|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
56-472 |
2.05e-175 |
|
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: 497.39 E-value: 2.05e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTlaqrlslltkFRLNFLSPELPAV 215
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNTLDG----------MLDDGLTDPFTGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 216 AefstnetMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVSKDNGIRP-SSLEQM 290
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 291 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLT 370
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 371 MNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG 450
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
|
410 420
....*....|....*....|..
gi 1958781811 451 GQYALVAACAAGGQGHAMIVEA 472
Cdd:cd00751 365 GRYGLATMCIGGGQGAAMVIER 386
|
|
| AcCoA-C-Actrans |
TIGR01930 |
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ... |
57-471 |
1.75e-172 |
|
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: 489.82 E-value: 1.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 57 VVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 136
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 137 MACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkMMLDLNKAKTLAQRLSLLTkfrlnflspelpava 216
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLR-WGVKPGNAELEDARLKDLT--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 217 EFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVSKDNGIRP-SSLEQMA 291
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 292 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTM 371
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 372 NDIDAFEFHEAFSGQILANFKAMdsdwfaqnymgrktkvgAPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKEL-----------------GLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
|
410 420
....*....|....*....|
gi 1958781811 452 QYALVAACAAGGQGHAMIVE 471
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
55-472 |
8.12e-162 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 464.46 E-value: 8.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLNFLSPELPA 214
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVPPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 215 VAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSDIV--PFKVPGKDTVSKDNGIRP-SSLEQMA 291
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDEVmtAHVPPYKQPLEEDNNIRGdSTLEDYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 292 KLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTM 371
Cdd:PRK08963 247 KLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAGLTL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 372 NDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGAPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:PRK08963 327 ADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGG 406
|
410 420
....*....|....*....|.
gi 1958781811 452 QYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08963 407 GLGLTTACAAGGLGAAMVLEV 427
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
53-472 |
1.06e-151 |
|
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: 437.19 E-value: 1.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 132
Cdd:COG0183 2 REVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 133 HTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAqrlslltkfrlnflspeL 212
Cdd:COG0183 82 VTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNAKLVDPMI-----------------N 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 213 PAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVSKDNGIRP-SSL 287
Cdd:COG0183 145 PGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTTL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 288 EQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEKA 367
Cdd:COG0183 225 EKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 368 GLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLR 447
Cdd:COG0183 303 GLTLDDIDLIEINEAFAAQVLAVLRELGLDP-----------------DKVNVNGGAIALGHPLGASGARILVTLLHELE 365
|
410 420
....*....|....*....|....*
gi 1958781811 448 KDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:COG0183 366 RRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
47-472 |
2.48e-121 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 361.14 E-value: 2.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 47 LAKPNLKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGF 126
Cdd:PRK09268 1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 127 SDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLN 206
Cdd:PRK09268 81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGDRLKALGKLRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 207 FLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKvpgkdTVSKDNGIRP- 284
Cdd:PRK09268 161 HLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFL-----GLTRDNNLRPd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 285 SSLEQMAKLKPAFIK-PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQD---PKDQLLLGPTYAT 360
Cdd:PRK09268 236 SSLEKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhGKEGLLMAPAYAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGAPPLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK09268 316 PRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVA 395
|
410 420 430
....*....|....*....|....*....|..
gi 1958781811 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09268 396 TLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
53-472 |
3.18e-110 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 332.75 E-value: 3.18e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 132
Cdd:PRK08170 3 RPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKVPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 133 HTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLAQRLSLLTKFRLNFLSPE- 211
Cdd:PRK08170 83 WTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKSIGQKLAALGKLRPSYLAPVi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 212 --LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSDIVPFkVPGKDTV-SKDNGIRP-SSL 287
Cdd:PRK08170 163 glLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPL-FDRDGKFyDHDDGVRPdSSM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 288 EQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKA 367
Cdd:PRK08170 242 EKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDP-SQMGLGPVHAATPLLQRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 368 GLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGAPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLR 447
Cdd:PRK08170 321 GLTLEDLDLWEINEAFAAQVLACLAAWADEEYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHALK 400
|
410 420
....*....|....*....|....*
gi 1958781811 448 KDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08170 401 RRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
53-472 |
4.64e-107 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 323.26 E-value: 4.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPA 132
Cdd:PRK05790 2 KDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 133 HTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDlnkakTLAQrlslltkfrln 206
Cdd:PRK05790 82 LTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRWGQKMgdveLVD-----TMIH----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 207 flspelPAVAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVSKDNG 281
Cdd:PRK05790 146 ------DGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTIKQRKgdpvVVDTDEH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 282 IRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYAT 360
Cdd:PRK05790 220 PRPdTTAESLAKLRPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPA-IMGIGPVPAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK05790 298 RKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLD-----------------PEKVNVNGGAIALGHPIGASGARILV 360
|
410 420 430
....*....|....*....|....*....|..
gi 1958781811 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK05790 361 TLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
55-325 |
1.17e-100 |
|
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: 302.30 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkmmldlnkaktlaQRLSLLTKFRLNFLSPElpA 214
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 215 VAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTVSKDNGIRP-SSLEQ 289
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958781811 290 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSED 325
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
52-474 |
3.79e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 269.94 E-value: 3.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrHSRNMRK--------MMLDLNKAKTLAQrlslltkf 203
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEF-YTTDMRWgvrgggvqLHDRLARGRETAG-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 204 rlnflsPElpavaEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVSK 278
Cdd:PRK06205 152 ------GR-----RFPVPGGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVTVPQRKgdptVVDR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 279 DNGIRP-SSLEQMAKLKPAFIK--PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLG 355
Cdd:PRK06205 221 DEHPRAdTTLESLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEP-SRMGIG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 356 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqnymgrktKVGAPPLEKFNIWGGSLSLGHPFGATG 435
Cdd:PRK06205 300 PVPATEKALARAGLTLDDIDLIELNEAFAAQVLAVLKEW--------------GFGADDEERLNVNGSGISLGHPVGATG 365
|
410 420 430
....*....|....*....|....*....|....*....
gi 1958781811 436 CRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PRK06205 366 GRILATLLRELQRRQARYGLETMCIGGGQGLAAVFERVN 404
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
56-473 |
5.99e-84 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 263.88 E-value: 5.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:PRK08235 5 VIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQTETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDLNKAKTLAqrlslltkfrlnfls 209
Cdd:PRK08235 85 NKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyiLPGARWGYRMgdneVIDLMVADGLT--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 210 pelpavAEFSTNEtMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVSKDNGIRP 284
Cdd:PRK08235 150 ------CAFSGVH-MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQRKgdpiVVAKDEAPRK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 285 -SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKV 363
Cdd:PRK08235 223 dTTIEKLAKLKPVF-DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKD-FPRTPGYAINAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 364 LEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATGCRLVMAAA 443
Cdd:PRK08235 301 LEKTGKTVEDIDLFEINEAFAAVALASTEIAGID-----------------PEKVNVNGGAVALGHPIGASGARIIVTLI 363
|
410 420 430
....*....|....*....|....*....|
gi 1958781811 444 NRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK08235 364 HELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
53-471 |
9.15e-80 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 253.34 E-value: 9.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK09051 3 REVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPtEPRDMYLSRVAAINAGVPQETP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKMmldlNKAKTLAQRLSLLTkfrlnflS 209
Cdd:PRK09051 83 AFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPylLPAARWGARM----GDAKLVDMMVGALH-------D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 210 PelpavaeFSTNEtMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPG-KDTV--SKDNGIRPS 285
Cdd:PRK09051 152 P-------FGTIH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVEIKTrKGEVvfDTDEHVRAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 286 -SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVL 364
Cdd:PRK09051 224 tTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDP-EYMGIGPVPATQKAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 365 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgaPplEKFNIWGGSLSLGHPFGATGCRLVMAAAN 444
Cdd:PRK09051 303 ERAGLTVADLDVIEANEAFAAQACAVTRELGLD---------------P--AKVNPNGSGISLGHPVGATGAIITVKALY 365
|
410 420
....*....|....*....|....*..
gi 1958781811 445 RLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09051 366 ELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
52-473 |
1.75e-79 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 252.34 E-value: 1.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGTS------YKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGA 124
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 125 GFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHS----RNMrKMMLDlnkaktlaqrlSLL 200
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiePNP-KLLTD-----------PKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 201 TKFRLNflspelpavaefsTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTV 276
Cdd:PRK06445 149 IEYDLT-------------TGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDeILPIEVEvegKKKVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 277 SKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLG 355
Cdd:PRK06445 216 DVDQSVRPdTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPP-AIMGKG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 356 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATG 435
Cdd:PRK06445 294 PVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD-----------------PETVNIKGGAIAIGHPLGATG 356
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958781811 436 CRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06445 357 ARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
57-471 |
1.66e-78 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 249.62 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 57 VVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:PRK07801 6 IVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTiGPQAGNIARTSWLAAGLPEEVPGVTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrhSRNMrkmmldlnkakTLAQRLSLLTKFrlnflSPELPAV 215
Cdd:PRK07801 86 DRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPI--SSAM-----------TAGEQLGFTSPF-----AESKGWL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 216 AEFSTNE-TMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVSKDNGIRPSSLEQMAKL 293
Cdd:PRK07801 148 HRYGDQEvSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPV-----GGVTVDEGPRETSLEKMAGL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 294 KPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMND 373
Cdd:PRK07801 223 KP--LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPV-FMLTAPIPATRYALEKTGLSIDD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 374 IDAFEFHEAFSGQILAnfkamdsdWFAQnymgrktkVGAPPlEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQY 453
Cdd:PRK07801 300 IDVVEINEAFAPVVLA--------WLKE--------TGADP-AKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGGRY 362
|
410
....*....|....*...
gi 1958781811 454 ALVAACAAGGQGHAMIVE 471
Cdd:PRK07801 363 GLQTMCEGGGTANVTIIE 380
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
53-471 |
5.56e-78 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 248.34 E-value: 5.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIPFLLS-GTSYKDLMPHDLARAALSGLLYRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK08947 2 EDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGfNIARNAALLAGIPHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSrnmrkmmLDLNKAktlaqrLSLltkfrlnfls 209
Cdd:PRK08947 82 VPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHG-------VDFHPG------LSK---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 210 pelpAVAEFSTNetMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPfkVPGKD------TVSKDNGI 282
Cdd:PRK08947 139 ----NVAKAAGM--MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNeIIP--TEGHDadgvlkLFDYDEVI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 283 RP-SSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATP 361
Cdd:PRK08947 211 RPeTTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPS-IMGYGPVPATQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 362 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqNYMGRKTkvgapplEKFNIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK08947 290 KALKRAGLSISDIDVFELNEAFAAQSLPCLKDL-------GLLDKMD-------EKVNLNGGAIALGHPLGCSGARISTT 355
|
410 420 430
....*....|....*....|....*....|
gi 1958781811 442 AANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08947 356 LLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
54-471 |
6.59e-78 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 248.10 E-value: 6.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 54 NIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPA 132
Cdd:PRK07850 3 NPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSnNITRTAWLHAGLPYHVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 133 HTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHsrnmrKMMLDLNKAKTLAQRLSLLTKFRlnflspel 212
Cdd:PRK07850 83 TTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVPLGA-----NAGPGRGLPRPDSWDIDMPNQFE-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 213 pavaefstnetmghSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHL-SDIVPFKVPGKD----------TVSKDNG 281
Cdd:PRK07850 150 --------------AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFdREISPVQAPVLDeegqptgetrLVTRDQG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 282 IRPSSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATP 361
Cdd:PRK07850 216 LRDTTMEGLAGLKP--VLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPY-YHLDGPVQATA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 362 KVLEKAGLTMNDIDAFEFHEAFSGQILAnfkamdsdwFAQnymgrktkVGAPPLEKFNIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK07850 293 KVLEKAGMKIGDIDLVEINEAFASVVLS---------WAQ--------VHEPDMDKVNVNGGAIALGHPVGSTGARLITT 355
|
410 420 430
....*....|....*....|....*....|
gi 1958781811 442 AANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07850 356 ALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
53-474 |
1.34e-74 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 239.99 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 53 KNIVVVEGVRIP---FLLSGTSYKdlmPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIqevkTSNV----AREAALGAG 125
Cdd:PLN02644 1 RDVCIVGVARTPiggFLGSLSSLS---ATELGSIAIQAALERAGVDPALVQEVFFGNVL----SANLgqapARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 126 FSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrKMMLDLNKAKTLAQrLSLLTKFRL 205
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAP--------KYLPEARKGSRLGH-DTVVDGMLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 206 NFLspelpavAEFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGK-----DTVSKD 279
Cdd:PLN02644 145 DGL-------WDVYNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWeIVPVEVPGGrgrpsVIVDKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 280 NGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYA 359
Cdd:PLN02644 218 EGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAP-ELFTTAPALA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqnymgrktkvGAPPlEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PLN02644 297 IPKALKHAGLEASQVDYYEINEAFSVVALANQKLL----------------GLDP-EKVNVHGGAVSLGHPIGCSGARIL 359
|
410 420 430
....*....|....*....|....*....|....*
gi 1958781811 440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PLN02644 360 VTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
52-471 |
3.49e-70 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 228.68 E-value: 3.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNrNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkmmLDLNKAKTLAQRLSLL--TKFRLNF 207
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAP-----------FVMGKADSAFSRQAEIfdTTIGWRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 208 LSPELPAvaEFSTnETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVSKDNGI 282
Cdd:PRK09050 150 VNPLMKA--QYGV-DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEeIVPVTIPQKKgdpvVVDRDEHP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 283 RPS-SLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATP 361
Cdd:PRK09050 227 RPEtTLEALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPR-IMGIGPAPATR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 362 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAM---DSDwfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK09050 305 KLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLglaDDD------------------ARVNPNGGAIALGHPLGMSGARL 366
|
410 420 430
....*....|....*....|....*....|...
gi 1958781811 439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09050 367 VLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
52-471 |
6.94e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 219.62 E-value: 6.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKgSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMLDLnkaktlaqrlslltkFRLNfls 209
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP---------MMGHV---------------VRPN--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 210 pelPAVAEFSTN--ETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVP----GKD-------- 274
Cdd:PRK07661 134 ---PRLVEAAPEyyMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADeIVPVDVTlrtvGENnklqeeti 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 275 TVSKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLL 353
Cdd:PRK07661 211 TFSQDEGVRAdTTLEILGKLRPAF-NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFA-VAGVPPEVMG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 354 LGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGA 433
Cdd:PRK07661 289 IGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE-----------------EKVNVNGGAIALGHPLGC 351
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958781811 434 TGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07661 352 TGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
54-472 |
4.23e-66 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 219.25 E-value: 4.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 54 NIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTP 131
Cdd:PLN02287 47 DVVIVAAYRTPICKAKRgGFKDTYPDDLLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPgSQRANECRMAAFYAGFPETVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkmmldlnkaktlaqrlslltkfrlnflspe 211
Cdd:PLN02287 127 VRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMAWEGGVN------------------------------ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 212 lPAVAEFSTNET----MGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---------TVS 277
Cdd:PLN02287 177 -PRVESFSQAQDcllpMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFKDeIVPVHTKIVDpktgeekpiVIS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 278 KDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PLN02287 256 VDDGIRPnTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPILGVFRSFAAVGVDPA-VMGIGP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGC 436
Cdd:PLN02287 334 AVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDP-----------------EKVNVNGGAIALGHPLGATGA 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958781811 437 RLVMAAANRLRKDG--GQYALVAACAAGGQGHAMIVEA 472
Cdd:PLN02287 397 RCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
56-471 |
1.09e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 214.48 E-value: 1.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 56 VVVEGVRIPFLLSGT-SYKDLMPHDLA----RAALS---GLlyrtnIPKDVVDyIIFGTVIQEVKT-SNVAREAALGAGF 126
Cdd:PRK07851 5 VIVSTARSPIGRAFKgSLKDMRPDDLAaqmvRAALDkvpAL-----DPTDIDD-LMLGCGLPGGEQgFNMARVVAVLLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 127 sDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNM---RKMMLDLNKAKTLAQRLSLLTKF 203
Cdd:PRK07851 79 -DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFAEAQARTAARAEGGAEAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 204 RLNFLSPELPAVAEfstneTMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLS-DIVPFKVPGKDTVSKDNGI 282
Cdd:PRK07851 158 HDPREDGLLPDVYI-----AMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFErEITPVTLPDGTVVSTDDGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 283 RP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDfIYVSQDPKDQLLLGPTYATP 361
Cdd:PRK07851 233 RAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVS-TGVSGLSPEIMGLGPVEASK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 362 KVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK07851 311 QALARAGMSIDDIDLVEINEAFAAQVLPSARELGID-----------------EDKLNVSGGAIALGHPFGMTGARITTT 373
|
410 420 430
....*....|....*....|....*....|
gi 1958781811 442 AANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07851 374 LLNNLQTHDKTFGLETMCVGGGQGMAMVLE 403
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
77-471 |
1.54e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 211.28 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 77 PHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQeV--KTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIA 154
Cdd:PRK08242 28 PVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTP-VgdQGADIARTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 155 SGQCDVVVAGGVELMSDVPIRHSRnmRKMMLDLNkaktlaqrlsllTKFRLNFLsPElpavaefstnetmGHSADRLAAA 234
Cdd:PRK08242 107 SGWDDLVIAGGVESMSRVPMGSDG--GAWAMDPS------------TNFPTYFV-PQ-------------GISADLIATK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 235 FAVSRMEQDKYALRSHSLAKKAQDEGHLSDIVpfkVPGKD-----TVSKDNGIRP-SSLEQMAKLKPAF----------- 297
Cdd:PRK08242 159 YGFSREDVDAYAVESQQRAAAAWAEGYFAKSV---VPVKDqngltILDHDEHMRPgTTMESLAKLKPSFammgemggfda 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 298 --IKPYGTV-------TAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAG 368
Cdd:PRK08242 236 vaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPT-IMLTGPVPATRKALAKAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 369 LTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgapPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDI-----------------PHDKVNVNGGAIAMGHPLGATGAMILGTVLDELER 377
|
410 420
....*....|....*....|...
gi 1958781811 449 DGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08242 378 RGKRTALITLCVGGGMGIATIIE 400
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
72-472 |
1.38e-62 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 208.70 E-value: 1.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 72 YKDLMPHDLARAALSGLLYRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTA 149
Cdd:PRK09052 26 FKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGlNVARIGALLAGLPNSVGGVTVNRFCASGLQAVAMA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 150 VGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMLdlNKAKtlaqrlslltkfrlnfLSPELpavaeFSTNET------ 223
Cdd:PRK09052 106 ADRIRVGEADVMIAAGVESMSMVP---------MMG--NKPS----------------MSPAI-----FARDENvgiayg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 224 MGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKV----PG---------KDTVSKDNGIRP-SSLE 288
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPYEIterfPDlatgevdvkTRTVDLDEGPRAdTSLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 289 QMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK09052 234 GLAKLKPVF-ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFA-VAGVPPEIMGIGPIEAIPAALKQAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 369 LTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK09052 312 LKQDDLDWIELNEAFAAQSLAVIRDLGLD-----------------PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRR 374
|
410 420
....*....|....*....|....
gi 1958781811 449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09052 375 TNLKYGMVTMCVGTGMGAAGIFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
59-471 |
2.24e-62 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 208.09 E-value: 2.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 59 EGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTM 137
Cdd:PRK08131 8 DGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSrNVARNALLLAGLPVTVPGQTVNR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 138 ACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPI-------RHSRNMRkmMLDlnkaKTLAQRlslltkfrlnFLSP 210
Cdd:PRK08131 88 LCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFvmgkaesAFSRDAK--VFD----TTIGAR----------FPNP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 211 ELpaVAEFStNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVP--GKDT---VSKDNGIRP 284
Cdd:PRK08131 152 KI--VAQYG-NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADeITPIEVPqgRKLPpklVAEDEHPRP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 285 SS-LEQMAKLKPAFIKpyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKV 363
Cdd:PRK08131 229 SStVEALTKLKPLFEG--GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPR-IMGIGPVEAIKKA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 364 LEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRLVMAAA 443
Cdd:PRK08131 306 LARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDD---------------PRVNPNGGAIAVGHPLGASGARLALTAA 370
|
410 420
....*....|....*....|....*...
gi 1958781811 444 NRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08131 371 RELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
77-472 |
5.68e-62 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 206.89 E-value: 5.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 77 PHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIAS 155
Cdd:PRK06504 26 PADLAAQVLDALVDRSGADPALIEDVIMGCVSQVgEQATNVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 156 GQCDVVVAGGVELMSDVPirhsrnmrkMMLdlnkAKTLAQRLSLLTkfrlnFLSPELPA---VAEFStnETMGhsADRLA 232
Cdd:PRK06504 106 GTMDIVIAAGVESMTRVP---------MGS----PSTLPAKNGLGH-----YKSPGMEErypGIQFS--QFTG--AEMMA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 233 AAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPG----KDTVSKDNGIR-PSSLEQMAKLKPafIKPYGTVTA 306
Cdd:PRK06504 164 KKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPLEITRadgsGEMHTVDEGIRfDATLEGIAGVKL--IAEGGRLTA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 307 ANSSFLTDGASAMLIMSEdRAL-AMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSG 385
Cdd:PRK06504 242 ATASQICDGASGVMVVNE-RGLkALGVKPLARIHHMTVIGGDPV-IMLEAPLPATERALKKAGMKIDDIDLYEVNEAFAS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 386 QILANFKAMdsdwfaqnymgrktkvGAPPlEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQG 465
Cdd:PRK06504 320 VPLAWLKAT----------------GADP-ERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGMA 382
|
....*..
gi 1958781811 466 HAMIVEA 472
Cdd:PRK06504 383 NVTIVER 389
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
56-471 |
3.18e-60 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 202.31 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 56 VVVEGVRIPFllsGTSYKDL--MPH--DLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGAGFSDKT 130
Cdd:PRK07108 5 VIVSTARTPL---AKSWRGAfnMTHgaTLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATgANIARQIALRAGLPVTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVpirhSRNMRKMMLdlnkaktlaqRLSLLTKFRlnflsP 210
Cdd:PRK07108 82 PGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV----QNEMNRHML----------REGWLVEHK-----P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 211 ELpavaefstNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPF--------KVPG-----KDTV 276
Cdd:PRK07108 143 EI--------YWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPItvtagvadKATGrlftkEVTV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 277 SKDNGIRP-SSLEQMAKLKPAFikPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLG 355
Cdd:PRK07108 215 SADEGIRPdTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP-DEMGIG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 356 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMgrKTKVGAPPlEKFNIWGGSLSLGHPFGATG 435
Cdd:PRK07108 292 PVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVL--------------YC--RDTLGIPM-DRLNVNGGAIAVGHPYGVSG 354
|
410 420 430
....*....|....*....|....*....|....*.
gi 1958781811 436 CRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07108 355 ARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
332-472 |
7.00e-59 |
|
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: 189.78 E-value: 7.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 332 YKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvg 411
Cdd:pfam02803 1 LKPLARIRSYATAGVDP-AIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP------------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958781811 412 applEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:pfam02803 67 ----EKVNVNGGAIALGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
52-471 |
7.81e-57 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 193.30 E-value: 7.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR---KMMLDLNkaktlaqrlsllTKFRLNFL 208
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgpKHLLHKN------------YKIDDAML 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 209 SPELPAVAEFstnETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVSKDNGIRPSSL 287
Cdd:PRK06366 149 VDGLIDAFYF---EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNeIVPF-----NDLDRDEGIRKTTM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 288 EQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEKA 367
Cdd:PRK06366 221 EDLAKLPPAFDKN-GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLD-FVEAPIPATRKLLEKQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 368 GLTMNDIDAFEFHEAFS--GQILANFKAMDSdwfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK06366 299 NKSIDYYDLVEHNEAFSiaSIIVRDQLKIDN-------------------ERFNVNGGAVAIGHPIGNSGSRIIVTLINA 359
|
410 420
....*....|....*....|....*.
gi 1958781811 446 LRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06366 360 LKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
52-472 |
1.16e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 190.24 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 52 LKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSdvPIRHSRNMRK-------MMLDLNKAKTLAQRLSLLTkfr 204
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS--LGMHGSYIRAgakfgdiKMVDLMQYDGLTDVFSGVF--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 205 lnflspelpavaefstnetMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKDTVS---KDN 280
Cdd:PRK06633 157 -------------------MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDeILPIEVTIKKTTSlfdHDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 281 GIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdqlLLG--PT 357
Cdd:PRK06633 218 TVRPdTSLEILSKLRPAFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPS---IMGtaPV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 358 YATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMGRKTKVGappLEKFNIWGGSLSLGHPFGATGCR 437
Cdd:PRK06633 294 PASQKALSKAGWSVNDLEVIEVNEAFAAQSI--------------YVNREMKWD---MEKVNINGGAIAIGHPIGASGGR 356
|
410 420 430
....*....|....*....|....*....|....*
gi 1958781811 438 LVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK06633 357 VLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
55-473 |
4.30e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 188.95 E-value: 4.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP-----------IRHSRNMRKMMLD-LNKAktlaqrlslltk 202
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDgLEDA------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 203 frlnflspelpavaeFSTNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLS-DIVPFKVPGKD---TVSK 278
Cdd:PRK06954 157 ---------------YDKGRLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAwEIAPVTVAGKKgdtVIDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 279 DNGIRPSSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTY 358
Cdd:PRK06954 222 DEQPFKANPEKIPTLKPAFSKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPS-KFTTAPVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 359 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgapPLEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK06954 300 AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL-----------------PHEKVNVNGGACALGHPIGASGARI 362
|
410 420 430
....*....|....*....|....*....|....*
gi 1958781811 439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06954 363 LVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
79-471 |
3.44e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 178.54 E-value: 3.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 79 DLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQC 158
Cdd:PRK05656 28 ELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVPAMTLNKVCGSGLKALHLAAQAIRCGDA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 159 DVVVAGGVELMSDVP-----------IRHSRNMRKMMLDlnkaktlaqrlSLLTKFrlnflspelpavaefsTNETMGHS 227
Cdd:PRK05656 108 EVIIAGGQENMSLAPyvlpgartglrMGHAQLVDSMITD-----------GLWDAF----------------NDYHMGIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 228 ADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVSKDNGIRP-SSLEQMAKLKPAFIKPy 301
Cdd:PRK05656 161 AENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDeITPILIPQRKgeplAFATDEQPRAgTTAESLAKLKPAFKKD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 302 GTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHE 381
Cdd:PRK05656 240 GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPA-IMGIGPVSATRRCLDKAGWSLAELDLIEANE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 382 AFSGQILANFKAMDSDwfaqnymgrktkvgappLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAA 461
Cdd:PRK05656 319 AFAAQSLAVGKELGWD-----------------AAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRRDAKKGLATLCIG 381
|
410
....*....|
gi 1958781811 462 GGQGHAMIVE 471
Cdd:PRK05656 382 GGQGVALAIE 391
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
74-471 |
8.20e-51 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 178.05 E-value: 8.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 74 DLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGL 152
Cdd:PRK06025 26 HLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 153 IASGQCDVVVAGGVELMSDVPIRHSRNMRK----MMLDLNKAktlaqrlslltkfRLNFLSPElpavaefstnETMGHSA 228
Cdd:PRK06025 106 IMSGMEDLVIAGGTEMMSYTAAMAAEDMAAgkppLGMGSGNL-------------RLRALHPQ----------SHQGVCG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 229 DRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLS-DIVPFKVP-GKDTVSKDNGIRP-SSLEQMAKLKPAF-------I 298
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFDkSLVPVYRDdGSVALDHEEFPRPqTTAEGLAALKPAFtaiadypL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 299 KPYGTVT------------------AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYAT 360
Cdd:PRK06025 243 DDKGTTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT-LMLNAPVPAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgapplEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK06025 322 KKVLAKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDR-----------------DKVNVNGGAIALGHPIGATGSILIG 384
|
410 420 430
....*....|....*....|....*....|.
gi 1958781811 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06025 385 TVLDELERRGLKRGLVTMCAAGGMAPAIIIE 415
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
54-471 |
1.95e-50 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 175.34 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 54 NIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLlyRTNIPKDVvDYIIFGTVIQevKTSNVAREAALGAGFSDKTPAH 133
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMEREI-DDVILGNVVG--PGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 134 TVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldlNKAKtlaqrlslltkfrlnfLSPELP 213
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ------------NRAR----------------FSPETI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 214 AvaefstNETMGHSADRLAAAFAVSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVSKDNGIRPSSLEQM-A 291
Cdd:PRK06690 129 G------DPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEeILSF-----NGLLDESIKKEMNYERIiK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 292 KLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLlGPTYATPKVLEKAGLTM 371
Cdd:PRK06690 198 RTKPAFLHN-GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGT-GPIFAVNKLLNEMNMKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 372 NDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgapPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:PRK06690 276 EDIDYFEINEAFASKVVACAKELQI-----------------PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDM 338
|
410 420
....*....|....*....|
gi 1958781811 452 QYALVAACAAGGQGHAMIVE 471
Cdd:PRK06690 339 KYGIATLGIGGGIGLALLFE 358
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
68-471 |
3.30e-39 |
|
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: 146.10 E-value: 3.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 68 SGTSYKDLmPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMT 147
Cdd:cd00826 15 NGADANDL-AHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 148 TAVGLIASGQCDVVVAGGVELMSdvpirhsrnmrkmMLDLNKAKTlAQRLSLLTKFRlnflspelpavaefstnetmghs 227
Cdd:cd00826 94 LAMQLIAGGDANCILAGGFEKME-------------TSAENNAKE-KHIDVLINKYG----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 228 adrlaaafavSRMEQDKYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVSKDNGIR---PSSLEQMAKLKPAFIKP 300
Cdd:cd00826 137 ----------MRACPDAFALAGQAGAEAAEKDGRFKDeFAKFGVKGRKgdiHSDADEYIQfgdEASLDEIAKLRPAFDKE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 301 yGTVTAANSSFLTDGASAMLIMSEDRA-------LAMGYKPKAYLRDFIYVSQDPKDQLLLG---PTYATPKVLEKAGLT 370
Cdd:cd00826 207 -DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVGgdgPIEAARKALEKAGLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 371 MNDIDAFEFHEAFSGQILANFKAMdsDWFAQNYMGRKTKVGAPPLEK---FNIWGGSLSLGHPFGATGCRLVMAAANRLR 447
Cdd:cd00826 286 IGDLDLIEAHDAFAANACATNEAL--GLCPEGQGGALVDRGDNTYGGksiINPNGGAIAIGHPIGASGAAICAELCFELK 363
|
410 420
....*....|....*....|....*....
gi 1958781811 448 KDGGQYA-----LVAACAAGGQGHAMIVE 471
Cdd:cd00826 364 GEAGKRQgagagLALLCIGGGGGAAMCIE 392
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
77-470 |
2.40e-22 |
|
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: 98.10 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 77 PHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00829 16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 157 QCDVVVAGGVELMSDVPIR-----HSRNMRKMMLDLNKAKTLAQRLSLLTKFRLnflspelpavAEFSTN-ETMghsadr 230
Cdd:cd00829 95 LADVVLVVGAEKMSDVPTGdeaggRASDLEWEGPEPPGGLTPPALYALAARRYM----------HRYGTTrEDL------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 231 laAAFAVsrmeqdkyALRSHSLA-KKAQdeghlsdivpFKvpgkdtvskdngiRPSSLEQMAKLKPafIKPYgtVTAANS 309
Cdd:cd00829 159 --AKVAV--------KNHRNAARnPYAQ----------FR-------------KPITVEDVLNSRM--IADP--LRLLDC 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 310 SFLTDGASAMLIMSEDRALAMGYKPkAYLR------DFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAF 383
Cdd:cd00829 202 CPVSDGAAAVVLASEERARELTDRP-VWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 384 SGQILANFKAM------DSDWFAQNymGRKTKVGAPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYA--- 454
Cdd:cd00829 281 TIAELLALEDLgfcekgEGGKLVRE--GDTAIGGDLPV---NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQvpg 355
|
410
....*....|....*...
gi 1958781811 455 --LVAACAAGGQGHAMIV 470
Cdd:cd00829 356 arVGLAHNIGGTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
79-449 |
1.10e-15 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 78.40 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 79 DLARAALSGLLYRTNIPKDVVDYIIFGTVI--QEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAPI-PATRVEAACASGGAALRQAYLAVASG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 157 QCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktlaqrlslltkfrlnflSPElpavaefsTNETMGHSADRLAAAFA 236
Cdd:PRK06064 103 EADVVLAAGVEKMTDVP-----------------------------------TPD--------ATEAIARAGDYEWEEFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 237 ----------VSRMEQDKYALRSHSLAK---KAQDEGHLSDIVPFKvpgkdtvskdngiRPSSLEQMAKLKPAF--IKPY 301
Cdd:PRK06064 140 gatfpglyalIARRYMHKYGTTEEDLALvavKNHYNGSKNPYAQFQ-------------KEITVEQVLNSPPVAdpLKLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 302 gtvtaaNSSFLTDGASAMLIMSEDRAlamgykpKAYLRDFIYVS-----------QDPKDQLLLGPT-YATPKVLEKAGL 369
Cdd:PRK06064 207 ------DCSPITDGAAAVILASEEKA-------KEYTDTPVWIKasgqasdtialHDRKDFTTLDAAvVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 370 TMNDIDAFEFHEAFSgqiLANFKAMDSDWFAQNYMGRK------TKVGAppleKF--NIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK06064 274 EPKDIDVAEVHDCFT---IAEILAYEDLGFAKKGEGGKlaregqTYIGG----DIpvNPSGGLKAKGHPVGATGVSQAVE 346
|
....*...
gi 1958781811 442 AANRLRKD 449
Cdd:PRK06064 347 IVWQLRGE 354
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
74-466 |
4.39e-10 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 61.40 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 74 DLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHtVTMACISSNQAMTTAVGLI 153
Cdd:PRK12578 18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGLAASLTAYTAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 154 ASGQCDVVVAGGVELMSDVpirhsrnmrkmmlDLNKAKTLAQRL-SLLTKFrlNFLSPELPAVAEFStnetmghsADRLA 232
Cdd:PRK12578 97 ASGLVDMAIAVGVDKMTEV-------------DTSTSLAIGGRGgNYQWEY--HFYGTTFPTYYALY--------ATRHM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 233 AAFAVSRMEQDKYALRSHSLAKKaQDEGHLSdivpfkvpgkdtvskdngiRPSSLEQMakLKPAFIK-PygtVTAANSSF 311
Cdd:PRK12578 154 AVYGTTEEQMALVSVKAHKYGAM-NPKAHFQ-------------------KPVTVEEV--LKSRAISwP---IKLLDSCP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 312 LTDGASAMLIMSEDRALAMGY------KPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSg 385
Cdd:PRK12578 209 ISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFT- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 386 qiLANFKAMDSDWFAQNYMGRK-------TKVGAPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG--QYALV 456
Cdd:PRK12578 288 --IAEIMGYEDLGFTEKGKGGKfieegqsEKGGKVGV---NLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGklQQPLK 362
|
410
....*....|....
gi 1958781811 457 AACA----AGGQGH 466
Cdd:PRK12578 363 KYIGlvhnVGGTGH 376
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
306-470 |
4.84e-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: 57.07 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 306 AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLL---GPTYATPKVLEKAGLTMNDIDAFEFHEA 382
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 383 FSGQILANFKAMDSDWFAQNYMgrktkvgapplekfNIWGGSLSLGHPFGATG-------CRLVMAAANRLRKDGGQYAL 455
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSP--------------AVSATLIMTGHPLGAAGlaildelLLMLEHEFIPPTPREPRTVL 239
|
170
....*....|....*
gi 1958781811 456 VAACAAGGQGHAMIV 470
Cdd:cd00327 240 LLGFGLGGTNAAVVL 254
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
310-442 |
8.70e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 54.18 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 310 SFLTDGASAMLIMSEDRALAM----GYKPKAYLRDFIYVSQdpKDQLLL-GPTYATPKVLEKAGLTMNDIDAFEFHEAFS 384
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSR--RDPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958781811 385 GQILANFKAMDSDWFAQNYM----GRKTKVGAPPLekfNIWGGSLSLGHPFGATGCRL-VMAA 442
Cdd:PRK07516 291 IAELIEYEAMGLAPPGQGARaireGWTAKDGKLPV---NPSGGLKAKGHPIGATGVSMhVLAA 350
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
96-462 |
1.30e-07 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 53.74 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 96 KDVVDYIIFGTVIQEVKTS--NVAREAALGAGFSDKT------PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PTZ00455 69 AALVDKVVVGNFLGELFSSqgHLGPAAVGSLGQSGASnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 168 LMSDVPIRHSRNMRKMMLDLNKAKTLAqrlslltkfrlNFLSPELPAVAEFSTNE----TMGHSADRLAAAFAVSrmeqD 243
Cdd:PTZ00455 149 VQTTVSARVGGDYLARAADYRRQRKLD-----------DFTFPCLFAKRMKYIQEhghfTMEDTARVAAKAYANG----N 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 244 KYALrSHSLAKKAQDEGHlsdivpfkvpgkdtvskdNGIRPSSLEQMAKlkpAFIKPYGTVTaaNSSFLTDGASAMLIMS 323
Cdd:PTZ00455 214 KNPL-AHMHTRKLSLEFC------------------TGASDKNPKFLGN---ETYKPFLRMT--DCSQVSDGGAGLVLAS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 324 EDRALAMGYKP--------KAYLRDFIYVSQDPKDQLLLGPTY-ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAM 394
Cdd:PTZ00455 270 EEGLQKMGLSPndsrlveiKSLACASGNLYEDPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEAL 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958781811 395 D-SDWFAQNYMGRK---TKVGAPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAG 462
Cdd:PTZ00455 350 GiAEYGHAKDLIRNgatALEGRIPV---NTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNIPALG 418
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
113-167 |
1.81e-07 |
|
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: 53.31 E-value: 1.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958781811 113 TSNVAREAALGAGFsdKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:cd00834 137 PNMAAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
131-167 |
2.19e-07 |
|
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: 52.79 E-value: 2.19e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:COG0304 153 PNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAE 189
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
131-169 |
3.17e-07 |
|
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: 51.48 E-value: 3.17e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELM 169
Cdd:pfam00109 165 PSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLL 203
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
78-168 |
1.22e-06 |
|
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: 49.75 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 78 HDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSdKTPAHTVTMACISSNQAMTTAVGLIASGQ 157
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90
....*....|.
gi 1958781811 158 CDVVVAGGVEL 168
Cdd:cd00327 87 ADIVLAGGSEE 97
|
|
| FabH |
COG0332 |
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ... |
73-172 |
1.43e-06 |
|
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: 50.11 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 73 KDLMPHDLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKT----SNVAREaaLGAgfsDKTPAHTVTMACISSNQAMTT 148
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFpstaCLVQHK--LGA---KNAAAFDINAACSGFVYALSV 121
|
90 100
....*....|....*....|....*
gi 1958781811 149 AVGLIASGQCD-VVVAGGvELMSDV 172
Cdd:COG0332 122 AAALIRSGQAKnVLVVGA-ETLSRI 145
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
131-181 |
6.06e-05 |
|
"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: 45.12 E-value: 6.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR 181
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMG 204
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
131-166 |
2.08e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 43.68 E-value: 2.08e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGV 166
Cdd:PRK09185 152 PAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGV 187
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
131-171 |
9.55e-04 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 41.39 E-value: 9.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958781811 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSD 171
Cdd:cd00833 162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILS 202
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
79-172 |
1.15e-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: 40.99 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 79 DLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAGfsdKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLvqARLGAK---NAAAFDINAACSGFLYGLSTAAGLIRSG 128
|
90
....*....|....*.
gi 1958781811 157 QCDVVVAGGVELMSDV 172
Cdd:cd00830 129 GAKNVLVVGAETLSRI 144
|
|
| PRK08313 |
PRK08313 |
thiolase domain-containing protein; |
313-470 |
3.72e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 181378 [Multi-domain] Cd Length: 386 Bit Score: 39.71 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 313 TDGASAMLIMSEDRALAMGYKPKAYL--------------RDFIyvsqDPKdqlllGPTYATPKVLEKAGLT--MNDIDA 376
Cdd:PRK08313 209 SDGACAVVIGDEEAADAAAGRPVAWIhgtamrteplafagRDQV----NPQ-----AGRDAAAALWKAAGITdpRDEIDV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 377 FEFHEAFSGqilanFKAMdsdW-----FAQNYMGRK-TKVGAPPLE---KFNIWGGSLSlGHPFGATGCRLVMAAANRLR 447
Cdd:PRK08313 280 AEIYVPFSW-----FEPM---WlenlgFAPEGEGWKlTEAGETAIGgrlPVNPSGGVLS-SNPIGASGMIRFAEAALQVM 350
|
170 180 190
....*....|....*....|....*....|
gi 1958781811 448 KDGGQY-------ALVAACAAGGQGHAMIV 470
Cdd:PRK08313 351 GKAGEHqvdgarkALGHAYGGGSQFFSMWV 380
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
79-172 |
3.82e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 39.46 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 79 DLARAALSGLLYRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAgfsDKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK12879 55 DLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQvqARLGI---PNAAAFDINAACAGFLYGLETANGLITSG 131
|
90
....*....|....*.
gi 1958781811 157 QCDVVVAGGVELMSDV 172
Cdd:PRK12879 132 LYKKVLVIGAERLSKV 147
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
129-167 |
4.23e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.39 E-value: 4.23e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1958781811 129 KTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PRK07314 152 KGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE 190
|
|
| PRK06059 |
PRK06059 |
lipid-transfer protein; Provisional |
81-169 |
6.14e-03 |
|
lipid-transfer protein; Provisional
Pssm-ID: 180373 [Multi-domain] Cd Length: 399 Bit Score: 38.98 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958781811 81 ARAAL--SGLLYRTnipkdvVDYIIFGTVIQEVKTSNVAreaalGAGFSDK-----TPAHTVTMACISSNQAMTTAVGLI 153
Cdd:PRK06059 31 ARAALadAGLDWRD------VQLVVGADTIRNGYPGFVA-----GATFAQAlgwngAPVSSSYAACASGSQALQSARAQI 99
|
90
....*....|....*.
gi 1958781811 154 ASGQCDVVVAGGVELM 169
Cdd:PRK06059 100 LAGLCDVALVVGADTT 115
|
|
| |
