|
Name |
Accession |
Description |
Interval |
E-value |
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
56-472 |
1.51e-176 |
|
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: 500.08 E-value: 1.51e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 56 VVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTV 135
Cdd:cd00751 1 VIVSAVRTPIGRFGGALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNPARQAALLAGLPESVPATTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 136 TMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKaktlgqrlslLSKFRLNFLSPELPAV 215
Cdd:cd00751 81 NRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYLLPKARRGGRLGLNT----------LDGMLDDGLTDPFTGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 216 AefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQM 290
Cdd:cd00751 151 S-------MGITAENVAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDeIVPVEVPGRkgpVVVDRDEGPRPdTTLEKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 291 AKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLT 370
Cdd:cd00751 224 AKLKPAF-KKDGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDP-AIMGIGPVPAIPKALKRAGLT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 371 MNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG 450
Cdd:cd00751 302 LDDIDLIEINEAFAAQALACLKELGLDP-----------------EKVNVNGGAIALGHPLGASGARIVVTLLHELKRRG 364
|
410 420
....*....|....*....|..
gi 1907162524 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 |
5.16e-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: 488.66 E-value: 5.16e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 57 VVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVT 136
Cdd:TIGR01930 1 IVAAARTPIGKFGGSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQQNIARQAALLAGLPESVPAYTVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 137 MACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkMMLDLNKAKTLGQRLSLLskfrlnflspelpavA 216
Cdd:TIGR01930 81 RQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRVPYGVPRSLR-WGVKPGNAELEDARLKDL---------------T 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 217 EFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK---DTVTKDNGIRP-SSLEQMA 291
Cdd:TIGR01930 145 DANTGLPMGVTAENLAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDeIVPVTVKGRkgpVTVSSDEGIRPnTTLEKLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 292 KLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTM 371
Cdd:TIGR01930 225 KLKPAF-DPDGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDP-EIMGLGPVPAIPKALKKAGLSI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 372 NDIDAFEFHEAFSGQILANFKAMDsdwfaqnymgrktkvgsPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:TIGR01930 303 SDIDLFEINEAFAAQVLACIKELG-----------------LDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG 365
|
410 420
....*....|....*....|
gi 1907162524 452 QYALVAACAAGGQGHAMIVE 471
Cdd:TIGR01930 366 RYGLATMCIGGGQGAAVILE 385
|
|
| fadI |
PRK08963 |
3-ketoacyl-CoA thiolase; Reviewed |
55-472 |
2.25e-163 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181597 [Multi-domain] Cd Length: 428 Bit Score: 468.31 E-value: 2.25e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK08963 7 IAIVSGLRTPFAKQATAFHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPELPA 214
Cdd:PRK08963 87 VSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGVSKKLARALVDLNKARTLGQRLKLFSRLRLRDLLPVPPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-----IVPfkvPGKDTVTKDNGIRP-SSLE 288
Cdd:PRK08963 167 VAEYSTGLRMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDevmtaHVP---PYKQPLEEDNNIRGdSTLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 289 QMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK08963 244 DYAKLRPAFDRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVWQDMLLGPAYATPLALERAG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 369 LTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08963 324 LTLADLTLIDMHEAFAAQTLANLQMFASERFAREKLGRSQAIGEVDMSKFNVLGGSIAYGHPFAATGARMITQTLHELRR 403
|
410 420
....*....|....*....|....
gi 1907162524 449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08963 404 RGGGLGLTTACAAGGLGAAMVLEV 427
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
52-472 |
4.52e-155 |
|
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: 445.66 E-value: 4.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:COG0183 1 MREVVIVDAVRTPFGRFGGALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNPARQAALLAGLPESVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLnkakTLGQRLSllskfrlnflspe 211
Cdd:COG0183 81 AVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRAPMLLPKARWGYRMNA----KLVDPMI------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 212 LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVTKDNGIRP-SS 286
Cdd:COG0183 144 NPGLTDPYTGLSMGETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDeIVPVEVPDRKgevVVDRDEGPRPdTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 287 LEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEK 366
Cdd:COG0183 224 LEKLAKLKPAF-KKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEI-MGIGPVPATRKALAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 367 AGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRL 446
Cdd:COG0183 302 AGLTLDDIDLIEINEAFAAQVLAVLRELGLDP-----------------DKVNVNGGAIALGHPLGASGARILVTLLHEL 364
|
410 420
....*....|....*....|....*.
gi 1907162524 447 RKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:COG0183 365 ERRGGRYGLATMCIGGGQGIALIIER 390
|
|
| PRK09268 |
PRK09268 |
acetyl-CoA C-acetyltransferase; |
47-472 |
6.88e-124 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236440 [Multi-domain] Cd Length: 427 Bit Score: 367.69 E-value: 6.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 47 LAKPNMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGF 126
Cdd:PRK09268 1 MTMPTVRRVAILGGNRIPFARSNGAYADASNQDMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNLTRECVLGSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 127 SDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLN 206
Cdd:PRK09268 81 SPYTPAYDLQQACGTGLEAAILVANKIALGQIDSGIAGGVDTTSDAPIAVNEGLRKILLELNRAKTTGDRLKALGKLRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 207 FLSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKvpgkdTVTKDNGIRP- 284
Cdd:PRK09268 161 HLAPEIPRNGEPRTGLSMGEHAAITAKEWGISREAQDELAAASHQNLAAAYDRGFFDDlITPFL-----GLTRDNNLRPd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 285 SSLEQMAKLKPAFIK-PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQD---PKDQLLLGPTYAT 360
Cdd:PRK09268 236 SSLEKLAKLKPVFGKgGRATMTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAETAAVDfvhGKEGLLMAPAYAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK09268 316 PRLLARNGLTLQDFDFYEIHEAFASQVLATLKAWEDEEYCRERLGLDAPLGSIDRSKLNVNGSSLAAGHPFAATGGRIVA 395
|
410 420 430
....*....|....*....|....*....|..
gi 1907162524 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09268 396 TLAKLLAEKGSGRGLISICAAGGQGVTAILER 427
|
|
| PRK08170 |
PRK08170 |
acetyl-CoA C-acetyltransferase; |
51-472 |
9.35e-112 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181265 [Multi-domain] Cd Length: 426 Bit Score: 336.60 E-value: 9.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 51 NMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKT 130
Cdd:PRK08170 1 MARPVYIVDGARTPFLKARGGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCAMPSPDEANIARVVALRLGCGEKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSP 210
Cdd:PRK08170 81 PAWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMSHAPLLFSEKMVRWLAGWYAAKSIGQKLAALGKLRPSYLAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 211 E---LPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVPFkVPGKDTV-TKDNGIRP-S 285
Cdd:PRK08170 161 ViglLRGLTDPVVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLKEVVPL-FDRDGKFyDHDDGVRPdS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 286 SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLE 365
Cdd:PRK08170 240 SMEKLAKLKPFFDRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDP-SQMGLGPVHAATPLLQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 366 KAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAQNYMGRKTKVGSPPLEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK08170 319 RHGLTLEDLDLWEINEAFAAQVLACLAAWADEEYCREQLGLDGALGELDRERLNVDGGAIALGHPVGASGARIVLHLLHA 398
|
410 420
....*....|....*....|....*..
gi 1907162524 446 LRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK08170 399 LKRRGTKRGIAAICIGGGQGGAMLLER 425
|
|
| PRK05790 |
PRK05790 |
putative acyltransferase; Provisional |
52-472 |
4.09e-109 |
|
putative acyltransferase; Provisional
Pssm-ID: 180261 [Multi-domain] Cd Length: 393 Bit Score: 328.65 E-value: 4.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK05790 1 MKDVVIVSAARTPIGKFGGALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQNPARQAALKAGLPVEVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDlnkaktlgqrlsllskfrl 205
Cdd:PRK05790 81 ALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQAPhvLPGSRWGQKMgdveLVD------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 206 nflSPELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDN 280
Cdd:PRK05790 142 ---TMIHDGLTDAFNGYHMGITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDeIVPVTIKQRKgdpvVVDTDE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 281 GIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYA 359
Cdd:PRK05790 219 HPRPdTTAESLAKLRPAFDKD-GTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPA-IMGIGPVPA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PRK05790 297 IRKALEKAGWSLADLDLIEINEAFAAQALAVEKELGLD-----------------PEKVNVNGGAIALGHPIGASGARIL 359
|
410 420 430
....*....|....*....|....*....|...
gi 1907162524 440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK05790 360 VTLLHEMKRRGAKKGLATLCIGGGQGVALIVER 392
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
55-325 |
7.41e-101 |
|
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: 302.68 E-value: 7.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:pfam00108 1 VVIVSAARTPFGSFGGSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPARQAALKAGIPDSAPAVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMRkmmldlnkaktlgQRLSLLSKFRLNFLSPElpA 214
Cdd:pfam00108 81 INKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMSHAPYALPTDAR-------------SGLKHGDEKKHDLLIPD--G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 215 VAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTVTKDNGIRP-SSLEQ 289
Cdd:pfam00108 146 LTDAFNGYHMGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDeIVPVTVKgrkGKPTVDKDEGIRPpTTAEP 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907162524 290 MAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSED 325
Cdd:pfam00108 226 LAKLKPAFDKE-GTVTAGNASPINDGAAAVLLMSES 260
|
|
| PRK06205 |
PRK06205 |
acetyl-CoA C-acetyltransferase; |
52-474 |
5.06e-88 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235741 [Multi-domain] Cd Length: 404 Bit Score: 274.94 E-value: 5.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06205 1 MRDAVICEPVRTPVGRFGGAFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIGRVAALDAGLPVTVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrHSRNMRKmmldlnKAKTLGQRLS-LLSKFRlnflsp 210
Cdd:PRK06205 81 GMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSNVEF-YTTDMRW------GVRGGGVQLHdRLARGR------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 211 ELPAVAEFSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDNGIRP- 284
Cdd:PRK06205 148 ETAGGRRFPVPGGMIETAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDeIVPVTVPQRKgdptVVDRDEHPRAd 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 285 SSLEQMAKLKPAFIK--PYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPK 362
Cdd:PRK06205 228 TTLESLAKLRPIMGKqdPEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEP-SRMGIGPVPATEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 363 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAA 442
Cdd:PRK06205 307 ALARAGLTLDDIDLIELNEAFAAQVLAVLKEWGFGADD--------------EERLNVNGSGISLGHPVGATGGRILATL 372
|
410 420 430
....*....|....*....|....*....|..
gi 1907162524 443 ANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PRK06205 373 LRELQRRQARYGLETMCIGGGQGLAAVFERVN 404
|
|
| PRK08235 |
PRK08235 |
acetyl-CoA C-acetyltransferase; |
52-473 |
8.09e-86 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181311 [Multi-domain] Cd Length: 393 Bit Score: 268.89 E-value: 8.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK08235 1 MSKTVIVSAARTPFGKFGGSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGGQGQIPSRQAARAAGIPWEVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKM----MLDLNKAKTLgqrlsllskfrl 205
Cdd:PRK08235 81 TETVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNAPyiLPGARWGYRMgdneVIDLMVADGL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 206 nflspelpaVAEFSTNEtMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDN 280
Cdd:PRK08235 149 ---------TCAFSGVH-MGVYGGEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEeIVPVTIPQRKgdpiVVAKDE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 281 GIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYA 359
Cdd:PRK08235 219 APRKdTTIEKLAKLKPVF-DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKD-FPRTPGYA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PRK08235 297 INALLEKTGKTVEDIDLFEINEAFAAVALASTEIAGID-----------------PEKVNVNGGAVALGHPIGASGARII 359
|
410 420 430
....*....|....*....|....*....|....
gi 1907162524 440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK08235 360 VTLIHELKRRGGGIGIAAICSGGGQGDAVLIEVH 393
|
|
| PRK09051 |
PRK09051 |
beta-ketothiolase BktB; |
51-471 |
2.45e-81 |
|
beta-ketothiolase BktB;
Pssm-ID: 181625 [Multi-domain] Cd Length: 394 Bit Score: 257.20 E-value: 2.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 51 NMKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDK 129
Cdd:PRK09051 1 MMREVVVVSGVRTAIGTFGGSLKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPtEPRDMYLSRVAAINAGVPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP--IRHSRNMRKMmldlNKAKTLGQRLSLLSkfrlnf 207
Cdd:PRK09051 81 TPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSRAPylLPAARWGARM----GDAKLVDMMVGALH------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 208 lSPelpavaeFSTNEtMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPG-KDTVT--KDNGIR 283
Cdd:PRK09051 151 -DP-------FGTIH-MGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDqIVPVEIKTrKGEVVfdTDEHVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 284 PS-SLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYATPK 362
Cdd:PRK09051 222 ADtTLEDLAKLKPVFKKENGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDP-EYMGIGPVPATQK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 363 VLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsPplEKFNIWGGSLSLGHPFGATGCRLVMAA 442
Cdd:PRK09051 301 ALERAGLTVADLDVIEANEAFAAQACAVTRELGLD---------------P--AKVNPNGSGISLGHPVGATGAIITVKA 363
|
410 420
....*....|....*....|....*....
gi 1907162524 443 ANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09051 364 LYELQRIGGRYALVTMCIGGGQGIAAIFE 392
|
|
| PRK07850 |
PRK07850 |
steroid 3-ketoacyl-CoA thiolase; |
52-471 |
3.77e-81 |
|
steroid 3-ketoacyl-CoA thiolase;
Pssm-ID: 181145 [Multi-domain] Cd Length: 387 Bit Score: 256.57 E-value: 3.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 130
Cdd:PRK07850 1 MGNPVIVEAVRTPIGKRNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSnNITRTAWLHAGLPYHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktLGQRLSL-LSKFRLNFLS 209
Cdd:PRK07850 81 GATTIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMSRVP-------------------LGANAGPgRGLPRPDSWD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 210 PELPAVAEfstnetmghSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHL-SDIVPFKVPGKD----------TVTK 278
Cdd:PRK07850 142 IDMPNQFE---------AAERIAKRRGITREDVDAFGLRSQRRAAQAWAEGRFdREISPVQAPVLDeegqptgetrLVTR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 279 DNGIRPSSLEQMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTY 358
Cdd:PRK07850 213 DQGLRDTTMEGLAGLKP--VLEGGIHTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPY-YHLDGPVQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 359 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILAnfkamdsdwFAQnymgrktkVGSPPLEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK07850 290 ATAKVLEKAGMKIGDIDLVEINEAFASVVLS---------WAQ--------VHEPDMDKVNVNGGAIALGHPVGSTGARL 352
|
410 420 430
....*....|....*....|....*....|...
gi 1907162524 439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07850 353 ITTALHELERTDKSTALITMCAGGALSTGTIIE 385
|
|
| PRK06445 |
PRK06445 |
acetyl-CoA C-acetyltransferase; |
52-473 |
4.89e-81 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180563 [Multi-domain] Cd Length: 394 Bit Score: 256.57 E-value: 4.89e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTS------YKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGA 124
Cdd:PRK06445 1 LEDVYLVDFARTAFSRFRPKdpqkdvFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENwLYGGRHPIFLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 125 GFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHS----RNMrKMMLDlnkaktlgqrlSLL 200
Cdd:PRK06445 81 RLPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMTRTPMGDNphiePNP-KLLTD-----------PKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 201 SKFRLNflspelpavaefsTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP---GKDTV 276
Cdd:PRK06445 149 IEYDLT-------------TGYVMGLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDeILPIEVEvegKKKVV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 277 TKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLG 355
Cdd:PRK06445 216 DVDQSVRPdTSLEKLAKLPPAF-KPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPP-AIMGKG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 356 PTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATG 435
Cdd:PRK06445 294 PVPASKKALEKAGLSVKDIDLWEINEAFAVVVLYAIKELGLD-----------------PETVNIKGGAIAIGHPLGATG 356
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907162524 436 CRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06445 357 ARIVGTLARQLQIKGKDYGVATLCVGGGQGGAVVLERV 394
|
|
| fadA |
PRK08947 |
3-ketoacyl-CoA thiolase; Reviewed |
52-471 |
2.63e-80 |
|
3-ketoacyl-CoA thiolase; Reviewed
Pssm-ID: 181592 [Multi-domain] Cd Length: 387 Bit Score: 254.50 E-value: 2.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLS-GTSYKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSD 128
Cdd:PRK08947 1 MEDVVIVDAIRTPMGRSkGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGfNIARNAALLAGIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 129 KTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSrnmrkmmLDLNKAktlgqrlslLSKFrlnfl 208
Cdd:PRK08947 81 SVPAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMGHVPMNHG-------VDFHPG---------LSKN----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 209 spelpaVAEFSTNetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPfkVPGKD------TVTKDNG 281
Cdd:PRK08947 140 ------VAKAAGM--MGLTAEMLGKMHGISREQQDAFAARSHQRAWAATQEGRFKNeIIP--TEGHDadgvlkLFDYDEV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 282 IRP-SSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYAT 360
Cdd:PRK08947 210 IRPeTTVEALAALRPAFDPVNGTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPS-IMGYGPVPAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqNYMGRKTkvgspplEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK08947 289 QKALKRAGLSISDIDVFELNEAFAAQSLPCLKDL-------GLLDKMD-------EKVNLNGGAIALGHPLGCSGARIST 354
|
410 420 430
....*....|....*....|....*....|.
gi 1907162524 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08947 355 TLLNLMERKDAQFGLATMCIGLGQGIATVFE 385
|
|
| PRK07801 |
PRK07801 |
acetyl-CoA C-acetyltransferase; |
52-471 |
8.47e-80 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181123 [Multi-domain] Cd Length: 382 Bit Score: 252.71 E-value: 8.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQ-EVKTSNVAREAALGAGFSDKT 130
Cdd:PRK07801 1 MAEAYIVDAVRTPVGKRKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTiGPQAGNIARTSWLAAGLPEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIrhSRNMrkmmldlnkakTLGQRLSLLSKFrlnflSP 210
Cdd:PRK07801 81 PGVTVDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMSQIPI--SSAM-----------TAGEQLGFTSPF-----AE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 211 ELPAVAEFSTNE-TMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSLE 288
Cdd:PRK07801 143 SKGWLHRYGDQEvSQFRGAELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNeIVPV-----GGVTVDEGPRETSLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 289 QMAKLKPafIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAG 368
Cdd:PRK07801 218 KMAGLKP--LVEGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPV-FMLTAPIPATRYALEKTG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 369 LTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK07801 295 LSIDDIDVVEINEAFAPVVLAWLKETGAD-----------------PAKVNPNGGAIALGHPLGATGAKLMTTLLHELER 357
|
410 420
....*....|....*....|...
gi 1907162524 449 DGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07801 358 TGGRYGLQTMCEGGGTANVTIIE 380
|
|
| PLN02644 |
PLN02644 |
acetyl-CoA C-acetyltransferase |
53-474 |
2.74e-76 |
|
acetyl-CoA C-acetyltransferase
Pssm-ID: 215347 [Multi-domain] Cd Length: 394 Bit Score: 244.23 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 53 KNIVVVEGVRIP---FLLSGTSYKdlmPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIqevkTSNV----AREAALGAG 125
Cdd:PLN02644 1 RDVCIVGVARTPiggFLGSLSSLS---ATELGSIAIQAALERAGVDPALVQEVFFGNVL----SANLgqapARQAALGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 126 FSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrKMMLDLNKAKTLGQRLSLLSKFRL 205
Cdd:PLN02644 74 LPPSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSNAP--------KYLPEARKGSRLGHDTVVDGMLKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 206 NFLSPelpavaefSTNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGK-----DTVTKD 279
Cdd:PLN02644 146 GLWDV--------YNDFGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWeIVPVEVPGGrgrpsVIVDKD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 280 NGIRPSSLEQMAKLKPAFIKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPkDQLLLGPTYA 359
Cdd:PLN02644 218 EGLGKFDPAKLRKLRPSFKEDGGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAP-ELFTTAPALA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 360 TPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMdsdwfaqnymgrktkvGSPPlEKFNIWGGSLSLGHPFGATGCRLV 439
Cdd:PLN02644 297 IPKALKHAGLEASQVDYYEINEAFSVVALANQKLL----------------GLDP-EKVNVHGGAVSLGHPIGCSGARIL 359
|
410 420 430
....*....|....*....|....*....|....*
gi 1907162524 440 MAAANRLRKDGGQYALVAACAAGGQGHAMIVEAYP 474
Cdd:PLN02644 360 VTLLGVLRSKNGKYGVAGICNGGGGASAIVVELMQ 394
|
|
| PRK09050 |
PRK09050 |
beta-ketoadipyl CoA thiolase; Validated |
52-471 |
1.67e-72 |
|
beta-ketoadipyl CoA thiolase; Validated
Pssm-ID: 181624 [Multi-domain] Cd Length: 401 Bit Score: 234.46 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK09050 1 MTEAFICDAIRTPIGRYGGALSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNrNVARMSALLAGLPVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPI-------RHSRNMRkmMLDlnkaKTLGQRlsllsk 202
Cdd:PRK09050 81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRAPFvmgkadsAFSRQAE--IFD----TTIGWR------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 203 frlnFLSPELPAvaEFSTnETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVT 277
Cdd:PRK09050 149 ----FVNPLMKA--QYGV-DSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEeIVPVTIPQKKgdpvVVD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 278 KDNGIRPS-SLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PRK09050 222 RDEHPRPEtTLEALAKLKPVF-RPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTPRARILGMATAGVEPR-IMGIGP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAM---DSDwfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGA 433
Cdd:PRK09050 300 APATRKLLARLGLTIDQFDVIELNEAFAAQGLAVLRQLglaDDD------------------ARVNPNGGAIALGHPLGM 361
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907162524 434 TGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK09050 362 SGARLVLTALHQLERTGGRYALCTMCIGVGQGIALAIE 399
|
|
| PRK07661 |
PRK07661 |
acetyl-CoA C-acetyltransferase; |
52-471 |
1.00e-67 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181072 [Multi-domain] Cd Length: 391 Bit Score: 221.93 E-value: 1.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDK 129
Cdd:PRK07661 1 MREAVIVAGARTPVGKAKKgSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGlNMARNIGALAGLPYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 130 TPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMldlnkaktlGQRLsllskfRLNfls 209
Cdd:PRK07661 81 VPAITINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSLVP---------MM---------GHVV------RPN--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 210 pelPAVAEFSTN--ETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP----GKD-------- 274
Cdd:PRK07661 134 ---PRLVEAAPEyyMGMGHTAEQVAVKYGISREDQDAFAVRSHQRAAKALAEGKFADeIVPVDVTlrtvGENnklqeeti 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 275 TVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLL 353
Cdd:PRK07661 211 TFSQDEGVRAdTTLEILGKLRPAF-NVKGSVTAGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFA-VAGVPPEVMG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 354 LGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGA 433
Cdd:PRK07661 289 IGPIAAIPKALKLAGLELSDIGLFELNEAFASQSIQVIRELGLDE-----------------EKVNVNGGAIALGHPLGC 351
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907162524 434 TGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07661 352 TGAKLTLSLIHEMKRRNEQFGIVTMCIGGGMGAAGVFE 389
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
20-472 |
3.31e-67 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 222.33 E-value: 3.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 20 LRSSIRPLSCSSQLHSAPAVQTKSKKTLAKPNM--KNIVVVEGVRIPFLLSGT-SYKDLMPHDLARAALSGLLHRTNIPK 96
Cdd:PLN02287 11 LLRHLRPSSSEPSSLSASACAAGDSAAYHRTTAfgDDVVIVAAYRTPICKAKRgGFKDTYPDDLLAPVLKAVVEKTGLNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 97 DVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIR 175
Cdd:PLN02287 91 SEVGDIVVGTVLAPgSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGVESMTTNPMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 176 hsrnmrkmmldlnkaktlgqrlsllSKFRLNflspelPAVAEFSTNET----MGHSADRLAAAFAVSRMEQDEYALRSHS 251
Cdd:PLN02287 171 -------------------------WEGGVN------PRVESFSQAQDcllpMGITSENVAERFGVTREEQDQAAVESHR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 252 LAKKAQDEGHLSD-IVPFKVPGKD---------TVTKDNGIRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAML 320
Cdd:PLN02287 220 KAAAATASGKFKDeIVPVHTKIVDpktgeekpiVISVDDGIRPnTTLADLAKLKPVF-KKNGTTTAGNSSQVSDGAGAVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 321 IMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfa 400
Cdd:PLN02287 299 LMKRSVAMQKGLPILGVFRSFAAVGVDPA-VMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDP-- 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907162524 401 qnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDG--GQYALVAACAAGGQGHAMIVEA 472
Cdd:PLN02287 376 ---------------EKVNVNGGAIALGHPLGATGARCVATLLHEMKRRGkdCRFGVVSMCIGTGMGAAAVFER 434
|
|
| PRK07851 |
PRK07851 |
acetyl-CoA C-acetyltransferase; |
52-471 |
1.63e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 181146 [Multi-domain] Cd Length: 406 Bit Score: 213.71 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGT-SYKDLMPHDLA----RAALSGLLHRTniPKDVVDyIIFGTVIQEVKT-SNVAREAALGAG 125
Cdd:PRK07851 1 MPEAVIVSTARSPIGRAFKgSLKDMRPDDLAaqmvRAALDKVPALD--PTDIDD-LMLGCGLPGGEQgFNMARVVAVLLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 126 FsDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNM---RKMMLDLNKAKTLGQRLSLLSK 202
Cdd:PRK07851 78 Y-DFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSRFAKGNSDSLpdtKNPLFAEAQARTAARAEGGAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 203 FRLNFLSPELPAVAEfstneTMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVPGKDTVTKDNG 281
Cdd:PRK07851 157 WHDPREDGLLPDVYI-----AMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFErEITPVTLPDGTVVSTDDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 282 IRP-SSLEQMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDfIYVSQDPKDQLLLGPTYAT 360
Cdd:PRK07851 232 PRAgTTYEKVSQLKPVF-RPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVS-TGVSGLSPEIMGLGPVEAS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 361 PKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVM 440
Cdd:PRK07851 310 KQALARAGMSIDDIDLVEINEAFAAQVLPSARELGID-----------------EDKLNVSGGAIALGHPFGMTGARITT 372
|
410 420 430
....*....|....*....|....*....|.
gi 1907162524 441 AAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07851 373 TLLNNLQTHDKTFGLETMCVGGGQGMAMVLE 403
|
|
| PRK09052 |
PRK09052 |
acetyl-CoA C-acyltransferase; |
72-472 |
1.83e-64 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 181626 [Multi-domain] Cd Length: 399 Bit Score: 213.71 E-value: 1.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 72 YKDLMPHDLARAALSGLLHRT-NIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTA 149
Cdd:PRK09052 26 FKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGlNVARIGALLAGLPNSVGGVTVNRFCASGLQAVAMA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 150 VGLIASGQCDVVVAGGVELMSDVPirhsrnmrkMMldlnkaktlGQRLSLlskfrlnflSPELpavaeFSTNET------ 223
Cdd:PRK09052 106 ADRIRVGEADVMIAAGVESMSMVP---------MM---------GNKPSM---------SPAI-----FARDENvgiayg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 224 MGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKV----PG---------KDTVTKDNGIRP-SSLE 288
Cdd:PRK09052 154 MGLTAEKVAEQWKVSREDQDAFALESHQKAIAAQQAGEFKDeITPYEIterfPDlatgevdvkTRTVDLDEGPRAdTSLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 289 QMAKLKPAFiKPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIyVSQDPKDQLLLGPTYATPKVLEKAG 368
Cdd:PRK09052 234 GLAKLKPVF-ANKGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFA-VAGVPPEIMGIGPIEAIPAALKQAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 369 LTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK09052 312 LKQDDLDWIELNEAFAAQSLAVIRDLGLD-----------------PSKVNPLGGAIALGHPLGATGAIRTATVVHGLRR 374
|
410 420
....*....|....*....|....
gi 1907162524 449 DGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK09052 375 TNLKYGMVTMCVGTGMGAAGIFER 398
|
|
| PRK08131 |
PRK08131 |
3-oxoadipyl-CoA thiolase; |
52-471 |
3.43e-64 |
|
3-oxoadipyl-CoA thiolase;
Pssm-ID: 181242 [Multi-domain] Cd Length: 401 Bit Score: 212.72 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKT 130
Cdd:PRK08131 1 MLDAYIYDGLRSPFGRHAGALASVRPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSrNVARNALLLAGLPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPI-------RHSRNMRkmMLDlnkaKTLGQRlsllskf 203
Cdd:PRK08131 81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRAPFvmgkaesAFSRDAK--VFD----TTIGAR------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 204 rlnFLSPELpaVAEFStNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVP--GKDT---VT 277
Cdd:PRK08131 148 ---FPNPKI--VAQYG-NDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADeITPIEVPqgRKLPpklVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 278 KDNGIRPSS-LEQMAKLKPAFIKpyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGP 356
Cdd:PRK08131 222 EDEHPRPSStVEALTKLKPLFEG--GVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPR-IMGIGP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 357 TYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWFAqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGC 436
Cdd:PRK08131 299 VEAIKKALARAGLTLDDMDIIEINEAFASQVLGCLKGLGVDFDD---------------PRVNPNGGAIAVGHPLGASGA 363
|
410 420 430
....*....|....*....|....*....|....*
gi 1907162524 437 RLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08131 364 RLALTAARELQRRGKRYAVVSLCIGVGQGLAMVIE 398
|
|
| PRK08242 |
PRK08242 |
acetyl-CoA C-acetyltransferase; |
77-471 |
3.81e-64 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 236197 [Multi-domain] Cd Length: 402 Bit Score: 212.82 E-value: 3.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQeV--KTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIA 154
Cdd:PRK08242 28 PVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTP-VgdQGADIARTAVLAAGLPETVPGVQINRFCASGLEAVNLAAAKVR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 155 SGQCDVVVAGGVELMSDVPIRHSRnmRKMMLDLNKAktlgqrlsllskFRLNFLsPElpavaefstnetmGHSADRLAAA 234
Cdd:PRK08242 107 SGWDDLVIAGGVESMSRVPMGSDG--GAWAMDPSTN------------FPTYFV-PQ-------------GISADLIATK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 235 FAVSRMEQDEYALRSHSLAKKAQDEGHLSDIVpfkVPGKD-----TVTKDNGIRP-SSLEQMAKLKPAF----------- 297
Cdd:PRK08242 159 YGFSREDVDAYAVESQQRAAAAWAEGYFAKSV---VPVKDqngltILDHDEHMRPgTTMESLAKLKPSFammgemggfda 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 298 --IKPYGTV-------TAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAG 368
Cdd:PRK08242 236 vaLQKYPEVerinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPT-IMLTGPVPATRKALAKAG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 369 LTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRK 448
Cdd:PRK08242 315 LTVDDIDLFELNEAFASVVLRFMQALDI-----------------PHDKVNVNGGAIAMGHPLGATGAMILGTVLDELER 377
|
410 420
....*....|....*....|...
gi 1907162524 449 DGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK08242 378 RGKRTALITLCVGGGMGIATIIE 400
|
|
| PRK06504 |
PRK06504 |
acetyl-CoA C-acetyltransferase; |
77-472 |
1.68e-63 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180595 [Multi-domain] Cd Length: 390 Bit Score: 210.74 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQE-VKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGLIAS 155
Cdd:PRK06504 26 PADLAAQVLDALVDRSGADPALIEDVIMGCVSQVgEQATNVARNAVLASKLPESVPGTSIDRQCGSSQQALHFAAQAVMS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 156 GQCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktLGQRLSLLSKFRL-NFLSPELPA---VAEFStnETMGhsADRL 231
Cdd:PRK06504 106 GTMDIVIAAGVESMTRVP-------------------MGSPSTLPAKNGLgHYKSPGMEErypGIQFS--QFTG--AEMM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 232 AAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPG----KDTVTKDNGIR-PSSLEQMAKLKPafIKPYGTVT 305
Cdd:PRK06504 163 AKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAeIVPLEITRadgsGEMHTVDEGIRfDATLEGIAGVKL--IAEGGRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 306 AANSSFLTDGASAMLIMSEdRAL-AMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFS 384
Cdd:PRK06504 241 AATASQICDGASGVMVVNE-RGLkALGVKPLARIHHMTVIGGDPV-IMLEAPLPATERALKKAGMKIDDIDLYEVNEAFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 385 GQILANFKAMDSDwfaqnymgrktkvgsPplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQ 464
Cdd:PRK06504 319 SVPLAWLKATGAD---------------P--ERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGKRYGLQTMCEGGGM 381
|
....*...
gi 1907162524 465 GHAMIVEA 472
Cdd:PRK06504 382 ANVTIVER 389
|
|
| PRK07108 |
PRK07108 |
acetyl-CoA C-acyltransferase; |
52-471 |
3.89e-61 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180843 [Multi-domain] Cd Length: 392 Bit Score: 204.62 E-value: 3.89e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFllsGTSYKDL--MPH--DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT-SNVAREAALGAGF 126
Cdd:PRK07108 1 MTEAVIVSTARTPL---AKSWRGAfnMTHgaTLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATgANIARQIALRAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 127 SDKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVpirhSRNMRKMMLD---LNKAKtlgqrlsllskf 203
Cdd:PRK07108 78 PVTVPGMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESISCV----QNEMNRHMLRegwLVEHK------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 204 rlnflsPELpavaefstNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPF--------KVPG-- 272
Cdd:PRK07108 142 ------PEI--------YWSMLQTAENVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDeIVPItvtagvadKATGrl 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 273 ---KDTVTKDNGIRP-SSLEQMAKLKPAFikPYGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDP 348
Cdd:PRK07108 208 ftkEVTVSADEGIRPdTTLEGVSKIRSAL--PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 349 kDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMgrKTKVGSPPlEKFNIWGGSLSLG 428
Cdd:PRK07108 286 -DEMGIGPVFAVPKLLKQAGLKVDDIDLWELNEAFAVQVL--------------YC--RDTLGIPM-DRLNVNGGAIAVG 347
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907162524 429 HPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK07108 348 HPYGVSGARLTGHALIEGKRRGAKYVVVTMCIGGGQGAAGLFE 390
|
|
| Thiolase_C |
pfam02803 |
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
332-472 |
5.19e-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: 5.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 332 YKPKAYLRDFIYVSQDPkDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvg 411
Cdd:pfam02803 1 LKPLARIRSYATAGVDP-AIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDP------------- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907162524 412 spplEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:pfam02803 67 ----EKVNVNGGAIALGHPLGASGARILVTLLHELKRRGGKYGLASLCIGGGQGVAMIIER 123
|
|
| PRK06366 |
PRK06366 |
acetyl-CoA C-acetyltransferase; |
52-471 |
5.23e-58 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 102340 [Multi-domain] Cd Length: 388 Bit Score: 196.38 E-value: 5.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06366 1 MKDVYIVSAKRTAIGKFGRSFSKIKAPQLGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQAAYHAGLPFGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR---KMMLDLNkaktlgqrlsllSKFRLNFL 208
Cdd:PRK06366 81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPFLLPSDLRwgpKHLLHKN------------YKIDDAML 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 209 SPELPAVAEFstnETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSL 287
Cdd:PRK06366 149 VDGLIDAFYF---EHMGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNeIVPF-----NDLDRDEGIRKTTM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 288 EQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDqLLLGPTYATPKVLEKA 367
Cdd:PRK06366 221 EDLAKLPPAFDKN-GILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLD-FVEAPIPATRKLLEKQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 368 GLTMNDIDAFEFHEAFS--GQILANFKAMDSdwfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK06366 299 NKSIDYYDLVEHNEAFSiaSIIVRDQLKIDN-------------------ERFNVNGGAVAIGHPIGNSGSRIIVTLINA 359
|
410 420
....*....|....*....|....*.
gi 1907162524 446 LRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06366 360 LKTRHMKTGLATLCHGGGGAHTLTLE 385
|
|
| PRK06633 |
PRK06633 |
acetyl-CoA C-acetyltransferase; |
52-472 |
5.23e-56 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168632 [Multi-domain] Cd Length: 392 Bit Score: 191.01 E-value: 5.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK06633 2 TKPVYITHAKRTAFGSFMGSLSTTPAPMLAAHLIKDILQNSKIDPALVNEVILGQVITGGSGQNPARQTLIHAGIPKEVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSdvPIRHSRNMRK-------MMLDLNkaktlgQRLSLLSKFR 204
Cdd:PRK06633 82 GYTINKVCGSGLKSVALAANSIMTGDNEIVIAGGQENMS--LGMHGSYIRAgakfgdiKMVDLM------QYDGLTDVFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 205 LNFlspelpavaefstnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKDTVT---KDN 280
Cdd:PRK06633 154 GVF----------------MGITAENISKQFNISRQEQDEFALSSHKKAAKAQLAGIFKDeILPIEVTIKKTTSlfdHDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 281 GIRP-SSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdqlLLG--PT 357
Cdd:PRK06633 218 TVRPdTSLEILSKLRPAFDKN-GVVTAGNASSINDGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPS---IMGtaPV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 358 YATPKVLEKAGLTMNDIDAFEFHEAFSGQILanfkamdsdwfaqnYMGRKTKVGsppLEKFNIWGGSLSLGHPFGATGCR 437
Cdd:PRK06633 294 PASQKALSKAGWSVNDLEVIEVNEAFAAQSI--------------YVNREMKWD---MEKVNINGGAIAIGHPIGASGGR 356
|
410 420 430
....*....|....*....|....*....|....*
gi 1907162524 438 LVMAAANRLRKDGGQYALVAACAAGGQGHAMIVEA 472
Cdd:PRK06633 357 VLITLIHGLRRAKAKKGLVTLCIGGGMGMAMCVEA 391
|
|
| PRK06954 |
PRK06954 |
acetyl-CoA C-acetyltransferase; |
55-473 |
1.12e-55 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 180775 [Multi-domain] Cd Length: 397 Bit Score: 190.49 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 55 IVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHT 134
Cdd:PRK06954 9 IVIASAARTPMAAFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVLPAGQGQAPARQAALGAGLPLSVGCTT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 135 VTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVP-----------IRHSRNMRKMMLD-LNKAKTLGQrlsllsk 202
Cdd:PRK06954 89 VNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPyllpkarggmrMGHGQVLDHMFLDgLEDAYDKGR------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 203 frlnflspelpavaefstneTMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVPGKD---TVTK 278
Cdd:PRK06954 162 --------------------LMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAwEIAPVTVAGKKgdtVIDR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 279 DNGIRPSSLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTY 358
Cdd:PRK06954 222 DEQPFKANPEKIPTLKPAFSKT-GTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPS-KFTTAPVG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 359 ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRL 438
Cdd:PRK06954 300 AIRKLFEKNGWRAAEVDLFEINEAFAVVTMAAMKEHGL-----------------PHEKVNVNGGACALGHPIGASGARI 362
|
410 420 430
....*....|....*....|....*....|....*
gi 1907162524 439 VMAAANRLRKDGGQYALVAACAAGGQGHAMIVEAY 473
Cdd:PRK06954 363 LVTLIGALRARGGKRGVASLCIGGGEATAMGIELI 397
|
|
| PRK05656 |
PRK05656 |
acetyl-CoA C-acetyltransferase; |
52-471 |
6.13e-53 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 168156 Cd Length: 393 Bit Score: 183.17 E-value: 6.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 52 MKNIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTP 131
Cdd:PRK05656 1 MQDVVIVAATRTAIGSFQGSLANIPAVELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQNPARQAAIKAGLPHSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 132 AHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldLNKAKTlGQRLSLLSKFRLNFLSPE 211
Cdd:PRK05656 81 AMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPYV-----------LPGART-GLRMGHAQLVDSMITDGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 212 LPAVAEFStnetMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD----TVTKDNGIRP-S 285
Cdd:PRK05656 149 WDAFNDYH----MGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDeITPILIPQRKgeplAFATDEQPRAgT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 286 SLEQMAKLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVLE 365
Cdd:PRK05656 225 TAESLAKLKPAFKKD-GSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPA-IMGIGPVSATRRCLD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 366 KAGLTMNDIDAFEFHEAFSGQILANFKAMDSDwfaqnymgrktkvgsppLEKFNIWGGSLSLGHPFGATGCRLVMAAANR 445
Cdd:PRK05656 303 KAGWSLAELDLIEANEAFAAQSLAVGKELGWD-----------------AAKVNVNGGAIALGHPIGASGCRVLVTLLHE 365
|
410 420
....*....|....*....|....*.
gi 1907162524 446 LRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK05656 366 MIRRDAKKGLATLCIGGGQGVALAIE 391
|
|
| PRK06025 |
PRK06025 |
acetyl-CoA C-acetyltransferase; |
74-471 |
5.21e-52 |
|
acetyl-CoA C-acetyltransferase;
Pssm-ID: 235675 [Multi-domain] Cd Length: 417 Bit Score: 181.13 E-value: 5.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 74 DLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTS-NVAREAALGAGFSDKTPAHTVTMACISSNQAMTTAVGL 152
Cdd:PRK06025 26 HLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGgDLGRMAALDAGYDIKASGVTLDRFCGGGITSVNLAAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 153 IASGQCDVVVAGGVELMSdvpirhsrnMRKMMLDLNKAKTLGQRLSLLSKFRLNFLSPElpavaefstnETMGHSADRLA 232
Cdd:PRK06025 106 IMSGMEDLVIAGGTEMMS---------YTAAMAAEDMAAGKPPLGMGSGNLRLRALHPQ----------SHQGVCGDAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 233 AAFAVSRMEQDEYALRSHSLAKKAQDEGHLS-DIVPFKVP-GKDTVTKDNGIRP-SSLEQMAKLKPAF-------IKPYG 302
Cdd:PRK06025 167 TMEGITREALDALGLESQRRAARAIKEGRFDkSLVPVYRDdGSVALDHEEFPRPqTTAEGLAALKPAFtaiadypLDDKG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 303 TVT------------------AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKdQLLLGPTYATPKVL 364
Cdd:PRK06025 247 TTYrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPT-LMLNAPVPAAKKVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 365 EKAGLTMNDIDAFEFHEAFSGQILANFKAMDSDWfaqnymgrktkvgspplEKFNIWGGSLSLGHPFGATGCRLVMAAAN 444
Cdd:PRK06025 326 AKAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDR-----------------DKVNVNGGAIALGHPIGATGSILIGTVLD 388
|
410 420
....*....|....*....|....*..
gi 1907162524 445 RLRKDGGQYALVAACAAGGQGHAMIVE 471
Cdd:PRK06025 389 ELERRGLKRGLVTMCAAGGMAPAIIIE 415
|
|
| PRK06690 |
PRK06690 |
acetyl-CoA C-acyltransferase; |
54-471 |
6.58e-51 |
|
acetyl-CoA C-acyltransferase;
Pssm-ID: 180659 [Multi-domain] Cd Length: 361 Bit Score: 176.88 E-value: 6.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 54 NIVVVEGVRIPFLLSGTSYKDLMPHDLARAALSGLlhRTNIPKDVvDYIIFGTVIQevKTSNVAREAALGAGFSDKTPAH 133
Cdd:PRK06690 2 RAVIVEAKRTPIGKKNGMLKDYEVQQLAAPLLTFL--SKGMEREI-DDVILGNVVG--PGGNVARLSALEAGLGLHIPGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 134 TVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRhsrnmrkmmldlNKAKtlgqrlsllskfrlnfLSPELP 213
Cdd:PRK06690 77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPFQ------------NRAR----------------FSPETI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 214 AvaefstNETMGHSADRLAAAFAVSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFkvpgkDTVTKDNGIRPSSLEQM-A 291
Cdd:PRK06690 129 G------DPDMGVAAEYVAERYNITREMQDEYACLSYKRTLQALEKGYIHEeILSF-----NGLLDESIKKEMNYERIiK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 292 KLKPAFIKPyGTVTAANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLlGPTYATPKVLEKAGLTM 371
Cdd:PRK06690 198 RTKPAFLHN-GTVTAGNSCGVNDGACAVLVMEEGQARKLGYKPVLRFVRSAVVGVDPNLPGT-GPIFAVNKLLNEMNMKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 372 NDIDAFEFHEAFSGQILANFKAMDSdwfaqnymgrktkvgspPLEKFNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG 451
Cdd:PRK06690 276 EDIDYFEINEAFASKVVACAKELQI-----------------PYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKREDM 338
|
410 420
....*....|....*....|
gi 1907162524 452 QYALVAACAAGGQGHAMIVE 471
Cdd:PRK06690 339 KYGIATLGIGGGIGLALLFE 358
|
|
| nondecarbox_cond_enzymes |
cd00826 |
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ... |
68-471 |
2.31e-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: 146.48 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 68 SGTSYKDLmPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHTVTMACISSNQAMT 147
Cdd:cd00826 15 NGADANDL-AHEAGAKAIAAALEPAGVAAGAVEEACLGQVLGAGEGQNCAQQAAMHAGGLQEAPAIGMNNLCGSGLRALA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 148 TAVGLIASGQCDVVVAGGVELMSdvpirhsrnmrkmMLDLNKAKTlGQRLSLLSKFRlnflspelpavaefstnetmghs 227
Cdd:cd00826 94 LAMQLIAGGDANCILAGGFEKME-------------TSAENNAKE-KHIDVLINKYG----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 228 adrlaaafavSRMEQDEYALRSHSLAKKAQDEGHLSD-IVPFKVPGKD---TVTKDNGIR---PSSLEQMAKLKPAFIKP 300
Cdd:cd00826 137 ----------MRACPDAFALAGQAGAEAAEKDGRFKDeFAKFGVKGRKgdiHSDADEYIQfgdEASLDEIAKLRPAFDKE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 301 yGTVTAANSSFLTDGASAMLIMSEDRA-------LAMGYKPKAYLRDFIYVSQDPKDQLLLG---PTYATPKVLEKAGLT 370
Cdd:cd00826 207 -DFLTAGNACGLNDGAAAAILMSEAEAqkhglqsKAREIQALEMITDMASTFEDKKVIKMVGgdgPIEAARKALEKAGLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 371 MNDIDAFEFHEAFSGQILANFKAMdsDWFAQNYMGRKTKVGSPPLEK---FNIWGGSLSLGHPFGATGCRLVMAAANRLR 447
Cdd:cd00826 286 IGDLDLIEAHDAFAANACATNEAL--GLCPEGQGGALVDRGDNTYGGksiINPNGGAIAIGHPIGASGAAICAELCFELK 363
|
410 420
....*....|....*....|....*....
gi 1907162524 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 |
3.10e-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: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 77 PHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00829 16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLGK-PATRVEAAGASGSAAVRAAAAAIASG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 157 QCDVVVAGGVELMSDVPirhsrnmrkmmldlnKAKTLGQRLSLLSKFRlnflsPELPAvaefstnetmGHSADRLAAAFA 236
Cdd:cd00829 95 LADVVLVVGAEKMSDVP---------------TGDEAGGRASDLEWEG-----PEPPG----------GLTPPALYALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 237 VSRMEQdeYALRSHSLAK---KAQDEGHLSDIVPFKVPgkDTVTKDNGIRPSSLeqmaklkpafikPYgtvTAANSSFLT 313
Cdd:cd00829 145 RRYMHR--YGTTREDLAKvavKNHRNAARNPYAQFRKP--ITVEDVLNSRMIAD------------PL---RLLDCCPVS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 314 DGASAMLIMSEDRALAMGYKPkAYLR------DFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSGQI 387
Cdd:cd00829 206 DGAAAVVLASEERARELTDRP-VWILgvgaasDTPSLSERDDFLSLDAARLAARRAYKMAGITPDDIDVAELYDCFTIAE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 388 LANFKAM------DSDWFAQNymGRKTKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYA-----LV 456
Cdd:cd00829 285 LLALEDLgfcekgEGGKLVRE--GDTAIGGDLPV---NTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAGARQvpgarVG 359
|
410
....*....|....
gi 1907162524 457 AACAAGGQGHAMIV 470
Cdd:cd00829 360 LAHNIGGTGSAAVV 373
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
79-449 |
8.07e-16 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 78.79 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 79 DLARAALSGLLHRTNIPKDVVDYIIFGTVI--QEVKTSNVAREAALGAGFSDKtPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK06064 24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSagLFVSQEHIAALIADYAGLAPI-PATRVEAACASGGAALRQAYLAVASG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 157 QCDVVVAGGVELMSDVPirhsrnmrkmmldlnkaktlgqrlsllskfrlnflSPElpavaefsTNETMGHSADRLAAAFA 236
Cdd:PRK06064 103 EADVVLAAGVEKMTDVP-----------------------------------TPD--------ATEAIARAGDYEWEEFF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 237 ----------VSRMEQDEYALRSHSLAK---KAQDEGHLSDIVPFKvpgkdtvtkdngiRPSSLEQMAKLKPAF--IKPY 301
Cdd:PRK06064 140 gatfpglyalIARRYMHKYGTTEEDLALvavKNHYNGSKNPYAQFQ-------------KEITVEQVLNSPPVAdpLKLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 302 gtvtaaNSSFLTDGASAMLIMSEDRAlamgykpKAYLRDFIYVS-----------QDPKDQLLLGPT-YATPKVLEKAGL 369
Cdd:PRK06064 207 ------DCSPITDGAAAVILASEEKA-------KEYTDTPVWIKasgqasdtialHDRKDFTTLDAAvVAAEKAYKMAGI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 370 TMNDIDAFEFHEAFSgqiLANFKAMDSDWFAQNYMGRK------TKVGSppleKF--NIWGGSLSLGHPFGATGCRLVMA 441
Cdd:PRK06064 274 EPKDIDVAEVHDCFT---IAEILAYEDLGFAKKGEGGKlaregqTYIGG----DIpvNPSGGLKAKGHPVGATGVSQAVE 346
|
....*...
gi 1907162524 442 AANRLRKD 449
Cdd:PRK06064 347 IVWQLRGE 354
|
|
| PRK12578 |
PRK12578 |
thiolase domain-containing protein; |
74-466 |
8.21e-11 |
|
thiolase domain-containing protein;
Pssm-ID: 183606 [Multi-domain] Cd Length: 385 Bit Score: 63.71 E-value: 8.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 74 DLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSDKTPAHtVTMACISSNQAMTTAVGLI 153
Cdd:PRK12578 18 DVSVQELAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEYSGLTGKVPLR-VEAMCATGLAASLTAYTAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 154 ASGQCDVVVAGGVELMSDVpirhsrnmrkmmlDLNKAKTLGQRL-SLLSKFrlNFLSPELPAVAEFStnetmghsADRLA 232
Cdd:PRK12578 97 ASGLVDMAIAVGVDKMTEV-------------DTSTSLAIGGRGgNYQWEY--HFYGTTFPTYYALY--------ATRHM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 233 AAFAVSRMEQDEYALRSHSLAKKaQDEGHLSdivpfkvpgkdtvtkdngiRPSSLEQMakLKPAFIK-PygtVTAANSSF 311
Cdd:PRK12578 154 AVYGTTEEQMALVSVKAHKYGAM-NPKAHFQ-------------------KPVTVEEV--LKSRAISwP---IKLLDSCP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 312 LTDGASAMLIMSEDRALAMGY------KPKAYLRDFIYVSQDPKDQLLLGPTYATPKVLEKAGLTMNDIDAFEFHEAFSg 385
Cdd:PRK12578 209 ISDGSATAIFASEEKVKELKIdspvwiTGIGYANDYAYVARRGEWVGFKATQLAARQAYNMAKVTPNDIEVATVHDAFT- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 386 qiLANFKAMDSDWFAQNYMGRK-------TKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGG--QYALV 456
Cdd:PRK12578 288 --IAEIMGYEDLGFTEKGKGGKfieegqsEKGGKVGV---NLFGGLKAKGHPLGATGLSMIYEITKQLRDEAGklQQPLK 362
|
410
....*....|....
gi 1907162524 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 |
4.50e-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: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 306 AANSSFLTDGASAMLIMSEDRALAMGYKPKAYLRDFIYVSQDPKDQLLL---GPTYATPKVLEKAGLTMNDIDAFEFHEA 382
Cdd:cd00327 94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASMVPAVsgeGLARAARKALEGAGLTPSDIDYVEAHGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 383 FSGQILANFKAMDSDWFAQNYMgrktkvgspplekfNIWGGSLSLGHPFGATG-------CRLVMAAANRLRKDGGQYAL 455
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRSP--------------AVSATLIMTGHPLGAAGlaildelLLMLEHEFIPPTPREPRTVL 239
|
170
....*....|....*
gi 1907162524 456 VAACAAGGQGHAMIV 470
Cdd:cd00327 240 LLGFGLGGTNAAVVL 254
|
|
| PRK07516 |
PRK07516 |
thiolase domain-containing protein; |
310-442 |
9.84e-08 |
|
thiolase domain-containing protein;
Pssm-ID: 181013 [Multi-domain] Cd Length: 389 Bit Score: 53.80 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 310 SFLTDGASAMLIMSEDRALAM----GYKPKAYLRDFIYVSQdpKDQLLL-GPTYATPKVLEKAGLTMNDIDAFEFHEAFS 384
Cdd:PRK07516 213 SLVSDGAAALVLADAETARALqravRFRARAHVNDFLPLSR--RDPLAFeGPRRAWQRALAQAGVTLDDLSFVETHDCFT 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907162524 385 GQILANFKAMDSDWFAQNYM----GRKTKVGSPPLekfNIWGGSLSLGHPFGATGCRL-VMAA 442
Cdd:PRK07516 291 IAELIEYEAMGLAPPGQGARaireGWTAKDGKLPV---NPSGGLKAKGHPIGATGVSMhVLAA 350
|
|
| PTZ00455 |
PTZ00455 |
3-ketoacyl-CoA thiolase; Provisional |
96-462 |
1.54e-07 |
|
3-ketoacyl-CoA thiolase; Provisional
Pssm-ID: 240424 [Multi-domain] Cd Length: 438 Bit Score: 53.36 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 96 KDVVDYIIFGTVIQEVKTS--NVAREAALGAGFSDKT------PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PTZ00455 69 AALVDKVVVGNFLGELFSSqgHLGPAAVGSLGQSGASnallykPAMRVEGACASGGLAVQSAWEALLAGTSDIALVVGVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 168 LMSDVPIRHSRNMRKMMLDLNKAKTLGqrlsllskfrlNFLSPELPAVAEFSTNETmGHSAdrlaaafavsrMEQDEYal 247
Cdd:PTZ00455 149 VQTTVSARVGGDYLARAADYRRQRKLD-----------DFTFPCLFAKRMKYIQEH-GHFT-----------MEDTAR-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 248 rshsLAKKAQDEGHLSDIVPFKVpGKDTVTKDNGIRPSSLEQMAKlkpAFIKPYGTVTaaNSSFLTDGASAMLIMSEDRA 327
Cdd:PTZ00455 204 ----VAAKAYANGNKNPLAHMHT-RKLSLEFCTGASDKNPKFLGN---ETYKPFLRMT--DCSQVSDGGAGLVLASEEGL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 328 LAMGYKP--------KAYLRDFIYVSQDPKDQLLLGPTY-ATPKVLEKAGLTMNDIDAFEFHEAFSGQILANFKAMD-SD 397
Cdd:PTZ00455 274 QKMGLSPndsrlveiKSLACASGNLYEDPPDATRMFTSRaAAQKALSMAGVKPSDLQVAEVHDCFTIAELLMYEALGiAE 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907162524 398 WFAQNYMGRK---TKVGSPPLekfNIWGGSLSLGHPFGATGCRLVMAAANRLRKDGGQYALVAACAAG 462
Cdd:PTZ00455 354 YGHAKDLIRNgatALEGRIPV---NTGGGLLSFGHPVGATGVKQIMEVYRQMKGQCGEYQMKNIPALG 418
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
113-167 |
1.91e-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: 52.93 E-value: 1.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907162524 113 TSNVAREAALGAGFsdKTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:cd00834 137 PNMAAGQVAIRLGL--RGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAE 189
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
131-167 |
2.26e-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: 2.26e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1907162524 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 1907162524 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 |
9.27e-07 |
|
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: 50.14 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 78 HDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVAREAALGAGFSdKTPAHTVTMACISSNQAMTTAVGLIASGQ 157
Cdd:cd00327 8 SELGFEAAEQAIADAGLSKGPIVGVIVGTTGGSGEFSGAAGQLAYHLGIS-GGPAYSVNQACATGLTALALAVQQVQNGK 86
|
90
....*....|.
gi 1907162524 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 |
1.02e-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: 50.49 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 73 KDLMPHDLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKT----SNVAREaaLGAgfsDKTPAHTVTMACISSNQAMTT 148
Cdd:COG0332 47 PDETTSDLAVEAARKALEAAGIDPEDIDLIIVATVTPDYLFpstaCLVQHK--LGA---KNAAAFDINAACSGFVYALSV 121
|
90 100
....*....|....*....|....*
gi 1907162524 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 |
6.11e-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: 6.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSDVPIRHSRNMR 181
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLSGFANMG 204
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
131-166 |
2.20e-04 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 43.29 E-value: 2.20e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGV 166
Cdd:PRK09185 152 PAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGV 187
|
|
| KAS_III |
cd00830 |
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ... |
79-172 |
8.07e-04 |
|
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: 41.37 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 79 DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAGfsdKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:cd00830 52 DLAVEAAKKALEDAGIDADDIDLIIVATSTPDYLFPATACLvqARLGAK---NAAAFDINAACSGFLYGLSTAAGLIRSG 128
|
90
....*....|....*.
gi 1907162524 157 QCDVVVAGGVELMSDV 172
Cdd:cd00830 129 GAKNVLVVGAETLSRI 144
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
131-171 |
9.98e-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: 9.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907162524 131 PAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVELMSD 171
Cdd:cd00833 162 PSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILS 202
|
|
| PRK12879 |
PRK12879 |
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed |
79-172 |
2.86e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
Pssm-ID: 237245 [Multi-domain] Cd Length: 325 Bit Score: 39.85 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907162524 79 DLARAALSGLLHRTNIPKDVVDYIIFGTVIQEVKTSNVARE--AALGAgfsDKTPAHTVTMACISSNQAMTTAVGLIASG 156
Cdd:PRK12879 55 DLAIKAAERALARAGLDAEDIDLIIVATTTPDYLFPSTASQvqARLGI---PNAAAFDINAACAGFLYGLETANGLITSG 131
|
90
....*....|....*.
gi 1907162524 157 QCDVVVAGGVELMSDV 172
Cdd:PRK12879 132 LYKKVLVIGAERLSKV 147
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
129-167 |
4.54e-03 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 39.39 E-value: 4.54e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907162524 129 KTPAHTVTMACISSNQAMTTAVGLIASGQCDVVVAGGVE 167
Cdd:PRK07314 152 KGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAE 190
|
|
| |
