|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
55-471 |
5.58e-174 |
|
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: 493.53 E-value: 5.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 55 VVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMgqrlsliskfRFNFLAPELPAV 214
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDGM----------LDDGLTDPFTGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 215 SefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQM 289
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 290 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLT 369
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 370 MNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG 449
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
|
410 420
....*....|....*....|..
gi 116241345 450 GQYGLVAACAAGGQGHAMIVEA 471
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
56-470 |
1.70e-165 |
|
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze the thiolysis of a linear fatty acid CoA (or acetoacetyl-CoA) using a second CoA molecule to produce acetyl-CoA and a CoA-ester product two carbons shorter (or, alternatively, the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA and CoA). This enzyme is also known as "thiolase", "3-ketoacyl-CoA thiolase", "beta-ketothiolase" and "Fatty oxidation complex beta subunit". When catalyzing the degradative reaction on fatty acids the corresponding EC number is 2.3.1.16. The condensation reaction corresponds to 2.3.1.9. Note that the enzymes which catalyze the condensation are generally not involved in fatty acid biosynthesis, which is carried out by a decarboxylating condensation of acetyl and malonyl esters of acyl carrier proteins. Rather, this activity may produce acetoacetyl-CoA for pathways such as IPP biosynthesis in the absence of sufficient fatty acid oxidation. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273881 [Multi-domain] Cd Length: 385 Bit Score: 472.10 E-value: 1.70e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 135
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 136 MACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKlMLDLNKAKSMGQRLSLiskfrfnflapelpaVS 215
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLRW-GVKPGNAELEDARLKD---------------LT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 216 EFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK---DTVTKDNGIRP-SSLEQMA 290
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 291 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLTM 370
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 371 NDIDAFEFHEAFSGQILANFKAMDsdwfaenymgrktkvglPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGG 450
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
|
410 420
....*....|....*....|
gi 116241345 451 QYGLVAACAAGGQGHAMIVE 470
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
52-471 |
2.45e-159 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 457.91 E-value: 2.45e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK08963 5 DRIAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPEL 211
Cdd:PRK08963 85 YSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVV--PFKVPGKDTVTKDNGIRP-SSLEQ 288
Cdd:PRK08963 165 PAVAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtAHVPPYKQPLEEDNNIRGdSTLED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 289 MAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGL 368
Cdd:PRK08963 245 YAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 369 TMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKE 448
Cdd:PRK08963 325 TLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRR 404
|
410 420
....*....|....*....|...
gi 116241345 449 GGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK08963 405 GGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
52-471 |
5.58e-153 |
|
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: 440.27 E-value: 5.58e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGqrlsliskfrfnflapeL 211
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMI-----------------N 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 212 PAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD---TVTKDNGIRP-SSL 286
Cdd:COG0183 145 PGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTTL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 287 EQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDqLLLGPTYATPKVLEKA 366
Cdd:COG0183 225 EKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 367 GLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRLR 446
Cdd:COG0183 303 GLTLDDIDLIEINEAFAAQVLAVLREL----------------GLDP-DKVNVNGGAIALGHPLGASGARILVTLLHELE 365
|
410 420
....*....|....*....|....*
gi 116241345 447 KEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:COG0183 366 RRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
46-471 |
7.10e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 359.98 E-value: 7.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 46 LAKPNIRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGF 125
Cdd:PRK09268 1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 126 SDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFN 205
Cdd:PRK09268 81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGDRLKALGKLRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 206 FLAPELPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKvpgkdTVTKDNGIRP- 283
Cdd:PRK09268 161 HLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFL-----GLTRDNNLRPd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 284 SSLEQMAKLKPAFIK-PYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQD---PKDQLLLGPTYAT 359
Cdd:PRK09268 236 SSLEKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhGKEGLLMAPAYAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVM 439
Cdd:PRK09268 316 PRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVA 395
|
410 420 430
....*....|....*....|....*....|..
gi 116241345 440 AAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK09268 396 TLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
52-471 |
1.42e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 338.53 E-value: 1.42e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK08170 3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSMGQRLSLISKFRFNFLAPE- 210
Cdd:PRK08170 83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKSIGQKLAALGKLRPSYLAPVi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 211 --LPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSDVVPFkVPGKDTV-TKDNGIRP-SSL 286
Cdd:PRK08170 163 glLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPL-FDRDGKFyDHDDGVRPdSSM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 287 EQMAKLKPAFIKPYGTVTAANSSFLTDGAsAMLIMAEEKALAM-GYKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEK 365
Cdd:PRK08170 242 EKLAKLKPFFDRPYGRVTAGNSSQITDGA-CWLLLASEEAVKKyGLPPLGRIVDSQWAALDP-SQMGLGPVHAATPLLQR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 366 AGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAENYMGRKTKVGLPPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRL 445
Cdd:PRK08170 320 HGLTLEDLDLWEINEAFAAQVLACLAAWADEEYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHAL 399
|
410 420
....*....|....*....|....*.
gi 116241345 446 RKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK08170 400 KRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
52-471 |
3.99e-106 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 320.95 E-value: 3.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP--IRHSR---KMRKL-MLDlnkaksmgqrlSLISkfrfn 205
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRwgqKMGDVeLVD-----------TMIH----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 206 flapelPAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDNG 280
Cdd:PRK05790 146 ------DGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTIKQRKgdpvVVDTDEH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 281 IRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYAT 359
Cdd:PRK05790 220 PRPdTTAESLAKLRPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPA-IMGIGPVPAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVM 439
Cdd:PRK05790 298 RKALEKAGWSLADLDLIEINEAFAAQALAVEKEL----------------GLDP-EKVNVNGGAIALGHPIGASGARILV 360
|
410 420 430
....*....|....*....|....*....|..
gi 116241345 440 AAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK05790 361 TLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
54-324 |
3.10e-96 |
|
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: 290.74 E-value: 3.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 54 VVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 133
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 134 VTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRklmldlnkaksmgQRLSLISKFRFNFLAPElpA 213
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 214 VSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP---GKDTVTKDNGIRP-SSLEQ 288
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 116241345 289 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEE 324
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
52-473 |
1.27e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 271.09 E-value: 1.27e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 131
Cdd:PRK06205 2 RDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrHSRKMRK--------LM--LDLNKAKSMGQRLSLISK 201
Cdd:PRK06205 82 MQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEF-YTTDMRWgvrgggvqLHdrLARGRETAGGRRFPVPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 202 frfnflapelpavsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVT 276
Cdd:PRK06205 161 ---------------------MIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVTVPQRKgdptVVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 277 KDNGIRP-SSLEQMAKLKPAFIK--PYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLL 353
Cdd:PRK06205 220 RDEHPRAdTTLESLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEP-SRMGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 354 GPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAEnymgrktkvglpplEKFNNWGGSLSLGHPFGAT 433
Cdd:PRK06205 299 GPVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADDE--------------ERLNVNGSGISLGHPVGAT 364
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 116241345 434 GCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYP 473
Cdd:PRK06205 365 GGRILATLLRELQRRQARYGLETMCIGGGQGLAAVFERVN 404
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
51-472 |
2.69e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 265.04 E-value: 2.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPI-----RHSRKM-RKLMLDLNKAKSmgqrlsLISKFrf 204
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPYilpgaRWGYRMgDNEVIDLMVADG------LTCAF-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 205 nflapelpavsefsTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDN 279
Cdd:PRK08235 153 --------------SGVHMGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQRKgdpiVVAKDE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 280 GIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDqLLLGPTYA 358
Cdd:PRK08235 219 APRKdTTIEKLAKLKPVF-DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKD-FPRTPGYA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 359 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAmdsdwfaenymgrktkVGLPPlEKFNNWGGSLSLGHPFGATGCRLV 438
Cdd:PRK08235 297 INALLEKTGKTVEDIDLFEINEAFAAVALASTEI----------------AGIDP-EKVNVNGGAVALGHPIGASGARII 359
|
410 420 430
....*....|....*....|....*....|....
gi 116241345 439 MAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK08235 360 VTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
51-472 |
1.97e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 257.34 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGTS------YKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT-SNVAREAALGA 123
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 124 GFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIR---HSRKMRKLMLDlnkaksmgqrlslis 200
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGdnpHIEPNPKLLTD--------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 201 kfrfnflaPELpAVSEFSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP---GKDTVT 276
Cdd:PRK06445 146 --------PKY-IEYDLTTGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDeILPIEVEvegKKKVVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 277 KDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGP 355
Cdd:PRK06445 217 VDQSVRPdTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPP-AIMGKGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 356 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKamdsdwfaenymgrktKVGLPPlEKFNNWGGSLSLGHPFGATGC 435
Cdd:PRK06445 295 VPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIK----------------ELGLDP-ETVNIKGGAIAIGHPLGATGA 357
|
410 420 430
....*....|....*....|....*....|....*..
gi 116241345 436 RLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK06445 358 RIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
52-470 |
7.54e-79 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 250.65 E-value: 7.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLS-GTSYKDLMPHDLARAALTGLLHRTS--VPKEVVDyIIFGTVIQEVKTS-NVAREAALGAGFSD 127
Cdd:PRK08947 2 EDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNPalDPAEIDD-IIWGCVQQTLEQGfNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 128 KTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSrkmrklmLDLNkaksmgqrlsliskfrfnfl 207
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHG-------VDFH-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 208 apelPAVSEFST--SETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPfkVPGKD------TVTKD 278
Cdd:PRK08947 134 ----PGLSKNVAkaAGMMGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNeIIP--TEGHDadgvlkLFDYD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 279 NGIRP-SSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK08947 208 EVIRPeTTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPS-IMGYGPVP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaeNYMGRKTkvglpplEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK08947 287 ATQKALKRAGLSISDIDVFELNEAFAAQSLPCLKDL-------GLLDKMD-------EKVNLNGGAIALGHPLGCSGARI 352
|
410 420 430
....*....|....*....|....*....|...
gi 116241345 438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08947 353 STTLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
52-470 |
1.71e-78 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 249.88 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPtEPRDMYLSRVAAINAGVPQETP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP-----IRHSRKMrklmldlNKAKSMGQRLSLISkfrfn 205
Cdd:PRK09051 83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPyllpaARWGARM-------GDAKLVDMMVGALH----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 206 flapelpavSEFSTSEtMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPG-KDTVT--KDNGI 281
Cdd:PRK09051 151 ---------DPFGTIH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVEIKTrKGEVVfdTDEHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 282 RPS-SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTYATP 360
Cdd:PRK09051 221 RADtTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDP-EYMGIGPVPATQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK09051 300 KALERAGLTVADLDVIEANEAFAAQACAVTREL----------------GLDP-AKVNPNGSGISLGHPVGATGAIITVK 362
|
410 420 430
....*....|....*....|....*....|
gi 116241345 441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK09051 363 ALYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
52-473 |
9.39e-78 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 248.08 E-value: 9.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTP---FLLSGTSYKdlmPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIqevkTSNV----AREAALGAG 124
Cdd:PLN02644 1 RDVCIVGVARTPiggFLGSLSSLS---ATELGSIAIQAALERAGVDPALVQEVFFGNVL----SANLgqapARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 125 FSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrKLMLDLNKAKSMGQrLSLISkfrf 204
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAP--------KYLPEARKGSRLGH-DTVVD---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 205 NFLAPELPAV-SEFStsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGK-----DTVTK 277
Cdd:PLN02644 141 GMLKDGLWDVyNDFG----MGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWeIVPVEVPGGrgrpsVIVDK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 278 DNGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQLLLGPTY 357
Cdd:PLN02644 217 DEGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAP-ELFTTAPAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPPlEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PLN02644 296 AIPKALKHAGLEASQVDYYEINEAFSVVALANQKLL----------------GLDP-EKVNVHGGAVSLGHPIGCSGARI 358
|
410 420 430
....*....|....*....|....*....|....*.
gi 116241345 438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAYP 473
Cdd:PLN02644 359 LVTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
56-470 |
2.02e-77 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 246.54 E-value: 2.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTiGPQAGNIARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlNKAKSMGQRLSLISKF--------RFNf 206
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPI-------------SSAMTAGEQLGFTSPFaeskgwlhRYG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 207 lapELPaVSEFstsetmgHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSS 285
Cdd:PRK07801 152 ---DQE-VSQF-------RGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPV-----GGVTVDEGPRETS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 286 LEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVLEK 365
Cdd:PRK07801 216 LEKMAGLKP--LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPV-FMLTAPIPATRYALEK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 366 AGLTMNDIDAFEFHEAFSGQILAnfkamdsdWFAEnymgrktkVGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRL 445
Cdd:PRK07801 293 TGLSIDDIDVVEINEAFAPVVLA--------WLKE--------TGADP-AKVNPNGGAIALGHPLGATGAKLMTTLLHEL 355
|
410 420
....*....|....*....|....*
gi 116241345 446 RKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07801 356 ERTGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
53-470 |
1.84e-74 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 239.24 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK07850 3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSnNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldlnkaKSMGQRLSLISKFRFNFlapEL 211
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLG---------------ANAGPGRGLPRPDSWDI---DM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 212 PAVSEfstsetmghSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLL-SDVVPFKVPGKD----------TVTKDNG 280
Cdd:PRK07850 145 PNQFE---------AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFdREISPVQAPVLDeegqptgetrLVTRDQG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 281 IRPSSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATP 360
Cdd:PRK07850 216 LRDTTMEGLAGLKP--VLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPY-YHLDGPVQATA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK07850 293 KVLEKAGMKIGDIDLVEINEAFASVVLSWAQVHEPD-----------------MDKVNVNGGAIALGHPVGSTGARLITT 355
|
410 420 430
....*....|....*....|....*....|
gi 116241345 441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07850 356 ALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
52-470 |
3.76e-71 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 231.00 E-value: 3.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 52 RNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRT-SVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 129
Cdd:PRK09050 2 TEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNrNVARMSALLAGLPVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklmLDLNKAKSMGQRLSLI--SKFRFNFL 207
Cdd:PRK09050 82 PGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAP-----------FVMGKADSAFSRQAEIfdTTIGWRFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 208 APELPAvsEFSTsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKDNGIR 282
Cdd:PRK09050 151 NPLMKA--QYGV-DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEeIVPVTIPQKKgdpvVVDRDEHPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 283 PS-SLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPK 361
Cdd:PRK09050 228 PEtTLEALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPR-IMGIGPAPATRK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 362 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPP-LEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK09050 306 LLARLGLTIDQFDVIELNEAFAAQGLAVLRQL----------------GLADdDARVNPNGGAIALGHPLGMSGARLVLT 369
|
410 420 430
....*....|....*....|....*....|
gi 116241345 441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK09050 370 ALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
51-470 |
4.16e-69 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 225.40 E-value: 4.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGT-SYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 128
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKgSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 129 TPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlnkaksMGQRLSLISKfrfnfLA 208
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVPM------------------MGHVVRPNPR-----LV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 209 PELPavsEFSTSetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP----GKD--------TV 275
Cdd:PRK07661 138 EAAP---EYYMG--MGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADeIVPVDVTlrtvGENnklqeetiTF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 276 TKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMyVSQDPKDQLLLG 354
Cdd:PRK07661 213 SQDEGVRAdTTLEILGKLRPAF-NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFA-VAGVPPEVMGIG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 355 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATG 434
Cdd:PRK07661 291 PIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE-----------------EKVNVNGGAIALGHPLGCTG 353
|
410 420 430
....*....|....*....|....*....|....*.
gi 116241345 435 CRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07661 354 AKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
23-471 |
7.27e-68 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 223.87 E-value: 7.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 23 IRPLSCSSQLRAAPAVQTKTKKTLAKPNI--RNVVVVDGVRTPFLLSGT-SYKDLMPHDLARAALTGLLHRTSV-PKEVV 98
Cdd:PLN02287 15 LRPSSSEPSSLSASACAAGDSAAYHRTTAfgDDVVIVAAYRTPICKAKRgGFKDTYPDDLLAPVLKAVVEKTGLnPSEVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 99 DyIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsr 177
Cdd:PLN02287 95 D-IVVGTVLAPgSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMA--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 178 kmrklmldlnkaksmgqrlsliSKFRFNflapelPAVSEFSTSET----MGHSADRLAAAFAVSRLEQDEYALRSHSLAK 253
Cdd:PLN02287 171 ----------------------WEGGVN------PRVESFSQAQDcllpMGITSENVAERFGVTREEQDQAAVESHRKAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 254 KAQDEGLLSD-VVPFKVPGKD---------TVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMA 322
Cdd:PLN02287 223 AATASGKFKDeIVPVHTKIVDpktgeekpiVISVDDGIRPnTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 323 EEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQilanfkamdsdwfaenY 402
Cdd:PLN02287 302 RSVAMQKGLPILGVFRSFAAVGVDPA-VMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQ----------------F 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116241345 403 MGRKTKVGLPPlEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEG--GQYGLVAACAAGGQGHAMIVEA 471
Cdd:PLN02287 365 VYCCKKLGLDP-EKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
51-471 |
2.40e-64 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 213.33 E-value: 2.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFllsGTS----YKDLMPHDLARAALTGLLHRTSV--PKEVVDYIIfGTVIQEVKTS-NVAREAALGA 123
Cdd:PRK09052 5 LQDAYIVAATRTPV---GKAprgmFKNTRPDDLLAHVLRSAVAQVPGldPKLIEDAIV-GCAMPEAEQGlNVARIGALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 124 GFSDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIrhsrkmrklmldlnkaksMGQRLSLiskfr 203
Cdd:PRK09052 81 GLPNSVGGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSMVPM------------------MGNKPSM----- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 204 fnflAPELPAVSE-FSTSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKV----PG------ 271
Cdd:PRK09052 138 ----SPAIFARDEnVGIAYGMGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPYEIterfPDlatgev 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 272 ---KDTVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAmLIMAEEKAL-AMGYKPKAYLRDFMyVSQD 346
Cdd:PRK09052 214 dvkTRTVDLDEGPRAdTSLEGLAKLKPVF-ANKGSVTAGNSSQTSDGAGA-VILVSEKALkQFNLTPLARFVSFA-VAGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 347 PKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKamdsdwfaenymgrktKVGLPPlEKFNNWGGSLSL 426
Cdd:PRK09052 291 PPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNEAFAAQSLAVIR----------------DLGLDP-SKVNPLGGAIAL 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 116241345 427 GHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK09052 354 GHPLGATGAIRTATVVHGLRRTNLKYGMVTMCVGTGMGAAGIFER 398
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
55-470 |
4.60e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 207.55 E-value: 4.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 55 VVVDGVRTPFLLSGT-SYKDLMPHDLA----RAALTgllhrtSVPK---EVVDYIIFGTVIQEVKT-SNVAREAALGAGF 125
Cdd:PRK07851 5 VIVSTARSPIGRAFKgSLKDMRPDDLAaqmvRAALD------KVPAldpTDIDDLMLGCGLPGGEQgFNMARVVAVLLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 126 sDKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKM---RKLMLDLNKAKSMGQRLSLISKF 202
Cdd:PRK07851 79 -DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFAEAQARTAARAEGGAEAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 203 RFNFLAPELPAVSEfstseTMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVPGKDTVTKDNGI 281
Cdd:PRK07851 158 HDPREDGLLPDVYI-----AMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFErEITPVTLPDGTVVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 282 RP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDfMYVSQDPKDQLLLGPTYATP 360
Cdd:PRK07851 233 RAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVS-TGVSGLSPEIMGLGPVEASK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 361 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK07851 311 QALARAGMSIDDIDLVEINEAFAAQVLPSARELGID-----------------EDKLNVSGGAIALGHPFGMTGARITTT 373
|
410 420 430
....*....|....*....|....*....|
gi 116241345 441 AANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07851 374 LLNNLQTHDKTFGLETMCVGGGQGMAMVLE 403
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
56-470 |
1.35e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 205.89 E-value: 1.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 56 VVDGVRTPfllSGTSYKD-----LMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQeV--KTSNVAREAALGAGFSDK 128
Cdd:PRK08242 6 IYDAVRTP---RGKGKKDgslheVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTP-VgdQGADIARTAVLAAGLPET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 129 TPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklMLDLNKAKSMGQRLSLISKFrfnflA 208
Cdd:PRK08242 82 VPGVQINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMSRVP----------MGSDGGAWAMDPSTNFPTYF-----V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 209 PElpavsefstsetmGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFK-VPGKDTVTKDNGIRP-SS 285
Cdd:PRK08242 147 PQ-------------GISADLIATKYGFSREDVDAYAVESQQRAAAAWAEGYFAkSVVPVKdQNGLTILDHDEHMRPgTT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 286 LEQMAKLKPAF-------------IKPYGTV-------TAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQ 345
Cdd:PRK08242 214 MESLAKLKPSFammgemggfdavaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 346 DPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLS 425
Cdd:PRK08242 294 DPT-IMLTGPVPATRKALAKAGLTVDDIDLFELNEAFASVVLRFMQALDI-----------------PHDKVNVNGGAIA 355
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 116241345 426 LGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08242 356 MGHPLGATGAMILGTVLDELERRGKRTALITLCVGGGMGIATIIE 400
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
56-471 |
7.36e-61 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 203.81 E-value: 7.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 56 VVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTV 134
Cdd:PRK06504 6 IVAAARTAGGRKGGRLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVgEQATNVARNAVLASKLPESVPGTSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 135 TMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPirhsrkmrklmldlnkaksMGQRLSLISKFRF-NFLAPEL-- 211
Cdd:PRK06504 86 DRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMTRVP-------------------MGSPSTLPAKNGLgHYKSPGMee 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 212 --PAVsEFStsETMGhsADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPG----KDTVTKDNGIR-P 283
Cdd:PRK06504 147 ryPGI-QFS--QFTG--AEMMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPLEITRadgsGEMHTVDEGIRfD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 284 SSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVL 363
Cdd:PRK06504 222 ATLEGIAGVKL--IAEGGRLTAATASQICDGASGVMVVNERGLKALGVKPLARIHHMTVIGGDPV-IMLEAPLPATERAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 364 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglpPlEKFNNWGGSLSLGHPFGATGCRLVMAAAN 443
Cdd:PRK06504 299 KKAGMKIDDIDLYEVNEAFASVPLAWLKATGAD----------------P-ERLNVNGGAIALGHPLGASGTKLMTTLVH 361
|
410 420
....*....|....*....|....*...
gi 116241345 444 RLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK06504 362 ALKQRGKRYGLQTMCEGGGMANVTIVER 389
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
53-470 |
9.55e-61 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 203.86 E-value: 9.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK08131 3 DAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSrNVARNALLLAGLPVTVPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKS-MGQRlsliskfrfnFLAPE 210
Cdd:PRK08131 83 QTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFVMGKAESAFSRDAKVFDTtIGAR----------FPNPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 211 LpaVSEFStSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVP--GKDT---VTKDNGIRPS 284
Cdd:PRK08131 153 I--VAQYG-NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADeITPIEVPqgRKLPpklVAEDEHPRPS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 285 S-LEQMAKLKPAFIKpyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTYATPKVL 363
Cdd:PRK08131 230 StVEALTKLKPLFEG--GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPR-IMGIGPVEAIKKAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 364 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwFAEnymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAAN 443
Cdd:PRK08131 307 ARAGLTLDDMDIIEINEAFASQVLGCLKGLGVD-FDD--------------PRVNPNGGAIAVGHPLGASGARLALTAAR 371
|
410 420
....*....|....*....|....*..
gi 116241345 444 RLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK08131 372 ELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
55-470 |
8.49e-59 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 198.45 E-value: 8.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 55 VVVDGVRTPFllsGTSYKDL--MPH--DLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT-SNVAREAALGAGFSDKT 129
Cdd:PRK07108 5 VIVSTARTPL---AKSWRGAfnMTHgaTLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATgANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVpirhSRKMRKLMLD---LNKAKsmgqrlsliskfrfnf 206
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV----QNEMNRHMLRegwLVEHK---------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 207 laPELpavsefstSETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPF--------KVPG-----K 272
Cdd:PRK07108 142 --PEI--------YWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPItvtagvadKATGrlftkE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 273 DTVTKDNGIRP-SSLEQMAKLKPAFikPYGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPkDQL 351
Cdd:PRK07108 212 VTVSADEGIRPdTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP-DEM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 352 LLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaenYMgrKTKVGLPPlEKFNNWGGSLSLGHPFG 431
Cdd:PRK07108 289 GIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVL--------------YC--RDTLGIPM-DRLNVNGGAIAVGHPYG 351
|
410 420 430
....*....|....*....|....*....|....*....
gi 116241345 432 ATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK07108 352 VSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
51-470 |
1.13e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 195.61 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMR---KLMLDLN-KAKSMGQRLSLISKFRFnf 206
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgpKHLLHKNyKIDDAMLVDGLIDAFYF-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 207 lapelpavsefstsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSS 285
Cdd:PRK06366 159 --------------EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNeIVPF-----NDLDRDEGIRKTT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 286 LEQMAKLKPAFIKPyGTVTAANSSFLTDGASAmLIMAEEKAL-AMGYKPKAYLRDFMYVSQDPKDqLLLGPTYATPKVLE 364
Cdd:PRK06366 220 MEDLAKLPPAFDKN-GILTAGNSAQLSDGGSA-LVMASEKAInEYGLKPIARITGYESASLDPLD-FVEAPIPATRKLLE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 365 KAGLTMNDIDAFEFHEAFS--GQILANFKAMDSdwfaenymgrktkvglpplEKFNNWGGSLSLGHPFGATGCRLVMAAA 442
Cdd:PRK06366 297 KQNKSIDYYDLVEHNEAFSiaSIIVRDQLKIDN-------------------ERFNVNGGAVAIGHPIGNSGSRIIVTLI 357
|
410 420
....*....|....*....|....*...
gi 116241345 443 NRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06366 358 NALKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
331-471 |
1.30e-57 |
|
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: 186.31 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 331 YKPKAYLRDFMYVSQDPkDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaenymgrktkvg 410
Cdd:pfam02803 1 LKPLARIRSYATAGVDP-AIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP------------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116241345 411 lpplEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:pfam02803 67 ----EKVNVNGGAIALGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
51-471 |
6.13e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 193.71 E-value: 6.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMS----DVPIRHSRKMRKL-MLDLNkaksmgQRLSLISKFRFN 205
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMSlgmhGSYIRAGAKFGDIkMVDLM------QYDGLTDVFSGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 206 FlapelpavsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKDTVT---KDNGI 281
Cdd:PRK06633 156 F----------------MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDeILPIEVTIKKTTSlfdHDETV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 282 RP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdqlLLG--PTYA 358
Cdd:PRK06633 220 RPdTSLEILSKLRPAFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPS---IMGtaPVPA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 359 TPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaenYMGRKTKVGLpplEKFNNWGGSLSLGHPFGATGCRLV 438
Cdd:PRK06633 296 SQKALSKAGWSVNDLEVIEVNEAFAAQSI--------------YVNREMKWDM---EKVNINGGAIAIGHPIGASGGRVL 358
|
410 420 430
....*....|....*....|....*....|...
gi 116241345 439 MAAANRLRKEGGQYGLVAACAAGGQGHAMIVEA 471
Cdd:PRK06633 359 ITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
54-472 |
1.45e-54 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 187.41 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 54 VVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 133
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 134 VTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVP-----------IRHSRKMRKLMLD-LNKAKSMGQrlslisk 201
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDgLEDAYDKGR------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 202 frfnflapelpavsefstseTMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVPGKD---TVTK 277
Cdd:PRK06954 162 --------------------LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAwEIAPVTVAGKKgdtVIDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 278 DNGIRPSSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK06954 222 DEQPFKANPEKIPTLKPAFSKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPS-KFTTAPVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK06954 300 AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL-----------------PHEKVNVNGGACALGHPIGASGARI 362
|
410 420 430
....*....|....*....|....*....|....*
gi 116241345 438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVEAY 472
Cdd:PRK06954 363 LVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
51-470 |
3.26e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 178.54 E-value: 3.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 51 IRNVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 130
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 131 AHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldLNKAKSmGQRL-------SLISKFR 203
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYV-----------LPGART-GLRMghaqlvdSMITDGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 204 FNflapelpAVSEFStsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD----TVTKD 278
Cdd:PRK05656 149 WD-------AFNDYH----MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDeITPILIPQRKgeplAFATD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 279 NGIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKdQLLLGPTY 357
Cdd:PRK05656 218 EQPRAgTTAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPA-IMGIGPVS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaenymgrktkvglppLEKFNNWGGSLSLGHPFGATGCRL 437
Cdd:PRK05656 296 ATRRCLDKAGWSLAELDLIEANEAFAAQSLAVGKELGWD-----------------AAKVNVNGGAIALGHPIGASGCRV 358
|
410 420 430
....*....|....*....|....*....|...
gi 116241345 438 VMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK05656 359 LVTLLHEMIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
53-470 |
1.42e-50 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 175.72 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 53 NVVVVDGVRTPFLLSGTSYKDLMPHDLARAALTGLlhRTSVPKEVvDYIIFGTVIQevKTSNVAREAALGAGFSDKTPAH 132
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMEREI-DDVILGNVVG--PGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 133 TVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRhsrkmrklmldlnkaksmgqrlsliSKFRFnflAPEL- 211
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ-------------------------NRARF---SPETi 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 212 --PAvsefstsetMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFkvpgkDTVTKDNGIRPSSLEQ 288
Cdd:PRK06690 129 gdPD---------MGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEeILSF-----NGLLDESIKKEMNYER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 289 M-AKLKPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDFMYVSQDPKDQlLLGPTYATPKVLEKAG 367
Cdd:PRK06690 195 IiKRTKPAFLHN-GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLP-GTGPIFAVNKLLNEMN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 368 LTMNDIDAFEFHEAFSGQILANFKAMDSdwfaenymgrktkvglpPLEKFNNWGGSLSLGHPFGATGCRLVMAAANRLRK 447
Cdd:PRK06690 273 MKVEDIDYFEINEAFASKVVACAKELQI-----------------PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKR 335
|
410 420
....*....|....*....|...
gi 116241345 448 EGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06690 336 EDMKYGIATLGIGGGIGLALLFE 358
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
56-470 |
1.19e-48 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 172.27 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 56 VVDGVRTPFLLSGT---SYKDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 131
Cdd:PRK06025 6 IIDAVRTPRGIGKVgkgALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYDIKASG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 132 HTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRK----LMLDLNKAksmgqrlsliskfRFNFL 207
Cdd:PRK06025 86 VTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSYTAAMAAEDMAAgkppLGMGSGNL-------------RLRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 208 APElpavsefstsETMGHSADRLAAAFAVSRLEQDEYALRSHSLAKKAQDEGLLS-DVVPFKVP-GKDTVTKDNGIRP-S 284
Cdd:PRK06025 153 HPQ----------SHQGVCGDAIATMEGITREALDALGLESQRRAARAIKEGRFDkSLVPVYRDdGSVALDHEEFPRPqT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 285 SLEQMAKLKPAF-------IKPYGTVT------------------AANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRD 339
Cdd:PRK06025 223 TAEGLAALKPAFtaiadypLDDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 340 FMYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSgqilanfkamdsdWFAENYMgRKTKVglpPLEKFNN 419
Cdd:PRK06025 303 MANMGDDPT-LMLNAPVPAAKKVLAKAGLTKDDIDLWEINEAFA-------------VVAEKFI-RDLDL---DRDKVNV 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 116241345 420 WGGSLSLGHPFGATGCRLVMAAANRLRKEGGQYGLVAACAAGGQGHAMIVE 470
Cdd:PRK06025 365 NGGAIALGHPIGATGSILIGTVLDELERRGLKRGLVTMCAAGGMAPAIIIE 415
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
60-470 |
4.07e-41 |
|
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: 151.49 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 60 VRTPFLLSGTSYKDLmPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACI 139
Cdd:cd00826 8 FGKFGGENGADANDL-AHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 140 SANQAMTTGVGLIASGQCDVIVAGGVELMSdVPIRHSRKMRKLMLDLNKAKSmgqrlsliskfrfnflapelpavsefst 219
Cdd:cd00826 87 SGLRALALAMQLIAGGDANCILAGGFEKME-TSAENNAKEKHIDVLINKYGM---------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 220 setmghsadrlaaafavsRLEQDEYALRSHSLAKKAQDEGLLSD-VVPFKVPGKD---TVTKDNGIR---PSSLEQMAKL 292
Cdd:cd00826 138 ------------------RACPDAFALAGQAGAEAAEKDGRFKDeFAKFGVKGRKgdiHSDADEYIQfgdEASLDEIAKL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 293 KPAFIKPyGTVTAANSSFLTDGASAMLIMAEEKA-------LAMGYKPKAYLRDFMYVSQDPKDQLLLG---PTYATPKV 362
Cdd:cd00826 200 RPAFDKE-DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVGgdgPIEAARKA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 363 LEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsDWFAENYMGRKTKVGLPPLEK---FNNWGGSLSLGHPFGATGCRLVM 439
Cdd:cd00826 279 LEKAGLGIGDLDLIEAHDAFAANACATNEAL--GLCPEGQGGALVDRGDNTYGGksiINPNGGAIAIGHPIGASGAAICA 356
|
410 420 430
....*....|....*....|....*....|....*.
gi 116241345 440 AAANRLRKEGGQY-----GLVAACAAGGQGHAMIVE 470
Cdd:cd00826 357 ELCFELKGEAGKRqgagaGLALLCIGGGGGAAMCIE 392
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
76-469 |
1.55e-19 |
|
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: 90.02 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 76 PHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKtPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:cd00829 16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 156 QCDVIVAGGVELMSDVPirhsrkmrklmldlnKAKSMGQRLSLISKFRFN-FLAPELPAVsefstsetMGHSADRLAAAF 234
Cdd:cd00829 95 LADVVLVVGAEKMSDVP---------------TGDEAGGRASDLEWEGPEpPGGLTPPAL--------YALAARRYMHRY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 235 AVSRLEQDEYALRSHSLAKK---AQdegllsdvvpFKVPgkDTVTKDNGIRPSSLeqmaklkpafikPYgtvTAANSSFL 311
Cdd:cd00829 152 GTTREDLAKVAVKNHRNAARnpyAQ----------FRKP--ITVEDVLNSRMIAD------------PL---RLLDCCPV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 312 TDGASAMLIMAEEKALAMGYKPkAYLR------DFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQ 385
Cdd:cd00829 205 SDGAAAVVLASEERARELTDRP-VWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 386 ILANFKAM------DSDWFAENymGRKTKVGLPPLekfNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQY-----GL 454
Cdd:cd00829 284 ELLALEDLgfcekgEGGKLVRE--GDTAIGGDLPV---NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARqvpgaRV 358
|
410
....*....|....*
gi 116241345 455 VAACAAGGQGHAMIV 469
Cdd:cd00829 359 GLAHNIGGTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
78-469 |
1.56e-12 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 68.77 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 78 DLARAALTGLLHRTSVPKEVVDYIIFGTVI--QEVKTSNVAREAALGAGFSDKtPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAPI-PATRVEAACASGGAALRQAYLAVASG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 156 QCDVIVAGGVELMSDVPirhsrkmrklmldlnkaksmgqrlsliskfrfnflAPElpavsefsTSETMGHSADRLAAAFA 235
Cdd:PRK06064 103 EADVVLAAGVEKMTDVP-----------------------------------TPD--------ATEAIARAGDYEWEEFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 236 ----------VSRLEQDEYALRSHSLAK---KAQDEGLLSDVVPFKvpgkdtvtkdngiRPSSLEQMAKLKPAF--IKPY 300
Cdd:PRK06064 140 gatfpglyalIARRYMHKYGTTEEDLALvavKNHYNGSKNPYAQFQ-------------KEITVEQVLNSPPVAdpLKLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 301 gtvtaaNSSFLTDGASAMLIMAEEKAlamgykpKAYLRDFMYVS-----------QDPKDQLLLGPT-YATPKVLEKAGL 368
Cdd:PRK06064 207 ------DCSPITDGAAAVILASEEKA-------KEYTDTPVWIKasgqasdtialHDRKDFTTLDAAvVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 369 TMNDIDAFEFHEAFSgqiLANFKAMDSDWFAENYMGRK------TKVG--LPplekFNNWGGSLSLGHPFGATGCRLVMA 440
Cdd:PRK06064 274 EPKDIDVAEVHDCFT---IAEILAYEDLGFAKKGEGGKlaregqTYIGgdIP----VNPSGGLKAKGHPVGATGVSQAVE 346
|
410 420 430
....*....|....*....|....*....|....*...
gi 116241345 441 AANRLRKE---GGQ------YGLvaACAAGGQGHAMIV 469
Cdd:PRK06064 347 IVWQLRGEaekGRQqvigagYGL--THNVGGTGHTAVV 382
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
73-465 |
3.00e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 64.87 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 73 DLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHtVTMACISANQAMTTGVGLI 152
Cdd:PRK12578 18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGLAASLTAYTAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 153 ASGQCDVIVAGGVELMSDVpirhsrkmrklmlDLNKAKSMGQRlSLISKFRFNFLAPELPAVSEFSTSETMghsadrlaA 232
Cdd:PRK12578 97 ASGLVDMAIAVGVDKMTEV-------------DTSTSLAIGGR-GGNYQWEYHFYGTTFPTYYALYATRHM--------A 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 233 AFAVSRLEQDEYALRSH---SLAKKAQdegllsdvvpFKvpgkdtvtkdngiRPSSLEQMakLKPAFIK-PygtVTAANS 308
Cdd:PRK12578 155 VYGTTEEQMALVSVKAHkygAMNPKAH----------FQ-------------KPVTVEEV--LKSRAISwP---IKLLDS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 309 SFLTDGASAMLIMAEEKALAMGY------KPKAYLRDFMYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAF 382
Cdd:PRK12578 207 CPISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 383 SgqiLANFKAMDSDWFAENYMGRK----------TKVGLpplekfNNWGGSLSLGHPFGATGCRLVMAAANRLRKEGGQY 452
Cdd:PRK12578 287 T---IAEIMGYEDLGFTEKGKGGKfieegqsekgGKVGV------NLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGKL 357
|
410 420
....*....|....*....|.
gi 116241345 453 --------GLVAacAAGGQGH 465
Cdd:PRK12578 358 qqplkkyiGLVH--NVGGTGH 376
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
305-469 |
6.42e-09 |
|
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: 56.68 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 305 AANSSFLTDGASAMLIMAEEKALAMGYKPKAYLRDfMYVSQDPKDQLLL----GPTYATPKVLEKAGLTMNDIDAFEFHE 380
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVS-TAATFDGASMVPAvsgeGLARAARKALEGAGLTPSDIDYVEAHG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 381 AFSGQILANFKAMDSDWFaenymgrktKVGLPPLEkfnnwGGSLSLGHPFGATG-------CRLVMAAANRLRKEGGQYG 453
Cdd:cd00327 173 TGTPIGDAVELALGLDPD---------GVRSPAVS-----ATLIMTGHPLGAAGlaildelLLMLEHEFIPPTPREPRTV 238
|
170
....*....|....*.
gi 116241345 454 LVAACAAGGQGHAMIV 469
Cdd:cd00327 239 LLLGFGLGGTNAAVVL 254
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
130-461 |
9.21e-08 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 54.13 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSmgqrlslISKFRFNFL-A 208
Cdd:PTZ00455 112 PAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLARAADYRRQRK-------LDDFTFPCLfA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 209 PELPAVSEfSTSETMGHSADRLAAAFAVSRLEQdeyalRSHSLAKKAQDEGLlsdvvpfkvpgkdtvtkdNGIRPSSLEQ 288
Cdd:PTZ00455 185 KRMKYIQE-HGHFTMEDTARVAAKAYANGNKNP-----LAHMHTRKLSLEFC------------------TGASDKNPKF 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 289 MAKlkpAFIKPYGTVTaaNSSFLTDGASAMLIMAEEKALAMGYKP--------KAYLRDFMYVSQDPKDQLLLGPTY-AT 359
Cdd:PTZ00455 241 LGN---ETYKPFLRMT--DCSQVSDGGAGLVLASEEGLQKMGLSPndsrlveiKSLACASGNLYEDPPDATRMFTSRaAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 360 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDsdwFAE-------NYMGRKTKVGLPPLekfNNWGGSLSLGHPFGA 432
Cdd:PTZ00455 316 QKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALG---IAEyghakdlIRNGATALEGRIPV---NTGGGLLSFGHPVGA 389
|
330 340
....*....|....*....|....*....
gi 116241345 433 TGCRLVMAAANRLRKEGGQYGLVAACAAG 461
Cdd:PTZ00455 390 TGVKQIMEVYRQMKGQCGEYQMKNIPALG 418
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
309-441 |
5.59e-07 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 51.49 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 309 SFLTDGASAMLIMAEEKALAM----GYKPKAYLRDFMYVSQdpKDQLLL-GPTYATPKVLEKAGLTMNDIDAFEFHEAFS 383
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSR--RDPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116241345 384 GQILANFKAM------------DSDWFAENymGRktkvgLPplekFNNWGGSLSLGHPFGATGCRL-VMAA 441
Cdd:PRK07516 291 IAELIEYEAMglappgqgaraiREGWTAKD--GK-----LP----VNPSGGLKAKGHPIGATGVSMhVLAA 350
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
112-166 |
2.48e-06 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 49.46 E-value: 2.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 116241345 112 TSNVAREAALGAGFsdKTPAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVE 166
Cdd:cd00834 137 PNMAAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
130-166 |
2.89e-06 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 49.32 E-value: 2.89e-06
10 20 30
....*....|....*....|....*....|....*..
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVE 166
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
130-168 |
1.67e-05 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 46.09 E-value: 1.67e-05
10 20 30
....*....|....*....|....*....|....*....
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELM 168
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
72-171 |
1.77e-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: 46.64 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 72 KDLMPHDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKT----SNVAREaaLGAgfsDKTPAHTVTMACISANQAMTT 147
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFpstaCLVQHK--LGA---KNAAAFDINAACSGFVYALSV 121
|
90 100
....*....|....*....|....*
gi 116241345 148 GVGLIASGQCD-VIVAGGvELMSDV 171
Cdd:COG0332 122 AAALIRSGQAKnVLVVGA-ETLSRI 145
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
77-167 |
2.39e-05 |
|
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: 45.90 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 77 HDLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVAREAALGAGFSdKTPAHTVTMACISANQAMTTGVGLIASGQ 156
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90
....*....|.
gi 116241345 157 CDVIVAGGVEL 167
Cdd:cd00327 87 ADIVLAGGSEE 97
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
130-192 |
2.83e-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: 40.11 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116241345 130 PAHTVTMACISANQAMTTGVGLIASGQCDVIVAGGVELMSDVPIRHSRKMRKLMLDLNKAKSM 192
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMGALSTAEEEPEEM 216
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
78-171 |
4.05e-03 |
|
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.
Pssm-ID: 238426 [Multi-domain] Cd Length: 320 Bit Score: 39.06 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 78 DLARAALTGLLHRTSVPKEVVDYIIFGTVIQEVKTSNVARE--AALGAGfsdKTPAHTVTMACISANQAMTTGVGLIASG 155
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLvqARLGAK---NAAAFDINAACSGFLYGLSTAAGLIRSG 128
|
90
....*....|....*..
gi 116241345 156 QCD-VIVAGGvELMSDV 171
Cdd:cd00830 129 GAKnVLVVGA-ETLSRI 144
|
|
| PRK08256 |
PRK08256 |
lipid-transfer protein; Provisional |
358-434 |
4.82e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 181327 [Multi-domain] Cd Length: 391 Bit Score: 39.11 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116241345 358 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaenymgrktkvGLPP---LEKF--------------NNW 420
Cdd:PRK08256 269 AAQQVYEQAGIGPEDIDVVELHDCFSANELLTYEAL----------------GLCPegeAEKFiddgdntyggrwvvNPS 332
|
90
....*....|....
gi 116241345 421 GGSLSLGHPFGATG 434
Cdd:PRK08256 333 GGLLSKGHPLGATG 346
|
|
| |
