
Cdd:PRK09268 308 LMAPAYAVPRLLARNGLTLQDFDFYEIHEAFASQvlatlkawedEEYCRERLGLDAplgsidrSKLNVNGSSLAAGHPFA 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 18700004 381 CTGARQVVTLLNELKRRGrRAYGVVSMCIGTGMGAAAVFE 420
Cdd:PRK09268 388 ATGGRIVATLAKLLAEKG-SGRGLISICAAGGQGVTAILE 426
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
298-421 |
1.19e-65 |
|
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 397094 [Multi-domain] Cd Length: 123 Bit Score: 205.57 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 298 LPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGH 377
Cdd:pfam02803 1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 18700004 378 PLGCTGARQVVTLLNELKRRGRRaYGVVSMCIGTGMGAAAVFEY 421
Cdd:pfam02803 81 PLGASGARILVTLLHELKRRGGK-YGLASLCIGGGQGVAMIIER 123
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
45-421 |
1.21e-54 |
|
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: 186.16 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 45 RTPIGR--ASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSTVNRQ 122
Cdd:cd00826 5 MTAFGKfgGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 123 CSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPgnissrlleSEKARDCLTPMGMtsenvaerfgiSRQKQDDF 202
Cdd:cd00826 85 CGSGLRALALAMQLIAGGDANCILAGGFEKMETSAENNA---------KEKHIDVLINKYG-----------MRACPDAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 203 ALASQQKAASAQSRGCFRAEIVPVTTtvlddKGDKKTITVSQDEGVR--PSTTMQGLAKLKPAFKDGGSTTAGNSSQVSD 280
Cdd:cd00826 145 ALAGQAGAEAAEKDGRFKDEFAKFGV-----KGRKGDIHSDADEYIQfgDEASLDEIAKLRPAFDKEDFLTAGNACGLND 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 281 GAAAVLLARRSKAEELGLPI-------LGVLRSYAVVGVPPD----VMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFA 349
Cdd:cd00826 220 GAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIEAHDAFA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 350 SQAVYCVEKLGIPAEK------------------VNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAY----GVVSM 407
Cdd:cd00826 300 ANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRQgagaGLALL 379
|
410
....*....|....
gi 18700004 408 CIGTGMGAAAVFEY 421
Cdd:cd00826 380 CIGGGGGAAMCIES 393
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
46-418 |
4.09e-23 |
|
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: 100.03 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 46 TPIGRASrggfkNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVL-EPGAGAVMARIAQFLSGIPetVPLSTVNRQCS 124
Cdd:cd00829 6 TPFGRRS-----DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAgGRFQSFPGALIAEYLGLLG--KPATRVEAAGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 125 SGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNP--GNISSRLLESEKARDCLTPMGMTSeNVA----ERFGISRqk 198
Cdd:cd00829 79 SGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEagGRASDLEWEGPEPPGGLTPPALYA-LAArrymHRYGTTR-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 199 qDDFAL--ASQQKAASAQSRGCFRAEIvpvtttvlddkgdkktiTVSQDEGVRPSTTmqglaklkPafkdggsTTAGNSS 276
Cdd:cd00829 156 -EDLAKvaVKNHRNAARNPYAQFRKPI-----------------TVEDVLNSRMIAD--------P-------LRLLDCC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 277 QVSDGAAAVLLARRSKAEELGLP---ILGV---LRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFAS 350
Cdd:cd00829 203 PVSDGAAAVVLASEERARELTDRpvwILGVgaaSDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 351 QAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELKRRGrRAYGV----VSM 407
Cdd:cd00829 283 AELLALEDLGF-CEKgeggklvregdtaiggdlpVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEA-GARQVpgarVGL 360
|
410
....*....|.
gi 18700004 408 CIGTGMGAAAV 418
Cdd:cd00829 361 AHNIGGTGSAA 371
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
272-418 |
1.15e-16 |
|
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: 79.41 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 272 AGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPD----VMGIGPAYAIPAALQKAGLTVNDIDIFEINEA 347
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 348 FASQAVYCVEKLGIPAEKVNPL---GGAIALGHPLGCTGARQVVTLLNELKRRGRRAY------GVVSMCIGTGMGAAAV 418
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSPavsATLIMTGHPLGAAGLAILDELLLMLEHEFIPPTpreprtVLLLGFGLGGTNAAVV 253
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
36-417 |
1.16e-14 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 74.93 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 36 SDVVVVHGRRTPIGRASRGGFknttPDELLSAVLTAvLQDVRLKPEQLGDISVGNVL------EPGAGAVMARIAQfLSG 109
Cdd:PRK06064 2 RDVAIIGVGQTKFGELWDVSL----RDLAVEAGLEA-LEDAGIDGKDIDAMYVGNMSaglfvsQEHIAALIADYAG-LAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 110 IPETvplsTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNP----GNISSRLLESEKArdcLTPMG--- 182
Cdd:PRK06064 76 IPAT----RVEAACASGGAALRQAYLAVASGEADVVLAAGVEKMTDVPTPDAteaiARAGDYEWEEFFG---ATFPGlya 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 183 MTSENVAERFGIsrqKQDDFALAS--QQKAASAQSRGCFRaeivpvtttvlddkgdkKTITVSQdegVRPSTTMQGLAKL 260
Cdd:PRK06064 149 LIARRYMHKYGT---TEEDLALVAvkNHYNGSKNPYAQFQ-----------------KEITVEQ---VLNSPPVADPLKL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 261 KpafkdggsttagNSSQVSDGAAAVLLARRSKAEELGLPILGVLRS-----YAVVGVPPDVMGIGPA-YAIPAALQKAGL 334
Cdd:PRK06064 206 L------------DCSPITDGAAAVILASEEKAKEYTDTPVWIKASgqasdTIALHDRKDFTTLDAAvVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 335 TVNDIDIFEINEAFASQAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELK 395
Cdd:PRK06064 274 EPKDIDVAEVHDCFTIAEILAYEDLGF-AKKgeggklaregqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLR 352
|
410 420
....*....|....*....|..
gi 18700004 396 RRGRRAYGVVsmcIGTGMGAAA 417
Cdd:PRK06064 353 GEAEKGRQQV---IGAGYGLTH 371
|
|
| PRK06289 |
PRK06289 |
acetyl-CoA acetyltransferase; Provisional |
63-385 |
5.14e-14 |
|
acetyl-CoA acetyltransferase; Provisional
Pssm-ID: 235771 [Multi-domain] Cd Length: 403 Bit Score: 73.18 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 63 ELLSAVLTAVLQDVRLKPEQLGDISVGNVlepgAGAVMARIAQfLSGIPETV-------PLSTVNRQCSSGLQAVANIAG 135
Cdd:PRK06289 28 DLTREVVDGTLAAAGVDADDIEVVHVGNF----FGELFAGQGH-LGAMPATVhpalwgvPASRHEAACASGSVATLAAMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 136 GIRNGSYDIGMACGVESM-SLSGMGNPGNISSRLLESEKARDCLTP----MGMTSENVAERFGISRQKQDDFA---LASQ 207
Cdd:PRK06289 103 DLRAGRYDVALVVGVELMkTVPGDVAAEHLGAAAWTGHEGQDARFPwpsmFARVADEYDRRYGLDEEHLRAIAeinFANA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 208 QKAASAQSRGCFraeiVPVTTTVLDDKgdkktitvsqdegvrpsttmqglakLKPAFkdGGSTTAGNSSQVSDGAAAVLL 287
Cdd:PRK06289 183 RRNPNAQTRGWA----FPDEATNDDDA-------------------------TNPVV--EGRLRRQDCSQVTDGGAGVVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 288 ARRSKAEELG----LP-ILGVLRSYAVVGVPPDV-MGIGPAYAIPA-------ALQKAGLTVNDIDIFEINEAFASQAVY 354
Cdd:PRK06289 232 ASDAYLRDYAdarpIPrIKGWGHRTAPLGLEQKLdRSAGDPYVLPHvrqavldAYRRAGVGLDDLDGFEVHDCFTPSEYL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18700004 355 CVEKLGI--PAEK----------------VNPLGGAIALGHPLGCTGAR 385
Cdd:PRK06289 312 AIDHIGLtgPGESwkaiengeiaiggrlpINPSGGLIGGGHPVGASGVR 360
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
48-395 |
2.85e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 61.40 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 48 IGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLStVNRQCSSGL 127
Cdd:PRK12578 8 VGNSKFGRRDDVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 128 QAVANIAGGIRNGSYDIGMACGVESM-------SLSGMGNPGNIssrLLESEKARDCL-TPMGMTSENVAERFGISrqkQ 199
Cdd:PRK12578 87 AASLTAYTAVASGLVDMAIAVGVDKMtevdtstSLAIGGRGGNY---QWEYHFYGTTFpTYYALYATRHMAVYGTT---E 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 200 DDFALAS--QQKAASAQSRGCFRaeivpvtttvlddkgdkKTITVsqdEGVRPSTTMQGLAKLKpafkdggsttagNSSQ 277
Cdd:PRK12578 161 EQMALVSvkAHKYGAMNPKAHFQ-----------------KPVTV---EEVLKSRAISWPIKLL------------DSCP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 278 VSDGAAAVLLARRSKAEELGL--PI----LGVLRSYAVVGVPPDVMGIGPAY-AIPAALQKAGLTVNDIDIFEINEAFAS 350
Cdd:PRK12578 209 ISDGSATAIFASEEKVKELKIdsPVwitgIGYANDYAYVARRGEWVGFKATQlAARQAYNMAKVTPNDIEVATVHDAFTI 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18700004 351 QAVYCVEKLGIpAEK-------------------VNPLGGAIALGHPLGCTGARQVVTLLNELK 395
Cdd:PRK12578 289 AEIMGYEDLGF-TEKgkggkfieegqsekggkvgVNLFGGLKAKGHPLGATGLSMIYEITKQLR 351
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
276-395 |
1.52e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 56.44 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 276 SQVSDGAAAVLLARRSKAEELGL-----PILGVLRSYAVVGV----PPDVMGIGPAY-AIPAALQKAGLTVNDIDIFEIN 345
Cdd:PTZ00455 256 SQVSDGGAGLVLASEEGLQKMGLspndsRLVEIKSLACASGNlyedPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVH 335
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18700004 346 EAFASQAVYCVEKLGIpAE-------------------KVNPLGGAIALGHPLGCTGARQVVTLLNELK 395
Cdd:PTZ00455 336 DCFTIAELLMYEALGI-AEyghakdlirngatalegriPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
276-421 |
1.47e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 53.03 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 276 SQVSDGAAAVLLARRSKAEELGLPIlgVLRSYAVVGvppDVMGI---------GPAYAIPAALQKAGLTVNDIDIFEINE 346
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALQRAV--RFRARAHVN---DFLPLsrrdplafeGPRRAWQRALAQAGVTLDDLSFVETHD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 347 AFASQAVYCVEKLGIPAE------------------KVNPLGGAIALGHPLGCTG-------ARQVVTLLNELKRRGRRA 401
Cdd:PRK07516 288 CFTIAELIEYEAMGLAPPgqgarairegwtakdgklPVNPSGGLKAKGHPIGATGvsmhvlaAMQLTGEAGGMQIPGAKL 367
|
170 180
....*....|....*....|
gi 18700004 402 YGVVSmcigtgMGAAAVFEY 421
Cdd:PRK07516 368 AGVFN------MGGAAVANY 381
|
|
| PRK06365 |
PRK06365 |
thiolase domain-containing protein; |
328-403 |
3.03e-06 |
|
thiolase domain-containing protein;
Pssm-ID: 235785 [Multi-domain] Cd Length: 430 Bit Score: 49.14 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 328 ALQKAGLT--VNDIDIFEINEAFASQAVYCVEKLGI--------------PAEK----VNPLGGAIALGHPLGCTGARQV 387
Cdd:PRK06365 302 AYEMAGITdpLNDLDLIELHDAYTSSEIQTYEDLGLckygeggqfiesgkPELPgklpVNPSGGLLAAGHAVGATGIMQA 381
|
90
....*....|....*.
gi 18700004 388 VTLLNELKRRGRRAYG 403
Cdd:PRK06365 382 VFMFWQLQGRIKKHFH 397
|
|
| ACP_syn_III_C |
pfam08541 |
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ... |
329-421 |
1.44e-05 |
|
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.
Pssm-ID: 430060 Cd Length: 90 Bit Score: 43.26 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 329 LQKAGLTVNDIDIFEINEA--FASQAVycVEKLGIPAEKVnplggAIALGHpLGCTGARQVVTLLNELKRRGRRAYGVVS 406
Cdd:pfam08541 1 LEKAGLTPEDIDWFVPHQAnlRIIDAV--AKRLGLPPEKV-----VVNLDE-YGNTSAASIPLALDEAVEEGKLKPGDLV 72
|
90
....*....|....*...
gi 18700004 407 MCIGTGMG---AAAVFEY 421
Cdd:pfam08541 73 LLVGFGAGltwGAALLRW 90
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
279-343 |
2.39e-05 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 46.40 E-value: 2.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 279 SDGAAAVLLARRSKAEELGLPILGVLRSYAV-------VGVPPDvmGIGPAYAIPAALQKAGLTVNDIDIFE 343
Cdd:cd00833 234 GEGVGVVVLKRLSDALRDGDRIYAVIRGSAVnqdgrtkGITAPS--GEAQAALIRRAYARAGVDPSDIDYVE 303
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
279-386 |
7.89e-05 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 44.50 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 279 SDGAAAVLLARRSKAEELGLPilgvlRSYAVVG-----------VPPDVMG-IGPAYAIPAALQ---KAGLTVNDIDIFE 343
Cdd:PRK08256 214 TCGAAAAIVCSEEFARKHGLD-----RAVEIVAqamttdtpstfDGRSMIDlVGYDMTRAAAQQvyeQAGIGPEDIDVVE 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18700004 344 INEAFASQAVYCVEKLGI----PAEK--------------VNPLGGAIALGHPLGCTGARQ 386
Cdd:PRK08256 289 LHDCFSANELLTYEALGLcpegEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATGLAQ 349
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
279-421 |
8.54e-05 |
|
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440101 [Multi-domain] Cd Length: 323 Bit Score: 44.33 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 279 SDGAAAVLLarrsKAEELGLPILG-VLRSYA-----------VVGVPPDVMGIGPAY------------------AIPAA 328
Cdd:COG0332 158 GDGAGAVVL----EASEEGPGILGsVLGSDGsgadllvvpagGSRNPPSPVDEGDHYlrmdgrevfkfavrnlpeVIREA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 329 LQKAGLTVNDIDIF-------EINEAFAsqavycvEKLGIPAEKVnplggaIALGHPLGCTGARQVVTLLNELKRRGRRA 401
Cdd:COG0332 234 LEKAGLTLDDIDWFiphqanlRIIEAVA-------KRLGLPEEKV------VVNIDRYGNTSAASIPLALDEALREGRIK 300
|
170 180
....*....|....*....|...
gi 18700004 402 YGVVSMCIGTGMG---AAAVFEY 421
Cdd:COG0332 301 PGDLVLLAGFGAGltwGAAVLRW 323
|
|
| PRK07937 |
PRK07937 |
lipid-transfer protein; Provisional |
278-383 |
1.22e-04 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181173 [Multi-domain] Cd Length: 352 Bit Score: 43.91 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 278 VSDGAAAVLLARRSKAEEL--------GL------PILGVlRSYAVVgvppdvmgigPAYAIpAALQKAGLTVNDIDIFE 343
Cdd:PRK07937 204 ITDGAAAVVLAAGDRARELrerpawitGIehriesPSLGA-RDLTRS----------PSTAL-AAEAATGGDAGGVDVAE 271
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18700004 344 INEAFASQAVYCVEKLGIPAE-KVNPLGGAIAlGHPLGCTG 383
Cdd:PRK07937 272 LHAPFTHQELILREALGLGDKtKVNPSGGALA-ANPMFAAG 311
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
279-397 |
1.46e-04 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 43.97 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 279 SDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPD----VMGIGPAYAIPAALQKAGLTVNDIDIfeINEAFASQAVY 354
Cdd:cd00828 230 AEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGrsvpAGGKGIARAIRTALAKAGLSLDDLDV--ISAHGTSTPAN 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18700004 355 CVEKLGIPAEKVNPLGGAIAL-------GHPLGCTGARQVVTLLNELKRR 397
Cdd:cd00828 308 DVAESRAIAEVAGALGAPLPVtaqkalfGHSKGAAGALQLIGALQSLEHG 357
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
279-384 |
4.45e-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: 42.14 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 279 SDGAAAVLLARRSKAEELGLPILGVLRSYAVVG-----VPPDVMGIGPAYAIPAALQKAGLTVNDIDIfeIN-------- 345
Cdd:cd00834 230 GEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahgtstpl 307
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18700004 346 ----EAFASQAVYCVEKLGIPaekVNPLGGAIalGHPLGCTGA 384
Cdd:cd00834 308 ndaaESKAIKRVFGEHAKKVP---VSSTKSMT--GHLLGAAGA 345
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
279-340 |
8.76e-04 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 41.23 E-value: 8.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18700004 279 SDGAAAVLLARRSKAEELGLPILGVLRSYA-------VVGVPPDvmGIGPAYAIPAALQKAGLTVNDID 340
Cdd:COG0304 230 GEGAGVLVLEELEHAKARGAKIYAEVVGYGassdayhITAPAPD--GEGAARAMRAALKDAGLSPEDID 296
|
|
| PRK06157 |
PRK06157 |
acetyl-CoA acetyltransferase; Validated |
61-387 |
1.37e-03 |
|
acetyl-CoA acetyltransferase; Validated
Pssm-ID: 180433 [Multi-domain] Cd Length: 398 Bit Score: 40.78 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 61 PDELLSAVLTAVLQDVRLKPEQLGDISVGNVL-EPGAGavmariaqfLSGIP-------ETVPLSTVNRQCSSGLQAVAN 132
Cdd:PRK06157 27 AEDLMVEAFLEALADAGIEPKDIDAAWFGTHYdEIGSG---------KSGTPlsralrlPNIPVTRVENFCATGSEAFRG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 133 IAGGIRNGSYDIGMACGVESMSLSGMG-----NPGNISSRLLESekardcLTPMGMTSENV---AERFGISRQkqddfal 204
Cdd:PRK06157 98 AVYAVASGAYDIALALGVEKLKDTGYGglpvaNPGTLADMTMPN------VTAPGNFAQLAsayAAKYGVSRE------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 205 asQQKAASAQsrgcfraeivpvtttvlddkgdkktITV-SQDEGVR--------PSTTMQGLAKLKPAFKDGGSTTAGns 275
Cdd:PRK06157 165 --DLKRAMAH-------------------------VSVkSHANGARnpkahlrkAVTEEQVLKAPMIAGPLGLFDCCG-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 276 sqVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGiGPAY----------AIPAALQKAGLT--VNDIDIFE 343
Cdd:PRK06157 216 --VSDGAAAAIVTTPEIARALGKKDPVYVKALQLAVSNGWELQ-YNGWdgsyfpttriAARKAYREAGITdpREELSMAE 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18700004 344 INEAFASQAVYCVEKLGIPAE------------------KVNPLGGAIALGHPLGCTGARQV 387
Cdd:PRK06157 293 VHDCFSITELVTMEDLGLSERgqawrdvldgffdadgglPCQIDGGLKCFGHPIGASGLRML 354
|
|
| PRK06158 |
PRK06158 |
thiolase; Provisional |
278-360 |
1.71e-03 |
|
thiolase; Provisional
Pssm-ID: 180434 [Multi-domain] Cd Length: 384 Bit Score: 40.40 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 278 VSDGAAAVLLARRSKAEELGLPILGVLRSYAVV-----GVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQA 352
Cdd:PRK06158 208 VTDGAGAVVMVRADRARDLPRPPVYVLGAAAATwhrqiSSMPDLTVTAAAESGPRAFAMAGLTPADIDVVELYDAFTINT 287
|
....*...
gi 18700004 353 VYCVEKLG 360
Cdd:PRK06158 288 ILFLEDLG 295
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
280-391 |
5.71e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 38.94 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18700004 280 DGAAAVLLARRSKAEELGLPILGVLRSYAVVG-----VPPDVMGIGPAYAIPAALQKAGLTVNDID----------IFEI 344
Cdd:PRK07910 242 EGGALMVIETEEHAKARGANILARIMGASITSdgfhmVAPDPNGERAGHAMTRAIELAGLTPGDIDhvnahatgtsVGDV 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18700004 345 NEAFASQAVYCVEKLGIPAEKVnplggaiALGHPLGCTGA-RQVVTLL 391
Cdd:PRK07910 322 AEGKAINNALGGHRPAVYAPKS-------ALGHSVGAVGAvESILTVL 362
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
281-340 |
8.59e-03 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 38.09 E-value: 8.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18700004 281 GAAAVLLARRSKAEELGLPILGVLRSYAVV-----GVPPDVmgIGPAYAIPAALQKAGLTVNDID 340
Cdd:PRK07103 240 ACGAVVLESAESARRRGARPYAKLLGWSMRldanrGPDPSL--EGEMRVIRAALRRAGLGPEDID 302
|
|
| |
