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Conserved domains on  [gi|30695564|ref|NP_568704|]
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peroxisomal 3-keto-acyl-CoA thiolase 2 [Arabidopsis thaliana]

Protein Classification

3-ketoacyl-CoA thiolase( domain architecture ID 11476600)

3-ketoacyl-CoA thiolase is responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs)

CATH:  3.40.47.10
EC:  2.3.1.-
Gene Ontology:  GO:0006635|GO:0016746

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-457 0e+00

3-ketoacyl-CoA thiolase


:

Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 851.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    1 MERAMERQKILLRHLNPVSSsnsslkhEPSLLSPVNCVSEVSP----MAAFGDDIVIVAAYRTAICKARRGGFKDTLPDD 76
Cdd:PLN02287   1 MEKAINRQRVLLRHLRPSSS-------EPSSLSASACAAGDSAayhrTTAFGDDVVIVAAYRTPICKAKRGGFKDTYPDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   77 LLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYY 156
Cdd:PLN02287  74 LLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  157 DIGIGAGVESMSTDHIPGGGfhGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLK 236
Cdd:PLN02287 154 DIGIGAGVESMTTNPMAWEG--GVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  237 DEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLP 316
Cdd:PLN02287 232 DEIVPVHTKIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  317 ILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPL 396
Cdd:PLN02287 312 ILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPL 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695564  397 GATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH 457
Cdd:PLN02287 392 GATGARCVATLLHEMKRRGKDCRFGVVSMCIGTGMGAAAVFERGDSVDELSNARKVEGNNL 452
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-457 0e+00

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 851.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    1 MERAMERQKILLRHLNPVSSsnsslkhEPSLLSPVNCVSEVSP----MAAFGDDIVIVAAYRTAICKARRGGFKDTLPDD 76
Cdd:PLN02287   1 MEKAINRQRVLLRHLRPSSS-------EPSSLSASACAAGDSAayhrTTAFGDDVVIVAAYRTPICKAKRGGFKDTYPDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   77 LLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYY 156
Cdd:PLN02287  74 LLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  157 DIGIGAGVESMSTDHIPGGGfhGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLK 236
Cdd:PLN02287 154 DIGIGAGVESMTTNPMAWEG--GVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  237 DEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLP 316
Cdd:PLN02287 232 DEIVPVHTKIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  317 ILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPL 396
Cdd:PLN02287 312 ILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPL 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695564  397 GATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH 457
Cdd:PLN02287 392 GATGARCVATLLHEMKRRGKDCRFGVVSMCIGTGMGAAAVFERGDSVDELSNARKVEGNNL 452
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
52-439 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 528.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  52 VIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMeCRVAAYFAGFPDSVPVR 131
Cdd:cd00751   1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNP-ARQAALLAGLPESVPAT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHI--------PGGGFHGSNPRAQDFPKARDCLLPMGITSEN 203
Cdd:cd00751  79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYllpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAEN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 204 VAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQ 283
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVP------GRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 284 NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINE 363
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695564 364 AFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:cd00751 313 AFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGG--RYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
49-439 1.35e-173

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: 491.89  E-value: 1.35e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  49 DDIVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMeCRVAAYFAGFPDSV 128
Cdd:COG0183   2 REVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNP-ARQAALLAGLPESV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGGFHGS-----NPRAQDfPKARDCL------LPM 197
Cdd:COG0183  80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMS--RAPMLLPKARwgyrmNAKLVD-PMINPGLtdpytgLSM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 198 GITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKL 277
Cdd:COG0183 157 GETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVP------DRKGEVVVDRDEGPRPDTTLEKLAKL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 278 KTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDID 357
Cdd:COG0183 231 KPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDID 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 358 LFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVF 437
Cdd:COG0183 311 LIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGG--RYGLATMCIGGGQGIALII 388

                ..
gi 30695564 438 ER 439
Cdd:COG0183 389 ER 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
53-438 3.30e-171

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: 485.96  E-value: 3.30e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    53 IVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQrAMECRVAAYFAGFPDSVPVRT 132
Cdd:TIGR01930   1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   133 VNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMST------DHIPGGGFHGSNPRAQDFPKAR---DCLLPMGITSEN 203
Cdd:TIGR01930  79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRvpygvpRSLRWGVKPGNAELEDARLKDLtdaNTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   204 VAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQ 283
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVK------GRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   284 NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINE 363
Cdd:TIGR01930 233 DGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695564   364 AFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFE 438
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG--RYGLATMCIGGGQGAAVILE 385
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
51-308 3.97e-81

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: 251.45  E-value: 3.97e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    51 IVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMEcRVAAYFAGFPDSVPV 130
Cdd:pfam00108   1 VVIVSAARTPFGSFG-GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPA-RQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   131 RTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGgfHGSNPRA---QDFPKARDCLLP----------- 196
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMS--HAPYA--LPTDARSglkHGDEKKHDLLIPdgltdafngyh 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   197 MGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETkaekaiVVSVDDGVRPNSNMADLAK 276
Cdd:pfam00108 155 MGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP------TVDKDEGIRPPTTAEPLAK 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 30695564   277 LKTVFKQNGSTTAGNASQISDGAGAVLLMKRS 308
Cdd:pfam00108 229 LKPAFDKEGTVTAGNASPINDGAAAVLLMSES 260
 
Name Accession Description Interval E-value
PLN02287 PLN02287
3-ketoacyl-CoA thiolase
1-457 0e+00

3-ketoacyl-CoA thiolase


Pssm-ID: 215161 [Multi-domain]  Cd Length: 452  Bit Score: 851.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    1 MERAMERQKILLRHLNPVSSsnsslkhEPSLLSPVNCVSEVSP----MAAFGDDIVIVAAYRTAICKARRGGFKDTLPDD 76
Cdd:PLN02287   1 MEKAINRQRVLLRHLRPSSS-------EPSSLSASACAAGDSAayhrTTAFGDDVVIVAAYRTPICKAKRGGFKDTYPDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   77 LLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYY 156
Cdd:PLN02287  74 LLAPVLKAVVEKTGLNPSEVGDIVVGTVLAPGSQRANECRMAAFYAGFPETVPVRTVNRQCSSGLQAVADVAAAIKAGFY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  157 DIGIGAGVESMSTDHIPGGGfhGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLK 236
Cdd:PLN02287 154 DIGIGAGVESMTTNPMAWEG--GVNPRVESFSQAQDCLLPMGITSENVAERFGVTREEQDQAAVESHRKAAAATASGKFK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  237 DEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLP 316
Cdd:PLN02287 232 DEIVPVHTKIVDPKTGEEKPIVISVDDGIRPNTTLADLAKLKPVFKKNGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  317 ILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPL 396
Cdd:PLN02287 312 ILGVFRSFAAVGVDPAVMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCCKKLGLDPEKVNVNGGAIALGHPL 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695564  397 GATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH 457
Cdd:PLN02287 392 GATGARCVATLLHEMKRRGKDCRFGVVSMCIGTGMGAAAVFERGDSVDELSNARKVEGNNL 452
thiolase cd00751
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ...
52-439 0e+00

Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.


Pssm-ID: 238383 [Multi-domain]  Cd Length: 386  Bit Score: 528.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  52 VIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMeCRVAAYFAGFPDSVPVR 131
Cdd:cd00751   1 VIVSAVRTPIGRFG-GALKDVSADDLGAAVIKALLERAGLDPEEVDDVIMGNVLQAGEGQNP-ARQAALLAGLPESVPAT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHI--------PGGGFHGSNPRAQDFPKARDCLLPMGITSEN 203
Cdd:cd00751  79 TVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESMSRAPYllpkarrgGRLGLNTLDGMLDDGLTDPFTGLSMGITAEN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 204 VAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQ 283
Cdd:cd00751 159 VAEKYGISREEQDEFALRSHQRAAAAQEAGRFKDEIVPVEVP------GRKGPVVVDRDEGPRPDTTLEKLAKLKPAFKK 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 284 NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINE 363
Cdd:cd00751 233 DGTVTAGNASGINDGAAAVLLMSEEKAKELGLKPLARIVGYAVAGVDPAIMGIGPVPAIPKALKRAGLTLDDIDLIEINE 312
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695564 364 AFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:cd00751 313 AFAAQALACLKELGLDPEKVNVNGGAIALGHPLGASGARIVVTLLHELKRRGG--RYGLATMCIGGGQGAAMVIER 386
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
49-439 1.35e-173

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: 491.89  E-value: 1.35e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  49 DDIVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMeCRVAAYFAGFPDSV 128
Cdd:COG0183   2 REVVIVDAVRTPFGRFG-GALADVRADDLGAAVIKALLERAGLDPEAVDDVILGCVLQAGQGQNP-ARQAALLAGLPESV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGGFHGS-----NPRAQDfPKARDCL------LPM 197
Cdd:COG0183  80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMS--RAPMLLPKARwgyrmNAKLVD-PMINPGLtdpytgLSM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 198 GITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKL 277
Cdd:COG0183 157 GETAENVAERYGISREEQDAFALRSHQRAAAAIAAGRFDDEIVPVEVP------DRKGEVVVDRDEGPRPDTTLEKLAKL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 278 KTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDID 357
Cdd:COG0183 231 KPAFKKDGTVTAGNASGINDGAAALLLMSEEAAKELGLKPLARIVAYAVAGVDPEIMGIGPVPATRKALARAGLTLDDID 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 358 LFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVF 437
Cdd:COG0183 311 LIEINEAFAAQVLAVLRELGLDPDKVNVNGGAIALGHPLGASGARILVTLLHELERRGG--RYGLATMCIGGGQGIALII 388

                ..
gi 30695564 438 ER 439
Cdd:COG0183 389 ER 390
AcCoA-C-Actrans TIGR01930
acetyl-CoA acetyltransferases; This model represents a large family of enzymes which catalyze ...
53-438 3.30e-171

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: 485.96  E-value: 3.30e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    53 IVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQrAMECRVAAYFAGFPDSVPVRT 132
Cdd:TIGR01930   1 IVAAARTPIGKFG-GSLKDVSAEDLGAAVIKELLERNPLDPELIDDVIFGNVLQAGEQ-QNIARQAALLAGLPESVPAYT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   133 VNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMST------DHIPGGGFHGSNPRAQDFPKAR---DCLLPMGITSEN 203
Cdd:TIGR01930  79 VNRQCASGLQAVILAAQLIRAGEADVVVAGGVESMSRvpygvpRSLRWGVKPGNAELEDARLKDLtdaNTGLPMGVTAEN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   204 VAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQ 283
Cdd:TIGR01930 159 LAKKYGISREEQDEYALRSHQRAAKAWEEGLFKDEIVPVTVK------GRKGPVTVSSDEGIRPNTTLEKLAKLKPAFDP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   284 NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINE 363
Cdd:TIGR01930 233 DGTVTAGNSSPLNDGAAALLLMSEEKAKELGLTPLARIVSFAVAGVDPEIMGLGPVPAIPKALKKAGLSISDIDLFEINE 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695564   364 AFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFE 438
Cdd:TIGR01930 313 AFAAQVLACIKELGLDLEKVNVNGGAIALGHPLGASGARIVTTLLHELKRRGG--RYGLATMCIGGGQGAAVILE 385
PRK05790 PRK05790
putative acyltransferase; Provisional
49-439 3.05e-146

putative acyltransferase; Provisional


Pssm-ID: 180261 [Multi-domain]  Cd Length: 393  Bit Score: 422.64  E-value: 3.05e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   49 DDIVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRaMECRVAAYFAGFPDSV 128
Cdd:PRK05790   2 KDVVIVSAARTPIGKFG-GALKDVSAVELGAIVIKAALERAGVPPEQVDEVIMGQVLQAGAGQ-NPARQAALKAGLPVEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMST-DHI---PGGGFHGSNPRAQDfPKARDCL------LPMG 198
Cdd:PRK05790  80 PALTINKVCGSGLKAVALAAQAIRAGDADIVVAGGQESMSQaPHVlpgSRWGQKMGDVELVD-TMIHDGLtdafngYHMG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  199 ITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpeTKAEKAIVVSVDDGVRPNSNMADLAKLK 278
Cdd:PRK05790 159 ITAENLAEQYGITREEQDEFALASQQKAEAAIKAGRFKDEIVPVTIK-----QRKGDPVVVDTDEHPRPDTTAESLAKLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  279 TVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDL 358
Cdd:PRK05790 234 PAFDKDGTVTAGNASGINDGAAAVVVMSEAKAKELGLTPLARIVSYAVAGVDPAIMGIGPVPAIRKALEKAGWSLADLDL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  359 FEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFE 438
Cdd:PRK05790 314 IEINEAFAAQALAVEKELGLDPEKVNVNGGAIALGHPIGASGARILVTLLHEMKRRGA--KKGLATLCIGGGQGVALIVE 391

                 .
gi 30695564  439 R 439
Cdd:PRK05790 392 R 392
PRK09052 PRK09052
acetyl-CoA C-acyltransferase;
50-439 1.02e-145

acetyl-CoA C-acyltransferase;


Pssm-ID: 181626 [Multi-domain]  Cd Length: 399  Bit Score: 421.72  E-value: 1.02e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERT-SLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSV 128
Cdd:PRK09052   7 DAYIVAATRTPVGKAPRGMFKNTRPDDLLAHVLRSAVAQVpGLDPKLIEDAIVGCAMPEAEQGLNVARIGALLAGLPNSV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTdhIPGGGFHGS-NPRAQDFPKARDCLLPMGITSENVAER 207
Cdd:PRK09052  87 GGVTVNRFCASGLQAVAMAADRIRVGEADVMIAAGVESMSM--VPMMGNKPSmSPAIFARDENVGIAYGMGLTAEKVAEQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  208 FGVTREEQDMAAVESHKRAAAAIASGKLKDEIIP--VATKIVDPETKA--EKAIVVSVDDGVRPNSNMADLAKLKTVFKQ 283
Cdd:PRK09052 165 WKVSREDQDAFALESHQKAIAAQQAGEFKDEITPyeITERFPDLATGEvdVKTRTVDLDEGPRADTSLEGLAKLKPVFAN 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  284 NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINE 363
Cdd:PRK09052 245 KGSVTAGNSSQTSDGAGAVILVSEKALKQFNLTPLARFVSFAVAGVPPEIMGIGPIEAIPAALKQAGLKQDDLDWIELNE 324
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695564  364 AFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:PRK09052 325 AFAAQSLAVIRDLGLDPSKVNPLGGAIALGHPLGATGAIRTATVVHGLRRTNL--KYGMVTMCVGTGMGAAGIFER 398
PRK07661 PRK07661
acetyl-CoA C-acetyltransferase;
52-439 6.32e-145

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181072 [Multi-domain]  Cd Length: 391  Bit Score: 419.16  E-value: 6.32e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   52 VIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVR 131
Cdd:PRK07661   5 VIVAGARTPVGKAKKGSLKTVRPDDLGALVVKETLKRAGNYEGPIDDLIIGCAMPEAEQGLNMARNIGALAGLPYTVPAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTdhIPGGGfHGSNPRAQDFPKARDCLLPMGITSENVAERFGVT 211
Cdd:PRK07661  85 TINRYCSSGLQSIAYGAERIMLGHSEAVIAGGAESMSL--VPMMG-HVVRPNPRLVEAAPEYYMGMGHTAEQVAVKYGIS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  212 REEQDMAAVESHKRAAAAIASGKLKDEIIP--VATKIVDPETK-AEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTT 288
Cdd:PRK07661 162 REDQDAFAVRSHQRAAKALAEGKFADEIVPvdVTLRTVGENNKlQEETITFSQDEGVRADTTLEILGKLRPAFNVKGSVT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  289 AGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQ 368
Cdd:PRK07661 242 AGNSSQMSDGAAAVLLMDREKAESDGLKPLAKFRSFAVAGVPPEVMGIGPIAAIPKALKLAGLELSDIGLFELNEAFASQ 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695564  369 YVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:PRK07661 322 SIQVIRELGLDEEKVNVNGGAIALGHPLGCTGAKLTLSLIHEMKRRNE--QFGIVTMCIGGGMGAAGVFEL 390
PRK09051 PRK09051
beta-ketothiolase BktB;
50-439 3.97e-123

beta-ketothiolase BktB;


Pssm-ID: 181625 [Multi-domain]  Cd Length: 394  Bit Score: 363.90  E-value: 3.97e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckarrGGF----KDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFP 125
Cdd:PRK09051   4 EVVVVSGVRTAI-----GTFggslKDVAPTDLGATVVREALARAGVDPDQVGHVVFGHVIPTEPRDMYLSRVAAINAGVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  126 DSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMS-TDHIPGGGFHGSnpRAQDFpKARDCLL--------- 195
Cdd:PRK09051  79 QETPAFNVNRLCGSGLQAIVSAAQAILLGDADVAIGGGAESMSrAPYLLPAARWGA--RMGDA-KLVDMMVgalhdpfgt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  196 -PMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVatkivdpETKAEKAIVV-SVDDGVRPNSNMAD 273
Cdd:PRK09051 156 iHMGVTAENVAAKYGISREAQDALALESHRRAAAAIAAGYFKDQIVPV-------EIKTRKGEVVfDTDEHVRADTTLED 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  274 LAKLKTVFKQ-NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLN 352
Cdd:PRK09051 229 LAKLKPVFKKeNGTVTAGNASGINDGAAAVVLAEADAAEARGLKPLARLVGYAHAGVDPEYMGIGPVPATQKALERAGLT 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  353 VSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMG 432
Cdd:PRK09051 309 VADLDVIEANEAFAAQACAVTRELGLDPAKVNPNGSGISLGHPVGATGAIITVKALYELQRIGG--RYALVTMCIGGGQG 386

                 ....*..
gi 30695564  433 AAAVFER 439
Cdd:PRK09051 387 IAAIFER 393
PRK06205 PRK06205
acetyl-CoA C-acetyltransferase;
50-439 4.46e-112

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235741 [Multi-domain]  Cd Length: 404  Bit Score: 335.80  E-value: 4.46e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckARRGG-FKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMEcRVAAYFAGFPDSV 128
Cdd:PRK06205   3 DAVICEPVRTPV--GRFGGaFKDVPAEELAATVIRALVERTGIDPARIDDVIFGQGYPNGEAPAIG-RVAALDAGLPVTV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMS------TDH---IPGGG--FHGSNPRAQDFPKARDCLLPM 197
Cdd:PRK06205  80 PGMQLDRRCGSGLQAVITAAMQVQTGAADVVIAGGAESMSnvefytTDMrwgVRGGGvqLHDRLARGRETAGGRRFPVPG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  198 GI--TSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdPETKAEkAIVVSVDDGVRPNSNMADLA 275
Cdd:PRK06205 160 GMieTAENLRREYGISREEQDALAVRSHQRAVAAQEAGRFDDEIVPVTV----PQRKGD-PTVVDRDEHPRADTTLESLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  276 KLKTVFKQ---NGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLN 352
Cdd:PRK06205 235 KLRPIMGKqdpEATVTAGNASGQNDAAAACLVTTEDKAEELGLRPLARLVSWAVAGVEPSRMGIGPVPATEKALARAGLT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  353 VSDIDLFEINEAFASQyVYSCKK----LELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRgkDCRFGVISMCIG 428
Cdd:PRK06205 315 LDDIDLIELNEAFAAQ-VLAVLKewgfGADDEERLNVNGSGISLGHPVGATGGRILATLLRELQRR--QARYGLETMCIG 391
                        410
                 ....*....|.
gi 30695564  429 TGMGAAAVFER 439
Cdd:PRK06205 392 GGQGLAAVFER 402
PRK07108 PRK07108
acetyl-CoA C-acyltransferase;
50-438 1.30e-111

acetyl-CoA C-acyltransferase;


Pssm-ID: 180843 [Multi-domain]  Cd Length: 392  Bit Score: 334.43  E-value: 1.30e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVP 129
Cdd:PRK07108   3 EAVIVSTARTPLAKSWRGAFNMTHGATLGGHVVQHAVERAKLDPAEVEDVIMGCANPEGATGANIARQIALRAGLPVTVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  130 VRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVES-------MSTDHIPGGGFHGSNPraqdfpkarDCLLPMGITSE 202
Cdd:PRK07108  83 GMTVNRFCSSGLQTIALAAQRVIAGEGDVFVAGGVESiscvqneMNRHMLREGWLVEHKP---------EIYWSMLQTAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  203 NVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIP--VATKIVDPETKA--EKAIVVSVDDGVRPNSNMADLAKLK 278
Cdd:PRK07108 154 NVAKRYGISKERQDEYGVQSQQRAAAAQAAGRFDDEIVPitVTAGVADKATGRlfTKEVTVSADEGIRPDTTLEGVSKIR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  279 TVFkQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDL 358
Cdd:PRK07108 234 SAL-PGGVITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLLKQAGLKVDDIDL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  359 FEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGkdCRFGVISMCIGTGMGAAAVFE 438
Cdd:PRK07108 313 WELNEAFAVQVLYCRDTLGIPMDRLNVNGGAIAVGHPYGVSGARLTGHALIEGKRRG--AKYVVVTMCIGGGQGAAGLFE 390
PRK06445 PRK06445
acetyl-CoA C-acetyltransferase;
49-439 9.45e-111

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180563 [Multi-domain]  Cd Length: 394  Bit Score: 332.07  E-value: 9.45e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   49 DDIVIVAAYRTAICKAR-----RGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAG 123
Cdd:PRK06445   2 EDVYLVDFARTAFSRFRpkdpqKDVFNNIRPEELAAMLINRLIEKTGIKPEEIDDIITGCALQVGENWLYGGRHPIFLAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  124 FPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGG--FHGSNPRAQDFPKARDCLLP----M 197
Cdd:PRK06445  82 LPYNIPAMAVDRQCASSLTTVSIGAMEIATGMADIVIAGGVEHMT--RTPMGDnpHIEPNPKLLTDPKYIEYDLTtgyvM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  198 GITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdpETKAEKaIVVSVDDGVRPNSNMADLAKL 277
Cdd:PRK06445 160 GLTAEKLAEEAGIKREEMDRWSLRSHQLAAKAIQEGYFKDEILPIEV-----EVEGKK-KVVDVDQSVRPDTSLEKLAKL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  278 KTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDID 357
Cdd:PRK06445 234 PPAFKPDGVITAGNSSPLNSGASYVLLMSKKAVKKYGLKPMAKIRSFGFAGVPPAIMGKGPVPASKKALEKAGLSVKDID 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  358 LFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDcrFGVISMCIGTGMGAAAVF 437
Cdd:PRK06445 314 LWEINEAFAVVVLYAIKELGLDPETVNIKGGAIAIGHPLGATGARIVGTLARQLQIKGKD--YGVATLCVGGGQGGAVVL 391

                 ..
gi 30695564  438 ER 439
Cdd:PRK06445 392 ER 393
fadA PRK08947
3-ketoacyl-CoA thiolase; Reviewed
50-439 4.00e-108

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181592 [Multi-domain]  Cd Length: 387  Bit Score: 325.38  E-value: 4.00e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERT-SLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSV 128
Cdd:PRK08947   3 DVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNpALDPAEIDDIIWGCVQQTLEQGFNIARNAALLAGIPHSV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIP---GGGFHGSNprAQDFPKARDCllpMGITSENVA 205
Cdd:PRK08947  83 PAVTVNRLCGSSMQALHDAARAIMTGDGDVFLIGGVEHMG--HVPmnhGVDFHPGL--SKNVAKAAGM---MGLTAEMLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  206 ERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKaekaiVVSVDDGVRPNSNMADLAKLKTVFK-QN 284
Cdd:PRK08947 156 KMHGISREQQDAFAARSHQRAWAATQEGRFKNEIIPTEGHDADGVLK-----LFDYDEVIRPETTVEALAALRPAFDpVN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  285 GSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEA 364
Cdd:PRK08947 231 GTVTAGTSSALSDGASAMLVMSESRAKELGLKPRARIRSMAVAGCDPSIMGYGPVPATQKALKRAGLSISDIDVFELNEA 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695564  365 FASQYVYSCKKLEL-DM--EKVNVNGGAIAIGHPLGATGARCVATLLHEMKRrgKDCRFGVISMCIGTGMGAAAVFER 439
Cdd:PRK08947 311 FAAQSLPCLKDLGLlDKmdEKVNLNGGAIALGHPLGCSGARISTTLLNLMER--KDAQFGLATMCIGLGQGIATVFER 386
PRK07851 PRK07851
acetyl-CoA C-acetyltransferase;
52-439 1.11e-104

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181146 [Multi-domain]  Cd Length: 406  Bit Score: 316.94  E-value: 1.11e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   52 VIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERT-SLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFpDSVPV 130
Cdd:PRK07851   5 VIVSTARSPIGRAFKGSLKDMRPDDLAAQMVRAALDKVpALDPTDIDDLMLGCGLPGGEQGFNMARVVAVLLGY-DFLPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  131 RTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMS------TDHIP-------------------GGGFHGSNPRAQ 185
Cdd:PRK07851  84 TTVNRYCSSSLQTTRMAFHAIKAGEGDVFISAGVETVSrfakgnSDSLPdtknplfaeaqartaaraeGGAEAWHDPRED 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  186 DfpKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpetkaeKAIVVSVDDGV 265
Cdd:PRK07851 164 G--LLPDVYIAMGQTAENVAQLTGISREEQDEWGVRSQNRAEEAIANGFFEREITPVTLP---------DGTVVSTDDGP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  266 RPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAA 345
Cdd:PRK07851 233 RAGTTYEKVSQLKPVFRPDGTVTAGNACPLNDGAAAVVIMSDTKARELGLTPLARIVSTGVSGLSPEIMGLGPVEASKQA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  346 TKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISM 425
Cdd:PRK07851 313 LARAGMSIDDIDLVEINEAFAAQVLPSARELGIDEDKLNVSGGAIALGHPFGMTGARITTTLLNNLQTHDK--TFGLETM 390
                        410
                 ....*....|....
gi 30695564  426 CIGTGMGAAAVFER 439
Cdd:PRK07851 391 CVGGGQGMAMVLER 404
PRK09050 PRK09050
beta-ketoadipyl CoA thiolase; Validated
50-439 6.36e-100

beta-ketoadipyl CoA thiolase; Validated


Pssm-ID: 181624 [Multi-domain]  Cd Length: 401  Bit Score: 304.57  E-value: 6.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckARRGG-FKDTLPDDLLASVLKAVVERT-SLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDS 127
Cdd:PRK09050   3 EAFICDAIRTPI--GRYGGaLSSVRADDLGAVPLKALMARNpGVDWEAVDDVIYGCANQAGEDNRNVARMSALLAGLPVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  128 VPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMST-------------------DHIPGGGFhgSNPRAqdfp 188
Cdd:PRK09050  81 VPGTTINRLCGSGMDAVGTAARAIKAGEAELMIAGGVESMSRapfvmgkadsafsrqaeifDTTIGWRF--VNPLM---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  189 KARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdPETKAEkAIVVSVDDGVRPN 268
Cdd:PRK09050 155 KAQYGVDSMPETAENVAEDYNISRADQDAFALRSQQRAAAAQAAGFLAEEIVPVTI----PQKKGD-PVVVDRDEHPRPE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  269 SNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLP----ILGvfrsFAVTGVEPSVMGIGPAVAIPA 344
Cdd:PRK09050 230 TTLEALAKLKPVFRPDGTVTAGNASGVNDGAAALLLASEAAAKKHGLTprarILG----MATAGVEPRIMGIGPAPATRK 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  345 ATKLAGLNVSDIDLFEINEAFASQYVYSCKKLEL--DMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGV 422
Cdd:PRK09050 306 LLARLGLTIDQFDVIELNEAFAAQGLAVLRQLGLadDDARVNPNGGAIALGHPLGMSGARLVLTALHQLERTGG--RYAL 383
                        410
                 ....*....|....*..
gi 30695564  423 ISMCIGTGMGAAAVFER 439
Cdd:PRK09050 384 CTMCIGVGQGIALAIER 400
PRK05656 PRK05656
acetyl-CoA C-acetyltransferase;
50-440 2.04e-96

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168156  Cd Length: 393  Bit Score: 295.64  E-value: 2.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckarrGGFKDTLPD----DLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAmECRVAAYFAGFP 125
Cdd:PRK05656   3 DVVIVAATRTAI-----GSFQGSLANipavELGAAVIRRLLEQTGLDPAQVDEVILGQVLTAGAGQN-PARQAAIKAGLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  126 DSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDH--IPGG--GFHGSNPRAQDfPKARDCLLP----- 196
Cdd:PRK05656  77 HSVPAMTLNKVCGSGLKALHLAAQAIRCGDAEVIIAGGQENMSLAPyvLPGArtGLRMGHAQLVD-SMITDGLWDafndy 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  197 -MGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPvatkIVDPETKAEkAIVVSVDDGVRPNSNMADLA 275
Cdd:PRK05656 156 hMGITAENLVEKYGISREAQDAFAAASQQKAVAAIEAGRFDDEITP----ILIPQRKGE-PLAFATDEQPRAGTTAESLA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  276 KLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSD 355
Cdd:PRK05656 231 KLKPAFKKDGSVTAGNASSLNDGAAAVLLMSAAKAKALGLPVLAKIAAYANAGVDPAIMGIGPVSATRRCLDKAGWSLAE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  356 IDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRgkDCRFGVISMCIGTGMGAAA 435
Cdd:PRK05656 311 LDLIEANEAFAAQSLAVGKELGWDAAKVNVNGGAIALGHPIGASGCRVLVTLLHEMIRR--DAKKGLATLCIGGGQGVAL 388

                 ....*
gi 30695564  436 VFERG 440
Cdd:PRK05656 389 AIERD 393
PRK08242 PRK08242
acetyl-CoA C-acetyltransferase;
53-439 6.41e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236197 [Multi-domain]  Cd Length: 402  Bit Score: 291.79  E-value: 6.41e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   53 IVAAYRTAICKARRGG-FKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVR 131
Cdd:PRK08242   6 IYDAVRTPRGKGKKDGsLHEVKPVRLAAGLLEALRDRNGLDTAAVDDVVLGCVTPVGDQGADIARTAVLAAGLPETVPGV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIP---GGGFHGSNPRAQdfpkARDCLLPMGITSENVAERF 208
Cdd:PRK08242  86 QINRFCASGLEAVNLAAAKVRSGWDDLVIAGGVESMS--RVPmgsDGGAWAMDPSTN----FPTYFVPQGISADLIATKY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  209 GVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVatkivdpeTKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGST- 287
Cdd:PRK08242 160 GFSREDVDAYAVESQQRAAAAWAEGYFAKSVVPV--------KDQNGLTILDHDEHMRPGTTMESLAKLKPSFAMMGEMg 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  288 --------------------TAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATK 347
Cdd:PRK08242 232 gfdavalqkypeverinhvhHAGNSSGIVDGAAAVLIGSEEAGKALGLKPRARIVATATIGSDPTIMLTGPVPATRKALA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  348 LAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCI 427
Cdd:PRK08242 312 KAGLTVDDIDLFELNEAFASVVLRFMQALDIPHDKVNVNGGAIAMGHPLGATGAMILGTVLDELERRGK--RTALITLCV 389
                        410
                 ....*....|..
gi 30695564  428 GTGMGAAAVFER 439
Cdd:PRK08242 390 GGGMGIATIIER 401
PRK08235 PRK08235
acetyl-CoA C-acetyltransferase;
52-438 8.19e-95

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181311 [Multi-domain]  Cd Length: 393  Bit Score: 291.23  E-value: 8.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   52 VIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGsQRAMECRVAAYFAGFPDSVPVR 131
Cdd:PRK08235   5 VIVSAARTPFGKFG-GSLKDVKATELGGIAIKEALERANVSAEDVEEVIMGTVLQGG-QGQIPSRQAARAAGIPWEVQTE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTD--HIPGG--GFHGSNPRAQDFpKARDCL------LPMGITS 201
Cdd:PRK08235  83 TVNKVCASGLRAVTLADQIIRAGDASVIVAGGMESMSNApyILPGArwGYRMGDNEVIDL-MVADGLtcafsgVHMGVYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  202 ENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdPETKAEKaIVVSVDDGVRPNSNMADLAKLKTVF 281
Cdd:PRK08235 162 GEVAKELGISREAQDEWAYRSHQRAVSAHEEGRFEEEIVPVTI----PQRKGDP-IVVAKDEAPRKDTTIEKLAKLKPVF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  282 KQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEI 361
Cdd:PRK08235 237 DKTGTITAGNAPGVNDGAAALVLMSEDRAKQEGRKPLATILAHTAIAVEAKDFPRTPGYAINALLEKTGKTVEDIDLFEI 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695564  362 NEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDcrFGVISMCIGTGMGAAAVFE 438
Cdd:PRK08235 317 NEAFAAVALASTEIAGIDPEKVNVNGGAVALGHPIGASGARIIVTLIHELKRRGGG--IGIAAICSGGGQGDAVLIE 391
PRK07850 PRK07850
steroid 3-ketoacyl-CoA thiolase;
52-439 9.35e-93

steroid 3-ketoacyl-CoA thiolase;


Pssm-ID: 181145 [Multi-domain]  Cd Length: 387  Bit Score: 285.85  E-value: 9.35e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   52 VIVAAYRTAICKaRRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVR 131
Cdd:PRK07850   5 VIVEAVRTPIGK-RNGWLSGLHAAELLGAVQRAVLDRAGIDPGDVEQVIGGCVTQAGEQSNNITRTAWLHAGLPYHVGAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGG---GFHGSNPRAQDFpkarDCLLPMGITS-ENVAER 207
Cdd:PRK07850  84 TIDCQCGSAQQANHLVAGLIAAGAIDVGIACGVEAMS--RVPLGanaGPGRGLPRPDSW----DIDMPNQFEAaERIAKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  208 FGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKAEKAI-VVSVDDGVRpNSNMADLAKLKTVFKqNGS 286
Cdd:PRK07850 158 RGITREDVDAFGLRSQRRAAQAWAEGRFDREISPVQAPVLDEEGQPTGETrLVTRDQGLR-DTTMEGLAGLKPVLE-GGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  287 TTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFA 366
Cdd:PRK07850 236 HTAGTSSQISDGAAAVLWMDEDRARALGLRPRARIVAQALVGAEPYYHLDGPVQATAKVLEKAGMKIGDIDLVEINEAFA 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695564  367 SQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:PRK07850 316 SVVLSWAQVHEPDMDKVNVNGGAIALGHPVGSTGARLITTALHELERTDK--STALITMCAGGALSTGTIIER 386
PRK06633 PRK06633
acetyl-CoA C-acetyltransferase;
72-438 1.97e-90

acetyl-CoA C-acetyltransferase;


Pssm-ID: 168632 [Multi-domain]  Cd Length: 392  Bit Score: 279.99  E-value: 1.97e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   72 TLPDDLLAS-VLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAmECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAAS 150
Cdd:PRK06633  24 TTPAPMLAAhLIKDILQNSKIDPALVNEVILGQVITGGSGQN-PARQTLIHAGIPKEVPGYTINKVCGSGLKSVALAANS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  151 IRAGYYDIGIGAGVESMSTdhipggGFHGSNPRA-QDFPKAR-------DCLLP------MGITSENVAERFGVTREEQD 216
Cdd:PRK06633 103 IMTGDNEIVIAGGQENMSL------GMHGSYIRAgAKFGDIKmvdlmqyDGLTDvfsgvfMGITAENISKQFNISRQEQD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  217 MAAVESHKRAAAAIASGKLKDEIIPVATKIvdpetkAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQIS 296
Cdd:PRK06633 177 EFALSSHKKAAKAQLAGIFKDEILPIEVTI------KKTTSLFDHDETVRPDTSLEILSKLRPAFDKNGVVTAGNASSIN 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  297 DGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKL 376
Cdd:PRK06633 251 DGAACLMVVSEEALKKHNLTPLARIVSYASAGVDPSIMGTAPVPASQKALSKAGWSVNDLEVIEVNEAFAAQSIYVNREM 330
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695564  377 ELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMkRRGKdCRFGVISMCIGTGMGAAAVFE 438
Cdd:PRK06633 331 KWDMEKVNINGGAIAIGHPIGASGGRVLITLIHGL-RRAK-AKKGLVTLCIGGGMGMAMCVE 390
fadI PRK08963
3-ketoacyl-CoA thiolase; Reviewed
48-439 2.13e-88

3-ketoacyl-CoA thiolase; Reviewed


Pssm-ID: 181597 [Multi-domain]  Cd Length: 428  Bit Score: 276.09  E-value: 2.13e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   48 GDDIVIVAAYRTAICKARRGgFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVI----APGSQRAMECRvaayfAG 123
Cdd:PRK08963   4 GDRIAIVSGLRTPFAKQATA-FHGIPAVDLGKMVVGELLARSEIDPELIEQLVFGQVVqmpeAPNIAREIVLG-----TG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  124 FPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHIPGggfhgSNPRAQ---DFPKARDC------- 193
Cdd:PRK08963  78 MNVHTDAYSVSRACATSFQAVANVAESIMAGTIDIGIAGGADSSSVLPIGV-----SKKLARalvDLNKARTLgqrlklf 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  194 -------LLP-------------MGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEiipVATKIVDPETKA 253
Cdd:PRK08963 153 srlrlrdLLPvppavaeystglrMGDTAEQMAKTYGISREEQDALAHRSHQLAAQAWAEGKLDDE---VMTAHVPPYKQP 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  254 ekaivVSVDDGVRPNSNMADLAKLKTVF-KQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEP- 331
Cdd:PRK08963 230 -----LEEDNNIRGDSTLEDYAKLRPAFdRKHGTVTAANSTPLTDGAAAVLLMSESRAKALGLTPLGYLRSYAFAAIDVw 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  332 SVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYV----------YSCKKL-------ELDMEKVNVNGGAIAIGH 394
Cdd:PRK08963 305 QDMLLGPAYATPLALERAGLTLADLTLIDMHEAFAAQTLanlqmfaserFAREKLgrsqaigEVDMSKFNVLGGSIAYGH 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 30695564  395 PLGATGARCVATLLHEMKRRGKDcrFGVISMCIGTGMGAAAVFER 439
Cdd:PRK08963 385 PFAATGARMITQTLHELRRRGGG--LGLTTACAAGGLGAAMVLEV 427
PRK07801 PRK07801
acetyl-CoA C-acetyltransferase;
53-439 5.48e-88

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181123 [Multi-domain]  Cd Length: 382  Bit Score: 273.51  E-value: 5.48e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   53 IVAAYRTAICKaRRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRT 132
Cdd:PRK07801   6 IVDAVRTPVGK-RKGGLAGVHPADLGAHVLKGLVDRTGIDPAAVDDVIFGCVDTIGPQAGNIARTSWLAAGLPEEVPGVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  133 VNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGGfhgsnpraqdfpkARDCLLPMGITS----------- 201
Cdd:PRK07801  85 VDRQCGSSQQAIHFAAQAVMSGTQDLVVAGGVQNMS--QIPISS-------------AMTAGEQLGFTSpfaeskgwlhr 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  202 ------------ENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdpetkaekaivVSVDDGVRpNS 269
Cdd:PRK07801 150 ygdqevsqfrgaELIAEKWGISREEMERFALESHRRAFAAIRAGRFDNEIVPVGG--------------VTVDEGPR-ET 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  270 NMADLAKLKTVFkQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLA 349
Cdd:PRK07801 215 SLEKMAGLKPLV-EGGRLTAAVASQISDGASAVLLASERAVKRHGLTPRARIHHLSVRGDDPVFMLTAPIPATRYALEKT 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  350 GLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGT 429
Cdd:PRK07801 294 GLSIDDIDVVEINEAFAPVVLAWLKETGADPAKVNPNGGAIALGHPLGATGAKLMTTLLHELERTGG--RYGLQTMCEGG 371
                        410
                 ....*....|
gi 30695564  430 GMGAAAVFER 439
Cdd:PRK07801 372 GTANVTIIER 381
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
50-439 9.13e-88

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 273.12  E-value: 9.13e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckarrGGFKDTLPD----DLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAmECRVAAYFAGFP 125
Cdd:PLN02644   2 DVCIVGVARTPI-----GGFLGSLSSlsatELGSIAIQAALERAGVDPALVQEVFFGNVLSANLGQA-PARQAALGAGLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  126 DSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMS-TDHIPGGGFHGSnpRAQDfPKARDCLL--------- 195
Cdd:PLN02644  76 PSTICTTVNKVCASGMKAVMLAAQSIQLGINDVVVAGGMESMSnAPKYLPEARKGS--RLGH-DTVVDGMLkdglwdvyn 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  196 --PMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdPETKAEKAIVVSVDDGvrPNS-NMA 272
Cdd:PLN02644 153 dfGMGVCAELCADQYSISREEQDAYAIQSYERAIAAQEAGAFAWEIVPVEV----PGGRGRPSVIVDKDEG--LGKfDPA 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  273 DLAKLKTVFKQN-GSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGL 351
Cdd:PLN02644 227 KLRKLRPSFKEDgGSVTAGNASSISDGAAALVLVSGEKALELGLQVIAKIRGYADAAQAPELFTTAPALAIPKALKHAGL 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  352 NVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGM 431
Cdd:PLN02644 307 EASQVDYYEINEAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGARILVTLLGVLRSKNG--KYGVAGICNGGGG 384

                 ....*...
gi 30695564  432 GAAAVFER 439
Cdd:PLN02644 385 ASAIVVEL 392
PRK08131 PRK08131
3-oxoadipyl-CoA thiolase;
50-439 1.51e-86

3-oxoadipyl-CoA thiolase;


Pssm-ID: 181242 [Multi-domain]  Cd Length: 401  Bit Score: 270.50  E-value: 1.51e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAIckARRGGFKDTL-PDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSV 128
Cdd:PRK08131   3 DAYIYDGLRSPF--GRHAGALASVrPDDLAATVIRRLLEKSGFPGDDIEDVILGCTNQAGEDSRNVARNALLLAGLPVTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  129 PVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMST-------------------DHIPGGGFhgSNPRAQdfpk 189
Cdd:PRK08131  81 PGQTVNRLCASGLAAVIDAARAITCGEGDLYLAGGVESMSRapfvmgkaesafsrdakvfDTTIGARF--PNPKIV---- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  190 ARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdPETKAEKAIVVSVDDGVRPNS 269
Cdd:PRK08131 155 AQYGNDSMPETGDNVAAEFGISREDADRFAAQSQAKYQAAKEEGFFADEITPIEV----PQGRKLPPKLVAEDEHPRPSS 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  270 NMADLAKLKTVFkQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLA 349
Cdd:PRK08131 231 TVEALTKLKPLF-EGGVVTAGNASGINDGAAALLIGSRAAGEKYGLKPMARILSSAAAGVEPRIMGIGPVEAIKKALARA 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  350 GLNVSDIDLFEINEAFASQYVYSCKKLELDME--KVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCI 427
Cdd:PRK08131 310 GLTLDDMDIIEINEAFASQVLGCLKGLGVDFDdpRVNPNGGAIAVGHPLGASGARLALTAARELQRRGK--RYAVVSLCI 387
                        410
                 ....*....|..
gi 30695564  428 GTGMGAAAVFER 439
Cdd:PRK08131 388 GVGQGLAMVIER 399
PRK06504 PRK06504
acetyl-CoA C-acetyltransferase;
53-439 3.23e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180595 [Multi-domain]  Cd Length: 390  Bit Score: 266.59  E-value: 3.23e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   53 IVAAYRTAicKARRGG-FKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVR 131
Cdd:PRK06504   6 IVAAARTA--GGRKGGrLAGWHPADLAAQVLDALVDRSGADPALIEDVIMGCVSQVGEQATNVARNAVLASKLPESVPGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESM--------STDHIPGGGFHGSNPRAQD-FPKARDCLLpMGitSE 202
Cdd:PRK06504  84 SIDRQCGSSQQALHFAAQAVMSGTMDIVIAAGVESMtrvpmgspSTLPAKNGLGHYKSPGMEErYPGIQFSQF-TG--AE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  203 NVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKAEKaivvsVDDGVRPNSNMADLAKLKTVfK 282
Cdd:PRK06504 161 MMAKKYGLSKDQLDEFALQSHQRAIAATQAGKFKAEIVPLEITRADGSGEMHT-----VDEGIRFDATLEGIAGVKLI-A 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  283 QNGSTTAGNASQISDGAGAVLLMKrslamKKGLPILGV-----FRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDID 357
Cdd:PRK06504 235 EGGRLTAATASQICDGASGVMVVN-----ERGLKALGVkplarIHHMTVIGGDPVIMLEAPLPATERALKKAGMKIDDID 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  358 LFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVF 437
Cdd:PRK06504 310 LYEVNEAFASVPLAWLKATGADPERLNVNGGAIALGHPLGASGTKLMTTLVHALKQRGK--RYGLQTMCEGGGMANVTIV 387

                 ..
gi 30695564  438 ER 439
Cdd:PRK06504 388 ER 389
PRK08170 PRK08170
acetyl-CoA C-acetyltransferase;
50-440 8.70e-85

acetyl-CoA C-acetyltransferase;


Pssm-ID: 181265 [Multi-domain]  Cd Length: 426  Bit Score: 266.50  E-value: 8.70e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTViAPGSQRAMECRVAAYFAGFPDSVP 129
Cdd:PRK08170   4 PVYIVDGARTPFLKAR-GGPGPFSASDLAVAAGRALLNRQPFAPDDLDEVILGCA-MPSPDEANIARVVALRLGCGEKVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  130 VRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIP-----------GGGFHGSNP--RAQDFPKARD---- 192
Cdd:PRK08170  82 AWTVQRNCASGMQALDSAAANIALGRADLVLAGGVEAMS--HAPllfsekmvrwlAGWYAAKSIgqKLAALGKLRPsyla 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  193 -------------CLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKdEIIPvatkIVDPETKaekaiVV 259
Cdd:PRK08170 160 pvigllrgltdpvVGLNMGQTAEVLAHRFGITREQMDAYAARSHQRLAAAQAEGRLK-EVVP----LFDRDGK-----FY 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  260 SVDDGVRPNSNMADLAKLKTVF-KQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGP 338
Cdd:PRK08170 230 DHDDGVRPDSSMEKLAKLKPFFdRPYGRVTAGNSSQITDGACWLLLASEEAVKKYGLPPLGRIVDSQWAALDPSQMGLGP 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  339 AVAIPAATKLAGLNVSDIDLFEINEAFASQyVYSCKKL------------------ELDMEKVNVNGGAIAIGHPLGATG 400
Cdd:PRK08170 310 VHAATPLLQRHGLTLEDLDLWEINEAFAAQ-VLACLAAwadeeycreqlgldgalgELDRERLNVDGGAIALGHPVGASG 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 30695564  401 ARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFERG 440
Cdd:PRK08170 389 ARIVLHLLHALKRRGT--KRGIAAICIGGGQGGAMLLERV 426
Thiolase_N pfam00108
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
51-308 3.97e-81

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: 251.45  E-value: 3.97e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564    51 IVIVAAYRTAICKARrGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMEcRVAAYFAGFPDSVPV 130
Cdd:pfam00108   1 VVIVSAARTPFGSFG-GSLKDVSAVELGAEAIKAALERAGVDPEDVDEVIVGNVLQAGEGQNPA-RQAALKAGIPDSAPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   131 RTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdHIPGGgfHGSNPRA---QDFPKARDCLLP----------- 196
Cdd:pfam00108  79 VTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESMS--HAPYA--LPTDARSglkHGDEKKHDLLIPdgltdafngyh 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   197 MGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETkaekaiVVSVDDGVRPNSNMADLAK 276
Cdd:pfam00108 155 MGLTAENVAKKYGISREEQDAFAVKSHQKAAAAPKAGKFKDEIVPVTVKGRKGKP------TVDKDEGIRPPTTAEPLAK 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 30695564   277 LKTVFKQNGSTTAGNASQISDGAGAVLLMKRS 308
Cdd:pfam00108 229 LKPAFDKEGTVTAGNASPINDGAAAVLLMSES 260
PRK06690 PRK06690
acetyl-CoA C-acyltransferase;
52-438 7.15e-76

acetyl-CoA C-acyltransferase;


Pssm-ID: 180659 [Multi-domain]  Cd Length: 361  Bit Score: 241.59  E-value: 7.15e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   52 VIVAAYRTAICKaRRGGFKDTLPDDLLASVLKAVVERTsldPSEVGDIVVGTVIAPGSQRAmecRVAAYFAGFPDSVPVR 131
Cdd:PRK06690   4 VIVEAKRTPIGK-KNGMLKDYEVQQLAAPLLTFLSKGM---EREIDDVILGNVVGPGGNVA---RLSALEAGLGLHIPGV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHIpgggfhgsNPRAQDFPKA---RDcllpMGITSENVAERF 208
Cdd:PRK06690  77 TIDRQCGAGLEAIRTACHFIQGGAGKCYIAGGVESTSTSPF--------QNRARFSPETigdPD----MGVAAEYVAERY 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  209 GVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIvdpetkaekaivvsvDDGVRPNSNMADL-AKLKTVFKQNGST 287
Cdd:PRK06690 145 NITREMQDEYACLSYKRTLQALEKGYIHEEILSFNGLL---------------DESIKKEMNYERIiKRTKPAFLHNGTV 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  288 TAGNASQISDGAGAVLLMKRSLAMKKGL-PILGVFRSfAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFA 366
Cdd:PRK06690 210 TAGNSCGVNDGACAVLVMEEGQARKLGYkPVLRFVRS-AVVGVDPNLPGTGPIFAVNKLLNEMNMKVEDIDYFEINEAFA 288
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695564  367 SQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRgkDCRFGVISMCIGTGMGAAAVFE 438
Cdd:PRK06690 289 SKVVACAKELQIPYEKLNVNGGAIALGHPYGASGAMLVTRLFYQAKRE--DMKYGIATLGIGGGIGLALLFE 358
PRK06025 PRK06025
acetyl-CoA C-acetyltransferase;
50-439 2.70e-69

acetyl-CoA C-acetyltransferase;


Pssm-ID: 235675 [Multi-domain]  Cd Length: 417  Bit Score: 226.20  E-value: 2.70e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRT--AICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDS 127
Cdd:PRK06025   3 EAYIIDAVRTprGIGKVGKGALAHLHPQHLAATVLKALAERNGLNTADVDDIIWSTSSQRGKQGGDLGRMAALDAGYDIK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  128 VPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMS--TDHIPGGGFHGSNPRAQDFPKAR-DCLLPM---GITS 201
Cdd:PRK06025  83 ASGVTLDRFCGGGITSVNLAAAQIMSGMEDLVIAGGTEMMSytAAMAAEDMAAGKPPLGMGSGNLRlRALHPQshqGVCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  202 ENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVatkivdpeTKAEKAIVVSVDDGVRPNSNMADLAKLKTVF 281
Cdd:PRK06025 163 DAIATMEGITREALDALGLESQRRAARAIKEGRFDKSLVPV--------YRDDGSVALDHEEFPRPQTTAEGLAALKPAF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  282 K-------QNGSTT-------------------AGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMG 335
Cdd:PRK06025 235 TaiadyplDDKGTTyrglinqkypdleikhvhhAGNSSGVVDGAAALLLASKAYAEKHGLKPRARIVAMANMGDDPTLML 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  336 IGPavaIPAATKL---AGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMK 412
Cdd:PRK06025 315 NAP---VPAAKKVlakAGLTKDDIDLWEINEAFAVVAEKFIRDLDLDRDKVNVNGGAIALGHPIGATGSILIGTVLDELE 391
                        410       420
                 ....*....|....*....|....*..
gi 30695564  413 RRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:PRK06025 392 RRGL--KRGLVTMCAAGGMAPAIIIER 416
PRK06954 PRK06954
acetyl-CoA C-acetyltransferase;
44-438 2.60e-65

acetyl-CoA C-acetyltransferase;


Pssm-ID: 180775 [Multi-domain]  Cd Length: 397  Bit Score: 215.14  E-value: 2.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   44 MAAFGDDIVIVAAYRTAICkARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIaPGSQRAMECRVAAYFAG 123
Cdd:PRK06954   2 TAVDQDPIVIASAARTPMA-AFQGEFASLTAPQLGAAAIAAAVERAGLKPEQIDEVVMGCVL-PAGQGQAPARQAALGAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  124 FPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDH--IPG--GGFHGSNPRAQD------FPKARDC 193
Cdd:PRK06954  80 LPLSVGCTTVNKMCGSGMRAAMFAHDMLVAGSVDVIVAGGMESMTNAPylLPKarGGMRMGHGQVLDhmfldgLEDAYDK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  194 LLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETkaekaiVVSVDDGVRpNSNMAD 273
Cdd:PRK06954 160 GRLMGTFAEECAGEYGFTREAQDAFAIESLARAKRANEDGSFAWEIAPVTVAGKKGDT------VIDRDEQPF-KANPEK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  274 LAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNV 353
Cdd:PRK06954 233 IPTLKPAFSKTGTVTAANSSSISDGAAALVMMRASTAKRLGLAPLARVVGHSTFAQAPSKFTTAPVGAIRKLFEKNGWRA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  354 SDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGA 433
Cdd:PRK06954 313 AEVDLFEINEAFAVVTMAAMKEHGLPHEKVNVNGGACALGHPIGASGARILVTLIGALRARGG--KRGVASLCIGGGEAT 390

                 ....*
gi 30695564  434 AAVFE 438
Cdd:PRK06954 391 AMGIE 395
PRK06366 PRK06366
acetyl-CoA C-acetyltransferase;
50-438 1.06e-62

acetyl-CoA C-acetyltransferase;


Pssm-ID: 102340 [Multi-domain]  Cd Length: 388  Bit Score: 208.33  E-value: 1.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   50 DIVIVAAYRTAICKARRGGFKDTLPDdLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRvAAYFAGFPDSVP 129
Cdd:PRK06366   3 DVYIVSAKRTAIGKFGRSFSKIKAPQ-LGGAAIKAVIDDAKLDPALVQEVIMGNVIQAGVGQNPAGQ-AAYHAGLPFGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  130 VRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDH--IPGGGFHGSNPRAQDFPKARDCLLP----------- 196
Cdd:PRK06366  81 KYTVNVVCASGMLAVESAAREIMLGERDLVIAGGMENMSNAPflLPSDLRWGPKHLLHKNYKIDDAMLVdglidafyfeh 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  197 MGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdpetkaekaivVSVDDGVRpNSNMADLAK 276
Cdd:PRK06366 161 MGVSAERTARKYGITREMADEYSVQSYERAIRATESGEFRNEIVPFND--------------LDRDEGIR-KTTMEDLAK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  277 LKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPavaIPAATKL---AGLNV 353
Cdd:PRK06366 226 LPPAFDKNGILTAGNSAQLSDGGSALVMASEKAINEYGLKPIARITGYESASLDPLDFVEAP---IPATRKLlekQNKSI 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  354 SDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRgkDCRFGVISMCIGTGMGA 433
Cdd:PRK06366 303 DYYDLVEHNEAFSIASIIVRDQLKIDNERFNVNGGAVAIGHPIGNSGSRIIVTLINALKTR--HMKTGLATLCHGGGGAH 380

                 ....*
gi 30695564  434 AAVFE 438
Cdd:PRK06366 381 TLTLE 385
Thiolase_C pfam02803
Thiolase, C-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ...
315-439 1.57e-60

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: 193.24  E-value: 1.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   315 LPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGH 394
Cdd:pfam02803   1 LKPLARIRSYATAGVDPAIMGIGPAYAIPKALKKAGLTVNDIDLFEINEAFAAQALAVAKDLGIDPEKVNVNGGAIALGH 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 30695564   395 PLGATGARCVATLLHEMKRRGKdcRFGVISMCIGTGMGAAAVFER 439
Cdd:pfam02803  81 PLGASGARILVTLLHELKRRGG--KYGLASLCIGGGQGVAMIIER 123
PRK09268 PRK09268
acetyl-CoA C-acetyltransferase;
76-439 1.64e-53

acetyl-CoA C-acetyltransferase;


Pssm-ID: 236440 [Multi-domain]  Cd Length: 427  Bit Score: 185.10  E-value: 1.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   76 DLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMeCRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGY 155
Cdd:PRK09268  33 DMLTAALDGLVDRFGLQGERLGEVVAGAVLKHSRDFNL-TRECVLGSALSPYTPAYDLQQACGTGLEAAILVANKIALGQ 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  156 YDIGIGAGVESMSTdhIPGGGFHGSNPRAQDFPKARDCL---------------------------LPMGITSENVAERF 208
Cdd:PRK09268 112 IDSGIAGGVDTTSD--APIAVNEGLRKILLELNRAKTTGdrlkalgklrpkhlapeiprngeprtgLSMGEHAAITAKEW 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  209 GVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATkivdpetkaekaivVSVDDGVRPNSNMADLAKLKTVF--KQNGS 286
Cdd:PRK09268 190 GISREAQDELAAASHQNLAAAYDRGFFDDLITPFLG--------------LTRDNNLRPDSSLEKLAKLKPVFgkGGRAT 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  287 TTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFA------VTGVEPSVMGigPAVAIPAATKLAGLNVSDIDLFE 360
Cdd:PRK09268 256 MTAGNSTPLTDGASVVLLASEEWAAEHGLPVLAYLVDAEtaavdfVHGKEGLLMA--PAYAVPRLLARNGLTLQDFDFYE 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  361 INEAFASQYVYSCKKLE-----------------LDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDcRfGVI 423
Cdd:PRK09268 334 IHEAFASQVLATLKAWEdeeycrerlgldaplgsIDRSKLNVNGSSLAAGHPFAATGGRIVATLAKLLAEKGSG-R-GLI 411
                        410
                 ....*....|....*.
gi 30695564  424 SMCIGTGMGAAAVFER 439
Cdd:PRK09268 412 SICAAGGQGVTAILER 427
nondecarbox_cond_enzymes cd00826
nondecarboxylating condensing enzymes; In general, thiolases catalyze the reversible thiolytic ...
54-438 1.94e-52

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: 181.15  E-value: 1.94e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  54 VAAYRTAICK--ARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIaPGSQRAMECRVAAYFAGFPDSVPVR 131
Cdd:cd00826   1 AGAAMTAFGKfgGENGADANDLAHEAGAKAIAAALEPAGVAAGAVEEACLGQVL-GAGEGQNCAQQAAMHAGGLQEAPAI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 132 TVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDhipgggfhgsnprAQDFPKARDCllpmgitseNVAERFGVT 211
Cdd:cd00826  80 GMNNLCGSGLRALALAMQLIAGGDANCILAGGFEKMETS-------------AENNAKEKHI---------DVLINKYGM 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 212 REEQDMAAVESHKRAAAAIASGKLKDEIIPVATKivdpETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGN 291
Cdd:cd00826 138 RACPDAFALAGQAGAEAAEKDGRFKDEFAKFGVK----GRKGDIHSDADEYIQFGDEASLDEIAKLRPAFDKEDFLTAGN 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 292 ASQISDGAGAVLLMKRSLAMKKGLPI-------LGVFRSFAVTGVEPS----VMGIGPAVAIPAATKLAGLNVSDIDLFE 360
Cdd:cd00826 214 ACGLNDGAAAAILMSEAEAQKHGLQSkareiqaLEMITDMASTFEDKKvikmVGGDGPIEAARKALEKAGLGIGDLDLIE 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 361 INEAFASQYVYSCKKLELDMEK------------------VNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDC---R 419
Cdd:cd00826 294 AHDAFAANACATNEALGLCPEGqggalvdrgdntyggksiINPNGGAIAIGHPIGASGAAICAELCFELKGEAGKRqgaG 373
                       410
                ....*....|....*....
gi 30695564 420 FGVISMCIGTGMGAAAVFE 438
Cdd:cd00826 374 AGLALLCIGGGGGAAMCIE 392
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
289-436 2.58e-18

Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.


Pssm-ID: 238201 [Multi-domain]  Cd Length: 254  Bit Score: 84.42  E-value: 2.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 289 AGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPS----VMGIGPAVAIPAATKLAGLNVSDIDLFEINEA 364
Cdd:cd00327  94 GSEEFVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDGASmvpaVSGEGLARAARKALEGAGLTPSDIDYVEAHGT 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 365 FASQYVYSCKKLELDMEKVN---VNGGAIAIGHPLGATGARCVATLLHEMKRRGKDC-----RFGVISMCIGTGMGAAAV 436
Cdd:cd00327 174 GTPIGDAVELALGLDPDGVRspaVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPtprepRTVLLLGFGLGGTNAAVV 253
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
71-437 2.88e-17

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: 83.08  E-value: 2.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  71 DTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPdsVPVRTVNRQCSSGLQAVADVAAS 150
Cdd:cd00829  13 DRSPLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFPGALIAEYLGLLG--KPATRVEAAGASGSAAVRAAAAA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 151 IRAGYYDIGIGAGVESMSTdhipGGGFHGSNPRAQDFPKARDcLLPMGITSENVA--------ERFGVTREEQDMAAVES 222
Cdd:cd00829  91 IASGLADVVLVVGAEKMSD----VPTGDEAGGRASDLEWEGP-EPPGGLTPPALYalaarrymHRYGTTREDLAKVAVKN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 223 HKRAAA---AIasgkLKDEIIPV----ATKIVDPetkaekaivvsvddgvrpnsnmadlaklktvfkqngsTTAGNASQI 295
Cdd:cd00829 166 HRNAARnpyAQ----FRKPITVEdvlnSRMIADP-------------------------------------LRLLDCCPV 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 296 SDGAGAVLLMKRSLAMKKGLP---ILGV-FRSFAVTGVEPSVMGIGPAV--AIPAATKLAGLNVSDIDLFEINEAFASQ- 368
Cdd:cd00829 205 SDGAAAVVLASEERARELTDRpvwILGVgAASDTPSLSERDDFLSLDAArlAARRAYKMAGITPDDIDVAELYDCFTIAe 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 369 YVYS-----CKK-----------LELDME-KVNVNGGAIAIGHPLGATGARCVATLLHEMKRRG-----KDCRFGVISMc 426
Cdd:cd00829 285 LLALedlgfCEKgeggklvregdTAIGGDlPVNTSGGLLSKGHPLGATGLAQAVEAVRQLRGEAgarqvPGARVGLAHN- 363
                       410
                ....*....|.
gi 30695564 427 IGtGMGAAAVF 437
Cdd:cd00829 364 IG-GTGSAAVV 373
PRK06289 PRK06289
acetyl-CoA acetyltransferase; Provisional
76-402 6.43e-11

acetyl-CoA acetyltransferase; Provisional


Pssm-ID: 235771 [Multi-domain]  Cd Length: 403  Bit Score: 63.94  E-value: 6.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   76 DLLASVLKAVVERTSLDPSEVGDIVVGTVIAP-----GSQRAMECRVAAYFAGFPDSvpvrtvnRQ---CSSGLQAVADV 147
Cdd:PRK06289  28 DLTREVVDGTLAAAGVDADDIEVVHVGNFFGElfagqGHLGAMPATVHPALWGVPAS-------RHeaaCASGSVATLAA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  148 AASIRAGYYDIGIGAGVESMST-------DHIPGGGFHGSNPRAQDFPKARdcllPMGITSENVAERFGVTreeqdmaav 220
Cdd:PRK06289 101 MADLRAGRYDVALVVGVELMKTvpgdvaaEHLGAAAWTGHEGQDARFPWPS----MFARVADEYDRRYGLD--------- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  221 ESHKRAAAAIASGKLKDEiiPVAT----KIVDPETKAEKAIVVSVDDGVRpnsnmadlaklktvfKQNgsttagnASQIS 296
Cdd:PRK06289 168 EEHLRAIAEINFANARRN--PNAQtrgwAFPDEATNDDDATNPVVEGRLR---------------RQD-------CSQVT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  297 DGAGAVLLMK----RSLAMKKGLP-ILGVFRSFAVTGVEPSVMG------IGPAV--AIPAATKLAGLNVSDIDLFEINE 363
Cdd:PRK06289 224 DGGAGVVLASdaylRDYADARPIPrIKGWGHRTAPLGLEQKLDRsagdpyVLPHVrqAVLDAYRRAGVGLDDLDGFEVHD 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695564  364 AF-ASQYVY-----------SCKKLE---LDME---KVNVNGGAIAIGHPLGATGAR 402
Cdd:PRK06289 304 CFtPSEYLAidhigltgpgeSWKAIEngeIAIGgrlPINPSGGLIGGGHPVGASGVR 360
PRK06064 PRK06064
thiolase domain-containing protein;
76-436 3.32e-10

thiolase domain-containing protein;


Pssm-ID: 235688 [Multi-domain]  Cd Length: 389  Bit Score: 61.45  E-value: 3.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   76 DLLASVLKAVVERTSLDPSEVGDIVVGTVIAPG-SQRAMECRVAAYFAGFPdSVPVRTVNRQCSSGLQAVADVAASIRAG 154
Cdd:PRK06064  24 DLAVEAGLEALEDAGIDGKDIDAMYVGNMSAGLfVSQEHIAALIADYAGLA-PIPATRVEAACASGGAALRQAYLAVASG 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  155 YYDIGIGAGVESM-------STDHIPGGG------FHGSNPRAQDFPKARDCLlpmgitsenvaERFGVTREEQDMAAVE 221
Cdd:PRK06064 103 EADVVLAAGVEKMtdvptpdATEAIARAGdyeweeFFGATFPGLYALIARRYM-----------HKYGTTEEDLALVAVK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  222 SHKRAAaaiasgklkdeiipvatkiVDPETKAEKAIvvSVDDGVrpNSNM-ADLAKLKtvfkqngsttagNASQISDGAG 300
Cdd:PRK06064 172 NHYNGS-------------------KNPYAQFQKEI--TVEQVL--NSPPvADPLKLL------------DCSPITDGAA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  301 AVLLMK--------------RSLAMKKGLPILGVFRSFavTGVEPSVmgigpaVAIPAATKLAGLNVSDIDLFEINEAFA 366
Cdd:PRK06064 217 AVILASeekakeytdtpvwiKASGQASDTIALHDRKDF--TTLDAAV------VAAEKAYKMAGIEPKDIDVAEVHDCFT 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  367 SQYVYS------CKK---LELDMEK---------VNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIG 428
Cdd:PRK06064 289 IAEILAyedlgfAKKgegGKLAREGqtyiggdipVNPSGGLKAKGHPVGATGVSQAVEIVWQLRGEAEKGRQQVIGAGYG 368
                        410
                 ....*....|...
gi 30695564  429 T-----GMGAAAV 436
Cdd:PRK06064 369 LthnvgGTGHTAV 381
PRK12578 PRK12578
thiolase domain-containing protein;
82-400 9.81e-09

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 57.16  E-value: 9.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   82 LKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYfAGFPDSVPVRtVNRQCSSGLQAVADVAASIRAGYYDIGIG 161
Cdd:PRK12578  29 IKEALNDAGVSQTDIELVVVGSTAYRGIELYPAPIVAEY-SGLTGKVPLR-VEAMCATGLAASLTAYTAVASGLVDMAIA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  162 AGVESM-----STDHIPGG---------GFHGSNpraqdFPKardcLLPMGITSEnvAERFGVTREEQDMAAVESHKRAA 227
Cdd:PRK12578 107 VGVDKMtevdtSTSLAIGGrggnyqweyHFYGTT-----FPT----YYALYATRH--MAVYGTTEEQMALVSVKAHKYGA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  228 aaiasgklkdeiipvatkiVDPETKAEKAIVVsvdDGVRPNSNMADLAKLKtvfkqngsttagNASQISDGAGAVLLMK- 306
Cdd:PRK12578 176 -------------------MNPKAHFQKPVTV---EEVLKSRAISWPIKLL------------DSCPISDGSATAIFASe 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  307 ---RSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPA---ATKLAGLNVSDI------DLFEINEAFASQYVYSCK 374
Cdd:PRK12578 222 ekvKELKIDSPVWITGIGYANDYAYVARRGEWVGFKATQLAarqAYNMAKVTPNDIevatvhDAFTIAEIMGYEDLGFTE 301
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 30695564  375 K-------LELDMEK-----VNVNGGAIAIGHPLGATG 400
Cdd:PRK12578 302 KgkggkfiEEGQSEKggkvgVNLFGGLKAKGHPLGATG 339
PTZ00455 PTZ00455
3-ketoacyl-CoA thiolase; Provisional
75-412 8.35e-07

3-ketoacyl-CoA thiolase; Provisional


Pssm-ID: 240424 [Multi-domain]  Cd Length: 438  Bit Score: 51.05  E-value: 8.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   75 DDLLASVLKAVVERTSLDPSE--VGDIVVGTVIAP--------GSQRAMECRVAAYFAGFPDSVPVRtVNRQCSSGLQAV 144
Cdd:PTZ00455  49 EELLATAIQGTLENTGLDGKAalVDKVVVGNFLGElfssqghlGPAAVGSLGQSGASNALLYKPAMR-VEGACASGGLAV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  145 ADVAASIRAGYYDIGIGAGVESMSTDHIPGGGFHGSnpRAQDFPKARD-------CLLpmgitsenvAERFGVTREEQDM 217
Cdd:PTZ00455 128 QSAWEALLAGTSDIALVVGVEVQTTVSARVGGDYLA--RAADYRRQRKlddftfpCLF---------AKRMKYIQEHGHF 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  218 AAVESHKRAAAAIASGKlKDEIIPVATKIVDPEtkaekaivvSVDDGVRPNSNMADLAKLKTVFKQNgsttagNASQISD 297
Cdd:PTZ00455 197 TMEDTARVAAKAYANGN-KNPLAHMHTRKLSLE---------FCTGASDKNPKFLGNETYKPFLRMT------DCSQVSD 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  298 GAGAVLLmkrslAMKKGLPILGVFRSFA-VTGVEPSVMGIG--------------PAVAIPAATKLAGLNVSDIDLFEIN 362
Cdd:PTZ00455 261 GGAGLVL-----ASEEGLQKMGLSPNDSrLVEIKSLACASGnlyedppdatrmftSRAAAQKALSMAGVKPSDLQVAEVH 335
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695564  363 EAF------------------ASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMK 412
Cdd:PTZ00455 336 DCFtiaellmyealgiaeyghAKDLIRNGATALEGRIPVNTGGGLLSFGHPVGATGVKQIMEVYRQMK 403
PRK08256 PRK08256
lipid-transfer protein; Provisional
128-403 1.45e-04

lipid-transfer protein; Provisional


Pssm-ID: 181327 [Multi-domain]  Cd Length: 391  Bit Score: 43.73  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  128 VPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMStdhiPG---GGFHGSNPRAQDFPKARDCL-----LPM-- 197
Cdd:PRK08256  71 IPIVNVNNNCSTGSTALFLARQAVRSGAADCALALGFEQMQ----PGalgSVWDDRPSPLERFDKALAELqgfdpAPPal 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  198 ---GITSENVAERFGVTREEQDMAAVESHKRAAA---AIASGKLKDEIIPVATKIVDPETKAEkaivvsvddgvrpnsnm 271
Cdd:PRK08256 147 rmfGGAGREHMEKYGTTAETFAKIGVKARRHAANnpyAQFRDEYTLEDVLASPMIWGPLTRLQ----------------- 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  272 adlaklktvfkqngsttagnASQISDGAGAVLLMKRSLAMKKGLP----ILG--VFRSFAVTGVEPSVMG-IGPAVAIPA 344
Cdd:PRK08256 210 --------------------CCPPTCGAAAAIVCSEEFARKHGLDraveIVAqaMTTDTPSTFDGRSMIDlVGYDMTRAA 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  345 ATKL---AGLNVSDIDLFEINEAFASQYVYSCKKLEL----DMEK--------------VNVNGGAIAIGHPLGATG-AR 402
Cdd:PRK08256 270 AQQVyeqAGIGPEDIDVVELHDCFSANELLTYEALGLcpegEAEKfiddgdntyggrwvVNPSGGLLSKGHPLGATGlAQ 349

                 .
gi 30695564  403 C 403
Cdd:PRK08256 350 C 350
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
295-408 2.98e-04

Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.


Pssm-ID: 238430 [Multi-domain]  Cd Length: 406  Bit Score: 42.91  E-value: 2.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 295 ISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTG-----VEPSVMGIGPAVAIPAATKLAGLNVSDIDLfeIN------- 362
Cdd:cd00834 229 LGEGAGVLVLESLEHAKARGAKIYAEILGYGASSdayhiTAPDPDGEGAARAMRAALADAGLSPEDIDY--INahgtstp 306
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30695564 363 -----EAFAsqyvysCKKLELD-MEKVNVNGGAIAIGHPLGATGA-RCVATLL 408
Cdd:cd00834 307 lndaaESKA------IKRVFGEhAKKVPVSSTKSMTGHLLGAAGAvEAIATLL 353
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
295-360 4.07e-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: 42.55  E-value: 4.07e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30695564 295 ISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVT-------GVEPSvmGIGPAVAIPAATKLAGLNVSDIDLFE 360
Cdd:cd00833 233 RGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNqdgrtkgITAPS--GEAQAALIRRAYARAGVDPSDIDYVE 303
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
320-438 2.46e-03

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: 39.71  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 320 VFRsFAVTGVEPsvmgigpavAIPAATKLAGLNVSDIDLF-------EINEAFAsqyvyscKKLELDMEKVNVNggaiaI 392
Cdd:COG0332 218 VFK-FAVRNLPE---------VIREALEKAGLTLDDIDWFiphqanlRIIEAVA-------KRLGLPEEKVVVN-----I 275
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30695564 393 GHpLGATGARCVATLLHEMKRRGKDCRfGVISMCIGTGMG---AAAVFE 438
Cdd:COG0332 276 DR-YGNTSAASIPLALDEALREGRIKP-GDLVLLAGFGAGltwGAAVLR 322
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
252-414 3.09e-03

"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.


Pssm-ID: 238424 [Multi-domain]  Cd Length: 407  Bit Score: 39.73  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 252 KAEKAIVVSVDD----GVRPNSNMADLAKLKTVFKQNGSTTAGNASQI--SDGAGAVLLMKRSLAMKKGLPILGVFRSFA 325
Cdd:cd00828 180 KADIVVVGGVEDpleeGLSGFANMGALSTAEEEPEEMSRPFDETRDGFveAEGAGVLVLERAELALARGAPIYGRVAGTA 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 326 VT--GVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIA-------IGHPL 396
Cdd:cd00828 260 STtdGAGRSVPAGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAPLPvtaqkalFGHSK 339
                       170
                ....*....|....*...
gi 30695564 397 GATGARCVATLLHEMKRR 414
Cdd:cd00828 340 GAAGALQLIGALQSLEHG 357
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
297-401 3.61e-03

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 39.39  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  297 DGAGAVLLMKRSLAMKKGLPILGVFRSFAVTG-----VEPSVMGIGPAVAIPAATKLAGLNVSDIDLF-------EINEA 364
Cdd:PRK07314 232 EGAGILVLEELEHAKARGAKIYAEVVGYGMTGdayhmTAPAPDGEGAARAMKLALKDAGINPEDIDYInahgtstPAGDK 311
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 30695564  365 FASQYVyscKKLELD-MEKVNVNGGAIAIGHPLGATGA 401
Cdd:PRK07314 312 AETQAI---KRVFGEhAYKVAVSSTKSMTGHLLGAAGA 346
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
295-436 4.02e-03

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 39.06  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 295 ISDGAGAVLLMKRSLAMKKGLPILG------------VFRsFAVTGVEPSVMgigpavaipAATKLAGLNVSDIDLF--- 359
Cdd:cd00830 180 GSDGSGADLLTIPAGGSRSPFEDAEggdpylvmdgreVFK-FAVRLMPESIE---------EALEKAGLTPDDIDWFvph 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564 360 ----EINEAFAsqyvyscKKLELDMEKVNVNggaiaiGHPLGATGARCVATLLHEMKRRGKDCRFGVISMC-IGTGM--G 432
Cdd:cd00830 250 qanlRIIEAVA-------KRLGLPEEKVVVN------LDRYGNTSAASIPLALDEAIEEGKLKKGDLVLLLgFGAGLtwG 316

                ....
gi 30695564 433 AAAV 436
Cdd:cd00830 317 AALL 320
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
300-405 4.55e-03

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 39.26  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  300 GAVLLMK-RSLAMKKGLPILGVFRSFAVT-----GVEPSVMGIGPAVAIPAATKLAGLNVSDIDLF-------EINEAFA 366
Cdd:PRK05952 212 GAILVLEsAELAQKRGAKIYGQILGFGLTcdayhMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIhahgtatRLNDQRE 291
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 30695564  367 SQYVYSckkleLDMEKVNVNGGAIAIGHPLGATGARCVA 405
Cdd:PRK05952 292 ANLIQA-----LFPHRVAVSSTKGATGHTLGASGALGVA 325
ACP_syn_III_C pfam08541
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on ...
349-438 5.79e-03

3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal; This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria.


Pssm-ID: 430060  Cd Length: 90  Bit Score: 35.94  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564   349 AGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNggaiaIGHpLGATGARCVATLLHEMKRRGKDCRFGVISMCiG 428
Cdd:pfam08541   4 AGLTPEDIDWFVPHQANLRIIDAVAKRLGLPPEKVVVN-----LDE-YGNTSAASIPLALDEAVEEGKLKPGDLVLLV-G 76
                          90
                  ....*....|...
gi 30695564   429 TGMG---AAAVFE 438
Cdd:pfam08541  77 FGAGltwGAALLR 89
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
84-169 1.00e-02

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: 38.29  E-value: 1.00e-02
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695564  84 AVVERTSLDPSEVGdIVVGTVIapGSQRAMECRVAAYFAGFPDSVPVRTVNRQ-------------------------CS 138
Cdd:cd00834  86 AGLDPEELDPERIG-VVIGSGI--GGLATIEEAYRALLEKGPRRVSPFFVPMAlpnmaagqvairlglrgpnytvstaCA 162
                        90       100       110
                ....*....|....*....|....*....|.
gi 30695564 139 SGLQAVADVAASIRAGYYDIGIGAGVESMST 169
Cdd:cd00834 163 SGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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